dbPTM

SP100_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SP100_HUMAN
UniProt AC	P23497
Protein Name	Nuclear autoantigen Sp-100
Gene Name	SP100
Organism	Homo sapiens (Human).
Sequence Length	879
Subcellular Localization	Nucleus. Nucleus, PML body. Cytoplasm. Differences in the subnuclear localization of the different isoforms seem to exist and may also be cell cycle- and interferon-dependent. Accumulates in the cytoplasm upon FAS activation. Isoform Sp100-C: Nucleu
Protein Description	Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2 according to PubMed:11909962. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to PubMed:15247905. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. Also plays a role in infection by viruses, including human cytomegalovirus and Epstein-Barr virus, through mechanisms that may involve chromatin and/or transcriptional regulation..
Protein Sequence	MAGGGGDLSTRRLNECISPVANEMNHLPAHSHDLQRMFTEDQGVDDRLLYDIVFKHFKRNKVEISNAIKKTFPFLEGLRDRDLITNKMFEDSQDSCRNLVPVQRVVYNVLSELEKTFNLPVLEALFSDVNMQEYPDLIHIYKGFENVIHDKLPLQESEEEEREERSGLQLSLEQGTGENSFRSLTWPPSGSPSHAGTTPPENGLSEHPCETEQINAKRKDTTSDKDDSLGSQQTNEQCAQKAEPTESCEQIAVQVNNGDAGREMPCPLPCDEESPEAELHNHGIQINSCSVRLVDIKKEKPFSNSKVECQAQARTHHNQASDIIVISSEDSEGSTDVDEPLEVFISAPRSEPVINNDNPLESNDEKEGQEATCSRPQIVPEPMDFRKLSTFRESFKKRVIGQDHDFSESSEEEAPAEASSGALRSKHGEKAPMTSRSTSTWRIPSRKRRFSSSDFSDLSNGEELQETCSSSLRRGSGSQPQEPENKKCSCVMCFPKGVPRSQEARTESSQASDMMDTMDVENNSTLEKHSGKRRKKRRHRSKVNGLQRGRKKDRPRKHLTLNNKVQKKRWQQRGRKANTRPLKRRRKRGPRIPKDENINFKQSELPVTCGEVKGTLYKERFKQGTSKKCIQSEDKKWFTPREFEIEGDRGASKNWKLSIRCGGYTLKVLMENKFLPEPPSTRKKRILESHNNTLVDPCEEHKKKNPDASVKFSEFLKKCSETWKTIFAKEKGKFEDMAKADKAHYEREMKTYIPPKGEKKKKFKDPNAPKRPPLAFFLFCSEYRPKIKGEHPGLSIDDVVKKLAGMWNNTAAADKQFYEKKAAKLKEKYKKDIAAYRAKGKPNSAKKRVVKAEKSKKKKEEEEDEEDEQEEENEEDDDK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGGGGDLS ------CCCCCCCCH	25.90	22814378
9	Phosphorylation	AGGGGDLSTRRLNEC CCCCCCCHHHHHHHH	25.30	29514088
10	Phosphorylation	GGGGDLSTRRLNECI CCCCCCHHHHHHHHH	27.40	26074081
14 (in isoform 6)	Phosphorylation	-	40.04	24275569
18	Phosphorylation	RRLNECISPVANEMN HHHHHHHHHHHHHCC	25.61	29255136
31	Phosphorylation	MNHLPAHSHDLQRMF CCCCCCCCHHHHHHH	22.32	23927012
39	Phosphorylation	HDLQRMFTEDQGVDD HHHHHHHHCCCCCCH	29.34	20068231
50	Phosphorylation	GVDDRLLYDIVFKHF CCCHHHHHHHHHHHH	14.28	20068231
55	Ubiquitination	LLYDIVFKHFKRNKV HHHHHHHHHHHHCCH	36.92	-
