dbPTM

PTN12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTN12_HUMAN
UniProt AC	Q05209
Protein Name	Tyrosine-protein phosphatase non-receptor type 12
Gene Name	PTPN12
Organism	Homo sapiens (Human).
Sequence Length	780
Subcellular Localization	Cytoplasm . Cell junction, focal adhesion . Cell projection, podosome . Partial translocation to focal adhesion sites may be mediated by interaction with SORBS2.
Protein Description	Dephosphorylates a range of proteins, and thereby regulates cellular signaling cascades. [PubMed: 18559503 Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2]
Protein Sequence	MEQVEILRKFIQRVQAMKSPDHNGEDNFARDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQLQLYEIHGAQKIADGVNEINTENMVSSIEPEKQDSPPPKPPRTRSCLVEGDAKEEILQPPEPHPVPPILTPSPPSAFPTVTTVWQDNDRYHPKPVLHMVSSEQHSADLNRNYSKSTELPGKNESTIEQIDKKLERNLSFEIKKVPLQEGPKSFDGNTLLNRGHAIKIKSASPCIADKISKPQELSSDLNVGDTSQNSCVDCSVTQSNKVSVTPPEESQNSDTPPRPDRLPLDEKGHVTWSFHGPENAIPIPDLSEGNSSDINYQTRKTVSLTPSPTTQVETPDLVDHDNTSPLFRTPLSFTNPLHSDDSDSDERNSDGAVTQNKTNISTASATVSAATSTESISTRKVLPMSIARHNIAGTTHSGAEKDVDVSEDSPPPLPERTPESFVLASEHNTPVRSEWSELQSQERSEQKKSEGLITSENEKCDHPAGGIHYEMCIECPPTFSDKREQISENPTEATDIGFGNRCGKPKGPRDPPSEWT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEQVEILR -------CHHHHHHH	7.99	22223895
19	Phosphorylation	QRVQAMKSPDHNGED HHHHHHCCCCCCCCC	23.60	29255136
39	Phosphorylation	FMRLRRLSTKYRTEK HHHHHHHHHHHCCCE	22.50	20068231
40	Phosphorylation	MRLRRLSTKYRTEKI HHHHHHHHHHCCCEE	36.37	20068231
42	Phosphorylation	LRRLSTKYRTEKIYP HHHHHHHHCCCEECC	23.90	20068231
48	Phosphorylation	KYRTEKIYPTATGEK HHCCCEECCCCCCCC	12.95	28674419
64	Phosphorylation	ENVKKNRYKDILPFD HHHCCCCCCCCCCCC	23.54	28152594
65	Malonylation	NVKKNRYKDILPFDH HHCCCCCCCCCCCCC	34.75	26320211
73	Phosphorylation	DILPFDHSRVKLTLK CCCCCCCCEEEEEEE	40.38	28857561
78	Phosphorylation	DHSRVKLTLKTPSQD CCCEEEEEEECCCCC	22.08	24719451
81	Phosphorylation	RVKLTLKTPSQDSDY EEEEEEECCCCCCCC	31.14	29978859
83	Phosphorylation	KLTLKTPSQDSDYIN EEEEECCCCCCCCCC	52.42	28258704
86	Phosphorylation	LKTPSQDSDYINANF EECCCCCCCCCCCCE	25.36	29978859
88	Phosphorylation	TPSQDSDYINANFIK CCCCCCCCCCCCEEC	10.46	30624053
95	Ubiquitination	YINANFIKGVYGPKA CCCCCEECCCCCCCE	37.88	-
146	Phosphorylation	GRKKCERYWPLYGED CHHHHHHHCCCCCCC	6.78	28270605
150	Phosphorylation	CERYWPLYGEDPITF HHHHCCCCCCCCCEE	17.87	28270605
156	Phosphorylation	LYGEDPITFAPFKIS CCCCCCCEECCEEEE	21.09	28270605
163	Phosphorylation	TFAPFKISCEDEQAR EECCEEEECCCHHHH	16.43	28270605
186	Phosphorylation	LLEFQNESRRLYQFH HHHHCCCCCCEEEEE	30.19	21082442
271	Phosphorylation	NLIQEMRTQRHSAVQ HHHHHHHHHCCCCCC	28.75	24719451
280	Ubiquitination	RHSAVQTKEQYELVH CCCCCCCHHHHHHHH	26.23	-
301	Phosphorylation	FEKQLQLYEIHGAQK HHHHHHHHHHCCHHH	10.40	25394399
318	Phosphorylation	DGVNEINTENMVSSI CCCCCCCCCCCHHCC	34.10	29255136
323	Phosphorylation	INTENMVSSIEPEKQ CCCCCCHHCCCCCCC	18.15	29255136
324	Phosphorylation	NTENMVSSIEPEKQD CCCCCHHCCCCCCCC	21.40	30266825
332	Phosphorylation	IEPEKQDSPPPKPPR CCCCCCCCCCCCCCC	36.49	30266825
