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Q15262

- PTPRK_HUMAN

UniProt

Q15262 - PTPRK_HUMAN

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Protein

Receptor-type tyrosine-protein phosphatase kappa

Gene

PTPRK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei643 – 6442CleavageCurated
Binding sitei1050 – 10501SubstrateBy similarity
Active sitei1082 – 10821Phosphocysteine intermediateBy similarity
Binding sitei1126 – 11261SubstrateBy similarity
Active sitei1376 – 13761Phosphocysteine intermediateBy similarity

GO - Molecular functioni

  1. beta-catenin binding Source: UniProtKB
  2. gamma-catenin binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. protein tyrosine phosphatase activity Source: UniProtKB
  5. transmembrane receptor protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. cell adhesion Source: UniProtKB
  2. cell migration Source: UniProtKB
  3. cellular response to reactive oxygen species Source: UniProtKB
  4. cellular response to UV Source: UniProtKB
  5. focal adhesion assembly Source: UniProtKB
  6. negative regulation of cell cycle Source: UniProtKB
  7. negative regulation of cell migration Source: UniProtKB
  8. negative regulation of cell proliferation Source: UniProtKB
  9. negative regulation of keratinocyte proliferation Source: UniProtKB
  10. negative regulation of transcription, DNA-templated Source: UniProtKB
  11. peptidyl-tyrosine dephosphorylation Source: GOC
  12. protein dephosphorylation Source: UniProtKB
  13. protein localization to cell surface Source: UniProtKB
  14. signal transduction Source: UniProtKB
  15. transforming growth factor beta receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase, Receptor

Enzyme and pathway databases

SignaLinkiQ15262.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase kappa (EC:3.1.3.48)
Short name:
Protein-tyrosine phosphatase kappa
Short name:
R-PTP-kappa
Gene namesi
Name:PTPRK
Synonyms:PTPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:9674. PTPRK.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 752726ExtracellularSequence AnalysisAdd
BLAST
Transmembranei753 – 77422HelicalSequence AnalysisAdd
BLAST
Topological domaini775 – 1439665CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. axon Source: Ensembl
  2. cell-cell junction Source: UniProtKB
  3. cell surface Source: UniProtKB
  4. dendrite Source: Ensembl
  5. integral component of membrane Source: UniProtKB
  6. integral component of plasma membrane Source: UniProtKB
  7. leading edge membrane Source: UniProtKB
  8. neuronal cell body Source: Ensembl
  9. photoreceptor outer segment Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34019.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 14391413Receptor-type tyrosine-protein phosphatase kappaPRO_0000025446Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi216 ↔ 270PROSITE-ProRule annotation
Glycosylationi416 – 4161N-linked (GlcNAc...)2 Publications
Glycosylationi424 – 4241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi436 – 4361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi552 – 5521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi586 – 5861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi590 – 5901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi607 – 6071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi690 – 6901N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

This protein undergoes proteolytic processing.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ15262.
PaxDbiQ15262.
PRIDEiQ15262.

PTM databases

PhosphoSiteiQ15262.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ15262.
CleanExiHS_PTPRK.
ExpressionAtlasiQ15262. baseline and differential.
GenevestigatoriQ15262.

Organism-specific databases

HPAiHPA054822.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ERBB2P046262EBI-474052,EBI-641062
LOXP283004EBI-474052,EBI-3893481
TEKQ027632EBI-474052,EBI-2257090

Protein-protein interaction databases

BioGridi111760. 91 interactions.
IntActiQ15262. 22 interactions.
MINTiMINT-1350116.
STRINGi9606.ENSP00000357209.

Structurei

Secondary structure

1
1439
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi869 – 8713Combined sources
Helixi872 – 8798Combined sources
Beta strandi883 – 8853Combined sources
Helixi887 – 8926Combined sources
Helixi903 – 9064Combined sources
Helixi908 – 9136Combined sources
Helixi923 – 9253Combined sources
Helixi936 – 9394Combined sources
Beta strandi942 – 9487Combined sources
Beta strandi951 – 9588Combined sources
Helixi963 – 9653Combined sources
Helixi966 – 97611Combined sources
Beta strandi980 – 9834Combined sources
Beta strandi987 – 9893Combined sources
Beta strandi1001 – 10066Combined sources
Beta strandi1009 – 101810Combined sources
Beta strandi1020 – 103112Combined sources
Beta strandi1038 – 10458Combined sources
Beta strandi1050 – 10534Combined sources
Helixi1058 – 107013Combined sources
Beta strandi1078 – 10814Combined sources
Beta strandi1083 – 10864Combined sources
Helixi1087 – 110519Combined sources
Beta strandi1106 – 11083Combined sources
Helixi1110 – 112011Combined sources
Helixi1128 – 114417Combined sources
Turni1150 – 11534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C7SX-ray1.95A865-1154[»]
ProteinModelPortaliQ15262.
SMRiQ15262. Positions 33-596, 864-1438.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15262.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 194164MAMPROSITE-ProRule annotationAdd
BLAST
Domaini196 – 28186Ig-like C2-typeAdd
BLAST
Domaini294 – 38996Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini392 – 48897Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini491 – 595105Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini597 – 68084Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini887 – 1141255Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
BLAST
Domaini1173 – 1435263Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1082 – 10887Substrate bindingBy similarity

Sequence similaritiesi

Contains 4 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 MAM domain.PROSITE-ProRule annotation
Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00760000118900.
HOGENOMiHOG000049029.
HOVERGENiHBG062785.
InParanoidiQ15262.
KOiK06776.
OrthoDBiEOG70KGNP.
PhylomeDBiQ15262.
TreeFamiTF312900.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.90.190.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR000998. MAM_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00041. fn3. 2 hits.
PF00629. MAM. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSiPR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 3 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEiPS50853. 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]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15262-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MDTTAAAALP AFVALLLLSP WPLLGSAQGQ FSAGGCTFDD GPGACDYHQD
60 70 80 90 100
LYDDFEWVHV SAQEPHYLPP EMPQGSYMIV DSSDHDPGEK ARLQLPTMKE
110 120 130 140 150
NDTHCIDFSY LLYSQKGLNP GTLNILVRVN KGPLANPIWN VTGFTGRDWL
160 170 180 190 200
RAELAVSTFW PNEYQVIFEA EVSGGRSGYI AIDDIQVLSY PCDKSPHFLR
210 220 230 240 250
LGDVEVNAGQ NATFQCIATG RDAVHNKLWL QRRNGEDIPV AQTKNINHRR
260 270 280 290 300
FAASFRLQEV TKTDQDLYRC VTQSERGSGV SNFAQLIVRE PPRPIAPPQL
310 320 330 340 350
LGVGPTYLLI QLNANSIIGD GPIILKEVEY RMTSGSWTET HAVNAPTYKL
360 370 380 390 400
WHLDPDTEYE IRVLLTRPGE GGTGLPGPPL ITRTKCAEPM RTPKTLKIAE
410 420 430 440 450
IQARRIAVDW ESLGYNITRC HTFNVTICYH YFRGHNESKA DCLDMDPKAP
460 470 480 490 500
QHVVNHLPPY TNVSLKMILT NPEGRKESEE TIIQTDEDVP GPVPVKSLQG
510 520 530 540 550
TSFENKIFLN WKEPLDPNGI ITQYEISYSS IRSFDPAVPV AGPPQTVSNL
560 570 580 590 600
WNSTHHVFMH LHPGTTYQFF IRASTVKGFG PATAINVTTN ISAPTLPDYE
610 620 630 640 650
GVDASLNETA TTITVLLRPA QAKGAPISAY QIVVEELHPH RTKREAGAME
660 670 680 690 700
CYQVPVTYQN AMSGGAPYYF AAELPPGNLP EPAPFTVGDN RTYQGFWNPP
710 720 730 740 750
LAPRKGYNIY FQAMSSVEKE TKTQCVRIAT KAATEEPEVI PDPAKQTDRV
760 770 780 790 800
VKIAGISAGI LVFILLLLVV ILIVKKSKLA KKRKDAMGNT RQEMTHMVNA
810 820 830 840 850
MDRSYADQST LHAEDPLSIT FMDQHNFSPR YENHSATAES SRLLDVPRYL
860 870 880 890 900
CEGTESPYQT GQLHPAIRVA DLLQHINLMK TSDSYGFKEE YESFFEGQSA
910 920 930 940 950
SWDVAKKDQN RAKNRYGNII AYDHSRVILQ PVEDDPSSDY INANYIDGYQ
960 970 980 990 1000
RPSHYIATQG PVHETVYDFW RMIWQEQSAC IVMVTNLVEV GRVKCYKYWP
1010 1020 1030 1040 1050
DDTEVYGDFK VTCVEMEPLA EYVVRTFTLE RRGYNEIREV KQFHFTGWPD
1060 1070 1080 1090 1100
HGVPYHATGL LSFIRRVKLS NPPSAGPIVV HCSAGAGRTG CYIVIDIMLD
1110 1120 1130 1140 1150
MAEREGVVDI YNCVKALRSR RINMVQTEEQ YIFIHDAILE ACLCGETAIP
1160 1170 1180 1190 1200
VCEFKAAYFD MIRIDSQTNS SHLKDEFQTL NSVTPRLQAE DCSIACLPRN
1210 1220 1230 1240 1250
HDKNRFMDML PPDRCLPFLI TIDGESSNYI NAALMDSYRQ PAAFIVTQYP
1260 1270 1280 1290 1300
LPNTVKDFWR LVYDYGCTSI VMLNEVDLSQ GCPQYWPEEG MLRYGPIQVE
1310 1320 1330 1340 1350
CMSCSMDCDV INRIFRICNL TRPQEGYLMV QQFQYLGWAS HREVPGSKRS
1360 1370 1380 1390 1400
FLKLILQVEK WQEECEEGEG RTIIHCLNGG GRSGMFCAIG IVVEMVKRQN
1410 1420 1430
VVDVFHAVKT LRNSKPNMVE APEQYRFCYD VALEYLESS
Length:1,439
Mass (Da):162,102
Last modified:May 1, 2007 - v2
Checksum:iEE1EA6EA3CCA31ED
GO
Isoform 2 (identifier: Q15262-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     732-732: A → AA

Show »
Length:1,440
Mass (Da):162,173
Checksum:i41B5AD638EE63969
GO
Isoform 3 (identifier: Q15262-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,446
Mass (Da):163,020
Checksum:i43919D3BA33C84C4
GO
Isoform 4 (identifier: Q15262-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     732-732: A → AA
     831-831: Y → LPNDPLVPTAVLVPITD
     946-946: I → IDIWLYR

Note: No experimental confirmation available.

Show »
Length:1,462
Mass (Da):164,613
Checksum:iC3CEA4670A00B758
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91L → V in AAC37599. (PubMed:9047348)Curated
Sequence conflicti158 – 1581T → S in CAA94519. (PubMed:8663237)Curated
Sequence conflicti284 – 2841A → P in AAC37599. (PubMed:9047348)Curated
Sequence conflicti422 – 4221T → S in AAC37599. (PubMed:9047348)Curated
Sequence conflicti672 – 6743AEL → CRT in AAC37599. (PubMed:9047348)Curated
Sequence conflicti715 – 7151S → T in AAC37599. (PubMed:9047348)Curated
Sequence conflicti1366 – 13661E → K in AAC37599. (PubMed:9047348)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei732 – 7321A → AA in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_024819
Alternative sequencei831 – 8311Y → LPNDPLVPTAVLVPITD in isoform 4. 1 PublicationVSP_054480
Alternative sequencei946 – 9461I → IDIWLYR in isoform 3 and isoform 4. 1 PublicationVSP_042049