65	Phosphorylation	KRNKVEISNAIKKTF HHCCHHHHHHHHHHH	13.50	23401153
70	Ubiquitination	EISNAIKKTFPFLEG HHHHHHHHHHHHHCC	49.65	-
87	Ubiquitination	DRDLITNKMFEDSQD CHHCCCCHHCCCCHH	35.99	-
92	Phosphorylation	TNKMFEDSQDSCRNL CCHHCCCCHHHHHHC	28.79	30108239
95	Phosphorylation	MFEDSQDSCRNLVPV HCCCCHHHHHHCHHH	13.82	30108239
111	Phosphorylation	RVVYNVLSELEKTFN HHHHHHHHHHHHHHC	35.53	-
151	Ubiquitination	FENVIHDKLPLQESE HHHHHHCCCCCCCCH	37.53	21906983
151 (in isoform 2)	Ubiquitination	-	37.53	21906983
151 (in isoform 1)	Ubiquitination	-	37.53	21906983
151 (in isoform 3)	Ubiquitination	-	37.53	21906983
151 (in isoform 4)	Ubiquitination	-	37.53	21906983
151 (in isoform 5)	Ubiquitination	-	37.53	21906983
157	Phosphorylation	DKLPLQESEEEEREE CCCCCCCCHHHHHHH	37.03	29255136
166	Phosphorylation	EEEREERSGLQLSLE HHHHHHHHCCEEEEE	47.32	30266825
171	Phosphorylation	ERSGLQLSLEQGTGE HHHCCEEEEECCCCC	19.52	23401153
176	Phosphorylation	QLSLEQGTGENSFRS EEEEECCCCCCCCCC	40.80	30266825
180	Phosphorylation	EQGTGENSFRSLTWP ECCCCCCCCCCEECC	20.10	30266825
183	Phosphorylation	TGENSFRSLTWPPSG CCCCCCCCEECCCCC	28.30	23403867
185	Phosphorylation	ENSFRSLTWPPSGSP CCCCCCEECCCCCCC	36.85	23403867
189	Phosphorylation	RSLTWPPSGSPSHAG CCEECCCCCCCCCCC	48.07	23401153
191	Phosphorylation	LTWPPSGSPSHAGTT EECCCCCCCCCCCCC	27.80	25159151
193	Phosphorylation	WPPSGSPSHAGTTPP CCCCCCCCCCCCCCC	27.89	25159151
197	Phosphorylation	GSPSHAGTTPPENGL CCCCCCCCCCCCCCC	36.59	25159151
198	Phosphorylation	SPSHAGTTPPENGLS CCCCCCCCCCCCCCC	35.61	25159151
205	Phosphorylation	TPPENGLSEHPCETE CCCCCCCCCCCCCHH	34.95	23403867
211	Phosphorylation	LSEHPCETEQINAKR CCCCCCCHHHHCCCC	39.65	23403867
217	Ubiquitination	ETEQINAKRKDTTSD CHHHHCCCCCCCCCC	56.33	-
219	Ubiquitination	EQINAKRKDTTSDKD HHHCCCCCCCCCCCC	59.73	-
221	Phosphorylation	INAKRKDTTSDKDDS HCCCCCCCCCCCCCC	31.10	23927012
222	Phosphorylation	NAKRKDTTSDKDDSL CCCCCCCCCCCCCCC	45.09	23401153
223	Phosphorylation	AKRKDTTSDKDDSLG CCCCCCCCCCCCCCC	44.76	29255136
225	Ubiquitination	RKDTTSDKDDSLGSQ CCCCCCCCCCCCCCH	64.30	2190698
225	Ubiquitination	RKDTTSDKDDSLGSQ CCCCCCCCCCCCCCH	64.30	-
225	Acetylation	RKDTTSDKDDSLGSQ CCCCCCCCCCCCCCH	64.30	26051181
225 (in isoform 1)	Ubiquitination	-	64.30	21906983
225 (in isoform 2)	Ubiquitination	-	64.30	21906983
225 (in isoform 3)	Ubiquitination	-	64.30	21906983
225 (in isoform 4)	Ubiquitination	-	64.30	21906983
225 (in isoform 5)	Ubiquitination	-	64.30	21906983
228	Phosphorylation	TTSDKDDSLGSQQTN CCCCCCCCCCCHHHH	44.77	29255136
231	Phosphorylation	DKDDSLGSQQTNEQC CCCCCCCCHHHHHHH	25.14	29255136
234	Phosphorylation	DSLGSQQTNEQCAQK CCCCCHHHHHHHHHH	32.84	23663014
241	Sumoylation	TNEQCAQKAEPTESC HHHHHHHHCCCCCCH	35.87	28112733
245	Phosphorylation	CAQKAEPTESCEQIA HHHHCCCCCCHHEEE	31.84	30108239
247	Phosphorylation	QKAEPTESCEQIAVQ HHCCCCCCHHEEEEE	25.98	30108239
274	Phosphorylation	PLPCDEESPEAELHN CCCCCCCCCCHHHHH	26.45	30108239
288	Phosphorylation	NHGIQINSCSVRLVD HCCEEEEECEEEEEE	14.92	27080861
290	Phosphorylation	GIQINSCSVRLVDIK CEEEEECEEEEEEEC	15.30	27080861
297	Sumoylation	SVRLVDIKKEKPFSN EEEEEEECCCCCCCC	50.87	-
297	Sumoylation	SVRLVDIKKEKPFSN EEEEEEECCCCCCCC	50.87	10212234
298	Ubiquitination	VRLVDIKKEKPFSNS EEEEEECCCCCCCCC	71.90	-
300	Acetylation	LVDIKKEKPFSNSKV EEEECCCCCCCCCCC	61.31	23749302
300	Ubiquitination	LVDIKKEKPFSNSKV EEEECCCCCCCCCCC	61.31	-
300	Acetylation	LVDIKKEKPFSNSKV EEEECCCCCCCCCCC	61.31	-
300	Ubiquitination	LVDIKKEKPFSNSKV EEEECCCCCCCCCCC	61.31	-
300	Sumoylation	LVDIKKEKPFSNSKV EEEECCCCCCCCCCC	61.31	28112733
303	Phosphorylation	IKKEKPFSNSKVECQ ECCCCCCCCCCCCHH	49.04	28509920
305	Phosphorylation	KEKPFSNSKVECQAQ CCCCCCCCCCCHHHH	36.56	28509920
306	Acetylation	EKPFSNSKVECQAQA CCCCCCCCCCHHHHH	46.43	25953088
306	Sumoylation	EKPFSNSKVECQAQA CCCCCCCCCCHHHHH	46.43	-
306	Sumoylation	EKPFSNSKVECQAQA CCCCCCCCCCHHHHH	46.43	28112733
306	Ubiquitination	EKPFSNSKVECQAQA CCCCCCCCCCHHHHH	46.43	-
306	Ubiquitination	EKPFSNSKVECQAQA CCCCCCCCCCHHHHH	46.43	-
327	Phosphorylation	ASDIIVISSEDSEGS CCEEEEEECCCCCCC	19.44	17081983
328	Phosphorylation	SDIIVISSEDSEGST CEEEEEECCCCCCCC	34.01	17081983
331	Phosphorylation	IVISSEDSEGSTDVD EEEECCCCCCCCCCC	39.54	17081983
334	Phosphorylation	SSEDSEGSTDVDEPL ECCCCCCCCCCCCCE	19.86	17081983
335	Phosphorylation	SEDSEGSTDVDEPLE CCCCCCCCCCCCCEE	51.39	30087585
350	Phosphorylation	VFISAPRSEPVINND EEEECCCCCCCCCCC	45.23	28355574
362	Phosphorylation	NNDNPLESNDEKEGQ CCCCCCCCCCCCCCC	58.21	29255136
366	Ubiquitination	PLESNDEKEGQEATC CCCCCCCCCCCCCCC	70.75	-
366	Sumoylation	PLESNDEKEGQEATC CCCCCCCCCCCCCCC	70.75	28112733
372	Phosphorylation	EKEGQEATCSRPQIV CCCCCCCCCCCCCCC	15.40	22167270
374	Phosphorylation	EGQEATCSRPQIVPE CCCCCCCCCCCCCCC	42.51	22167270
387	Sumoylation	PEPMDFRKLSTFRES CCCCCHHHHHHHHHH	46.94	-
387	Sumoylation	PEPMDFRKLSTFRES CCCCCHHHHHHHHHH	46.94	25218447
389	Phosphorylation	PMDFRKLSTFRESFK CCCHHHHHHHHHHHH	28.65	29691806
