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Q15262 (PTPRK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Receptor-type tyrosine-protein phosphatase kappa

Short name=Protein-tyrosine phosphatase kappa
Short name=R-PTP-kappa
EC=3.1.3.48
Gene names
Name:PTPRK
Synonyms:PTPK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1439 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Negative regulator of EGFR signaling pathway. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTPRK/PTP-kappa. Ref.6

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

Cell junctionadherens junction. Cell membrane; Single-pass type I membrane protein.

Tissue specificity

High levels in lung, brain and colon; less in liver, pancreas, stomach, kidney, placenta and mammary carcinoma.

Post-translational modification

This protein undergoes proteolytic processing.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 2B subfamily.

Contains 4 fibronectin type-III domains.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 MAM domain.

Contains 2 tyrosine-protein phosphatase domains.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from mutant phenotype PubMed 15899872. Source: UniProtKB

cell migration

Inferred from mutant phenotype PubMed 15899872. Source: UniProtKB

cellular response to UV

Inferred from direct assay PubMed 16849327. Source: UniProtKB

cellular response to reactive oxygen species

Inferred from direct assay PubMed 16849327. Source: UniProtKB

focal adhesion assembly

Inferred from mutant phenotype PubMed 15899872. Source: UniProtKB

negative regulation of cell cycle

Inferred from direct assay PubMed 15899872. Source: UniProtKB

negative regulation of cell migration

Inferred from direct assay PubMed 18276111. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay PubMed 15899872PubMed 18276111. Source: UniProtKB

negative regulation of keratinocyte proliferation

Inferred from direct assay PubMed 16263724. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18276111. Source: UniProtKB

protein dephosphorylation

Inferred from direct assay PubMed 16263724. Source: UniProtKB

protein localization to cell surface

Inferred from direct assay PubMed 18276111. Source: UniProtKB

signal transduction

Inferred from direct assay PubMed 16849327. Source: UniProtKB

transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 15899872. Source: UniProtKB

   Cellular_componentadherens junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

axon

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 18276111. Source: UniProtKB

cell-cell junction

Inferred from direct assay Ref.1. Source: UniProtKB

dendrite

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Non-traceable author statement Ref.2. Source: UniProtKB

integral component of plasma membrane

Non-traceable author statement Ref.2. Source: UniProtKB

leading edge membrane

Inferred from direct assay PubMed 15899872. Source: UniProtKB

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

photoreceptor outer segment

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionbeta-catenin binding

Inferred from physical interaction Ref.1. Source: UniProtKB

gamma-catenin binding

Inferred from physical interaction Ref.1. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 15899872. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay PubMed 16263724PubMed 16849327Ref.1. Source: UniProtKB

transmembrane receptor protein tyrosine phosphatase activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15262-1)

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: Q15262-2)

The sequence of this isoform differs from the canonical sequence as follows:
     732-732: A → AA
Isoform 3 (identifier: Q15262-3)

The sequence of this isoform differs from the canonical sequence as follows:
     732-732: A → AA
     946-946: I → IDIWLYR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 14391413Receptor-type tyrosine-protein phosphatase kappa
PRO_0000025446

Regions

Topological domain27 – 752726Extracellular Potential
Transmembrane753 – 77422Helical; Potential
Topological domain775 – 1439665Cytoplasmic Potential
Domain31 – 194164MAM
Domain196 – 28186Ig-like C2-type
Domain294 – 38996Fibronectin type-III 1
Domain392 – 48897Fibronectin type-III 2
Domain491 – 595105Fibronectin type-III 3
Domain597 – 68084Fibronectin type-III 4
Domain887 – 1141255Tyrosine-protein phosphatase 1
Domain1173 – 1435263Tyrosine-protein phosphatase 2
Region1082 – 10887Substrate binding By similarity

Sites

Active site10821Phosphocysteine intermediate By similarity
Active site13761Phosphocysteine intermediate By similarity
Binding site10501Substrate By similarity
Binding site11261Substrate By similarity
Site643 – 6442Cleavage Probable