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z70660 mRNA. Translation: CAA94519.1.
L77886 mRNA. Translation: AAC37599.1.
AL035470
, AL034349, AL035465, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI21516.1.
AL035470
, AL034349, AL035465, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI21517.1.
AL034349
, AL035465, AL035470, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI23054.1.
AL034349
, AL035465, AL035470, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI23055.1.
AL590006
, AL034349, AL035465, AL035470, AL035594, AL357621, AL451073 Genomic DNA. Translation: CAI39438.1.
AL590006
, AL034349, AL035465, AL035470, AL035594, AL357621, AL451073 Genomic DNA. Translation: CAI39440.1.
AL451073
, AL034349, AL035465, AL035470, AL035594, AL357621, AL590006 Genomic DNA. Translation: CAI40499.1.
AL451073
, AL034349, AL035465, AL035470, AL035594, AL357621, AL590006 Genomic DNA. Translation: CAI40501.1.
AL357621
, AL034349, AL035465, AL035470, AL035594, AL451073, AL590006 Genomic DNA. Translation: CAI41222.1.
AL357621
, AL034349, AL035465, AL035470, AL035594, AL451073, AL590006 Genomic DNA. Translation: CAI41224.1.
AL035465
, AL034349, AL035470, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI42410.1.
AL035465
, AL034349, AL035470, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI42412.1.
AL035594
, AL034349, AL035465, AL035470, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI43011.1.
AL035594
, 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.
BC144513 mRNA. Translation: AAI44514.1.
CCDSiCCDS47473.1. [Q15262-3]
CCDS5137.1. [Q15262-2]
CCDS75517.1. [Q15262-1]
PIRiJC6312.
RefSeqiNP_001129120.1. NM_001135648.2. [Q15262-3]
NP_001278910.1. NM_001291981.1. [Q15262-4]
NP_001278913.1. NM_001291984.1. [Q15262-1]
NP_002835.2. NM_002844.3. [Q15262-2]
UniGeneiHs.155919.

Genome annotation databases

EnsembliENST00000368213; ENSP00000357196; ENSG00000152894. [Q15262-3]
ENST00000368215; ENSP00000357198; ENSG00000152894. [Q15262-1]
ENST00000368226; ENSP00000357209; ENSG00000152894. [Q15262-2]
ENST00000532331; ENSP00000432973; ENSG00000152894. [Q15262-4]
GeneIDi5796.
KEGGihsa:5796.
UCSCiuc003qbj.3. human. [Q15262-2]
uc003qbk.3. human. [Q15262-1]
uc010kfc.3. human. [Q15262-3]
uc011ebu.2. human.

Polymorphism databases

DMDMi146345496.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z70660 mRNA. Translation: CAA94519.1 .
L77886 mRNA. Translation: AAC37599.1 .
AL035470
, AL034349 , AL035465 , AL035594 , AL357621 , AL451073 , AL590006 Genomic DNA. Translation: CAI21516.1 .
AL035470
, AL034349 , AL035465 , AL035594 , AL357621 , AL451073 , AL590006 Genomic DNA. Translation: CAI21517.1 .
AL034349
, AL035465 , AL035470 , AL035594 , AL357621 , AL451073 , AL590006 Genomic DNA. Translation: CAI23054.1 .
AL034349
, AL035465 , AL035470 , AL035594 , AL357621 , AL451073 , AL590006 Genomic DNA. Translation: CAI23055.1 .
AL590006
, AL034349 , AL035465 , AL035470 , AL035594 , AL357621 , AL451073 Genomic DNA. Translation: CAI39438.1 .
AL590006
, AL034349 , AL035465 , AL035470 , AL035594 , AL357621 , AL451073 Genomic DNA. Translation: CAI39440.1 .
AL451073
, AL034349 , AL035465 , AL035470 , AL035594 , AL357621 , AL590006 Genomic DNA. Translation: CAI40499.1 .
AL451073
, AL034349 , AL035465 , AL035470 , AL035594 , AL357621 , AL590006 Genomic DNA. Translation: CAI40501.1 .
AL357621
, AL034349 , AL035465 , AL035470 , AL035594 , AL451073 , AL590006 Genomic DNA. Translation: CAI41222.1 .
AL357621
, AL034349 , AL035465 , AL035470 , AL035594 , AL451073 , AL590006 Genomic DNA. Translation: CAI41224.1 .
AL035465
, AL034349 , AL035470 , AL035594 , AL357621 , AL451073 , AL590006 Genomic DNA. Translation: CAI42410.1 .
AL035465
, AL034349 , AL035470 , AL035594 , AL357621 , AL451073 , AL590006 Genomic DNA. Translation: CAI42412.1 .
AL035594
, AL034349 , AL035465 , AL035470 , AL357621 , AL451073 , AL590006 Genomic DNA. Translation: CAI43011.1 .
AL035594
, 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 .
BC144513 mRNA. Translation: AAI44514.1 .
CCDSi CCDS47473.1. [Q15262-3 ]
CCDS5137.1. [Q15262-2 ]
CCDS75517.1. [Q15262-1 ]
PIRi JC6312.
RefSeqi NP_001129120.1. NM_001135648.2. [Q15262-3 ]
NP_001278910.1. NM_001291981.1. [Q15262-4 ]
NP_001278913.1. NM_001291984.1. [Q15262-1 ]
NP_002835.2. NM_002844.3. [Q15262-2 ]
UniGenei Hs.155919.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C7S X-ray 1.95 A 865-1154 [» ]
ProteinModelPortali Q15262.
SMRi Q15262. Positions 33-596, 864-1438.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111760. 91 interactions.
IntActi Q15262. 22 interactions.
MINTi MINT-1350116.
STRINGi 9606.ENSP00000357209.