390	Phosphorylation	MDFRKLSTFRESFKK CCHHHHHHHHHHHHH	36.83	23401153
394	Phosphorylation	KLSTFRESFKKRVIG HHHHHHHHHHHHHCC	37.80	23401153
396	Sumoylation	STFRESFKKRVIGQD HHHHHHHHHHHCCCC	49.28	-
396	Sumoylation	STFRESFKKRVIGQD HHHHHHHHHHHCCCC	49.28	-
407	Phosphorylation	IGQDHDFSESSEEEA CCCCCCCCCCCCCCC	42.50	29255136
409	Phosphorylation	QDHDFSESSEEEAPA CCCCCCCCCCCCCCH	41.68	29255136
410	Phosphorylation	DHDFSESSEEEAPAE CCCCCCCCCCCCCHH	45.00	29255136
416 (in isoform 7)	Phosphorylation	-	31.84	26133373
417 (in isoform 7)	Phosphorylation	-	48.28	26133373
419	Phosphorylation	EEAPAEASSGALRSK CCCCHHHHHCCHHHC	22.32	23927012
420	Phosphorylation	EAPAEASSGALRSKH CCCHHHHHCCHHHCC	34.82	24260401
423 (in isoform 6)	Phosphorylation	-	7.88	26133373
424 (in isoform 6)	Phosphorylation	-	43.03	26133373
425	Phosphorylation	ASSGALRSKHGEKAP HHHCCHHHCCCCCCC	29.83	28985074
430	Acetylation	LRSKHGEKAPMTSRS HHHCCCCCCCCCCCC	63.48	23749302
430	Ubiquitination	LRSKHGEKAPMTSRS HHHCCCCCCCCCCCC	63.48	-
430	Acetylation	LRSKHGEKAPMTSRS HHHCCCCCCCCCCCC	63.48	-
434 (in isoform 7)	Phosphorylation	-	21.67	26133373
439	Phosphorylation	PMTSRSTSTWRIPSR CCCCCCCCCCCCCCC	27.50	23882029
440	Phosphorylation	MTSRSTSTWRIPSRK CCCCCCCCCCCCCCC	20.89	23882029
441 (in isoform 6)	Phosphorylation	-	8.93	26133373
445	Phosphorylation	TSTWRIPSRKRRFSS CCCCCCCCCCCCCCC	48.33	26074081
451	Phosphorylation	PSRKRRFSSSDFSDL CCCCCCCCCCCHHCC	27.41	23401153
451 (in isoform 2)	Phosphorylation	-	27.41	26133373
452	Phosphorylation	SRKRRFSSSDFSDLS CCCCCCCCCCHHCCC	31.08	27273156
452 (in isoform 2)	Phosphorylation	-	31.08	26133373
453	Phosphorylation	RKRRFSSSDFSDLSN CCCCCCCCCHHCCCC	41.29	30266825
456	Phosphorylation	RFSSSDFSDLSNGEE CCCCCCHHCCCCCHH	42.50	30266825
459	Phosphorylation	SSDFSDLSNGEELQE CCCHHCCCCCHHHHH	48.02	23927012
467	Phosphorylation	NGEELQETCSSSLRR CCHHHHHHHHHHHHC	12.53	30108239
469	Phosphorylation	EELQETCSSSLRRGS HHHHHHHHHHHHCCC	30.31	23927012
469 (in isoform 2)	Phosphorylation	-	30.31	26133373
470	Phosphorylation	ELQETCSSSLRRGSG HHHHHHHHHHHCCCC	35.22	23927012
471	Phosphorylation	LQETCSSSLRRGSGS HHHHHHHHHHCCCCC	15.03	23927012
476	Phosphorylation	SSSLRRGSGSQPQEP HHHHHCCCCCCCCCC	33.20	29255136
478	Phosphorylation	SLRRGSGSQPQEPEN HHHCCCCCCCCCCCC	40.14	29255136
486	Acetylation	QPQEPENKKCSCVMC CCCCCCCCCCCEEEE	54.19	30592573
506	Phosphorylation	PRSQEARTESSQASD CCCHHHHHHHHHHHH	47.47	23403867