Amino acid modifications

Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation1401N-linked (GlcNAc...) Potential
Glycosylation2111N-linked (GlcNAc...) Potential
Glycosylation4161N-linked (GlcNAc...) Ref.7 Ref.8
Glycosylation4241N-linked (GlcNAc...) Potential
Glycosylation4361N-linked (GlcNAc...) Potential
Glycosylation4621N-linked (GlcNAc...) Potential
Glycosylation5521N-linked (GlcNAc...) Potential
Glycosylation5861N-linked (GlcNAc...) Potential
Glycosylation5901N-linked (GlcNAc...) Potential
Glycosylation6071N-linked (GlcNAc...) Potential
Glycosylation6901N-linked (GlcNAc...) Potential
Disulfide bond216 ↔ 270 Potential

Natural variations

Alternative sequence7321A → AA in isoform 2 and isoform 3.
VSP_024819
Alternative sequence9461I → IDIWLYR in isoform 3.
VSP_042049

Experimental info

Sequence conflict91L → V in AAC37599. Ref.2
Sequence conflict1581T → S in CAA94519. Ref.1
Sequence conflict2841A → P in AAC37599. Ref.2
Sequence conflict4221T → S in AAC37599. Ref.2
Sequence conflict672 – 6743AEL → CRT in AAC37599. Ref.2
Sequence conflict7151S → T in AAC37599. Ref.2
Sequence conflict13661E → K in AAC37599. Ref.2

Secondary structure

................................................... 1439
Helix Strand Turn

Details...

Sequences

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

Last modified May 1, 2007. Version 2.
Checksum: EE1EA6EA3CCA31ED

FASTA1,439162,102
        10         20         30         40         50         60 
MDTTAAAALP AFVALLLLSP WPLLGSAQGQ FSAGGCTFDD GPGACDYHQD LYDDFEWVHV 

        70         80         90        100        110        120 
SAQEPHYLPP EMPQGSYMIV DSSDHDPGEK ARLQLPTMKE NDTHCIDFSY LLYSQKGLNP 

       130        140        150        160        170        180 
GTLNILVRVN KGPLANPIWN VTGFTGRDWL RAELAVSTFW PNEYQVIFEA EVSGGRSGYI 

       190        200        210        220        230        240 
AIDDIQVLSY PCDKSPHFLR LGDVEVNAGQ NATFQCIATG RDAVHNKLWL QRRNGEDIPV 

       250        260        270        280        290        300 
AQTKNINHRR FAASFRLQEV TKTDQDLYRC VTQSERGSGV SNFAQLIVRE PPRPIAPPQL 

       310        320        330        340        350        360 
LGVGPTYLLI QLNANSIIGD GPIILKEVEY RMTSGSWTET HAVNAPTYKL WHLDPDTEYE 

       370        380        390        400        410        420 
IRVLLTRPGE GGTGLPGPPL ITRTKCAEPM RTPKTLKIAE IQARRIAVDW ESLGYNITRC 

       430        440        450        460        470        480 
HTFNVTICYH YFRGHNESKA DCLDMDPKAP QHVVNHLPPY TNVSLKMILT NPEGRKESEE 

       490        500        510        520        530        540 
TIIQTDEDVP GPVPVKSLQG TSFENKIFLN WKEPLDPNGI ITQYEISYSS IRSFDPAVPV 

       550        560        570        580        590        600 
AGPPQTVSNL WNSTHHVFMH LHPGTTYQFF IRASTVKGFG PATAINVTTN ISAPTLPDYE 

       610        620        630        640        650        660 
GVDASLNETA TTITVLLRPA QAKGAPISAY QIVVEELHPH RTKREAGAME CYQVPVTYQN 

       670        680        690        700        710        720 
AMSGGAPYYF AAELPPGNLP EPAPFTVGDN RTYQGFWNPP LAPRKGYNIY FQAMSSVEKE 

       730        740        750        760        770        780 
TKTQCVRIAT KAATEEPEVI PDPAKQTDRV VKIAGISAGI LVFILLLLVV ILIVKKSKLA 

