dbPTM

PININ_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PININ_HUMAN
UniProt AC	Q9H307
Protein Name	Pinin
Gene Name	PNN
Organism	Homo sapiens (Human).
Sequence Length	717
Subcellular Localization	Nucleus speckle. Cell junction, desmosome. Cell-cell contact area, predominantly desmosome of intercellular adherens junction. Not a nucleocytoplasmic shuttling protein.
Protein Description	Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Component of the PSAP complex which binds RNA in a sequence-independent manner and is proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. Involved in the establishment and maintenance of epithelia cell-cell adhesion. Potential tumor suppressor for renal cell carcinoma..
Protein Sequence	MAVAVRTLQEQLEKAKESLKNVDENIRKLTGRDPNDVRPIQARLLALSGPGGGRGRGSLLLRRGFSDSGGGPPAKQRDLEGAVSRLGGERRTRRESRQESDPEDDDVKKPALQSSVVATSKERTRRDLIQDQNMDEKGKQRNRRIFGLLMGTLQKFKQESTVATERQKRRQEIEQKLEVQAEEERKQVENERRELFEERRAKQTELRLLEQKVELAQLQEEWNEHNAKIIKYIRTKTKPHLFYIPGRMCPATQKLIEESQRKMNALFEGRRIEFAEQINKMEARPRRQSMKEKEHQVVRNEEQKAEQEEGKVAQREEELEETGNQHNDVEIEEAGEEEEKEIAIVHSDAEKEQEEEEQKQEMEVKMEEETEVRESEKQQDSQPEEVMDVLEMVENVKHVIADQEVMETNRVESVEPSENEASKELEPEMEFEIEPDKECKTLSPGKENVSALDMEKESEEKEEKESEPQPEPVAQPQPQSQPQLQLQSQSQPVLQSQPPSQPEDLSLAVLQPTPQVTQEQGHLLPERKDFPVESVKLTEVPVEPVLTVHPESKSKTKTRSRSRGRARNKTSKSRSRSSSSSSSSSSSTSSSSGSSSSSGSSSSRSSSSSSSSTSGSSSRDSSSSTSSSSESRSRSRGRGHNRDRKHRRSVDRKRRDTSGLERSHKSSKGGSSRDTKGSKDKNSRSDRKRSISESSRSGKRSSRSERDRKSDRKDKRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAVAVRTLQ ------CCHHHHHHH	9.66	19413330
14	2-Hydroxyisobutyrylation	TLQEQLEKAKESLKN HHHHHHHHHHHHHHC	73.65	-
14	Acetylation	TLQEQLEKAKESLKN HHHHHHHHHHHHHHC	73.65	26051181
16	Ubiquitination	QEQLEKAKESLKNVD HHHHHHHHHHHHCHH	59.93	-
30	Phosphorylation	DENIRKLTGRDPNDV HHHHHHHHCCCCCCC	32.95	20068231
48	Phosphorylation	QARLLALSGPGGGRG HHHHHHHCCCCCCCC	37.02	21712546
54	Dimethylation	LSGPGGGRGRGSLLL HCCCCCCCCHHHEEE	34.60	-
54	Methylation	LSGPGGGRGRGSLLL HCCCCCCCCHHHEEE	34.60	12020235
56	Dimethylation	GPGGGRGRGSLLLRR CCCCCCCHHHEEECC	30.11	-
56	Methylation	GPGGGRGRGSLLLRR CCCCCCCHHHEEECC	30.11	12020247
58	Phosphorylation	GGGRGRGSLLLRRGF CCCCCHHHEEECCCC	17.93	22617229
62	Dimethylation	GRGSLLLRRGFSDSG CHHHEEECCCCCCCC	36.32	-
62	Methylation	GRGSLLLRRGFSDSG CHHHEEECCCCCCCC	36.32	12020259
63	Methylation	RGSLLLRRGFSDSGG HHHEEECCCCCCCCC	50.94	54558095
66	Phosphorylation	LLLRRGFSDSGGGPP EEECCCCCCCCCCCC	33.42	29255136
68	Phosphorylation	LRRGFSDSGGGPPAK ECCCCCCCCCCCCHH	37.83	30266825
75	2-Hydroxyisobutyrylation	SGGGPPAKQRDLEGA CCCCCCHHHCCHHHH	52.20	-
84	Phosphorylation	RDLEGAVSRLGGERR CCHHHHHHHHCCCHH	22.66	23401153
92	Phosphorylation	RLGGERRTRRESRQE HHCCCHHHHHHHHCC	40.06	26657352
96	Phosphorylation	ERRTRRESRQESDPE CHHHHHHHHCCCCCC	37.14	25159151
100	Phosphorylation	RRESRQESDPEDDDV HHHHHCCCCCCCCCC	50.56	29255136
108	Ubiquitination	DPEDDDVKKPALQSS CCCCCCCCCHHHHHH	61.09	23000965
109	Sumoylation	PEDDDVKKPALQSSV CCCCCCCCHHHHHHH	35.06	-
109	Sumoylation	PEDDDVKKPALQSSV CCCCCCCCHHHHHHH	35.06	28112733
109	Ubiquitination	PEDDDVKKPALQSSV CCCCCCCCHHHHHHH	35.06	23000965
114	Phosphorylation	VKKPALQSSVVATSK CCCHHHHHHHHCCCC	26.42	23927012
115	Phosphorylation	KKPALQSSVVATSKE CCHHHHHHHHCCCCH	13.98	25159151
119	Phosphorylation	LQSSVVATSKERTRR HHHHHHCCCCHHHHH	28.81	23927012
120	Phosphorylation	QSSVVATSKERTRRD HHHHHCCCCHHHHHH	23.84	23927012
121	Sumoylation	SSVVATSKERTRRDL HHHHCCCCHHHHHHH	47.03	28112733
121	Ubiquitination	SSVVATSKERTRRDL HHHHCCCCHHHHHHH	47.03	29967540
124	Phosphorylation	VATSKERTRRDLIQD HCCCCHHHHHHHHHC	31.02	20068231
134	Sulfoxidation	DLIQDQNMDEKGKQR HHHHCCCCCHHHHHH	6.14	21406390
137	2-Hydroxyisobutyrylation	QDQNMDEKGKQRNRR HCCCCCHHHHHHHHH	68.12	-
137	Acetylation	QDQNMDEKGKQRNRR HCCCCCHHHHHHHHH	68.12	26051181
137	Sumoylation	QDQNMDEKGKQRNRR HCCCCCHHHHHHHHH	68.12	28112733
137	Ubiquitination	QDQNMDEKGKQRNRR HCCCCCHHHHHHHHH	68.12	22817900
137 (in isoform 1)	Ubiquitination	-	68.12	21906983
139	Ubiquitination	QNMDEKGKQRNRRIF CCCCHHHHHHHHHHH	58.09	22817900
152	Phosphorylation	IFGLLMGTLQKFKQE HHHHHHHHHHHHHHH	16.43	24173317
155	Sumoylation	LLMGTLQKFKQESTV HHHHHHHHHHHHHHH	58.61	28112733
157	Sumoylation	MGTLQKFKQESTVAT HHHHHHHHHHHHHHH	61.26	-
157	Acetylation	MGTLQKFKQESTVAT HHHHHHHHHHHHHHH	61.26	26051181
157	Methylation	MGTLQKFKQESTVAT HHHHHHHHHHHHHHH	61.26	110871807
157	Sumoylation	MGTLQKFKQESTVAT HHHHHHHHHHHHHHH	61.26	25114211
157	Ubiquitination	MGTLQKFKQESTVAT HHHHHHHHHHHHHHH	61.26	32142685
160	Phosphorylation	LQKFKQESTVATERQ HHHHHHHHHHHHHHH	26.20	23312004
161	Phosphorylation	QKFKQESTVATERQK HHHHHHHHHHHHHHH	17.26	24173317
164	Phosphorylation	KQESTVATERQKRRQ HHHHHHHHHHHHHHH	27.62	-
204	Phosphorylation	EERRAKQTELRLLEQ HHHHHHHHHHHHHHH	35.96	21601212
212	Acetylation	ELRLLEQKVELAQLQ HHHHHHHHHHHHHHH	28.44	26051181
212	Ubiquitination	ELRLLEQKVELAQLQ HHHHHHHHHHHHHHH	28.44	29967540
228	Acetylation	EWNEHNAKIIKYIRT HHHHHHHHHHHHHHH	50.73	26051181
228	Sumoylation	EWNEHNAKIIKYIRT HHHHHHHHHHHHHHH	50.73	28112733
228	Ubiquitination	EWNEHNAKIIKYIRT HHHHHHHHHHHHHHH	50.73	29967540
238	Acetylation	KYIRTKTKPHLFYIP HHHHHCCCCCEEECC	31.81	19608861
238	Malonylation	KYIRTKTKPHLFYIP HHHHHCCCCCEEECC	31.81	26320211
238	Succinylation	KYIRTKTKPHLFYIP HHHHHCCCCCEEECC	31.81	-
238	Succinylation	KYIRTKTKPHLFYIP HHHHHCCCCCEEECC	31.81	-
238	Ubiquitination	KYIRTKTKPHLFYIP HHHHHCCCCCEEECC	31.81	29967540
243	Phosphorylation	KTKPHLFYIPGRMCP CCCCCEEECCCCCCH	16.74	-
254	Acetylation	RMCPATQKLIEESQR CCCHHHHHHHHHHHH	47.26	25953088
254	Ubiquitination	RMCPATQKLIEESQR CCCHHHHHHHHHHHH	47.26	32015554
262	Malonylation	LIEESQRKMNALFEG HHHHHHHHHHHHHHC	28.95	26320211
262	Ubiquitination	LIEESQRKMNALFEG HHHHHHHHHHHHHHC	28.95	29967540
280	Sumoylation	EFAEQINKMEARPRR HHHHHHHHHHCCHHH	39.48	28112733
280	Ubiquitination	EFAEQINKMEARPRR HHHHHHHHHHCCHHH	39.48	29967540
289	Phosphorylation	EARPRRQSMKEKEHQ HCCHHHHHHHHHHHH	29.97	29496963
304	Sumoylation	VVRNEEQKAEQEEGK HHHCHHHHHHHHHCH	58.11	-
304	Sumoylation	VVRNEEQKAEQEEGK HHHCHHHHHHHHHCH	58.11	28112733
311	Acetylation	KAEQEEGKVAQREEE HHHHHHCHHHHHHHH	37.36	26051181
311	Sumoylation	KAEQEEGKVAQREEE HHHHHHCHHHHHHHH	37.36	28112733
322	Phosphorylation	REEELEETGNQHNDV HHHHHHHHCCCCCCC	31.86	30576142
347	Phosphorylation	KEIAIVHSDAEKEQE HCEEEEECHHHHHHH	27.85	29255136
359	Sumoylation	EQEEEEQKQEMEVKM HHHHHHHHHHHHHHH	52.05	28112733
365	Sumoylation	QKQEMEVKMEEETEV HHHHHHHHHHHHHHH	27.56	28112733
370	Phosphorylation	EVKMEEETEVRESEK HHHHHHHHHHHHHHH	42.96	29214152
375	Phosphorylation	EETEVRESEKQQDSQ HHHHHHHHHHHCCCC	39.26	30278072
381	Phosphorylation	ESEKQQDSQPEEVMD HHHHHCCCCCHHHHH	43.21	22167270
408	Phosphorylation	ADQEVMETNRVESVE CCHHHHHHCCCCCCC	15.38	30266825
413	Phosphorylation	METNRVESVEPSENE HHHCCCCCCCCCCCH	28.99	19664994
417	Phosphorylation	RVESVEPSENEASKE CCCCCCCCCCHHHHC	39.28	30266825
422	Phosphorylation	EPSENEASKELEPEM CCCCCHHHHCCCCCC	22.08	25159151
437	Acetylation	EFEIEPDKECKTLSP EEEECCCCCCCCCCC	75.60	26051181
441	Phosphorylation	EPDKECKTLSPGKEN CCCCCCCCCCCCCCC	45.82	22167270
443	Phosphorylation	DKECKTLSPGKENVS CCCCCCCCCCCCCCC	38.40	19664994
450	Phosphorylation	SPGKENVSALDMEKE CCCCCCCCHHHHHHH	34.39	22167270
458	Phosphorylation	ALDMEKESEEKEEKE HHHHHHHHHHHHHHC	63.22	25159151
528	Sumoylation	GHLLPERKDFPVESV CCCCCCCCCCCCCEE	63.16	28112733
528	Ubiquitination	GHLLPERKDFPVESV CCCCCCCCCCCCCEE	63.16	23000965
534	Phosphorylation	RKDFPVESVKLTEVP CCCCCCCEEECEECC	25.45	27251275
536	Acetylation	DFPVESVKLTEVPVE CCCCCEEECEECCCC	60.00	26051181
536	Sumoylation	DFPVESVKLTEVPVE CCCCCEEECEECCCC	60.00	28112733
536	Ubiquitination	DFPVESVKLTEVPVE CCCCCEEECEECCCC	60.00	33845483
538	Phosphorylation	PVESVKLTEVPVEPV CCCEEECEECCCCCC	29.26	24732914
547	Phosphorylation	VPVEPVLTVHPESKS CCCCCCEEECCCCCC	19.59	30266825
552	Phosphorylation	VLTVHPESKSKTKTR CEEECCCCCCCCCCC	46.83	30266825
553	Sumoylation	LTVHPESKSKTKTRS EEECCCCCCCCCCCC	55.07	-