PTM databases

PhosphoSitei Q15262.

Polymorphism databases

DMDMi 146345496.

Proteomic databases

MaxQBi Q15262.
PaxDbi Q15262.
PRIDEi Q15262.

Protocols and materials databases

DNASUi 5796.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368213 ; ENSP00000357196 ; ENSG00000152894 . [Q15262-3 ]
ENST00000368215 ; ENSP00000357198 ; ENSG00000152894 . [Q15262-1 ]
ENST00000368226 ; ENSP00000357209 ; ENSG00000152894 . [Q15262-2 ]
ENST00000532331 ; ENSP00000432973 ; ENSG00000152894 . [Q15262-4 ]
GeneIDi 5796.
KEGGi hsa:5796.
UCSCi uc003qbj.3. human. [Q15262-2 ]
uc003qbk.3. human. [Q15262-1 ]
uc010kfc.3. human. [Q15262-3 ]
uc011ebu.2. human.

Organism-specific databases

CTDi 5796.
GeneCardsi GC06M128289.
H-InvDB HIX0006208.
HIX0033189.
HGNCi HGNC:9674. PTPRK.
HPAi HPA054822.
MIMi 602545. gene.
neXtProti NX_Q15262.
PharmGKBi PA34019.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00760000118900.
HOGENOMi HOG000049029.
HOVERGENi HBG062785.
InParanoidi Q15262.
KOi K06776.
OrthoDBi EOG70KGNP.
PhylomeDBi Q15262.
TreeFami TF312900.

Enzyme and pathway databases

SignaLinki Q15262.

Miscellaneous databases

ChiTaRSi PTPRK. human.
EvolutionaryTracei Q15262.
GeneWikii PTPRK.
GenomeRNAii 5796.
NextBioi 22570.
PROi Q15262.
SOURCEi Search...

Gene expression databases

Bgeei Q15262.
CleanExi HS_PTPRK.
ExpressionAtlasi Q15262. baseline and differential.
Genevestigatori Q15262.

Family and domain databases

Gene3Di 2.60.40.10. 4 hits.
3.90.190.10. 2 hits.
InterProi IPR013320. ConA-like_dom.
IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR000998. MAM_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00041. fn3. 2 hits.
PF00629. MAM. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view ]
PRINTSi PR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.
SMARTi SM00060. FN3. 3 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEi PS50853. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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] (ISOFORMS 3 AND 4).
    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.

Entry informationi

Entry nameiPTPRK_HUMAN
AccessioniPrimary (citable) accession number: Q15262
Secondary accession number(s): B2RTQ8
, B7ZMG0, Q14763, Q5TG10, Q5TG11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 2007
Last modified: November 26, 2014
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3