       790        800        810        820        830        840 
KKRKDAMGNT RQEMTHMVNA MDRSYADQST LHAEDPLSIT FMDQHNFSPR YENHSATAES 

       850        860        870        880        890        900 
SRLLDVPRYL CEGTESPYQT GQLHPAIRVA DLLQHINLMK TSDSYGFKEE YESFFEGQSA 

       910        920        930        940        950        960 
SWDVAKKDQN RAKNRYGNII AYDHSRVILQ PVEDDPSSDY INANYIDGYQ RPSHYIATQG 

       970        980        990       1000       1010       1020 
PVHETVYDFW RMIWQEQSAC IVMVTNLVEV GRVKCYKYWP DDTEVYGDFK VTCVEMEPLA 

      1030       1040       1050       1060       1070       1080 
EYVVRTFTLE RRGYNEIREV KQFHFTGWPD HGVPYHATGL LSFIRRVKLS NPPSAGPIVV 

      1090       1100       1110       1120       1130       1140 
HCSAGAGRTG CYIVIDIMLD MAEREGVVDI YNCVKALRSR RINMVQTEEQ YIFIHDAILE 

      1150       1160       1170       1180       1190       1200 
ACLCGETAIP VCEFKAAYFD MIRIDSQTNS SHLKDEFQTL NSVTPRLQAE DCSIACLPRN 

      1210       1220       1230       1240       1250       1260 
HDKNRFMDML PPDRCLPFLI TIDGESSNYI NAALMDSYRQ PAAFIVTQYP LPNTVKDFWR 

      1270       1280       1290       1300       1310       1320 
LVYDYGCTSI VMLNEVDLSQ GCPQYWPEEG MLRYGPIQVE CMSCSMDCDV INRIFRICNL 

      1330       1340       1350       1360       1370       1380 
TRPQEGYLMV QQFQYLGWAS HREVPGSKRS FLKLILQVEK WQEECEEGEG RTIIHCLNGG 

      1390       1400       1410       1420       1430 
GRSGMFCAIG IVVEMVKRQN VVDVFHAVKT LRNSKPNMVE APEQYRFCYD VALEYLESS 

« Hide

Isoform 2 [UniParc].

Checksum: 41B5AD638EE63969
Show »

FASTA1,440162,173
Isoform 3 [UniParc].

Checksum: 43919D3BA33C84C4
Show »