553	Acetylation	LTVHPESKSKTKTRS EEECCCCCCCCCCCC	55.07	25953088
553	Malonylation	LTVHPESKSKTKTRS EEECCCCCCCCCCCC	55.07	26320211
553	Sumoylation	LTVHPESKSKTKTRS EEECCCCCCCCCCCC	55.07	28112733
553	Ubiquitination	LTVHPESKSKTKTRS EEECCCCCCCCCCCC	55.07	33845483
554	Phosphorylation	TVHPESKSKTKTRSR EECCCCCCCCCCCCH	55.63	26852163
556	Phosphorylation	HPESKSKTKTRSRSR CCCCCCCCCCCCHHH	44.75	23312004
558	Phosphorylation	ESKSKTKTRSRSRGR CCCCCCCCCCHHHHC	38.82	-
560	Phosphorylation	KSKTKTRSRSRGRAR CCCCCCCCHHHHCCC	39.58	-
562	Phosphorylation	KTKTRSRSRGRARNK CCCCCCHHHHCCCCC	40.09	21601212
575	Phosphorylation	NKTSKSRSRSSSSSS CCCCCCCCCCCCCCC	43.54	24260401
578	Phosphorylation	SKSRSRSSSSSSSSS CCCCCCCCCCCCCCC	32.88	-
579	Phosphorylation	KSRSRSSSSSSSSSS CCCCCCCCCCCCCCC	35.17	30576142
580	Phosphorylation	SRSRSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
581	Phosphorylation	RSRSSSSSSSSSSST CCCCCCCCCCCCCCC	35.87	-
582	Phosphorylation	SRSSSSSSSSSSSTS CCCCCCCCCCCCCCC	35.87	-
583	Phosphorylation	RSSSSSSSSSSSTSS CCCCCCCCCCCCCCC	35.87	-
584	Phosphorylation	SSSSSSSSSSSTSSS CCCCCCCCCCCCCCC	35.87	30576142
587	Phosphorylation	SSSSSSSSTSSSSGS CCCCCCCCCCCCCCC	33.97	30576142
588	Phosphorylation	SSSSSSSTSSSSGSS CCCCCCCCCCCCCCC	34.28	30576142
589	Phosphorylation	SSSSSSTSSSSGSSS CCCCCCCCCCCCCCC	30.12	30576142
590	Phosphorylation	SSSSSTSSSSGSSSS CCCCCCCCCCCCCCC	28.72	-
591	Phosphorylation	SSSSTSSSSGSSSSS CCCCCCCCCCCCCCC	38.19	-
592	Phosphorylation	SSSTSSSSGSSSSSG CCCCCCCCCCCCCCC	44.64	21601212
594	Phosphorylation	STSSSSGSSSSSGSS CCCCCCCCCCCCCCC	29.06	-
597	Phosphorylation	SSSGSSSSSGSSSSR CCCCCCCCCCCCCCC	40.44	30576142
598	Phosphorylation	SSGSSSSSGSSSSRS CCCCCCCCCCCCCCC	44.64	30576142
600	Phosphorylation	GSSSSSGSSSSRSSS CCCCCCCCCCCCCCC	29.06	-
601	Phosphorylation	SSSSSGSSSSRSSSS CCCCCCCCCCCCCCC	35.54	-
602	Phosphorylation	SSSSGSSSSRSSSSS CCCCCCCCCCCCCCC	31.31	-
603	Phosphorylation	SSSGSSSSRSSSSSS CCCCCCCCCCCCCCC	37.82	-
604	Methylation	SSGSSSSRSSSSSSS CCCCCCCCCCCCCCC	42.37	115388677
605	Phosphorylation	SGSSSSRSSSSSSSS CCCCCCCCCCCCCCC	36.20	-
606	Phosphorylation	GSSSSRSSSSSSSST CCCCCCCCCCCCCCC	32.88	21601212
607	Phosphorylation	SSSSRSSSSSSSSTS CCCCCCCCCCCCCCC	35.17	30576142
609	Phosphorylation	SSRSSSSSSSSTSGS CCCCCCCCCCCCCCC	35.87	30576142
610	Phosphorylation	SRSSSSSSSSTSGSS CCCCCCCCCCCCCCC	30.20	30576142
611	Phosphorylation	RSSSSSSSSTSGSSS CCCCCCCCCCCCCCC	39.31	-
614	Phosphorylation	SSSSSSTSGSSSRDS CCCCCCCCCCCCCCC	38.33	21601212
617	Phosphorylation	SSSTSGSSSRDSSSS CCCCCCCCCCCCCCC	32.68	24505115
618	Phosphorylation	SSTSGSSSRDSSSST CCCCCCCCCCCCCCC	41.63	30576142
