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Q05209 (PTN12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length780 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2. Ref.14

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.11 Ref.14

Subcellular location

Cytoplasm. Cell projectionpodosome By similarity.

Post-translational modification

Phosphorylated by STK24/MST3 and this results in inhibition of its activity. Ref.12

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.

Alternative products

This entry describes 3 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.
Isoform 3 (identifier: Q05209-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.
Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 780780Tyrosine-protein phosphatase non-receptor type 12
PRO_0000094771

Regions

Domain28 – 293266Tyrosine-protein phosphatase
Region231 – 2377Substrate binding By similarity
Region345 – 43894Interaction with TGFB1I1 By similarity

Sites

Active site2311Phosphocysteine intermediate By similarity
Binding site1991Substrate By similarity
Binding site2781Substrate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9 Ref.21 Ref.22
Modified residue191Phosphoserine Ref.18
Modified residue3321Phosphoserine Ref.17 Ref.20
Modified residue4351Phosphoserine Ref.18 Ref.20
Modified residue4491Phosphoserine Ref.18 Ref.20
Modified residue4681Phosphoserine Ref.17
Modified residue5191Phosphothreonine Ref.17
Modified residue5671Phosphoserine Ref.17
Modified residue5691Phosphothreonine Ref.17
Modified residue5711Phosphoserine Ref.17
Modified residue5961Phosphoserine By similarity
Modified residue5981Phosphothreonine By similarity
Modified residue6031Phosphoserine Ref.16 Ref.17 Ref.20
Modified residue6061Phosphoserine Ref.17 Ref.20
Modified residue6081Phosphoserine Ref.17
Modified residue6131Phosphoserine Ref.17
Modified residue6731Phosphoserine Ref.13 Ref.16 Ref.18 Ref.20
Modified residue6891Phosphoserine Ref.15 Ref.17
Modified residue6931Phosphothreonine Ref.15 Ref.17

Natural variations

Alternative sequence1 – 130130Missing in isoform 2.
VSP_046274
Alternative sequence1 – 119119Missing in isoform 3.
VSP_054168
Natural variant611K → R in colon cancer. Ref.10
VAR_006385
Natural variant3221V → I. Ref.1 Ref.4 Ref.5 Ref.17
Corresponds to variant rs9640663 [ dbSNP | Ensembl ].
VAR_019512
Natural variant5731T → A. Ref.4
Corresponds to variant rs3750050 [ dbSNP | Ensembl ].
VAR_020297
Natural variant7061E → K.
Corresponds to variant rs2230602 [ dbSNP | Ensembl ].
VAR_057129

Experimental info

Sequence conflict1211I → V in BAA02648. Ref.1
Sequence conflict1211I → V in AAB30047. Ref.10
Sequence conflict6121N → D in BAG59344. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 663DB3E5176FD7FD

FASTA78088,106
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 217EF3041B7E5EDB
Show »

FASTA65072,778
Isoform 3 [UniParc].

Checksum: 74E2947477636633
Show »

FASTA66174,138

References

« Hide '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. expand/collapse author list , 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] (ISOFORMS 1 AND 2), VARIANTS ILE-322 AND ALA-573.
Tissue: Cerebellum and 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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.
[15]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13380 mRNA. Translation: BAA02648.1.
M93425 mRNA. Translation: AAA36529.1.
AK289573 mRNA. Translation: BAF82262.1.
AK296764 mRNA. Translation: BAG59344.1.
AB209524 mRNA. Translation: BAD92761.1. Different initiation.
AC006451 Genomic DNA. Translation: AAQ96881.1.
CH236949 Genomic DNA. Translation: EAL24198.1.
CH471091 Genomic DNA. Translation: EAW77036.1.
CH471091 Genomic DNA. Translation: EAW77037.1.
BC050008 mRNA. Translation: AAH50008.2.
S69184 mRNA. Translation: AAB30047.2.
CCDSCCDS47620.1. [Q05209-2]
CCDS5592.1. [Q05209-1]
PIRJC1368.
RefSeqNP_001124480.1. NM_001131008.1. [Q05209-3]
NP_001124481.1. NM_001131009.1. [Q05209-2]
NP_002826.3. NM_002835.3. [Q05209-1]
UniGeneHs.61812.

3D structure databases

ProteinModelPortalQ05209.
SMRQ05209. Positions 3-298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111746. 41 interactions.
IntActQ05209. 37 interactions.
MINTMINT-243699.
STRING9606.ENSP00000248594.

Chemistry

BindingDBQ05209.
ChEMBLCHEMBL3236.

PTM databases

PhosphoSiteQ05209.

Polymorphism databases

DMDM317373522.

Proteomic databases

MaxQBQ05209.
PaxDbQ05209.
PRIDEQ05209.

Protocols and materials databases

DNASU5782.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000248594; ENSP00000248594; ENSG00000127947. [Q05209-1]
ENST00000415482; ENSP00000392429; ENSG00000127947.
ENST00000435495; ENSP00000397991; ENSG00000127947. [Q05209-2]
GeneID5782.
KEGGhsa:5782.
UCSCuc003ugh.2. human. [Q05209-1]

Organism-specific databases

CTD5782.
GeneCardsGC07P077166.
H-InvDBHIX0033626.
HGNCHGNC:9645. PTPN12.
HPAHPA007097.
MIM600079. gene.
neXtProtNX_Q05209.
PharmGKBPA33987.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000252955.
HOVERGENHBG007666.
InParanoidQ05209.
KOK18024.
OMATWSFHGP.
OrthoDBEOG744T8Z.
PhylomeDBQ05209.
TreeFamTF351977.

Gene expression databases

ArrayExpressQ05209.
BgeeQ05209.
CleanExHS_PTPN12.
GenevestigatorQ05209.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR029021. Prot-tyrosine_phosphatase-like.
IPR012266. Ptpn_12.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFPIRSF000932. Tyr-Ptase_nr12. 1 hit.
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPN12. human.
GeneWikiPTPN12.
GenomeRNAi5782.
NextBio22488.
PROQ05209.
SOURCESearch...

Entry information

Entry namePTN12_HUMAN
AccessionPrimary (citable) accession number: Q05209
Secondary accession number(s): A4D1C5 expand/collapse secondary AC list , B4DKY2, E9PBR5, E9PEH9, Q16130, Q59FD6, Q75MN8, Q86XU4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM