PML_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PML_HUMAN
• UniProt AC: P29590
• Protein Name: Protein PML
• Gene Name: PML
• Organism: Homo sapiens (Human).
• Sequence Length: 882
• Subcellular Localization: Nucleus. Nucleus, nucleoplasm. Cytoplasm. Nucleus, PML body . Nucleus, nucleolus. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Isoform PML-1 can
• Protein Description: Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Isoform PML-4 has a multifaceted role in the regulation of apoptosis and growth suppression: activates RB1 and inhibits AKT1 via interactions with PP1 and PP2A phosphatases respectively, negatively affects the PI3K pathway by inhibiting MTOR and activating PTEN, and positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Isoform PML-4 also: acts as a transcriptional repressor of TBX2 during cellular senescence and the repression is dependent on a functional RBL2/E2F4 repressor complex, regulates double-strand break repair in gamma-irradiation-induced DNA damage responses via its interaction with WRN, acts as a negative regulator of telomerase by interacting with TERT, and regulates PER2 nuclear localization and circadian function. Isoform PML-6 inhibits specifically the activity of the tetrameric form of PKM. The nuclear isoforms (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5) in concert with SATB1 are involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Isoform PML-2 is required for efficient IFN-gamma induced MHC II gene transcription via regulation of CIITA. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. PML also regulates transcription activity of ELF4 and can act as an important mediator for TNF-alpha- and IFN-alpha-mediated inhibition of endothelial cell network formation and migration.; Exhibits antiviral activity against both DNA and RNA viruses. The antiviral activity can involve one or several isoform(s) and can be enhanced by the permanent PML-NB-associated protein DAXX or by the recruitment of p53/TP53 within these structures. Isoform PML-4 restricts varicella zoster virus (VZV) via sequestration of virion capsids in PML-NBs thereby preventing their nuclear egress and inhibiting formation of infectious virus particles. The sumoylated isoform PML-4 restricts rabies virus by inhibiting viral mRNA and protein synthesis. The cytoplasmic isoform PML-14 can restrict herpes simplex virus-1 (HHV-1) replication by sequestering the viral E3 ubiquitin-protein ligase ICP0 in the cytoplasm. Isoform PML-6 shows restriction activity towards human cytomegalovirus (HCMV) and influenza A virus strains PR8(H1N1) and ST364(H3N2). Sumoylated isoform PML-4 and isoform PML-12 show antiviral activity against encephalomyocarditis virus (EMCV) by promoting nuclear sequestration of viral polymerase (P3D-POL) within PML NBs. Isoform PML-3 exhibits antiviral activity against poliovirus by inducing apoptosis in infected cells through the recruitment and the activation of p53/TP53 in the PML-NBs. Isoform PML-3 represses human foamy virus (HFV) transcription by complexing the HFV transactivator, bel1/tas, preventing its binding to viral DNA. PML may positively regulate infectious hepatitis C viral (HCV) production and isoform PML-2 may enhance adenovirus transcription..
• Protein Sequence: MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPALARAEGVSTPLAGRGLAERASQQS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MEPAPARSPRPQQDP CCCCCCCCCCCCCCC	27.63	23401153
22	Phosphorylation	PARPQEPTMPPPETP CCCCCCCCCCCCCCC	41.37	29255136
28	Phosphorylation	PTMPPPETPSEGRQP CCCCCCCCCCCCCCC	37.58	26657352
30	Phosphorylation	MPPPETPSEGRQPSP CCCCCCCCCCCCCCC	61.17	26657352
36	Phosphorylation	PSEGRQPSPSPSPTE CCCCCCCCCCCCCCC	29.67	29255136
38	Phosphorylation	EGRQPSPSPSPTERA CCCCCCCCCCCCCCC	42.20	30266825
40	Phosphorylation	RQPSPSPSPTERAPA CCCCCCCCCCCCCCC	49.11	29255136
42	Phosphorylation	PSPSPSPTERAPASE CCCCCCCCCCCCCCH	42.30	30266825
48	Phosphorylation	PTERAPASEEEFQFL CCCCCCCCHHHHHHH	44.47	29255136
65	Sumoylation	QQCQAEAKCPKLLPC HHHHHHHCCCCHHHH	42.44	-
65	Sumoylation	QQCQAEAKCPKLLPC HHHHHHHCCCCHHHH	42.44	9756909
65	Ubiquitination	QQCQAEAKCPKLLPC HHHHHHHCCCCHHHH	42.44	-
68	Ubiquitination	QAEAKCPKLLPCLHT HHHHCCCCHHHHHHH	72.61	-
117	Phosphorylation	ESLQRRLSVYRQIVD HHHHHHHHHHHHHHH	18.45	12402044
119	Phosphorylation	LQRRLSVYRQIVDAQ HHHHHHHHHHHHHHH	8.07	21712546
160	Sumoylation	EAHQWFLKHEARPLA HHHHHHHHHCCHHHH	29.89	-
160	Sumoylation	EAHQWFLKHEARPLA HHHHHHHHHCCHHHH	29.89	9756909
173	Phosphorylation	LAELRNQSVREFLDG HHHHCCHHHHHHHHC	27.05	27080861
183	Ubiquitination	EFLDGTRKTNNIFCS HHHHCCCCCCCEECC	56.28	-
184	Phosphorylation	FLDGTRKTNNIFCSN HHHCCCCCCCEECCC	30.15	25307156
190	Phosphorylation	KTNNIFCSNPNHRTP CCCCEECCCCCCCCC	44.57	25307156
196	Phosphorylation	CSNPNHRTPTLTSIY CCCCCCCCCCCCEEE	17.05	21815630
198	Phosphorylation	NPNHRTPTLTSIYCR CCCCCCCCCCEEEEC	41.89	30108239
200	Phosphorylation	NHRTPTLTSIYCRGC CCCCCCCCEEEECCC	18.63	23312004
201	Phosphorylation	HRTPTLTSIYCRGCS CCCCCCCEEEECCCC	18.05	28857561
203	Phosphorylation	TPTLTSIYCRGCSKP CCCCCEEEECCCCCC	3.94	30631047
208	Phosphorylation	SIYCRGCSKPLCCSC EEEECCCCCCCHHHH	39.88	24719451
220	Phosphorylation	CSCALLDSSHSELKC HHHHHHCCCCCHHCC	29.89	28348404
221	Phosphorylation	SCALLDSSHSELKCD HHHHHCCCCCHHCCC	30.60	28348404
226	Sumoylation	DSSHSELKCDISAEI CCCCCHHCCCHHHHH	26.30	-
226	Sumoylation	DSSHSELKCDISAEI CCCCCHHCCCHHHHH	26.30	17000644
226	Ubiquitination	DSSHSELKCDISAEI CCCCCHHCCCHHHHH	26.30	-
309	Phosphorylation	DARYQRDYEEMASRL HHHHHHCHHHHHHHH	18.91	-
337	Ubiquitination	SALVQRMKCYASDQE HHHHHHHCCCCCCHH	26.70	-
339	Phosphorylation	LVQRMKCYASDQEVL HHHHHCCCCCCHHHH	12.01	24719451
341	Phosphorylation	QRMKCYASDQEVLDM HHHCCCCCCHHHHHH	17.22	24719451
366	Phosphorylation	LRQEEPQSLQAAVRT HHHCCCCHHHHHHHC	32.91	28555341
380	Sumoylation	TDGFDEFKVRLQDLS CCCCCHHHHHHHHHH	25.13	-
380	2-Hydroxyisobutyrylation	TDGFDEFKVRLQDLS CCCCCHHHHHHHHHH	25.13	-
380	Acetylation	TDGFDEFKVRLQDLS CCCCCHHHHHHHHHH	25.13	26822725
380	Sumoylation	TDGFDEFKVRLQDLS CCCCCHHHHHHHHHH	25.13	28112733
380	Ubiquitination	TDGFDEFKVRLQDLS CCCCCHHHHHHHHHH	25.13	21963094
380 (in isoform 1)	Ubiquitination	-	25.13	21890473
380 (in isoform 2)	Ubiquitination	-	25.13	21890473
380 (in isoform 3)	Ubiquitination	-	25.13	21890473
380 (in isoform 4)	Ubiquitination	-	25.13	21890473
380 (in isoform 5)	Ubiquitination	-	25.13	21890473
387	Phosphorylation	KVRLQDLSSCITQGK HHHHHHHHHHHHCCC	31.30	26074081
388	Phosphorylation	VRLQDLSSCITQGKD HHHHHHHHHHHCCCH	19.48	26074081
391	Phosphorylation	QDLSSCITQGKDAAV HHHHHHHHCCCHHHH	35.28	26074081
394	Acetylation	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	26051181
394	Malonylation	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	26320211
394	Sumoylation	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	28112733
394	Ubiquitination	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	23000965
394 (in isoform 1)	Ubiquitination	-	34.08	21890473
394 (in isoform 2)	Ubiquitination	-	34.08	21890473
394 (in isoform 3)	Ubiquitination	-	34.08	21890473
394 (in isoform 4)	Ubiquitination	-	34.08	21890473
394 (in isoform 5)	Ubiquitination	-	34.08	21890473
394	Ubiquitination	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	21890473
394	Ubiquitination	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	21890473
394	Ubiquitination	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	21890473
394	Ubiquitination	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	21890473
394	Ubiquitination	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	21890473
394	Ubiquitination	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	21890473
394	Ubiquitination	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	21890473
394	Ubiquitination	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	21890473
394	Ubiquitination	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	21890473
394	Ubiquitination	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	21890473
394	Ubiquitination	SSCITQGKDAAVSKK HHHHHCCCHHHHHCC	34.08	21890473
399	Phosphorylation	QGKDAAVSKKASPEA CCCHHHHHCCCCHHH	24.58	30108239
400	Sumoylation	GKDAAVSKKASPEAA CCHHHHHCCCCHHHH	45.84	-
400	Sumoylation	GKDAAVSKKASPEAA CCHHHHHCCCCHHHH	45.84	-
400	Ubiquitination	GKDAAVSKKASPEAA CCHHHHHCCCCHHHH	45.84	23000965
400 (in isoform 1)	Ubiquitination	-	45.84	21890473
400 (in isoform 2)	Ubiquitination	-	45.84	21890473
400 (in isoform 3)	Ubiquitination	-	45.84	21890473
400 (in isoform 4)	Ubiquitination	-	45.84	21890473
400 (in isoform 5)	Ubiquitination	-	45.84	21890473
401	Sumoylation	KDAAVSKKASPEAAS CHHHHHCCCCHHHHC	46.74	28112733
401	Ubiquitination	KDAAVSKKASPEAAS CHHHHHCCCCHHHHC	46.74	22817900
401 (in isoform 1)	Ubiquitination	-	46.74	21890473
401 (in isoform 11)	Ubiquitination	-	46.74	-
401 (in isoform 2)	Ubiquitination	-	46.74	21890473
401 (in isoform 3)	Ubiquitination	-	46.74	21890473
401 (in isoform 4)	Ubiquitination	-	46.74	21890473
401 (in isoform 5)	Ubiquitination	-	46.74	21890473
403	Phosphorylation	AAVSKKASPEAASTP HHHHCCCCHHHHCCC	31.95	29255136
403 (in isoform 11)	Phosphorylation	-	31.95	23927012
403 (in isoform 12)	Phosphorylation	-	31.95	23927012
403 (in isoform 13)	Phosphorylation	-	31.95	23927012
403 (in isoform 14)	Phosphorylation	-	31.95	22617229
408	Phosphorylation	KASPEAASTPRDPID CCCHHHHCCCCCCCC	46.09	23401153
408 (in isoform 11)	Phosphorylation	-	46.09	26657352
408 (in isoform 12)	Phosphorylation	-	46.09	26657352
408 (in isoform 13)	Phosphorylation	-	46.09	26657352
408 (in isoform 14)	Phosphorylation	-	46.09	24719451
409	Phosphorylation	ASPEAASTPRDPIDV CCHHHHCCCCCCCCC	20.02	29255136
409 (in isoform 11)	Phosphorylation	-	20.02	26657352
409 (in isoform 12)	Phosphorylation	-	20.02	26657352
409 (in isoform 13)	Phosphorylation	-	20.02	26657352
409 (in isoform 14)	Phosphorylation	-	20.02	21712546
421 (in isoform 11)	Phosphorylation	-	54.62	23927012
421 (in isoform 12)	Phosphorylation	-	54.62	23927012
421 (in isoform 13)	Phosphorylation	-	54.62	23927012
423 (in isoform 11)	Phosphorylation	-	62.38	23927012
423 (in isoform 12)	Phosphorylation	-	62.38	23927012
423 (in isoform 13)	Phosphorylation	-	62.38	23927012
424 (in isoform 11)	Phosphorylation	-	42.14	23927012
424 (in isoform 12)	Phosphorylation	-	42.14	23927012
424 (in isoform 13)	Phosphorylation	-	42.14	23927012
425 (in isoform 11)	Phosphorylation	-	4.54	27542207
425 (in isoform 12)	Phosphorylation	-	4.54	27542207
425 (in isoform 13)	Phosphorylation	-	4.54	27542207
426	Ubiquitination	PEEAERVKAQVQALG CHHHHHHHHHHHHHC	39.04	21963094
428	Ubiquitination	EAERVKAQVQALGLA HHHHHHHHHHHHCCC	23.34	22817900
428 (in isoform 11)	Ubiquitination	-	23.34	-
430	Ubiquitination	ERVKAQVQALGLAEA HHHHHHHHHHCCCCC	20.84	22817900
432 (in isoform 10)	Phosphorylation	-	3.02	-
432 (in isoform 11)	Phosphorylation	-	3.02	22210691
432 (in isoform 12)	Phosphorylation	-	3.02	22210691
432 (in isoform 13)	Phosphorylation	-	3.02	22210691
434 (in isoform 11)	Phosphorylation	-	3.96	22210691
434 (in isoform 12)	Phosphorylation	-	3.96	22210691
434 (in isoform 13)	Phosphorylation	-	3.96	22210691
442	Ubiquitination	AEAQPMAVVQSVPGA CCCCCCEEEEECCCC	3.07	24816145
449	Ubiquitination	VVQSVPGAHPVPVYA EEEECCCCCCCCEEE	9.57	22817900
458	Phosphorylation	PVPVYAFSIKGPSYG CCCEEEEEEECCCCC	18.41	24719451
460	Sumoylation	PVYAFSIKGPSYGED CEEEEEEECCCCCCC	64.67	28112733
460	Ubiquitination	PVYAFSIKGPSYGED CEEEEEEECCCCCCC	64.67	29967540
463	Phosphorylation	AFSIKGPSYGEDVSN EEEEECCCCCCCCCC	55.21	28857561
464	Phosphorylation	FSIKGPSYGEDVSNT EEEECCCCCCCCCCC	27.89	28857561
469	Phosphorylation	PSYGEDVSNTTTAQK CCCCCCCCCCCHHHH	40.56	28857561
470	Phosphorylation	SYGEDVSNTTTAQKR CCCCCCCCCCHHHHH	41.09	32645325
471	Phosphorylation	YGEDVSNTTTAQKRK CCCCCCCCCHHHHHC	20.30	28857561
472	Phosphorylation	GEDVSNTTTAQKRKC CCCCCCCCHHHHHCC	25.12	24043423
473	Phosphorylation	EDVSNTTTAQKRKCS CCCCCCCHHHHHCCC	25.67	24043423
476	Acetylation	SNTTTAQKRKCSQTQ CCCCHHHHHCCCCCC	51.89	25953088
476	Sumoylation	SNTTTAQKRKCSQTQ CCCCHHHHHCCCCCC	51.89	28112733
476	Ubiquitination	SNTTTAQKRKCSQTQ CCCCHHHHHCCCCCC	51.89	21906983
476 (in isoform 1)	Ubiquitination	-	51.89	21890473
476 (in isoform 2)	Ubiquitination	-	51.89	21890473
476 (in isoform 3)	Ubiquitination	-	51.89	21890473
476 (in isoform 4)	Ubiquitination	-	51.89	21890473
476 (in isoform 5)	Ubiquitination	-	51.89	21890473
478	Sumoylation	TTTAQKRKCSQTQCP CCHHHHHCCCCCCCC	45.32	28112733
478	Ubiquitination	TTTAQKRKCSQTQCP CCHHHHHCCCCCCCC	45.32	22817900
479	Phosphorylation	TTAQKRKCSQTQCPR CHHHHHCCCCCCCCC	4.18	32142685
480	Phosphorylation	TAQKRKCSQTQCPRK HHHHHCCCCCCCCCC	39.02	27794612
482	Phosphorylation	QKRKCSQTQCPRKVI HHHCCCCCCCCCCEE	18.82	30242111
487	Sumoylation	SQTQCPRKVIKMESE CCCCCCCCEEECCCH	33.19	-
487	Acetylation	SQTQCPRKVIKMESE CCCCCCCCEEECCCH	33.19	22274616
487	Sumoylation	SQTQCPRKVIKMESE CCCCCCCCEEECCCH	33.19	28112733
490	Sumoylation	QCPRKVIKMESEEGK CCCCCEEECCCHHHH	39.33	-
490	Acetylation	QCPRKVIKMESEEGK CCCCCEEECCCHHHH	39.33	12653403
490	Sumoylation	QCPRKVIKMESEEGK CCCCCEEECCCHHHH	39.33	17000644
490	Ubiquitination	QCPRKVIKMESEEGK CCCCCEEECCCHHHH	39.33	24816145
493	Phosphorylation	RKVIKMESEEGKEAR CCEEECCCHHHHHHH	37.13	26657352
497	Sumoylation	KMESEEGKEARLARS ECCCHHHHHHHHHCC	52.02	-
497	Acetylation	KMESEEGKEARLARS ECCCHHHHHHHHHCC	52.02	26051181
497	Sumoylation	KMESEEGKEARLARS ECCCHHHHHHHHHCC	52.02	28112733
497	Ubiquitination	KMESEEGKEARLARS ECCCHHHHHHHHHCC	52.02	21906983
497 (in isoform 1)	Ubiquitination	-	52.02	21890473
497 (in isoform 2)	Ubiquitination	-	52.02	21890473
497 (in isoform 3)	Ubiquitination	-	52.02	21890473
497 (in isoform 4)	Ubiquitination	-	52.02	21890473
497 (in isoform 5)	Ubiquitination	-	52.02	21890473
504	Phosphorylation	KEARLARSSPEQPRP HHHHHHCCCCCCCCC	44.64	22167270
505	Phosphorylation	EARLARSSPEQPRPS HHHHHCCCCCCCCCC	27.23	25159151
512	Phosphorylation	SPEQPRPSTSKAVSP CCCCCCCCCCCCCCC	46.74	20201521
513	Phosphorylation	PEQPRPSTSKAVSPP CCCCCCCCCCCCCCC	36.61	23927012
514	Phosphorylation	EQPRPSTSKAVSPPH CCCCCCCCCCCCCCC	23.97	20201521
515	Acetylation	QPRPSTSKAVSPPHL CCCCCCCCCCCCCCC	53.55	18621739
518	Phosphorylation	PSTSKAVSPPHLDGP CCCCCCCCCCCCCCC	37.26	29255136
518 (in isoform 4)	Phosphorylation	-	37.26	23927012
527	Phosphorylation	PHLDGPPSPRSPVIG CCCCCCCCCCCCCCC	35.76	29255136
527 (in isoform 4)	Phosphorylation	-	35.76	23927012
530	Phosphorylation	DGPPSPRSPVIGSEV CCCCCCCCCCCCCEE	27.23	29255136
530 (in isoform 4)	Phosphorylation	-	27.23	30266825
535	Phosphorylation	PRSPVIGSEVFLPNS CCCCCCCCEEECCCC	21.33	30266825
535 (in isoform 4)	Phosphorylation	-	21.33	30266825
542	Phosphorylation	SEVFLPNSNHVASGA CEEECCCCCCCCCCC	26.77	23927012
542 (in isoform 4)	Phosphorylation	-	26.77	23927012
547	Phosphorylation	PNSNHVASGAGEAEE CCCCCCCCCCCCCCC	28.25	23927012
547 (in isoform 4)	Phosphorylation	-	28.25	22777824
560	Phosphorylation	EERVVVISSSEDSDA CCEEEEEECCCCCCC	19.05	29255136
560 (in isoform 2)	Phosphorylation	-	19.05	30108239
560	Ubiquitination	EERVVVISSSEDSDA CCEEEEEECCCCCCC	19.05	21890473
560	Ubiquitination	EERVVVISSSEDSDA CCEEEEEECCCCCCC	19.05	21890473
561	Phosphorylation	ERVVVISSSEDSDAE CEEEEEECCCCCCCC	26.99	29255136
561 (in isoform 2)	Phosphorylation	-	26.99	30108239
562	Phosphorylation	RVVVISSSEDSDAEN EEEEEECCCCCCCCC	38.34	29255136
562 (in isoform 2)	Phosphorylation	-	38.34	30108239
565	Phosphorylation	VISSSEDSDAENSSS EEECCCCCCCCCCCC	34.37	23401153
565 (in isoform 2)	Phosphorylation	-	34.37	30108239
565 (in isoform 9)	Phosphorylation	-	34.37	19651622
570	Phosphorylation	EDSDAENSSSRELDD CCCCCCCCCCCCCCC	22.61	29255136
570 (in isoform 2)	Phosphorylation	-	22.61	30108239
571	Phosphorylation	DSDAENSSSRELDDS CCCCCCCCCCCCCCC	45.02	29255136
572	Phosphorylation	SDAENSSSRELDDSS CCCCCCCCCCCCCCC	29.60	29255136
572 (in isoform 2)	Phosphorylation	-	29.60	30108239
578	Phosphorylation	SSRELDDSSSESSDL CCCCCCCCCCCCCCC	35.12	22115753
579	Phosphorylation	SRELDDSSSESSDLQ CCCCCCCCCCCCCCC	45.15	22115753
580	Phosphorylation	RELDDSSSESSDLQL CCCCCCCCCCCCCCC	45.51	22115753
580 (in isoform 2)	Phosphorylation	-	45.51	29116813
582	Phosphorylation	LDDSSSESSDLQLEG CCCCCCCCCCCCCCC	30.97	22115753
583	Phosphorylation	DDSSSESSDLQLEGP CCCCCCCCCCCCCCC	37.98	22115753
583 (in isoform 2)	Phosphorylation	-	37.98	25849741
591	Phosphorylation	DLQLEGPSTLRVLDE CCCCCCCCHHHCCCC	51.43	22115753
592	Phosphorylation	LQLEGPSTLRVLDEN CCCCCCCHHHCCCCC	23.01	22115753
597 (in isoform 2)	Phosphorylation	-	39.62	-
613 (in isoform 9)	Phosphorylation	-	9.30	27067055
616	Sumoylation	PLVFFDLKIDNETQK CEEEEEEEECCCHHH	50.27	-
616	Sumoylation	PLVFFDLKIDNETQK CEEEEEEEECCCHHH	50.27	17000644
623	Ubiquitination	KIDNETQKISQLAAV EECCCHHHHHHHHCC	52.31	23000965
623 (in isoform 1)	Ubiquitination	-	52.31	21890473
623	Ubiquitination	KIDNETQKISQLAAV EECCCHHHHHHHHCC	52.31	21890473
625	Phosphorylation	DNETQKISQLAAVNR CCCHHHHHHHHCCCC	26.61	20068231
637 (in isoform 9)	Phosphorylation	-	26.06	27067055
672 (in isoform 13)	Phosphorylation	-	18.64	25106551
715 (in isoform 3)	Phosphorylation	-	33.09	25106551
720 (in isoform 8)	Phosphorylation	-	34.92	25106551
722	Phosphorylation	RERVPGASSFKLKNL HHHCCCCCCHHHHHH	42.07	26437602
723	Phosphorylation	ERVPGASSFKLKNLA HHCCCCCCHHHHHHH	26.35	27067055
725	Methylation	VPGASSFKLKNLAQT CCCCCCHHHHHHHHH	61.57	54409323
725	Ubiquitination	VPGASSFKLKNLAQT CCCCCCHHHHHHHHH	61.57	-
727	Methylation	GASSFKLKNLAQTYL CCCCHHHHHHHHHHH	50.97	115975197
727	Ubiquitination	GASSFKLKNLAQTYL CCCCHHHHHHHHHHH	50.97	-
733	Phosphorylation	LKNLAQTYLARNMSE HHHHHHHHHHCCCCH	6.05	28509920
739	Phosphorylation	TYLARNMSERSAMAA HHHHCCCCHHHHHHH	33.15	23403867
742	Phosphorylation	ARNMSERSAMAAVLA HCCCCHHHHHHHHHH	20.53	23403867
742 (in isoform 13)	Phosphorylation	-	20.53	27251275
746 (in isoform 13)	Phosphorylation	-	5.47	27251275
755 (in isoform 13)	Phosphorylation	-	49.99	27251275
758 (in isoform 13)	Phosphorylation	-	45.61	27251275
771 (in isoform 13)	Phosphorylation	-	22.89	26657352
785 (in isoform 3)	Phosphorylation	-	4.66	27251275
789 (in isoform 3)	Phosphorylation	-	9.42	27251275
790 (in isoform 8)	Phosphorylation	-	1.72	27251275
794 (in isoform 8)	Phosphorylation	-	35.29	27251275
798 (in isoform 3)	Phosphorylation	-	3.87	27251275
801 (in isoform 3)	Phosphorylation	-	27.34	27251275
803 (in isoform 8)	Phosphorylation	-	3.04	27251275
804	Phosphorylation	LLALHNVSFMELLSA HHHHHCCCHHHHHHH	24.96	-
806 (in isoform 8)	Phosphorylation	-	2.49	27251275
814 (in isoform 3)	Phosphorylation	-	33.33	26657352
819 (in isoform 8)	Phosphorylation	-	26.45	26657352
828	Phosphorylation	KKYSRYLSLQTTTLP HHHHHHCCCEECCCC	14.97	27251275
866	Phosphorylation	LARAEGVSTPLAGRG HHHCCCCCCCCCCCH	34.85	29255136
867	Phosphorylation	ARAEGVSTPLAGRGL HHCCCCCCCCCCCHH	21.66	23401153
872	Methylation	VSTPLAGRGLAERAS CCCCCCCCHHHHHHH	31.20	83364561
879	Phosphorylation	RGLAERASQQS---- CHHHHHHHHCC----	34.67	23312004
882	Phosphorylation	AERASQQS------- HHHHHHCC-------	34.25	27067055

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
8	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	GPS
8	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	Uniprot
28	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
28	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
36	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	Uniprot
36	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
36	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
36	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
38	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
38	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	Uniprot
38	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	GPS
38	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
38	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
40	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
40	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
117	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
117	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
117	S	Phosphorylation	Kinase	CHEK2	O96017	Uniprot
403	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
403	S	Phosphorylation	Kinase	ERK5	Q13164	PSP
409	T	Phosphorylation	Kinase	MAPK7	Q13164	GPS
505	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
518	S	Phosphorylation	Kinase	CDK2	P24941	PSP
518	S	Phosphorylation	Kinase	CDK1	P06493	PSP
527	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
527	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
530	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
530	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
560	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
561	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
562	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
565	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL20	Q9Y2M5	PMID:31279627:21840486
-	K	Ubiquitination	E3 ubiquitin ligase	RNF4	P78317	PMID:18408733
-	K	Ubiquitination	E3 ubiquitin ligase	UBE3A	Q05086	PMID:25231954
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH1	Q8IUQ4	PMID:14645235
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH2	O43255	PMID:14645235
-	K	Ubiquitination	E3 ubiquitin ligase	RNF111	Q6ZNA4	PMID:23530056
-	K	Ubiquitination	E3 ubiquitin ligase	UHRF1	Q96T88	PMID:22945642
-	K	Ubiquitination	E3 ubiquitin ligase	RNF8	O76064	PMID:23708797
-	K	Ubiquitination	E3 ubiquitin ligase	ICP0	P08393	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
6	K	ubiquitylation	'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent.	9756909
6	K	Sumoylation	'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent.	9756909
8	S	Sumoylation	HIPK2-mediated phosphorylation at Ser-8, Ser-36 and Ser-38 leads to increased accumulation of PML protein and its sumoylation and is required for the maximal pro-apoptotic activity of PML after DNA damage.	19015637
8	S	Phosphorylation	HIPK2-mediated phosphorylation at Ser-8, Ser-36 and Ser-38 leads to increased accumulation of PML protein and its sumoylation and is required for the maximal pro-apoptotic activity of PML after DNA damage.	19015637
11	K	ubiquitylation	'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent.	18408734
11	K	Sumoylation	'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent.	18408734
36	S	Sumoylation	HIPK2-mediated phosphorylation at Ser-8, Ser-36 and Ser-38 leads to increased accumulation of PML protein and its sumoylation and is required for the maximal pro-apoptotic activity of PML after DNA damage.	23186163
36	S	Phosphorylation	HIPK2-mediated phosphorylation at Ser-8, Ser-36 and Ser-38 leads to increased accumulation of PML protein and its sumoylation and is required for the maximal pro-apoptotic activity of PML after DNA damage.	23186163
38	S	Sumoylation	HIPK2-mediated phosphorylation at Ser-8, Ser-36 and Ser-38 leads to increased accumulation of PML protein and its sumoylation and is required for the maximal pro-apoptotic activity of PML after DNA damage.	19015637
38	S	Phosphorylation	HIPK2-mediated phosphorylation at Ser-8, Ser-36 and Ser-38 leads to increased accumulation of PML protein and its sumoylation and is required for the maximal pro-apoptotic activity of PML after DNA damage.	19015637
48	K	ubiquitylation	'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent.	18298799
48	K	Sumoylation	'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent.	18298799
65	K	Sumoylation	Lys-65 and Lys-160 are sumoylated by PISA1 and PIAS2.	9756909
65	K	Sumoylation	Sumoylation on Lys-160 is a prerequisite for sumoylation on Lys-65.	9756909
65	K	Sumoylation	Sumoylation on all three sites (Lys-65, Lys-160 and Lys-490) is required for nuclear body formation.	9756909
117	S	Phosphorylation	CHEK2-mediated phosphorylation at Ser-117 is important for PML-mediated apoptosis following DNA damage.	12402044
160	K	Sumoylation	Sumoylation on all three sites (Lys-65, Lys-160 and Lys-490) is required for nuclear body formation.	9756909
160	K	Sumoylation	Lys-65 and Lys-160 are sumoylated by PISA1 and PIAS2.	9756909
160	K	Sumoylation	Sumoylation on Lys-160 is a prerequisite for sumoylation on Lys-65.	9756909
403	S	Phosphorylation	MAPK1-mediated phosphorylations at Ser-403, Ser-505, Ser-527 and Ser-530 and CDK1/2-mediated phosphorylation at Ser-518 promote PIN1-dependent PML degradation.	17081983
487	K	Acetylation	Acetylation at Lys-487 is essential for its nuclear localization.	18298799
487	K	Acetylation	Deacetylated at Lys-487 by SIRT1 and this deacetylation promotes PML control of PER2 nuclear localization.	18298799
490	K	Sumoylation	Sumoylation on all three sites (Lys-65, Lys-160 and Lys-490) is required for nuclear body formation.	9756909
490	K	Sumoylation	Sumoylation at Lys-490 by RANBP2 is essential for the proper assembly of PML-NBs.	9756909
505	S	Phosphorylation	MAPK1-mediated phosphorylations at Ser-403, Ser-505, Ser-527 and Ser-530 and CDK1/2-mediated phosphorylation at Ser-518 promote PIN1-dependent PML degradation.	22033920
518	S	Phosphorylation	MAPK1-mediated phosphorylations at Ser-403, Ser-505, Ser-527 and Ser-530 and CDK1/2-mediated phosphorylation at Ser-518 promote PIN1-dependent PML degradation.	17081983
518	S	Phosphorylation	Ubiquitination by BCR(KLHL20) E3 ubiquitin ligase complex E3 ligase complex requires CDK1/2-mediated phosphorylation at Ser-518 which in turn is recognized by prolyl-isopeptidase PIN1 and PIN1-catalyzed isomerization further potentiates PML interaction with KLHL20.	17081983
518	S	ubiquitylation	Ubiquitination by BCR(KLHL20) E3 ubiquitin ligase complex E3 ligase complex requires CDK1/2-mediated phosphorylation at Ser-518 which in turn is recognized by prolyl-isopeptidase PIN1 and PIN1-catalyzed isomerization further potentiates PML interaction with KLHL20.	17081983
527	S	Phosphorylation	MAPK1-mediated phosphorylations at Ser-403, Ser-505, Ser-527 and Ser-530 and CDK1/2-mediated phosphorylation at Ser-518 promote PIN1-dependent PML degradation.	17081983
530	S	Phosphorylation	MAPK1-mediated phosphorylations at Ser-403, Ser-505, Ser-527 and Ser-530 and CDK1/2-mediated phosphorylation at Ser-518 promote PIN1-dependent PML degradation.	17081983
565	S	Phosphorylation	CK2-mediated phosphorylation at Ser-565 primes PML ubiquitination via an unidentified ubiquitin ligase.	17081983
565	S	Phosphorylation	PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 and phosphorylation at Ser-565 which in turn triggers its ubiquitin-mediated degradation.	17081983
565	S	Sumoylation	PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 and phosphorylation at Ser-565 which in turn triggers its ubiquitin-mediated degradation.	17081983
565	S	ubiquitylation	CK2-mediated phosphorylation at Ser-565 primes PML ubiquitination via an unidentified ubiquitin ligase.	17081983
565	S	ubiquitylation	PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 and phosphorylation at Ser-565 which in turn triggers its ubiquitin-mediated degradation.	17081983

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PML_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TDG_HUMAN	TDG	physical	15569683
DAXX_HUMAN	DAXX	physical	10525530
SMAD2_HUMAN	SMAD2	physical	15356634
ZFYV9_HUMAN	ZFYVE9	physical	15356634
MK11_HUMAN	MAPK11	physical	15273249
MDM2_HUMAN	MDM2	physical	15195100
RL11_HUMAN	RPL11	physical	15195100
MYB_HUMAN	MYB	physical	15194430
ANKR2_HUMAN	ANKRD2	physical	15136035
MDM2_HUMAN	MDM2	physical	14507915
TRI69_HUMAN	TRIM69	physical	12837286
TOPB1_HUMAN	TOPBP1	physical	12773567
MDM2_HUMAN	MDM2	physical	12759344
CCNT1_HUMAN	CCNT1	physical	12727882
SRF_HUMAN	SRF	physical	12622724
CBP_HUMAN	CREBBP	physical	12622724
SUMO1_HUMAN	SUMO1	physical	11948183
NCOR2_HUMAN	NCOR2	physical	11430826
SIN3A_HUMAN	SIN3A	physical	11430826
NCOR1_HUMAN	NCOR1	physical	11430826
SKI_HUMAN	SKI	physical	11430826
HDAC1_HUMAN	HDAC1	physical	11259576
HDAC3_HUMAN	HDAC3	physical	11259576
DAXX_HUMAN	DAXX	physical	10669754
PML_HUMAN	PML	physical	10669754
RARA_HUMAN	RARA	physical	10610177
RXRA_HUMAN	RXRA	physical	10610177
RB_HUMAN	RB1	physical	9448006
IF4E_HUMAN	EIF4E	physical	11500381
TF65_HUMAN	RELA	physical	12540841
DAXX_HUMAN	DAXX	physical	11244500
HHEX_HUMAN	HHEX	physical	10597310
NR4A1_HUMAN	NR4A1	physical	12032831
JUN_HUMAN	JUN	physical	9671405
FOS_HUMAN	FOS	physical	9671405
ATF2_HUMAN	ATF2	physical	9671405
P53_HUMAN	TP53	physical	11080164
ZBT16_HUMAN	ZBTB16	physical	9294197
SP1_HUMAN	SP1	physical	9819401
ARNT_HUMAN	ARNT	physical	12354770
DAXX_HUMAN	DAXX	physical	10684855
PLAL1_HUMAN	PLAGL1	physical	20097304
KAT5_HUMAN	KAT5	physical	19150978
MDM2_HUMAN	MDM2	physical	19150978
SATB1_HUMAN	SATB1	physical	17173041
TERT_HUMAN	TERT	physical	19567472
RPAB1_HUMAN	POLR2E	physical	20211142
PPARG_HUMAN	PPARG	physical	20211142
MED7_HUMAN	MED7	physical	20211142
PHS2_HUMAN	PCBD2	physical	20211142
CHD4_HUMAN	CHD4	physical	18644863
ZN506_HUMAN	ZNF506	physical	16412420
FOXO1_HUMAN	FOXO1	physical	16154098
HDAC7_HUMAN	HDAC7	physical	18463162
TOP2B_HUMAN	TOP2B	physical	18212063
SP130_HUMAN	SAP130	physical	18212063
HNRPU_HUMAN	HNRNPU	physical	18212063
RFC4_HUMAN	RFC4	physical	18212063
NPM_HUMAN	NPM1	physical	18212063
MRT4_HUMAN	MRTO4	physical	18212063
SNR40_HUMAN	SNRNP40	physical	18212063
RARA_HUMAN	RARA	physical	10882117
SIAH1_HUMAN	SIAH1	physical	18073335
RARA_HUMAN	RARA	physical	18073335
HDAC2_HUMAN	HDAC2	physical	18073335
SPI1_HUMAN	SPI1	physical	20159610
RARA_HUMAN	RARA	physical	20159610
UBE3A_HUMAN	UBE3A	physical	19325566
SP100_HUMAN	SP100	physical	21779164
DAXX_HUMAN	DAXX	physical	20972456
P53_HUMAN	TP53	physical	20972456
MDM2_HUMAN	MDM2	physical	20972456
AXIN1_HUMAN	AXIN1	physical	21057547
P53_HUMAN	TP53	physical	21057547
MAGA2_HUMAN	MAGEA2	physical	22117195
SETB1_HUMAN	SETDB1	physical	21921037
RARA_HUMAN	RARA	physical	11050004
BANP_HUMAN	BANP	physical	22013068
PSME3_HUMAN	PSME3	physical	19556897
ATX3_HUMAN	ATXN3	physical	11572863
DAXX_HUMAN	DAXX	physical	17360386
PIAS1_HUMAN	PIAS1	physical	22406621
PIAS2_HUMAN	PIAS2	physical	22406621
CSK21_HUMAN	CSNK2A1	physical	22406621
IF4E_HUMAN	EIF4E	physical	11575918
SUMO1_HUMAN	SUMO1	physical	19380586
RNF4_HUMAN	RNF4	physical	19380586
CSK2B_HUMAN	CSNK2B	physical	20719947
UBC9_HUMAN	UBE2I	physical	15809060
SUMO1_HUMAN	SUMO1	physical	22875967
YAP1_HUMAN	YAP1	physical	19111660
CTNB1_HUMAN	CTNNB1	physical	22155184
RBP2_HUMAN	RANBP2	physical	22155184
HDAC7_HUMAN	HDAC7	physical	22155184
UBP7_HUMAN	USP7	physical	21305000
FBX3_HUMAN	FBXO3	physical	18809579
CUL1_HUMAN	CUL1	physical	18809579
SKP1_HUMAN	SKP1	physical	18809579
RBX1_HUMAN	RBX1	physical	18809579
SUMO1_HUMAN	SUMO1	physical	9885291
UBC9_HUMAN	UBE2I	physical	9885291
PIN1_HUMAN	PIN1	physical	18039859
UHRF1_HUMAN	UHRF1	physical	22945642
IKKE_HUMAN	IKBKE	physical	20188669
HIPK2_HUMAN	HIPK2	physical	21192925
ZMYM2_HUMAN	ZMYM2	physical	17027752
HIPK2_HUMAN	HIPK2	physical	19015637
IEX1_HUMAN	IER3	physical	15855159
CHK2_HUMAN	CHEK2	physical	12402044
SYNE2_HUMAN	SYNE2	physical	19861416
MK03_HUMAN	MAPK3	physical	19861416
MK01_HUMAN	MAPK1	physical	19861416
PML_HUMAN	PML	physical	16778193
SIAH2_HUMAN	SIAH2	physical	14645235
JUN_HUMAN	JUN	physical	15626733
PML_HUMAN	PML	physical	9671498
VIE1_HCMVM	UL123	physical	9671498
DAXX_HUMAN	DAXX	physical	21482821
RUNX1_HUMAN	RUNX1	physical	15331439
RUNX3_HUMAN	RUNX3	physical	15331439
RUNX2_HUMAN	RUNX2	physical	15331439
KPYM_HUMAN	PKM	physical	18298799
PML_HUMAN	PML	physical	9230084
PML_HUMAN	PML	physical	16540467
RARA_HUMAN	RARA	physical	16540467
RXRA_HUMAN	RXRA	physical	16540467
IF4E_HUMAN	EIF4E	physical	12167712
PLCG1_HUMAN	PLCG1	physical	17419608
DAXX_HUMAN	DAXX	physical	17419608
ELF4_HUMAN	ELF4	physical	14976184
TGIF1_HUMAN	TGIF1	physical	16916642
JUN_HUMAN	JUN	physical	16916642
BCL2_HUMAN	BCL2	physical	15231068
TOPB1_HUMAN	TOPBP1	physical	19023333
AURKA_HUMAN	AURKA	physical	15749021
CTNB1_HUMAN	CTNNB1	physical	12384561
SIR1_HUMAN	SIRT1	physical	12006491
MK01_HUMAN	MAPK1	physical	22033920
P63_HUMAN	TP63	physical	16007146
P53_HUMAN	TP53	physical	16007146
RNF4_HUMAN	RNF4	physical	23028697
MYC_HUMAN	MYC	physical	17146439
NFAC1_HUMAN	NFATC1	physical	18246125
TNR6_HUMAN	FAS	physical	21803845
CSK21_HUMAN	CSNK2A1	physical	20625391
CSK23_HUMAN	CSNK2A3	physical	20625391
MTOR_HUMAN	MTOR	physical	16915281
KC1D_HUMAN	CSNK1D	physical	18246126
RARA_HUMAN	RARA	physical	17560333
EZH2_HUMAN	EZH2	physical	17560333
SUZ12_HUMAN	SUZ12	physical	17560333
MK07_HUMAN	MAPK7	physical	20832753
KLH20_HUMAN	KLHL20	physical	21840486
PML_HUMAN	PML	physical	22773875
PML_HUMAN	PML	physical	22493164
PSA3_HUMAN	PSMA3	physical	21988832
SH3G1_HUMAN	SH3GL1	physical	21988832
UBC9_HUMAN	UBE2I	physical	21988832
GLIS2_HUMAN	GLIS2	physical	24500717
JAK1_HUMAN	JAK1	physical	20409569
PML_HUMAN	PML	physical	12438698
IF4E_HUMAN	EIF4E	physical	12438698
ATX1_HUMAN	ATXN1	physical	24882209
HD_HUMAN	HTT	physical	24882209
EHMT2_HUMAN	EHMT2	physical	23768491
ATRX_HUMAN	ATRX	physical	23222847
DAXX_HUMAN	DAXX	physical	23222847
H33_HUMAN	H3F3A	physical	23222847
HIRA_HUMAN	HIRA	physical	23222847
ASF1A_HUMAN	ASF1A	physical	23222847
NCOA2_HUMAN	NCOA2	physical	23542129
EGFR_HUMAN	EGFR	physical	23563092
HDAC1_HUMAN	HDAC1	physical	23563092
MK07_HUMAN	MAPK7	physical	22869143
P53_HUMAN	TP53	physical	22869143
MDM2_HUMAN	MDM2	physical	22869143
DAXX_HUMAN	DAXX	physical	24637324
SP100_HUMAN	SP100	physical	24637324
