Reviewed, UniProtKB/Swiss-Prot Q15262 (PTPRK_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1439 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTP-kappa.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subcellular location	Cell junction › adherens 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 component	Cell junction Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Immunoglobulin domain Repeat Signal Transmembrane
Molecular function	Hydrolase Protein phosphatase Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell migration Inferred from mutant phenotype. Source: UniProtKB cellular response to UV Inferred from direct assay. Source: UniProtKB cellular response to reactive oxygen species Inferred from direct assay. Source: UniProtKB focal adhesion formation Inferred from mutant phenotype. Source: UniProtKB negative regulation of cell cycle Inferred from direct assay. Source: UniProtKB negative regulation of cell migration Inferred from direct assay. Source: UniProtKB negative regulation of keratinocyte proliferation Inferred from direct assay. Source: UniProtKB negative regulation of transcription Inferred from direct assay. Source: UniProtKB protein amino acid dephosphorylation Inferred from direct assay. Source: UniProtKB protein localization at cell surface Inferred from direct assay. Source: UniProtKB transforming growth factor beta receptor signaling pathway Inferred from direct assay. Source: UniProtKB
Cellular component	adherens junction Inferred from electronic annotation. Source: UniProtKB-SubCell cell surface Inferred from direct assay. Source: UniProtKB cell-cell junction Ref.1 Inferred from direct assay. Source: UniProtKB integral to plasma membrane Ref.2 Non-traceable author statement. Source: UniProtKB leading edge membrane Inferred from direct assay. Source: UniProtKB
Molecular function	beta-catenin binding Ref.1 Inferred from physical interaction. Source: UniProtKB gamma-catenin binding Ref.1 Inferred from physical interaction. Source: UniProtKB protein kinase binding Inferred from physical interaction. Source: UniProtKB transmembrane receptor protein tyrosine phosphatase activity Ref.2 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CBL	P22681	1	EBI-474052,EBI-518228
CDH2	P19022	1	EBI-474052,EBI-2256711
CSK	P41240	1	EBI-474052,EBI-1380630
ERBB2	P04626	1	EBI-474052,EBI-641062
GHR	P10912	1	EBI-474052,EBI-286316
INSR	P06213	1	EBI-474052,EBI-475899
LCK	P06239	1	EBI-474052,EBI-1348
MAPK3	P27361	1	EBI-474052,EBI-73995
MET	P08581	1	EBI-474052,EBI-1039152
NSF	P46459	1	EBI-474052,EBI-712251
PDGFRB	P09619	1	EBI-474052,EBI-641237
PDPK1	O15530	1	EBI-474052,EBI-717097
PXN	P49023	1	EBI-474052,EBI-702209
TEC	P42680	1	EBI-474052,EBI-1383480
TEK	Q02763	1	EBI-474052,EBI-2257090

Alternative products

This entry describes 2 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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Potential

Chain

27 – 1439

1413

Receptor-type tyrosine-protein phosphatase kappa

PRO_0000025446

Regions

Topological domain

27 – 752

726

Extracellular Potential

Transmembrane

753 – 774

22

Potential

Topological domain

775 – 1439

665

Cytoplasmic Potential

Domain

31 – 194

164

MAM

Domain

196 – 281

86

Ig-like C2-type

Domain

291 – 383

93

Fibronectin type-III 1

Domain

389 – 485

97

Fibronectin type-III 2

Domain

490 – 589

100

Fibronectin type-III 3

Domain

597 – 680

84

Fibronectin type-III 4

Domain

887 – 1141

255

Tyrosine-protein phosphatase 1

Domain

1173 – 1435

263

Tyrosine-protein phosphatase 2

Sites

Active site

1082

1

Phosphocysteine intermediate By similarity

Active site

1376

1

Phosphocysteine intermediate By similarity

Site

643 – 644

2

Cleavage Probable

Amino acid modifications

Modified residue

805

1

Phosphotyrosine Ref.6

Modified residue

858

1

Phosphotyrosine Ref.6

Glycosylation

101

1

N-linked (GlcNAc...) Potential

Glycosylation

140

1

N-linked (GlcNAc...) Ref.5

Glycosylation

211

1

N-linked (GlcNAc...) Potential

Glycosylation

416

1

N-linked (GlcNAc...) Ref.4 Ref.7

Glycosylation

424

1

N-linked (GlcNAc...) Potential

Glycosylation

436

1

N-linked (GlcNAc...) Potential

Glycosylation

462

1

N-linked (GlcNAc...) Ref.5

Glycosylation

552

1

N-linked (GlcNAc...) Potential

Glycosylation

586

1

N-linked (GlcNAc...) Potential

Glycosylation

590

1

N-linked (GlcNAc...) Potential

Glycosylation

607

1

N-linked (GlcNAc...) Potential

Glycosylation

690

1

N-linked (GlcNAc...) Potential

Disulfide bond

216 ↔ 270

Potential

Natural variations

Alternative sequence

732

1

A → AA in isoform 2.

VSP_024819

Experimental info

Sequence conflict

9

1

L → V in AAC37599. Ref.2

Sequence conflict

158

1

T → S in CAA94519. Ref.1

Sequence conflict

284

1

A → P in AAC37599. Ref.2

Sequence conflict

422

1

T → S in AAC37599. Ref.2

Sequence conflict

672 – 674

3

AEL → CRT in AAC37599. Ref.2

Sequence conflict

715

1

S → T in AAC37599. Ref.2

Sequence conflict

1366

1

E → K in AAC37599. Ref.2

Secondary structure

1

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1439

Helix Strand Turn

Details...

Helix

869 – 871

3

Helix

872 – 879

8

Beta strand

883 – 885

3

Helix

887 – 892

6

Helix

903 – 906

4

Helix

908 – 913

6

Helix

923 – 925

3

Helix

936 – 939

4

Beta strand

942 – 948

7

Beta strand

951 – 958

8

Helix

963 – 965

3

Helix

966 – 976

11

Beta strand

980 – 983

4

Beta strand

987 – 989

3

Beta strand

1001 – 1006

6

Beta strand

1009 – 1018

10

Beta strand

1020 – 1031

12

Beta strand

1038 – 1045

8

Beta strand

1050 – 1053

4

Helix

1058 – 1070

13

Beta strand

1078 – 1081

4

Beta strand

1083 – 1086

4

Helix

1087 – 1105

19

Beta strand

1106 – 1108

3

Helix

1110 – 1120

11

Helix

1128 – 1144

17

Turn

1150 – 1153

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: EE1EA6EA3CCA31ED	FASTA	1,439	162,102
	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
	Isoform 2. Checksum: 41B5AD638EE63969	FASTA	1,440	162,173
	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 KAAATEEPEV IPDPAKQTDR VVKIAGISAG ILVFILLLLV VILIVKKSKL 790 800 810 820 830 840 AKKRKDAMGN TRQEMTHMVN AMDRSYADQS TLHAEDPLSI TFMDQHNFSP RYENHSATAE 850 860 870 880 890 900 SSRLLDVPRY LCEGTESPYQ TGQLHPAIRV ADLLQHINLM KTSDSYGFKE EYESFFEGQS 910 920 930 940 950 960 ASWDVAKKDQ NRAKNRYGNI IAYDHSRVIL QPVEDDPSSD YINANYIDGY QRPSHYIATQ 970 980 990 1000 1010 1020 GPVHETVYDF WRMIWQEQSA CIVMVTNLVE VGRVKCYKYW PDDTEVYGDF KVTCVEMEPL 1030 1040 1050 1060 1070 1080 AEYVVRTFTL ERRGYNEIRE VKQFHFTGWP DHGVPYHATG LLSFIRRVKL SNPPSAGPIV 1090 1100 1110 1120 1130 1140 VHCSAGAGRT GCYIVIDIML DMAEREGVVD IYNCVKALRS RRINMVQTEE QYIFIHDAIL 1150 1160 1170 1180 1190 1200 EACLCGETAI PVCEFKAAYF DMIRIDSQTN SSHLKDEFQT LNSVTPRLQA EDCSIACLPR 1210 1220 1230 1240 1250 1260 NHDKNRFMDM LPPDRCLPFL ITIDGESSNY INAALMDSYR QPAAFIVTQY PLPNTVKDFW 1270 1280 1290 1300 1310 1320 RLVYDYGCTS IVMLNEVDLS QGCPQYWPEE GMLRYGPIQV ECMSCSMDCD VINRIFRICN 1330 1340 1350 1360 1370 1380 LTRPQEGYLM VQQFQYLGWA SHREVPGSKR SFLKLILQVE KWQEECEEGE GRTIIHCLNG 1390 1400 1410 1420 1430 1440 GGRSGMFCAI GIVVEMVKRQ NVVDVFHAVK TLRNSKPNMV EAPEQYRFCY DVALEYLESS

References

	« Hide 'large scale' referencesShow '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: 8663237] [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: 9047348] [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: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Identification of N-glycosylation sites on secreted proteins of human hepatocellular carcinoma cells with a complementary proteomics approach." Cao J., Shen C., Wang H., Shen H., Chen Y., Nie A., Yan G., Lu H., Liu Y., Yang P. J. Proteome Res. 8:662-672(2009) [PubMed: 19196183] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140 AND ASN-462, MASS SPECTROMETRY.
[6]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-805 AND TYR-858, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[7]	"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: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416, MASS SPECTROMETRY.
[8]	"Large-scale structural analysis of the classical human protein tyrosine phosphatome." Barr A.J., Ugochukwu E., Lee W.H., King O.N., Filippakopoulos P., Alfano I., Savitsky P., Burgess-Brown N.A., Muller S., Knapp S. Cell 136:352-363(2009) [PubMed: 19167335] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 865-1154.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z70660 mRNA. Translation: CAA94519.1.
L77886 mRNA. Translation: AAC37599.1.
AL034349 , AL035465, AL035470, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI23055.1.
AL035465 , AL034349, AL035470, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI42412.1.
AL035470 , AL034349, AL035465, AL035594, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI21517.1.
AL035594 , AL034349, AL035465, AL035470, AL357621, AL451073, AL590006 Genomic DNA. Translation: CAI43013.1.
AL357621 , AL034349, AL035465, AL035470, AL035594, AL451073, AL590006 Genomic DNA. Translation: CAI41224.1.
AL451073 , AL034349, AL035465, AL035470, AL035594, AL357621, AL590006 Genomic DNA. Translation: CAI40501.1.
AL590006 , AL034349, AL035465, AL035470, AL035594, AL357621, AL451073 Genomic DNA. Translation: CAI39440.1.

IPI

IPI00015756.
IPI00644648.

PIR

JC6312.

UniGene

Hs.155919

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C7S	X-ray	1.95	A	865-1154	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15262. 20 interactions.

STRING

Q15262.

PTM databases

PhosphoSite

Q15262.

Proteomic databases

PRIDE

Q15262.

Genome annotation databases

Ensembl

ENST00000368202; ENSP00000357185; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000368204; ENSP00000357187; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000368205; ENSP00000357188; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000368207; ENSP00000357190; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000368210; ENSP00000357193; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000368213; ENSP00000357196; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000368215; ENSP00000357198; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000368226; ENSP00000357209; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000368227; ENSP00000357210; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000392448; ENSP00000376242; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000392449; ENSP00000376243; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000415046; ENSP00000406825; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000415055; ENSP00000408180; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000427676; ENSP00000412387; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000429595; ENSP00000388676; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000434424; ENSP00000413342; ENSG00000152894; Homo sapiens. [Genome view]
ENST00000450869; ENSP00000401768; ENSG00000152894; Homo sapiens. [Genome view]

UCSC

uc003qbk.1. human.

Organism-specific databases

GeneCards

GC06M128331.

H-InvDB

HIX0006208.
HIX0033189.

HGNC

HGNC:9674. PTPRK.

MIM

602545. gene.

PharmGKB

PA34019.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q15262.

Enzyme and pathway databases

BRENDA

3.1.3.48. 247.

Pathway_Interaction_DB

nfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.

Gene expression databases

ArrayExpress

Q15262.

Bgee

Q15262.

CleanEx

HS_PTPRK.

Genevestigator

Q15262.

GermOnline

ENSG00000152894. Homo sapiens.

Family and domain databases

InterPro

IPR000387. Dual-sp/Tyr_phosphatase.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR000998. MAM.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Gene3D

G3DSA:2.60.40.30. FN_III-like. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

Pfam

PF00041. fn3. 2 hits.
PF07679. I-set. 1 hit.
PF00629. MAM. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]

PRINTS

PR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.

SMART

SM00060. FN3. 3 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]

PROSITE

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]

ProtoNet

Search...

Other Resources

NextBio

22570.

SOURCE

Search...

Entry information

Entry name

PTPRK_HUMAN

Accession

Primary (citable) accession number: Q15262
Secondary accession number(s): Q14763, Q5TG10

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 2007
Last modified:	November 3, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.