FASTA1,446163,020

References

« Hide 'large scale' references
[1]"Association of human protein-tyrosine phosphatase kappa with members of the armadillo family."
Fuchs M., Mueller T., Lerch M., Ullrich A.
J. Biol. Chem. 271:16712-16719(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular cloning and chromosomal localization of a human gene homologous to the murine R-PTP-kappa, a receptor-type protein tyrosine phosphatase."
Yang Y., Gil M.C., Choi E.Y., Park S.H., Pyun K.H., Ha H.
Gene 186:77-82(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Foreskin.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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].
[5]"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 3).
Tissue: Brain.
[6]"An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis."
Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F., Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.
Curr. Biol. 19:1788-1798(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN EGFR REGULATION.
[7]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416.
Tissue: Liver.
[8]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416.
Tissue: Leukemic T-cell.
[9]"Large-scale structural analysis of the classical human protein tyrosine phosphatome."
Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P., Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.
Cell 136:352-363(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 865-1154.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z70660 mRNA. Translation: CAA94519.1.
L77886 mRNA. Translation: AAC37599.1.
AL035470 expand/collapse EMBL AC list , AL034349, AL035465, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI21516.1.
AL035470 expand/collapse EMBL AC list , AL034349, AL035465, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI21517.1.
AL034349 expand/collapse EMBL AC list , AL035465, AL035470, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI23054.1.
AL034349 expand/collapse EMBL AC list , AL035465, AL035470, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI23055.1.
AL590006 expand/collapse EMBL AC list , AL034349, AL035465, AL035470, AL035594, AL357621, AL451073 Genomic DNA. Translation: CAI39438.1.
AL590006 expand/collapse EMBL AC list , AL034349, AL035465, AL035470, AL035594, AL357621, AL451073 Genomic DNA. Translation: CAI39440.1.
AL451073 expand/collapse EMBL AC list , AL034349, AL035465, AL035470, AL035594, AL357621, AL590006 Genomic DNA. Translation: CAI40499.1.
AL451073 expand/collapse EMBL AC list , AL034349, AL035465, AL035470, AL035594, AL357621, AL590006 Genomic DNA. Translation: CAI40501.1.
AL357621 expand/collapse EMBL AC list , AL034349, AL035465, AL035470, AL035594, AL451073, AL590006 Genomic DNA. Translation: CAI41222.1.
AL357621 expand/collapse EMBL AC list , AL034349, AL035465, AL035470, AL035594, AL451073, AL590006 Genomic DNA. Translation: CAI41224.1.
AL035465 expand/collapse EMBL AC list , AL034349, AL035470, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI42410.1.
AL035465 expand/collapse EMBL AC list , AL034349, AL035470, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI42412.1.
AL035594 expand/collapse EMBL AC list , AL034349, AL035465, AL035470, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI43011.1.
AL035594 expand/collapse EMBL AC list , AL034349, AL035465, AL035470, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI43013.1.
CH471051 Genomic DNA. Translation: EAW48086.1.
BC140775 mRNA. Translation: AAI40776.1.
BC144512 mRNA. Translation: AAI44513.1.
PIRJC6312.
RefSeqNP_001129120.1. NM_001135648.1.
NP_002835.2. NM_002844.3.
XP_005267142.1. XM_005267085.1.
UniGeneHs.155919.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C7SX-ray1.95A865-1154[»]
ProteinModelPortalQ15262.
SMRQ15262. Positions 33-596, 864-1438.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111760. 9 interactions.
IntActQ15262. 22 interactions.
MINTMINT-1350116.
STRING9606.ENSP00000357209.

PTM databases

PhosphoSiteQ15262.

Polymorphism databases

DMDM146345496.

Proteomic databases

PaxDbQ15262.
PRIDEQ15262.

Protocols and materials databases

DNASU5796.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368213; ENSP00000357196; ENSG00000152894. [Q15262-3]
ENST00000368215; ENSP00000357198; ENSG00000152894. [Q15262-1]
ENST00000368226; ENSP00000357209; ENSG00000152894. [Q15262-2]
GeneID5796.
KEGGhsa:5796.
UCSCuc003qbj.3. human. [Q15262-2]
uc003qbk.3. human. [Q15262-1]
uc010kfc.3. human. [Q15262-3]

Organism-specific databases

CTD5796.
GeneCardsGC06M128331.
H-InvDBHIX0006208.
HIX0033189.
HGNCHGNC:9674. PTPRK.
HPAHPA054822.
MIM602545. gene.
neXtProtNX_Q15262.
PharmGKBPA34019.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000049029.
HOVERGENHBG062785.
KOK06776.
OrthoDBEOG70KGNP.
PhylomeDBQ15262.
TreeFamTF312900.

Enzyme and pathway databases

SignaLinkQ15262.

Gene expression databases

ArrayExpressQ15262.
BgeeQ15262.
CleanExHS_PTPRK.
GenevestigatorQ15262.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR000998. MAM_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 2 hits.
PF00629. MAM. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 3 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
SSF49899. SSF49899. 1 hit.
PROSITEPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 1 hit.
PS00740. MAM_1. 1 hit.
PS50060. MAM_2. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPRK. human.
EvolutionaryTraceQ15262.
GeneWikiPTPRK.
GenomeRNAi5796.
NextBio22570.
PROQ15262.
SOURCESearch...

Entry information

Entry namePTPRK_HUMAN
AccessionPrimary (citable) accession number: Q15262
Secondary accession number(s): B2RTQ8 expand/collapse secondary AC list , Q14763, Q5TG10, Q5TG11
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 150 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM