dbPTM

CIP2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CIP2A_HUMAN
UniProt AC	Q8TCG1
Protein Name	Protein CIP2A {ECO:0000305}
Gene Name	CIP2A {ECO:0000312\|HGNC:HGNC:29302}
Organism	Homo sapiens (Human).
Sequence Length	905
Subcellular Localization	Membrane Single-pass membrane protein . Cytoplasm . Slightly concentrates in the perinuclear region (PubMed:12118381).
Protein Description	Oncoprotein that inhibits PP2A and stabilizes MYC in human malignancies. Promotes anchorage-independent cell growth and tumor formation..
Protein Sequence	MDSTACLKSLLLTVSQYKAVKSEANATQLLRHLEVISGQKLTRLFTSNQILTSECLSCLVELLEDPNISASLILSIIGLLSQLAVDIETRDCLQNTYNLNSVLAGVVCRSSHTDSVFLQCIQLLQKLTYNVKIFYSGANIDELITFLIDHIQSSEDELKMPCLGLLANLCRHNLSVQTHIKTLSNVKSFYRTLITLLAHSSLTVVVFALSILSSLTLNEEVGEKLFHARNIHQTFQLIFNILINGDGTLTRKYSVDLLMDLLKNPKIADYLTRYEHFSSCLHQVLGLLNGKDPDSSSKVLELLLAFCSVTQLRHMLTQMMFEQSPPGSATLGSHTKCLEPTVALLRWLSQPLDGSENCSVLALELFKEIFEDVIDAANCSSADRFVTLLLPTILDQLQFTEQNLDEALTRKKCERIAKAIEVLLTLCGDDTLKMHIAKILTTVKCTTLIEQQFTYGKIDLGFGTKVADSELCKLAADVILKTLDLINKLKPLVPGMEVSFYKILQDPRLITPLAFALTSDNREQVQSGLRILLEAAPLPDFPALVLGESIAANNAYRQQETEHIPRKMPWQSSNHSFPTSIKCLTPHLKDGVPGLNIEELIEKLQSGMVVKDQICDVRISDIMDVYEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMIAMIHSLSGGKINPETVNLSI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDSTACLK -------CCHHHHHH	9.18	19413330
3	Phosphorylation	-----MDSTACLKSL -----CCHHHHHHHH	19.33	30631047
4	Phosphorylation	----MDSTACLKSLL ----CCHHHHHHHHH	19.68	30631047
8	Ubiquitination	MDSTACLKSLLLTVS CCHHHHHHHHHHHHH	38.65	-
9	Phosphorylation	DSTACLKSLLLTVSQ CHHHHHHHHHHHHHH	15.99	21406692
13	Phosphorylation	CLKSLLLTVSQYKAV HHHHHHHHHHHHHHH	20.34	21406692
15	Phosphorylation	KSLLLTVSQYKAVKS HHHHHHHHHHHHHHC	23.66	21406692
17	Phosphorylation	LLLTVSQYKAVKSEA HHHHHHHHHHHHCCC	8.07	21406692
18	Ubiquitination	LLTVSQYKAVKSEAN HHHHHHHHHHHCCCC	38.78	29967540
21	Acetylation	VSQYKAVKSEANATQ HHHHHHHHCCCCHHH	47.65	25953088
21	Ubiquitination	VSQYKAVKSEANATQ HHHHHHHHCCCCHHH	47.65	27667366
40	Malonylation	LEVISGQKLTRLFTS HHHHCCCCHHHHHCC	56.18	26320211
40 (in isoform 1)	Ubiquitination	-	56.18	21906983
40	Ubiquitination	LEVISGQKLTRLFTS HHHHCCCCHHHHHCC	56.18	27667366
40	Acetylation	LEVISGQKLTRLFTS HHHHCCCCHHHHHCC	56.18	23236377
92	S-nitrosylation	VDIETRDCLQNTYNL CCCCHHHHHHHCCCC	3.67	19483679
92	S-nitrosocysteine	VDIETRDCLQNTYNL CCCCHHHHHHHCCCC	3.67	-
108	S-nitrosylation	SVLAGVVCRSSHTDS HHHHHHHHCCCCCCH	3.03	19483679
108	S-nitrosocysteine	SVLAGVVCRSSHTDS HHHHHHHHCCCCCCH	3.03	-
234	Phosphorylation	HARNIHQTFQLIFNI HHCCHHHHHHHHHHH	10.13	-
248	Phosphorylation	ILINGDGTLTRKYSV HHHCCCCCCCEEHHH	29.69	-
250	Phosphorylation	INGDGTLTRKYSVDL HCCCCCCCEEHHHHH	25.59	-
253	Phosphorylation	DGTLTRKYSVDLLMD CCCCCEEHHHHHHHH	15.61	-
275	Ubiquitination	ADYLTRYEHFSSCLH HHHHHHHHHHHHHHH	34.86	22505724
297	Ubiquitination	GKDPDSSSKVLELLL CCCCCCHHHHHHHHH	30.64	22505724
315	Ubiquitination	SVTQLRHMLTQMMFE HHHHHHHHHHHHHHH	3.33	22817900
322	Ubiquitination	MLTQMMFEQSPPGSA HHHHHHHHCCCCCCC	32.05	27667366
333	Ubiquitination	PGSATLGSHTKCLEP CCCCCCCCCCCCCHH	30.97	21963094
402	Ubiquitination	DQLQFTEQNLDEALT HHHHHHHCCHHHHHH	53.37	22053931
409	Phosphorylation	QNLDEALTRKKCERI CCHHHHHHHHHHHHH	47.71	20071362
430	Ubiquitination	LLTLCGDDTLKMHIA HHHHHCCHHHHHHHH	38.94	22505724
438	Ubiquitination	TLKMHIAKILTTVKC HHHHHHHHHHHHHCC	37.33	29967540
441	Phosphorylation	MHIAKILTTVKCTTL HHHHHHHHHHCCCHH	32.77	-
442	Phosphorylation	HIAKILTTVKCTTLI HHHHHHHHHCCCHHH	17.96	-
452	Ubiquitination	CTTLIEQQFTYGKID CCHHHHHHCCCCEEE	21.62	22505724
465	Ubiquitination	IDLGFGTKVADSELC EEECCCCCCCCHHHH	35.49	29967540
470 (in isoform 2)	Ubiquitination	-	59.75	21906983
470	Ubiquitination	GTKVADSELCKLAAD CCCCCCHHHHHHHHH	59.75	22817900
473	Ubiquitination	VADSELCKLAADVIL CCCHHHHHHHHHHHH	54.51	29967540
474	Ubiquitination	ADSELCKLAADVILK CCHHHHHHHHHHHHH	4.66	24816145
477	Ubiquitination	ELCKLAADVILKTLD HHHHHHHHHHHHHHH	23.53	27667366
488	Ubiquitination	KTLDLINKLKPLVPG HHHHHHHHHCCCCCC	51.39	21963094
488 (in isoform 2)	Ubiquitination	-	51.39	21906983
502	Ubiquitination	GMEVSFYKILQDPRL CCEEEHHHHHCCCCC	34.62	-
557	Ubiquitination	IAANNAYRQQETEHI HHHCCHHHHHCCCCC	29.33	22053931
567	Ubiquitination	ETEHIPRKMPWQSSN CCCCCCCCCCCCCCC	43.91	29967540
572	Phosphorylation	PRKMPWQSSNHSFPT CCCCCCCCCCCCCCC	29.28	25159151
573	Phosphorylation	RKMPWQSSNHSFPTS CCCCCCCCCCCCCCC	24.38	25159151
576	Phosphorylation	PWQSSNHSFPTSIKC CCCCCCCCCCCCCHH	36.85	27732954
582	Ubiquitination	HSFPTSIKCLTPHLK CCCCCCCHHCCCHHH	23.98	29967540
585	Phosphorylation	PTSIKCLTPHLKDGV CCCCHHCCCHHHCCC	20.38	23312004
588	Ubiquitination	IKCLTPHLKDGVPGL CHHCCCHHHCCCCCC	5.95	22505724
589	Ubiquitination	KCLTPHLKDGVPGLN HHCCCHHHCCCCCCC	49.77	22505724
603	Ubiquitination	NIEELIEKLQSGMVV CHHHHHHHHHCCCCC	44.85	29967540
610	Ubiquitination	KLQSGMVVKDQICDV HHHCCCCCCCCCCCE	4.14	22505724
611	Ubiquitination	LQSGMVVKDQICDVR HHCCCCCCCCCCCEE	32.29	32015554
626	Phosphorylation	ISDIMDVYEMKLSTL HHHHHHHHHHHHHHH	13.17	-
628	Ubiquitination	DIMDVYEMKLSTLAS HHHHHHHHHHHHHCC	2.64	22817900
629 (in isoform 1)	Ubiquitination	-	27.61	21906983
629	Ubiquitination	IMDVYEMKLSTLASK HHHHHHHHHHHHCCC	27.61	21906983
635	Ubiquitination	MKLSTLASKESRLQD HHHHHHCCCHHHHHH	39.82	27667366
636	Ubiquitination	KLSTLASKESRLQDL HHHHHCCCHHHHHHH	54.85	27667366
638	Phosphorylation	STLASKESRLQDLLE HHHCCCHHHHHHHHH	41.86	-
646	Ubiquitination	RLQDLLETKALALAQ HHHHHHHHHHHHHHH	22.91	21963094
647 (in isoform 1)	Ubiquitination	-	31.84	21906983
