Q05209 (PTN12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein phosphatase non-receptor type 12
EC=3.1.3.48

Alternative name(s):
PTP-PEST
Protein-tyrosine phosphatase G1
Short name=PTPG1

Gene names

Name:

PTPN12

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	780 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2. Ref.13
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Interacts with TGFB1I1 By similarity. Interacts with PSTPIP1. Interacts with PTK2B/PYK2. Interacts with LPXN By similarity. Ref.10 Ref.13
Subcellular location	Cytoplasm. Cell projection › podosome By similarity.
Post-translational modification	Phosphorylated by STK24/MST3 and this results in inhibition of its activity. Ref.11
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class 4 subfamily. Contains 1 tyrosine-protein phosphatase domain.
Sequence caution	The sequence BAD92761.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cell junction Cell projection Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cell projection Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from direct assay. Source: HPA cytosol Inferred from electronic annotation. Source: Compara plasma membrane Inferred from direct assay. Source: HPA podosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	non-membrane spanning protein tyrosine phosphatase activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERBB2	P04626	4	EBI-2266035,EBI-641062
PDGFRB	P09619	2	EBI-2266035,EBI-641237
TEK	Q02763	2	EBI-2266035,EBI-2257090

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q05209-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q05209-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-130: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 780	780	Tyrosine-protein phosphatase non-receptor type 12		PRO_0000094771
Regions
	Domain	28 – 293	266	Tyrosine-protein phosphatase
	Region	231 – 237	7	Substrate binding By similarity
	Region	345 – 438	94	Interaction with TGFB1I1 By similarity
Sites
	Active site	231	1	Phosphocysteine intermediate By similarity
	Binding site	199	1	Substrate By similarity
	Binding site	278	1	Substrate By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.8
	Modified residue	19	1	Phosphoserine Ref.17
	Modified residue	186	1	Phosphoserine By similarity
	Modified residue	332	1	Phosphoserine Ref.16 Ref.19
	Modified residue	435	1	Phosphoserine Ref.17 Ref.19
	Modified residue	449	1	Phosphoserine Ref.17 Ref.19
	Modified residue	468	1	Phosphoserine Ref.16
	Modified residue	519	1	Phosphothreonine Ref.16
	Modified residue	567	1	Phosphoserine Ref.16
	Modified residue	569	1	Phosphothreonine Ref.16
	Modified residue	571	1	Phosphoserine Ref.16
	Modified residue	596	1	Phosphoserine By similarity
	Modified residue	598	1	Phosphothreonine By similarity
	Modified residue	603	1	Phosphoserine Ref.15 Ref.16 Ref.19
	Modified residue	606	1	Phosphoserine Ref.16 Ref.19
	Modified residue	608	1	Phosphoserine Ref.16
	Modified residue	613	1	Phosphoserine Ref.16
	Modified residue	673	1	Phosphoserine Ref.12 Ref.15 Ref.17 Ref.19
	Modified residue	689	1	Phosphoserine Ref.14 Ref.16
	Modified residue	693	1	Phosphothreonine Ref.14 Ref.16
Natural variations
	Alternative sequence	1 – 130	130	Missing in isoform 2.		VSP_046274
	Natural variant	61	1	K → R in colon cancer. Ref.9		VAR_006385
	Natural variant	322	1	V → I. Ref.1 Ref.4 Ref.5 Ref.16 Corresponds to variant rs9640663 [ dbSNP | Ensembl ].		VAR_019512
	Natural variant	573	1	T → A. Ref.4 Corresponds to variant rs3750050 [ dbSNP | Ensembl ].		VAR_020297
	Natural variant	706	1	E → K. Corresponds to variant rs2230602 [ dbSNP | Ensembl ].		VAR_057129
Experimental info
	Sequence conflict	121	1	I → V in BAA02648. Ref.1
	Sequence conflict	121	1	I → V in AAB30047. Ref.9
	Sequence conflict	612	1	N → D in BAG59344. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: 663DB3E5176FD7FD	FASTA	780	88,106
	10 20 30 40 50 60 MEQVEILRKF IQRVQAMKSP DHNGEDNFAR DFMRLRRLST KYRTEKIYPT ATGEKEENVK 70 80 90 100 110 120 KNRYKDILPF DHSRVKLTLK TPSQDSDYIN ANFIKGVYGP KAYVATQGPL ANTVIDFWRM 130 140 150 160 170 180 IWEYNVVIIV MACREFEMGR KKCERYWPLY GEDPITFAPF KISCEDEQAR TDYFIRTLLL 190 200 210 220 230 240 EFQNESRRLY QFHYVNWPDH DVPSSFDSIL DMISLMRKYQ EHEDVPICIH CSAGCGRTGA 250 260 270 280 290 300 ICAIDYTWNL LKAGKIPEEF NVFNLIQEMR TQRHSAVQTK EQYELVHRAI AQLFEKQLQL 310 320 330 340 350 360 YEIHGAQKIA DGVNEINTEN MVSSIEPEKQ DSPPPKPPRT RSCLVEGDAK EEILQPPEPH 370 380 390 400 410 420 PVPPILTPSP PSAFPTVTTV WQDNDRYHPK PVLHMVSSEQ HSADLNRNYS KSTELPGKNE 430 440 450 460 470 480 STIEQIDKKL ERNLSFEIKK VPLQEGPKSF DGNTLLNRGH AIKIKSASPC IADKISKPQE 490 500 510 520 530 540 LSSDLNVGDT SQNSCVDCSV TQSNKVSVTP PEESQNSDTP PRPDRLPLDE KGHVTWSFHG 550 560 570 580 590 600 PENAIPIPDL SEGNSSDINY QTRKTVSLTP SPTTQVETPD LVDHDNTSPL FRTPLSFTNP 610 620 630 640 650 660 LHSDDSDSDE RNSDGAVTQN KTNISTASAT VSAATSTESI STRKVLPMSI ARHNIAGTTH 670 680 690 700 710 720 SGAEKDVDVS EDSPPPLPER TPESFVLASE HNTPVRSEWS ELQSQERSEQ KKSEGLITSE 730 740 750 760 770 780 NEKCDHPAGG IHYEMCIECP PTFSDKREQI SENPTEATDI GFGNRCGKPK GPRDPPSEWT
	Isoform 2 [UniParc]. Checksum: 217EF3041B7E5EDB	FASTA	650	72,778
	10 20 30 40 50 60 MACREFEMGR KKCERYWPLY GEDPITFAPF KISCEDEQAR TDYFIRTLLL EFQNESRRLY 70 80 90 100 110 120 QFHYVNWPDH DVPSSFDSIL DMISLMRKYQ EHEDVPICIH CSAGCGRTGA ICAIDYTWNL 130 140 150 160 170 180 LKAGKIPEEF NVFNLIQEMR TQRHSAVQTK EQYELVHRAI AQLFEKQLQL YEIHGAQKIA 190 200 210 220 230 240 DGVNEINTEN MVSSIEPEKQ DSPPPKPPRT RSCLVEGDAK EEILQPPEPH PVPPILTPSP 250 260 270 280 290 300 PSAFPTVTTV WQDNDRYHPK PVLHMVSSEQ HSADLNRNYS KSTELPGKNE STIEQIDKKL 310 320 330 340 350 360 ERNLSFEIKK VPLQEGPKSF DGNTLLNRGH AIKIKSASPC IADKISKPQE LSSDLNVGDT 370 380 390 400 410 420 SQNSCVDCSV TQSNKVSVTP PEESQNSDTP PRPDRLPLDE KGHVTWSFHG PENAIPIPDL 430 440 450 460 470 480 SEGNSSDINY QTRKTVSLTP SPTTQVETPD LVDHDNTSPL FRTPLSFTNP LHSDDSDSDE 490 500 510 520 530 540 RNSDGAVTQN KTNISTASAT VSAATSTESI STRKVLPMSI ARHNIAGTTH SGAEKDVDVS 550 560 570 580 590 600 EDSPPPLPER TPESFVLASE HNTPVRSEWS ELQSQERSEQ KKSEGLITSE NEKCDHPAGG 610 620 630 640 650 IHYEMCIECP PTFSDKREQI SENPTEATDI GFGNRCGKPK GPRDPPSEWT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a human cDNA encoding a novel putative cytoplasmic protein-tyrosine-phosphatase." Takekawa M., Itoh F., Hinoda Y., Arimura Y., Toyota M., Sekiya M., Adachi M., Imai K., Yachi A. Biochem. Biophys. Res. Commun. 189:1223-1230(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-322. Tissue: Colon.
[2]	"Cloning and expression of PTP-PEST. A novel, human, nontransmembrane protein tyrosine phosphatase." Yang Q., Co D., Sommercorn J., Tonks N.K. J. Biol. Chem. 268:6622-6628(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	Erratum Yang Q., Co D., Sommercorn J., Tonks N.K. J. Biol. Chem. 268:17650-17650(1993) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 495-517 AND 526-780.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS ILE-322 AND ALA-573. Tissue: Tongue.
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-322. Tissue: Brain.
[6]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis.
[8]	"Exploring proteomes and analyzing protein processing by mass spectrometric 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) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-8, ACETYLATION AT MET-1. Tissue: Platelet.
[9]	"Chromosomal localization of the protein tyrosine phosphatase G1 gene and characterization of the aberrant transcripts in human colon cancer cells." Takekawa M., Itoh F., Hinoda Y., Adachi M., Ariyama T., Inazawa J., Imai K., Yachi A. FEBS Lett. 339:222-228(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-136 (ISOFORM 1), VARIANT COLON CANCER ARG-61.
[10]	"A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion." Li J., Nishizawa K., An W., Hussey R.E., Lialios F.E., Salgia R., Sunder-Plassmann R., Reinherz E.L. EMBO J. 17:7320-7336(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PSTPIP1.
[11]	"Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase-PEST." Lu T.J., Lai W.Y., Huang C.Y., Hsieh W.J., Yu J.S., Hsieh Y.J., Chang W.T., Leu T.H., Chang W.C., Chuang W.J., Tang M.J., Chen T.Y., Lu T.L., Lai M.D. J. Biol. Chem. 281:38405-38417(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY STK24.
[12]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancer cells." Sahu S.N., Nunez S., Bai G., Gupta A. Am. J. Physiol. 292:C2288-C2296(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTK2B/PYK2, FUNCTION.
[14]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689 AND THR-693, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603 AND SER-673, MASS SPECTROMETRY. Tissue: Platelet.
[16]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-468; THR-519; SER-567; THR-569; SER-571; SER-603; SER-606; SER-608; SER-613; SER-689 AND THR-693, VARIANT [LARGE SCALE ANALYSIS] ILE-322, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-435; SER-449 AND SER-673, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-435; SER-449; SER-603; SER-606 AND SER-673, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D13380 mRNA. Translation: BAA02648.1. M93425 mRNA. Translation: AAA36529.1. AK296764 mRNA. Translation: BAG59344.1. AB209524 mRNA. Translation: BAD92761.1. Different initiation. AC006451 Genomic DNA. Translation: AAQ96881.1. BC050008 mRNA. Translation: AAH50008.2. S69184 mRNA. Translation: AAB30047.2.
IPI	IPI00289082. IPI00908446.
PIR	JC1368.
RefSeq	NP_001124480.1. NM_001131008.1. NP_001124481.1. NM_001131009.1. NP_002826.3. NM_002835.3.
UniGene	Hs.61812.
3D structure databases
ProteinModelPortal	Q05209.
SMR	Q05209. Positions 3-298.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q05209. 22 interactions.
MINT	MINT-243699.
STRING	9606.ENSP00000248594.
PTM databases
PhosphoSite	Q05209.
Polymorphism databases
DMDM	50403764.
Proteomic databases
PaxDb	Q05209.
PRIDE	Q05209.
Protocols and materials databases
DNASU	5782.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000248594; ENSP00000248594; ENSG00000127947. ENST00000435495; ENSP00000397991; ENSG00000127947.
GeneID	5782.
KEGG	hsa:5782.
UCSC	uc003ugh.2. human.
Organism-specific databases
CTD	5782.
GeneCards	GC07P077166.
H-InvDB	HIX0033626.
HGNC	HGNC:9645. PTPN12.
HPA	HPA007097.
MIM	600079. gene.
neXtProt	NX_Q05209.
PharmGKB	PA33987.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5599.
HOGENOM	HOG000252955.
HOVERGEN	HBG007666.
InParanoid	Q05209.
KO	K01104.
OMA	ERYWPLY.
OrthoDB	EOG42BX89.
Gene expression databases
ArrayExpress	Q05209.
Bgee	Q05209.
CleanEx	HS_PTPN12.
Genevestigator	Q05209.
GermOnline	ENSG00000127947. Homo sapiens.
Family and domain databases
InterPro	IPR012266. Ptpn_12. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. IPR000242. Tyr_Pase_rcpt/non-rcpt. [Graphical view]
Pfam	PF00102. Y_phosphatase. 1 hit. [Graphical view]
PIRSF	PIRSF000932. Tyr-Ptase_nr12. 1 hit.
PRINTS	PR00700. PRTYPHPHTASE.
SMART	SM00194. PTPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50055. TYR_PHOSPHATASE_PTP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q05209.
ChEMBL	CHEMBL3236.
ChiTaRS	PTPN12. human.
GenomeRNAi	5782.
NextBio	22488.
SOURCE	Search...

Entry information

Entry name

PTN12_HUMAN

Accession

Primary (citable) accession number: Q05209
Secondary accession number(s): B4DKY2 , E9PEH9, Q16130, Q59FD6, Q75MN8, Q86XU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 131 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.