P53_HUMAN	TP53	physical	15375079
RBL2_HUMAN	RBL2	physical	22002537
E2F4_HUMAN	E2F4	physical	22002537
TBX3_HUMAN	TBX3	physical	22002537
ASC_HUMAN	PYCARD	physical	24407287
KAT6A_HUMAN	KAT6A	physical	23431171
RNF4_HUMAN	RNF4	physical	24637324
DAXX_HUMAN	DAXX	physical	17081986
ZMYM2_HUMAN	ZMYM2	physical	25133527
PER2_MOUSE	Per2	physical	22274616
PER2_HUMAN	PER2	physical	22274616
TF7L2_HUMAN	TCF7L2	physical	22155184
PARK7_HUMAN	PARK7	physical	22683601
DYN2_HUMAN	DNM2	physical	26496610
SQSTM_HUMAN	SQSTM1	physical	26496610
PLOD3_HUMAN	PLOD3	physical	26496610
HOME3_HUMAN	HOMER3	physical	26496610
ATPK_HUMAN	ATP5J2	physical	26496610
TOM20_HUMAN	TOMM20	physical	26496610
HMGX4_HUMAN	HMGXB4	physical	26496610
WDR5_HUMAN	WDR5	physical	26496610
INT7_HUMAN	INTS7	physical	26496610
TECT3_HUMAN	TCTN3	physical	26496610
QCR8_HUMAN	UQCRQ	physical	26496610
TBC14_HUMAN	TBC1D14	physical	26496610
GT251_HUMAN	COLGALT1	physical	26496610
SFXN3_HUMAN	SFXN3	physical	26496610
DPH7_HUMAN	DPH7	physical	26496610
C1QT6_HUMAN	C1QTNF6	physical	26496610
NANP_HUMAN	NANP	physical	26496610
EME1_HUMAN	EME1	physical	26496610
GOG6A_HUMAN	GOLGA6A	physical	26496610
TIM23_HUMAN	TIMM23	physical	26496610
MLP3B_HUMAN	MAP1LC3B	physical	25419843
SUMO1_HUMAN	SUMO1	physical	25497731
VIE1_HCMVM	UL123	physical	25412268
SP1_HUMAN	SP1	physical	24728382
GATA1_HUMAN	GATA1	physical	24255919
CBP_HUMAN	CREBBP	physical	25733689
TF65_HUMAN	RELA	physical	25733689
STAT1_HUMAN	STAT1	physical	25733689
STAT1_HUMAN	STAT1	physical	25812002
STAT2_HUMAN	STAT2	physical	25812002
HDAC1_HUMAN	HDAC1	physical	25812002
HDAC2_HUMAN	HDAC2	physical	25812002
NACC1_HUMAN	NACC1	physical	25891951
NR1I3_HUMAN	NR1I3	physical	26407237
PRGC1_HUMAN	PPARGC1A	physical	26407237
CDN2A_HUMAN	CDKN2A	physical	26578773
ARF_HUMAN	CDKN2A	physical	26578773
UBP11_HUMAN	USP11	physical	24487962
TBA3C_HUMAN	TUBA3C	physical	28514442
GOPC_HUMAN	GOPC	physical	28514442
NDUS1_HUMAN	NDUFS1	physical	28514442
WIPI3_HUMAN	WDR45B	physical	28514442
NDUA2_HUMAN	NDUFA2	physical	28514442
RN123_HUMAN	RNF123	physical	28514442
PSME3_HUMAN	PSME3	physical	28514442
SPTA1_HUMAN	SPTA1	physical	16889989
VIE1_HCMVM	UL123	physical	27903803
PML_HUMAN	PML	physical	27903803
UBC9_HUMAN	UBE2I	physical	27903803
CCNT1_HUMAN	CCNT1	physical	28555140
VIE1_HCMVM	UL123	physical	28250117
SUMO1_HUMAN	SUMO1	physical	28851805
SUMO2_HUMAN	SUMO2	physical	28851805
CACL1_HUMAN	CACUL1	physical	27889610
VIE1_HCMVM	UL123	physical	26559840

Drug and Disease Associations

• Kegg Disease
• H00003: Acute myeloid leukemia (AML)
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• D00094: Tretinoin (JAN/USP/INN); Avita (TN); Renova (TN); Retin A (TN); Tretinoin (TN); Vesanoid (TN)
• D02106: Arsenic trioxide (JP16/USAN); Trisenox (TN)
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530 AND THR-867, ANDMASS SPECTROMETRY.
PubMed: 19690332

"PML tumor suppressor is regulated by HIPK2-mediated phosphorylationin response to DNA damage.";
Gresko E., Ritterhoff S., Sevilla-Perez J., Roscic A., Froebius K.,Kotevic I., Vichalkovski A., Hess D., Hemmings B.A., Schmitz M.L.;
Oncogene 28:698-708(2009).
Cited for: PHOSPHORYLATION AT SER-8 AND SER-38 BY HIPK2, AND INTERACTION WITHHIPK2.
PubMed: 19015637

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; THR-409; SER-518;SER-527 AND SER-530, AND MASS SPECTROMETRY.
PubMed: 18669648

"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-504, ANDMASS SPECTROMETRY.
PubMed: 19007248

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-512, ANDMASS SPECTROMETRY.
PubMed: 17287340

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-403; SER-518;SER-527; SER-530; SER-535; SER-560; SER-561; SER-562 AND SER-565, ANDMASS SPECTROMETRY.
PubMed: 17081983

"PML-dependent apoptosis after DNA damage is regulated by thecheckpoint kinase hCds1/Chk2.";
Yang S., Kuo C., Bisi J.E., Kim M.K.;
Nat. Cell Biol. 4:865-870(2002).
Cited for: FUNCTION IN DNA REPAIR, PHOSPHORYLATION AT SER-117 BY CHEK2, ANDINTERACTION WITH CHEK2.
PubMed: 12402044

Sumoylation

"Identification of three major sentrinization sites in PML.";
Kamitani T., Kito K., Nguyen H.P., Wada H., Fukuda-Kamitani T.,Yeh E.T.H.;
J. Biol. Chem. 273:26675-26682(1998).
Cited for: SUMOYLATION AT LYS-65; LYS-160 AND LYS-490, MUTAGENESIS OF LYS-65;LYS-133; LYS-150; LYS-160 AND LYS-490, SUBCELLULAR LOCATION, ANDFUNCTION.
PubMed: 9756909

Ubiquitylation

"RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required forarsenic-induced PML degradation.";
Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N.,Jaffray E.G., Palvimo J.J., Hay R.T.;
Nat. Cell Biol. 10:538-546(2008).
Cited for: POLYUBIQUITINATION AT LYS-380; LYS-400; LYS-401 AND LYS-476 BY RNF4,PROTEASOMAL DEGRADATION, AND SUMOYLATION.
PubMed: 18408734