621	Phosphorylation	SGSSSRDSSSSTSSS CCCCCCCCCCCCCCC	30.89	24043423
622	Phosphorylation	GSSSRDSSSSTSSSS CCCCCCCCCCCCCCC	32.37	24043423
623	Phosphorylation	SSSRDSSSSTSSSSE CCCCCCCCCCCCCCH	41.40	30576142
624	Phosphorylation	SSRDSSSSTSSSSES CCCCCCCCCCCCCHH	33.97	30576142
625	Phosphorylation	SRDSSSSTSSSSESR CCCCCCCCCCCCHHH	34.28	24043423
626	Phosphorylation	RDSSSSTSSSSESRS CCCCCCCCCCCHHHH	30.12	30576142
627	Phosphorylation	DSSSSTSSSSESRSR CCCCCCCCCCHHHHC	37.66	24043423
628	Phosphorylation	SSSSTSSSSESRSRS CCCCCCCCCHHHHCC	37.58	24043423
629	Phosphorylation	SSSTSSSSESRSRSR CCCCCCCCHHHHCCC	41.35	24043423
631	Phosphorylation	STSSSSESRSRSRGR CCCCCCHHHHCCCCC	37.19	30576142
633	Phosphorylation	SSSSESRSRSRGRGH CCCCHHHHCCCCCCC	43.84	-
649	Phosphorylation	RDRKHRRSVDRKRRD CHHHHHHHHHHHHHC	28.46	22817900
657	Phosphorylation	VDRKRRDTSGLERSH HHHHHHCCCCCCHHC	23.92	27273156
658	Phosphorylation	DRKRRDTSGLERSHK HHHHHCCCCCCHHCC	45.74	21955146
663	Phosphorylation	DTSGLERSHKSSKGG CCCCCCHHCCCCCCC	26.37	22817900
666	Phosphorylation	GLERSHKSSKGGSSR CCCHHCCCCCCCCCC	31.68	22817900
667	Phosphorylation	LERSHKSSKGGSSRD CCHHCCCCCCCCCCC	39.87	22817900
668	Acetylation	ERSHKSSKGGSSRDT CHHCCCCCCCCCCCC	74.51	12433911
671	Phosphorylation	HKSSKGGSSRDTKGS CCCCCCCCCCCCCCC	30.76	22817900
672	Phosphorylation	KSSKGGSSRDTKGSK CCCCCCCCCCCCCCC	37.13	22817900
678	Phosphorylation	SSRDTKGSKDKNSRS CCCCCCCCCCCCCHH	38.96	21601212
679	Ubiquitination	SRDTKGSKDKNSRSD CCCCCCCCCCCCHHH	79.83	24816145
683	Phosphorylation	KGSKDKNSRSDRKRS CCCCCCCCHHHHHHH	38.61	21601212
685	Phosphorylation	SKDKNSRSDRKRSIS CCCCCCHHHHHHHHH	41.40	21601212
690	Phosphorylation	SRSDRKRSISESSRS CHHHHHHHHHHHHHH	33.24	23401153
692	Phosphorylation	SDRKRSISESSRSGK HHHHHHHHHHHHHCC	32.45	30266825
694	Phosphorylation	RKRSISESSRSGKRS HHHHHHHHHHHCCCC	25.02	30266825
695	Phosphorylation	KRSISESSRSGKRSS HHHHHHHHHHCCCCC	26.81	30266825
697	Phosphorylation	SISESSRSGKRSSRS HHHHHHHHCCCCCHH	51.09	26074081
702	Phosphorylation	SRSGKRSSRSERDRK HHHCCCCCHHHHHHH	43.81	21601212
704	Phosphorylation	SGKRSSRSERDRKSD HCCCCCHHHHHHHHH	38.64	-

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	APC/C	-	PMID:32203416

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPIG_HUMAN	PPIG	physical	15358154
SRRM2_HUMAN	SRRM2	physical	14578391
SRSF4_HUMAN	SRSF4	physical	14578391
PNISR_HUMAN	PNISR	physical	14578391
RNPS1_HUMAN	RNPS1	physical	14517304
NO40_HUMAN	ZCCHC17	physical	12893261
K1C19_HUMAN	KRT19	physical	10809736
K2C8_HUMAN	KRT8	physical	10809736
K1C18_HUMAN	KRT18	physical	10809736
RNPS1_HUMAN	RNPS1	physical	22388736
SAP18_HUMAN	SAP18	physical	22388736
SRRM1_HUMAN	SRRM1	physical	26344197
ZCH18_HUMAN	ZC3H18	physical	26344197
CCDC9_HUMAN	CCDC9	physical	28514442
ZC3HE_HUMAN	ZC3H14	physical	28514442
CLK2_HUMAN	CLK2	physical	28514442
RNPS1_HUMAN	RNPS1	physical	28514442
PPIG_HUMAN	PPIG	physical	28514442
VANG2_HUMAN	VANGL2	physical	28514442
ACINU_HUMAN	ACIN1	physical	28514442
CASC3_HUMAN	CASC3	physical	28514442
SFR19_HUMAN	SCAF1	physical	28514442
NCBP3_HUMAN	C17orf85	physical	28514442
VANG1_HUMAN	VANGL1	physical	28514442
TR150_HUMAN	THRAP3	physical	28514442
PRP4B_HUMAN	PRPF4B	physical	28514442
SYF1_HUMAN	XAB2	physical	28514442
RBM22_HUMAN	RBM22	physical	28514442
PRP17_HUMAN	CDC40	physical	28514442
NKTR_HUMAN	NKTR	physical	28514442
UIF_HUMAN	FYTTD1	physical	28514442
TOPRS_HUMAN	TOPORS	physical	28514442
BCLF1_HUMAN	BCLAF1	physical	28514442
CAPON_HUMAN	NOS1AP	physical	28514442
PPIE_HUMAN	PPIE	physical	28514442
CRNL1_HUMAN	CRNKL1	physical	28514442
ISY1_HUMAN	ISY1	physical	28514442
RBBP6_HUMAN	RBBP6	physical	28514442
GPAM1_HUMAN	GPALPP1	physical	28514442
IF4A3_HUMAN	EIF4A3	physical	28514442
SRRM2_HUMAN	SRRM2	physical	28514442
SRS10_HUMAN	SRSF10	physical	28514442
DHX8_HUMAN	DHX8	physical	28514442
AQR_HUMAN	AQR	physical	28514442

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 PININ_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-66; SER-347; SER-381; SER-441; SER-443 ANDSER-450, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-238, 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-66; SER-381; SER-443 ANDSER-450, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-66; SER-347; SER-381; SER-441; SER-443 ANDSER-450, AND MASS SPECTROMETRY.	19413330 [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-66; SER-100; SER-381;SER-443; SER-450 AND SER-552, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND MASSSPECTROMETRY.	18691976 [Abstract]
"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-66; SER-100; SER-347;SER-441 AND SER-443, AND MASS SPECTROMETRY.	19007248 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND MASSSPECTROMETRY.	17525332 [Abstract]
"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-96; SER-100; SER-114;SER-443; SER-649; SER-663; SER-666; SER-667; SER-671; SER-672;SER-690; SER-692 AND SER-695, AND MASS SPECTROMETRY.	17287340 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND SER-443, ANDMASS SPECTROMETRY.	16565220 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASSSPECTROMETRY.	16964243 [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-66; SER-100; SER-347;SER-381; SER-658 AND SER-692, AND MASS SPECTROMETRY.	17081983 [Abstract]