647	Ubiquitination	LQDLLETKALALAQA HHHHHHHHHHHHHHH	31.84	21963094
656	Methylation	LALAQADRLIAQHRC HHHHHHHHHHHHHHH	30.89	-
685	Ubiquitination	MLREVERKNEELSVL HHHHHHHHHHHHHHH	56.03	29967540
694	Ubiquitination	EELSVLLKAQQVESE HHHHHHHHHHHHHHH	39.73	29967540
715	Ubiquitination	EHLFQHNRKLESVAE HHHHHHCHHHHHHHH	42.69	22053931
716	Ubiquitination	HLFQHNRKLESVAEE HHHHHCHHHHHHHHH	63.02	22053931
719	Phosphorylation	QHNRKLESVAEEHEI HHCHHHHHHHHHHHH	36.74	28555341
729	Ubiquitination	EEHEILTKSYMELLQ HHHHHHHHHHHHHHH	35.82	29967540
740	Phosphorylation	ELLQRNESTEKKNKD HHHHCCCCHHHHHCC	45.47	22210691
741	Phosphorylation	LLQRNESTEKKNKDL HHHCCCCHHHHHCCC	45.72	22210691
746	Ubiquitination	ESTEKKNKDLQITCD CCHHHHHCCCHHHHH	69.56	-
751	Phosphorylation	KNKDLQITCDSLNKQ HHCCCHHHHHHHHHH	9.41	20873877
754	Phosphorylation	DLQITCDSLNKQIET CCHHHHHHHHHHHHH	35.67	20873877
761	Phosphorylation	SLNKQIETVKKLNES HHHHHHHHHHHHHHH	38.97	17192257
764	Acetylation	KQIETVKKLNESLKE HHHHHHHHHHHHHHH	52.81	7822405
775	Ubiquitination	SLKEQNEKSIAQLIE HHHHHHHHHHHHHHH	55.50	29967540
783	Ubiquitination	SIAQLIEKEEQRKEV HHHHHHHHHHHHHHH	60.60	29967540
787	Ubiquitination	LIEKEEQRKEVQNQL HHHHHHHHHHHHHHH	40.14	24816145
788	Ubiquitination	IEKEEQRKEVQNQLV HHHHHHHHHHHHHHH	63.03	24816145
800	Ubiquitination	QLVDREHKLANLHQK HHHHHHHHHHHHHHH	44.54	29967540
820	Acetylation	EKIKTLQKEREDKEE HHHHHHHHHHCCHHH	62.95	20167786
828	Phosphorylation	EREDKEETIDILRKE HHCCHHHHHHHHHHH	25.66	24719451
847	Phosphorylation	EQIRKELSIKASSLE HHHHHHHHHHHHHHH	24.12	23401153
857	Ubiquitination	ASSLEVQKAQLEGRL HHHHHHHHHHHCCCH	43.19	29967540
872	Ubiquitination	EEKESLVKLQQEELN HHHHHHHHHHHHHHH	45.96	32015554
890	Phosphorylation	HMIAMIHSLSGGKIN HHHHHHHHHHCCCCC	17.19	29449344
892	Phosphorylation	IAMIHSLSGGKINPE HHHHHHHHCCCCCHH	48.81	29449344
900	Phosphorylation	GGKINPETVNLSI-- CCCCCHHHCCCCC--	18.89	27251275
904	Phosphorylation	NPETVNLSI------ CHHHCCCCC------	22.50	25159151

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
904	S	Phosphorylation	Kinase	PLK1	P53350	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:24293411

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CIP2A_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 CIP2A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
2AAA_HUMAN	PPP2R1A	physical	17632056
MYC_HUMAN	MYC	physical	17632056
EGFR_HUMAN	EGFR	physical	23956138
CHIP_HUMAN	STUB1	physical	24293411
STOM_HUMAN	STOM	physical	27173435

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 CIP2A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-761 AND SER-904, ANDMASS SPECTROMETRY.	18691976 [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-904, AND MASSSPECTROMETRY.	16964243 [Abstract]