dbPTM

PP12C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PP12C_HUMAN
UniProt AC	Q9BZL4
Protein Name	Protein phosphatase 1 regulatory subunit 12C
Gene Name	PPP1R12C {ECO:0000312\|HGNC:HGNC:14947}
Organism	Homo sapiens (Human).
Sequence Length	782
Subcellular Localization	Cytoplasm . Along actomyosin filaments and stress fibers.
Protein Description	Regulates myosin phosphatase activity..
Protein Sequence	MSGEDGPAAGPGAAAAAARERRREQLRQWGARAGAEPGPGERRARTVRFERAAEFLAACAGGDLDEARLMLRAADPGPGAELDPAAPPPARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESDAMEGLLKAEIARRGVDVEAAKRAEEELLLHDTRCWLNGGAMPEARHPRTGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLADEEVLSLLEELARKQEDLRNQKEASQSRGQEPQAPSSSKHRRSSVCRLSSREKISLQDLSKERRPGGAGGPPIQDEDEGEEGPTEPPPAEPRTLNGVSSPPHPSPKSPVQLEEAPFSRRFGLLKTGSSGALGPPERRTAEGAPGAGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEPSVLSEVTKPPPCLENSSPPSRIPEPESPAKPNVPTASTAPPADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKAPESEKPAQSLDPSRRPRVPGVENSDSPAQRAEAPDGQGPGPQAAREHRKVGKEWRGPAEGEEAEPADRSQESSTLEGGPSARRQRWQRDLNPEPEPESEEPDGGFRTLYAELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPALLELERFERRALERKAAELEEELKALSDLRADNQRLKDENAALIRVISKLSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGEDGPAA ------CCCCCCCCC	51.38	26434776
2	Acetylation	------MSGEDGPAA ------CCCCCCCCC	51.38	22814378
46	Phosphorylation	PGERRARTVRFERAA CCCCHHHEHHHHHHH	18.30	-
198	Ubiquitination	GVDVEAAKRAEEELL CCCHHHHHHHHHHHH	60.22	29967540
226	O-linked_Glycosylation	PEARHPRTGASALHV CCCCCCCCCCHHHHH	41.36	30620550
239	Phosphorylation	HVAAAKGYIEVMRLL HHHHHCHHHHHHHHH	8.00	-
288	Phosphorylation	EHGGGMDSLTHAGQR HCCCCHHHHCCCCCC	26.69	21406692
290	Phosphorylation	GGGMDSLTHAGQRPC CCCHHHHCCCCCCCC	17.40	21406692
325	Phosphorylation	LRNQKEASQSRGQEP HHHHHHHHHHCCCCC	29.76	25159151
336	Phosphorylation	GQEPQAPSSSKHRRS CCCCCCCCCCHHCCH	50.70	25159151
337	Phosphorylation	QEPQAPSSSKHRRSS CCCCCCCCCHHCCHH	42.20	-
338	Phosphorylation	EPQAPSSSKHRRSSV CCCCCCCCHHCCHHC	36.50	25627689
343	Phosphorylation	SSSKHRRSSVCRLSS CCCHHCCHHCHHHHC	27.38	23882029
344	Phosphorylation	SSKHRRSSVCRLSSR CCHHCCHHCHHHHCC	24.35	22798277
355	Phosphorylation	LSSREKISLQDLSKE HHCCCCCCHHHHHHC	30.92	28555341
361	Ubiquitination	ISLQDLSKERRPGGA CCHHHHHHCCCCCCC	63.64	29967540
393	Phosphorylation	PPPAEPRTLNGVSSP CCCCCCCCCCCCCCC	34.98	23186163
398 (in isoform 3)	Phosphorylation	-	38.23	24114839
398	Phosphorylation	PRTLNGVSSPPHPSP CCCCCCCCCCCCCCC	38.23	25159151
399	Phosphorylation	RTLNGVSSPPHPSPK CCCCCCCCCCCCCCC	39.79	25159151
399 (in isoform 3)	Phosphorylation	-	39.79	25849741
404	Phosphorylation	VSSPPHPSPKSPVQL CCCCCCCCCCCCCCC	41.76	28450419
404 (in isoform 3)	Phosphorylation	-	41.76	28450419
407	Phosphorylation	PPHPSPKSPVQLEEA CCCCCCCCCCCCCCC	33.42	23401153
407 (in isoform 3)	Phosphorylation	-	33.42	25159151
416 (in isoform 3)	Phosphorylation	-	13.14	28450419
417	Phosphorylation	QLEEAPFSRRFGLLK CCCCCCCCHHCCCCC	22.84	28450419
425	Phosphorylation	RRFGLLKTGSSGALG HHCCCCCCCCCCCCC	42.12	29255136
427	Phosphorylation	FGLLKTGSSGALGPP CCCCCCCCCCCCCCC	30.72	23401153
428	Phosphorylation	GLLKTGSSGALGPPE CCCCCCCCCCCCCCC	29.45	29255136
438	Phosphorylation	LGPPERRTAEGAPGA CCCCCCCCCCCCCCC	34.97	26074081
450	Phosphorylation	PGAGLQRSASSSWLE CCCCCCCCCCCCCCC	21.39	30266825
451	Phosphorylation	GAGLQRSASSSWLEG CCCCCCCCCCCCCCC	18.67	32645325
452	Phosphorylation	AGLQRSASSSWLEGT CCCCCCCCCCCCCCC	26.59	22167270
453	Phosphorylation	GLQRSASSSWLEGTS CCCCCCCCCCCCCCC	25.83	30266825
454	Phosphorylation	LQRSASSSWLEGTST CCCCCCCCCCCCCCH	32.93	30266825
459	Phosphorylation	SSSWLEGTSTQAKEL CCCCCCCCCHHHHHH	21.16	23403867
460	Phosphorylation	SSWLEGTSTQAKELR CCCCCCCCHHHHHHH	29.40	23403867
461	Phosphorylation	SWLEGTSTQAKELRL CCCCCCCHHHHHHHH	32.17	23403867
472	Phosphorylation	ELRLARITPTPSPKL HHHHCCCCCCCCCCC	18.63	29396449
474	Phosphorylation	RLARITPTPSPKLPE HHCCCCCCCCCCCCC	27.96	29396449
476	Phosphorylation	ARITPTPSPKLPEPS CCCCCCCCCCCCCCC	36.83	22985185
483	Phosphorylation	SPKLPEPSVLSEVTK CCCCCCCCHHCCCCC	33.75	28270605
486	Phosphorylation	LPEPSVLSEVTKPPP CCCCCHHCCCCCCCC	28.06	30206219
489	Phosphorylation	PSVLSEVTKPPPCLE CCHHCCCCCCCCCCC	33.51	22167270
498	Phosphorylation	PPPCLENSSPPSRIP CCCCCCCCCCCCCCC	34.54	22167270
499	Phosphorylation	PPCLENSSPPSRIPE CCCCCCCCCCCCCCC	53.03	22167270
502	Phosphorylation	LENSSPPSRIPEPES CCCCCCCCCCCCCCC	46.34	23663014
509	Phosphorylation	SRIPEPESPAKPNVP CCCCCCCCCCCCCCC	40.65	23401153
517	Phosphorylation	PAKPNVPTASTAPPA CCCCCCCCCCCCCCC	29.02	30266825
519	Phosphorylation	KPNVPTASTAPPADS CCCCCCCCCCCCCCC	27.81	25850435
520	Phosphorylation	PNVPTASTAPPADSR CCCCCCCCCCCCCCC	40.49	25850435
526	Phosphorylation	STAPPADSRDRRRSY CCCCCCCCCCCHHHC	37.88	25850435
530 (in isoform 5)	Phosphorylation	-	35.86	25159151
532	Phosphorylation	DSRDRRRSYQMPVRD CCCCCHHHCCCCCCC	20.22	26657352
533	Phosphorylation	SRDRRRSYQMPVRDE CCCCHHHCCCCCCCC	13.66	27134283
542	Phosphorylation	MPVRDEESESQRKAR CCCCCCCCHHHHHHH	40.26	28555341
544	Phosphorylation	VRDEESESQRKARSR CCCCCCHHHHHHHHH	44.56	-
556	Phosphorylation	RSRLMRQSRRSTQGV HHHHHHHHHHHCCCC	21.21	-
559	Phosphorylation	LMRQSRRSTQGVTLT HHHHHHHHCCCCCHH	24.79	29255136
560	Phosphorylation	MRQSRRSTQGVTLTD HHHHHHHCCCCCHHH	27.77	29255136
564	Phosphorylation	RRSTQGVTLTDLKEA HHHCCCCCHHHHHHH	30.66	29255136
566	Phosphorylation	STQGVTLTDLKEAEK HCCCCCHHHHHHHHH	29.89	23403867
573	Acetylation	TDLKEAEKAAGKAPE HHHHHHHHHCCCCCC	51.05	7926107
583	Acetylation	GKAPESEKPAQSLDP CCCCCCCCCHHHCCC	55.74	7926119
602	Phosphorylation	RVPGVENSDSPAQRA CCCCCCCCCCHHHHH	26.42	29255136
603 (in isoform 3)	Phosphorylation	-	70.94	25159151
604	Phosphorylation	PGVENSDSPAQRAEA CCCCCCCCHHHHHCC	23.19	29255136
604 (in isoform 4)	Phosphorylation	-	23.19	25159151
647	Phosphorylation	EAEPADRSQESSTLE CCCCCCCCCCCCCCC	38.56	28555341
658	Phosphorylation	STLEGGPSARRQRWQ CCCCCCHHHHHHHHH	37.37	28857561
757	Phosphorylation	EEELKALSDLRADNQ HHHHHHHHHHHHHHH	39.19	24719451
781	Phosphorylation	IRVISKLSK------ HHHHHHHCC------	39.80	-

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
452	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
452	S	Phosphorylation	Kinase	PRKAA2	P54646	GPS
509	S	Phosphorylation	Kinase	CDK2	P24941	PSP
560	T	Phosphorylation	Kinase	CDC42BP	Q9Y5S2	Uniprot
560	T	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
560	T	Phosphorylation	Kinase	MRCK-SUBFAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
560	T	Phosphorylation		11399775
Phosphorylation at Thr-560 is essential for its interaction with PPP1CB.

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 PP12C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMAD3_HUMAN	SMAD3	physical	21988832
PP12C_HUMAN	PPP1R12C	physical	25416956
CA109_HUMAN	C1orf109	physical	25416956
SPF45_HUMAN	RBM17	physical	25416956

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 PP12C_HUMAN

Related Literatures of Post-Translational Modification

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-427, AND MASSSPECTROMETRY.	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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND MASSSPECTROMETRY.	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-604, AND MASSSPECTROMETRY.	18669648 [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 THR-560, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Phosphorylation of a novel myosin binding subunit of proteinphosphatase 1 reveals a conserved mechanism in the regulation of actincytoskeleton."; Tan I., Ng C.H., Lim L., Leung T.; J. Biol. Chem. 276:21209-21216(2001). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITHPPP1CB, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATIONAT THR-560.	11399775 [Abstract]

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