340	Phosphorylation	PPPKPPRTRSCLVEG CCCCCCCCCEEEEEC	32.48	23090842
342	Phosphorylation	PKPPRTRSCLVEGDA CCCCCCCEEEEECCC	15.93	29255136
367	Phosphorylation	HPVPPILTPSPPSAF CCCCCCCCCCCCCCC	23.57	23663014
369	Phosphorylation	VPPILTPSPPSAFPT CCCCCCCCCCCCCCC	44.18	23663014
372	Phosphorylation	ILTPSPPSAFPTVTT CCCCCCCCCCCCEEE	46.02	23663014
376	Phosphorylation	SPPSAFPTVTTVWQD CCCCCCCCEEEEEEC	24.83	23663014
378	Phosphorylation	PSAFPTVTTVWQDND CCCCCCEEEEEECCC	20.36	23663014
379	Phosphorylation	SAFPTVTTVWQDNDR CCCCCEEEEEECCCC	18.53	23663014
397	Phosphorylation	KPVLHMVSSEQHSAD CCEEEECCCHHHCHH	22.15	25850435
398	Phosphorylation	PVLHMVSSEQHSADL CEEEECCCHHHCHHH	29.84	25850435
402	Phosphorylation	MVSSEQHSADLNRNY ECCCHHHCHHHCCCC	24.15	25850435
412	Phosphorylation	LNRNYSKSTELPGKN HCCCCCCCCCCCCCC	22.60	28102081
413	Phosphorylation	NRNYSKSTELPGKNE CCCCCCCCCCCCCCH	45.32	28102081
421	Phosphorylation	ELPGKNESTIEQIDK CCCCCCHHHHHHHHH	44.04	21815630
422	Phosphorylation	LPGKNESTIEQIDKK CCCCCHHHHHHHHHH	23.50	28555341
435	Phosphorylation	KKLERNLSFEIKKVP HHHHHHCCEEEEECC	25.12	22167270
449	Phosphorylation	PLQEGPKSFDGNTLL CCCCCCCCCCCCCCC	31.53	29255136
454	Phosphorylation	PKSFDGNTLLNRGHA CCCCCCCCCCCCCCC	37.85	29255136
466	Phosphorylation	GHAIKIKSASPCIAD CCCEEEECCCCCCHH	37.14	21815630
468	Phosphorylation	AIKIKSASPCIADKI CEEEECCCCCCHHHC	27.65	25159151
490	Phosphorylation	SDLNVGDTSQNSCVD CCCCCCCCCCCCCEE	26.70	25159151
491	Phosphorylation	DLNVGDTSQNSCVDC CCCCCCCCCCCCEEC	31.91	25159151
494	Phosphorylation	VGDTSQNSCVDCSVT CCCCCCCCCEECEEC	14.10	21712546
501	Phosphorylation	SCVDCSVTQSNKVSV CCEECEECCCCCEEC	15.24	28985074
507	Phosphorylation	VTQSNKVSVTPPEES ECCCCCEECCCCHHH	23.14	30266825
509	Phosphorylation	QSNKVSVTPPEESQN CCCCEECCCCHHHCC	26.14	23401153
514	Phosphorylation	SVTPPEESQNSDTPP ECCCCHHHCCCCCCC	32.76	23401153
517	Phosphorylation	PPEESQNSDTPPRPD CCHHHCCCCCCCCCC	34.91	30266825
519	Phosphorylation	EESQNSDTPPRPDRL HHHCCCCCCCCCCCC	34.71	30266825
535	Phosphorylation	LDEKGHVTWSFHGPE CCCCCCEEEEEECCC	15.09	27251275
537	Phosphorylation	EKGHVTWSFHGPENA CCCCEEEEEECCCCC	9.67	27251275
551	Phosphorylation	AIPIPDLSEGNSSDI CEECCCCCCCCCCCC	51.33	28450419
555	Phosphorylation	PDLSEGNSSDINYQT CCCCCCCCCCCCCEE	40.00	28450419
556	Phosphorylation	DLSEGNSSDINYQTR CCCCCCCCCCCCEEC	46.65	28450419
560	Phosphorylation	GNSSDINYQTRKTVS CCCCCCCCEECCEEE	16.17	28450419
562	Phosphorylation	SSDINYQTRKTVSLT CCCCCCEECCEEECC	24.63	28450419
565	Phosphorylation	INYQTRKTVSLTPSP CCCEECCEEECCCCC	16.43	30266825
567	Phosphorylation	YQTRKTVSLTPSPTT CEECCEEECCCCCCC	31.58	30266825
569	Phosphorylation	TRKTVSLTPSPTTQV ECCEEECCCCCCCCC	17.76	29255136
571	Phosphorylation	KTVSLTPSPTTQVET CEEECCCCCCCCCCC	29.64	29255136
573	Phosphorylation	VSLTPSPTTQVETPD EECCCCCCCCCCCCC	33.91	30266825
574	Phosphorylation	SLTPSPTTQVETPDL ECCCCCCCCCCCCCC	33.72	30266825
578	Phosphorylation	SPTTQVETPDLVDHD CCCCCCCCCCCCCCC	24.20	30266825
587	Phosphorylation	DLVDHDNTSPLFRTP CCCCCCCCCCCCCCC	37.47	23401153
588	Phosphorylation	LVDHDNTSPLFRTPL CCCCCCCCCCCCCCC	26.34	29255136