508	Phosphorylation	SQEARTESSQASDMM CHHHHHHHHHHHHHH	27.43	23403867
509	Phosphorylation	QEARTESSQASDMMD HHHHHHHHHHHHHHH	24.43	23403867
512	Phosphorylation	RTESSQASDMMDTMD HHHHHHHHHHHHHCC	20.57	23403867
517	Phosphorylation	QASDMMDTMDVENNS HHHHHHHHCCCCCCC	9.43	23403867
524	Phosphorylation	TMDVENNSTLEKHSG HCCCCCCCHHHHCCC	46.05	23403867
525	Phosphorylation	MDVENNSTLEKHSGK CCCCCCCHHHHCCCC	40.85	-
530	Phosphorylation	NSTLEKHSGKRRKKR CCHHHHCCCCHHHHH	58.01	-
557	Ubiquitination	RKKDRPRKHLTLNNK CCCCCCCCCCCCCHH	45.72	-
560	Phosphorylation	DRPRKHLTLNNKVQK CCCCCCCCCCHHHHH	27.45	-
564	Ubiquitination	KHLTLNNKVQKKRWQ CCCCCCHHHHHHHHH	44.99	-
594	Ubiquitination	KRGPRIPKDENINFK HCCCCCCCCCCCCCC	75.26	-
594	Sumoylation	KRGPRIPKDENINFK HCCCCCCCCCCCCCC	75.26	28112733
601	Ubiquitination	KDENINFKQSELPVT CCCCCCCCHHCCCCC	48.72	-
613	Ubiquitination	PVTCGEVKGTLYKER CCCHHCCCCCCHHHH	41.71	-
639	O-linked_Glycosylation	SEDKKWFTPREFEIE CCCCCCCCCCEEEEE	21.96	28411811
658	Phosphorylation	ASKNWKLSIRCGGYT CCCCEEEEEEECCEE	12.31	29691806
664	Phosphorylation	LSIRCGGYTLKVLME EEEEECCEEHHHHHH	8.32	29691806
665	Phosphorylation	SIRCGGYTLKVLMEN EEEECCEEHHHHHHC	24.31	29691806
673	Ubiquitination	LKVLMENKFLPEPPS HHHHHHCCCCCCCCC	34.66	-
680	O-linked_Glycosylation	KFLPEPPSTRKKRIL CCCCCCCCHHHHHHH	52.11	28411811
681	O-linked_Glycosylation	FLPEPPSTRKKRILE CCCCCCCHHHHHHHH	52.89	28411811
681	Phosphorylation	FLPEPPSTRKKRILE CCCCCCCHHHHHHHH	52.89	22210691
689	Phosphorylation	RKKRILESHNNTLVD HHHHHHHHCCCCCCC	28.24	28258704
710 (in isoform 4)	Ubiquitination	-	8.54	-
731	Acetylation	KTIFAKEKGKFEDMA HHHHHHHCCCHHHHH	67.69	7662349
733	Methylation	IFAKEKGKFEDMAKA HHHHHCCCHHHHHHH	57.56	22641281
733	Acetylation	IFAKEKGKFEDMAKA HHHHHCCCHHHHHHH	57.56	22641281
733	Ubiquitination	IFAKEKGKFEDMAKA HHHHHCCCHHHHHHH	57.56	-
739	Acetylation	GKFEDMAKADKAHYE CCHHHHHHHHHHHHH	50.94	7494143
739	Ubiquitination	GKFEDMAKADKAHYE CCHHHHHHHHHHHHH	50.94	-
739 (in isoform 1)	Ubiquitination	-	50.94	21906983
745	Phosphorylation	AKADKAHYEREMKTY HHHHHHHHHHHHHHC	22.88	26074081
749 (in isoform 4)	Phosphorylation	-	5.01	-
750	Ubiquitination	AHYEREMKTYIPPKG HHHHHHHHHCCCCCC	33.16	-
751	Phosphorylation	HYEREMKTYIPPKGE HHHHHHHHCCCCCCC	25.93	24719451
752	Phosphorylation	YEREMKTYIPPKGEK HHHHHHHCCCCCCCC	13.10	26074081
757 (in isoform 4)	Phosphorylation	-	58.70	29978859
759 (in isoform 4)	Phosphorylation	-	77.79	29978859
764	Acetylation	GEKKKKFKDPNAPKR CCCCCCCCCCCCCCC	79.67	-
764	Ubiquitination	GEKKKKFKDPNAPKR CCCCCCCCCCCCCCC	79.67	-
764 (in isoform 4)	Phosphorylation	-	79.67	29978859
783	Phosphorylation	FFLFCSEYRPKIKGE EEHHCCCCCCCCCCC	18.87	20068231
786	Ubiquitination	FCSEYRPKIKGEHPG HCCCCCCCCCCCCCC	48.31	-
818	Phosphorylation	AAADKQFYEKKAAKL HHHHHHHHHHHHHHH	25.09	-
836	Phosphorylation	YKKDIAAYRAKGKPN HHHHHHHHHHCCCCC	11.33	-
848 (in isoform 4)	Phosphorylation	-	37.44	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	CDC20	Q12834	PMID:22086178
-	K	Ubiquitination	E3 ubiquitin ligase	ICP0	P08393	PMID:32416261

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SP100_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of SP100_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SUMO1_HUMAN	SUMO1	physical	16189514
UBC9_HUMAN	UBE2I	physical	18691969
CBX5_HUMAN	CBX5	physical	9636146
CBX3_HUMAN	CBX3	physical	9636146
CBX1_HUMAN	CBX1	physical	9636146
CBX5_HUMAN	CBX5	physical	11313457
LZTR1_HUMAN	LZTR1	physical	20211142
TRI29_HUMAN	TRIM29	physical	20211142
CBX5_HUMAN	CBX5	physical	15882967
PML_HUMAN	PML	physical	21779164
PML_HUMAN	PML	physical	21172801
SP100_HUMAN	SP100	physical	10212234
PML_HUMAN	PML	physical	11112690
PML_HUMAN	PML	physical	9230084
ETS1_HUMAN	ETS1	physical	15247905
SUMO2_HUMAN	SUMO2	physical	21988832
GDE_HUMAN	AGL	physical	22863883
CRTAP_HUMAN	CRTAP	physical	22863883
GDN_HUMAN	SERPINE2	physical	22863883
TM1L1_HUMAN	TOM1L1	physical	22863883
SP100_HUMAN	SP100	physical	25416956
SUMO1_HUMAN	SUMO1	physical	25416956
DYRK2_HUMAN	DYRK2	physical	25416956
RBM39_HUMAN	RBM39	physical	25416956
CBX5_HUMAN	CBX5	physical	25416956
ZC21A_HUMAN	ZC2HC1A	physical	25416956
AMOL2_HUMAN	AMOTL2	physical	25416956
GIPC2_HUMAN	GIPC2	physical	25416956
T3JAM_HUMAN	TRAF3IP3	physical	25416956
LMBL3_HUMAN	L3MBTL3	physical	25416956
RTP5_HUMAN	RTP5	physical	25416956
VIE1_HCMVM	UL123	physical	28750047

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SP100_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-733, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-171; SER-407; SER-409AND SER-410, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-157; SER-407; SER-409AND SER-410, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-18; SER-157; SER-327;SER-328; SER-331; SER-334; THR-335; SER-407; SER-409; SER-410;SER-451; SER-452; SER-453; SER-456 AND SER-459, AND MASS SPECTROMETRY.	17081983 [Abstract]