593	Phosphorylation	NTSPLFRTPLSFTNP CCCCCCCCCCCCCCC	22.65	23927012
596	Phosphorylation	PLFRTPLSFTNPLHS CCCCCCCCCCCCCCC	31.09	23927012
598	Phosphorylation	FRTPLSFTNPLHSDD CCCCCCCCCCCCCCC	32.33	30266825
603	Phosphorylation	SFTNPLHSDDSDSDE CCCCCCCCCCCCCCC	51.28	29255136
606	Phosphorylation	NPLHSDDSDSDERNS CCCCCCCCCCCCCCC	43.96	29255136
608	Phosphorylation	LHSDDSDSDERNSDG CCCCCCCCCCCCCCC	45.37	29255136
613	Phosphorylation	SDSDERNSDGAVTQN CCCCCCCCCCCCCCC	43.58	30278072
618	Phosphorylation	RNSDGAVTQNKTNIS CCCCCCCCCCCCCCC	26.37	23927012
622	Phosphorylation	GAVTQNKTNISTASA CCCCCCCCCCCCCEE	45.38	23312004
625	Phosphorylation	TQNKTNISTASATVS CCCCCCCCCCEEEEE	21.71	28060719
626	Phosphorylation	QNKTNISTASATVSA CCCCCCCCCEEEEEC	22.34	28060719
628	Phosphorylation	KTNISTASATVSAAT CCCCCCCEEEEECCC	25.26	28270605
630	Phosphorylation	NISTASATVSAATST CCCCCEEEEECCCCC	16.70	28270605
632	Phosphorylation	STASATVSAATSTES CCCEEEEECCCCCCC	14.08	28060719
635	Phosphorylation	SATVSAATSTESIST EEEEECCCCCCCCCC	35.58	28985074
636	Phosphorylation	ATVSAATSTESISTR EEEECCCCCCCCCCC	26.00	28060719
637	Phosphorylation	TVSAATSTESISTRK EEECCCCCCCCCCCC	29.42	25849741
639	Phosphorylation	SAATSTESISTRKVL ECCCCCCCCCCCCEE	23.17	28270605
641	Phosphorylation	ATSTESISTRKVLPM CCCCCCCCCCCEEEC	31.29	25159151
642	Phosphorylation	TSTESISTRKVLPMS CCCCCCCCCCEEECC	32.60	28270605
649	Phosphorylation	TRKVLPMSIARHNIA CCCEEECCHHHCCCC	15.91	26434776
658	Phosphorylation	ARHNIAGTTHSGAEK HHCCCCCCCCCCCCC	16.59	23927012
659	Phosphorylation	RHNIAGTTHSGAEKD HCCCCCCCCCCCCCC	17.08	23927012
661	Phosphorylation	NIAGTTHSGAEKDVD CCCCCCCCCCCCCCC	37.29	23927012
670	Phosphorylation	AEKDVDVSEDSPPPL CCCCCCCCCCCCCCC	31.09	30266825
673	Phosphorylation	DVDVSEDSPPPLPER CCCCCCCCCCCCCCC	34.94	19664994
681	Phosphorylation	PPPLPERTPESFVLA CCCCCCCCCCCEEEE	29.73	21815630
684	Phosphorylation	LPERTPESFVLASEH CCCCCCCCEEEECCC	23.12	22199227
689	Phosphorylation	PESFVLASEHNTPVR CCCEEEECCCCCCCH	34.92	25159151
693	Phosphorylation	VLASEHNTPVRSEWS EEECCCCCCCHHHHH	25.68	25159151
697	Phosphorylation	EHNTPVRSEWSELQS CCCCCCHHHHHHHHH	43.59	25627689
700	Phosphorylation	TPVRSEWSELQSQER CCCHHHHHHHHHHHH	25.11	25627689
704	Phosphorylation	SEWSELQSQERSEQK HHHHHHHHHHHHHHH	46.78	25627689
708	Phosphorylation	ELQSQERSEQKKSEG HHHHHHHHHHHHHCC	43.56	25159151
713	Phosphorylation	ERSEQKKSEGLITSE HHHHHHHHCCCCCCC	43.88	21815630
718	Phosphorylation	KKSEGLITSENEKCD HHHCCCCCCCCCCCC	34.72	30108239
719	Phosphorylation	KSEGLITSENEKCDH HHCCCCCCCCCCCCC	31.28	23403867
733	Phosphorylation	HPAGGIHYEMCIECP CCCCCCCEEEEEECC	11.93	29978859
780	Phosphorylation	RDPPSEWT------- CCCCCCCC-------	25.36	22199227

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
19	S	Phosphorylation	Kinase	CDK2	P24941	PSP
39	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
39	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
39	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
39	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
39	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
39	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
435	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
435	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
435	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
435	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
435	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
435	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
571	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
571	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PTN12_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 PTN12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPIP1_HUMAN	PSTPIP1	physical	9422760
SHC1_HUMAN	SHC1	physical	7929214
PAXI_HUMAN	PXN	physical	10625692
BCAR1_HUMAN	BCAR1	physical	9285683
SHC1_HUMAN	SHC1	physical	8626541
BCAR1_HUMAN	BCAR1	physical	9748319
TGFI1_HUMAN	TGFB1I1	physical	10092676
GRB2_HUMAN	GRB2	physical	9135065
BCAR1_HUMAN	BCAR1	physical	8887669
PAXI_HUMAN	PXN	physical	9497381
FAK2_HUMAN	PTK2B	physical	11337490
SRBS2_HUMAN	SORBS2	physical	18559503
WASF1_HUMAN	WASF1	physical	18559503
A4_HUMAN	APP	physical	21832049
STX16_HUMAN	STX16	physical	15231748
GLHA_HUMAN	CGA	physical	15231748
CSH1_HUMAN	CSH1	physical	15231748
CSH2_HUMAN	CSH1	physical	15231748
BAG6_HUMAN	BAG6	physical	15231748
UTRO_HUMAN	UTRN	physical	15231748
PSG9_HUMAN	PSG9	physical	15231748
ZFP2_HUMAN	ZFP2	physical	15231748
IFT20_HUMAN	IFT20	physical	15231748
THAP2_HUMAN	THAP2	physical	15231748
TEX10_HUMAN	TEX10	physical	15231748
RBM19_HUMAN	RBM19	physical	15231748
ANS1A_HUMAN	ANKS1A	physical	22863883
EPN1_HUMAN	EPN1	physical	22863883
NUSAP_HUMAN	NUSAP1	physical	22863883
PACN2_HUMAN	PACSIN2	physical	22863883
PLOD2_HUMAN	PLOD2	physical	22863883
UGPA_HUMAN	UGP2	physical	22863883
VASN_HUMAN	VASN	physical	22863883
PPIP2_HUMAN	PSTPIP2	physical	27880917
SHC1_HUMAN	SHC1	physical	27880917
RHG10_HUMAN	ARHGAP10	physical	27880917
BCAR1_HUMAN	BCAR1	physical	27880917
ASAP1_HUMAN	ASAP1	physical	27880917
NCK2_HUMAN	NCK2	physical	27880917
PAXI_HUMAN	PXN	physical	27880917
CSK_HUMAN	CSK	physical	27880917
PPIP2_HUMAN	PSTPIP2	physical	28514442
PAXI_HUMAN	PXN	physical	28514442
SHC1_HUMAN	SHC1	physical	28514442
AIFM1_HUMAN	AIFM1	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 PTN12_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 1-8, AND ACETYLATION AT MET-1.	12665801 [Abstract]
Phosphorylation
Reference	PubMed
"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-332; SER-435; SER-468;SER-514; THR-519; SER-571; SER-588; SER-603; SER-606; SER-608;SER-613; SER-689 AND THR-693, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689 AND THR-693, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-569; SER-571; SER-603;SER-606 AND SER-673, AND MASS SPECTROMETRY.	18088087 [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-673, 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-332; SER-603 ANDSER-606, AND MASS SPECTROMETRY.	17081983 [Abstract]