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O14522 (PTPRT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 T

Short name=R-PTP-T
EC=3.1.3.48
Alternative name(s):
Receptor-type tyrosine-protein phosphatase rho
Short name=RPTP-rho
Gene names
Name:PTPRT
Synonyms:KIAA0283
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1441 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in both signal transduction and cellular adhesion in the CNS.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in colon, lung, heart and testis, as well as in fetal and adult brain. Not detected in muscle and peripheral blood leukocytes. Ref.8

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.

Sequence caution

The sequence BAA22952.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAH72555.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI19251.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI19867.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI19879.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI19983.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI20439.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI22491.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI22911.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI23312.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   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

Non-traceable author statement PubMed 16973135. Source: UniProtKB

homophilic cell adhesion

Inferred from direct assay PubMed 18644975. Source: UniProtKB

peptidyl-tyrosine dephosphorylation

Inferred from mutant phenotype PubMed 16973135PubMed 17360477. Source: GOC

protein dephosphorylation

Inferred from direct assay PubMed 16973135. Source: UniProtKB

signal transduction

Non-traceable author statement PubMed 16973135. Source: UniProtKB

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from mutant phenotype PubMed 16973135. Source: UniProtKB

   Cellular_componentcell surface

Inferred from direct assay PubMed 18644975. Source: UniProtKB

integral component of membrane

Non-traceable author statement Ref.1. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 18644975. Source: UniProtKB

   Molecular_functionalpha-catenin binding

Inferred from direct assay PubMed 16973135. Source: UniProtKB

beta-catenin binding

Inferred from physical interaction PubMed 16973135. Source: UniProtKB

cadherin binding

Inferred from physical interaction PubMed 16973135. Source: UniProtKB

delta-catenin binding

Inferred from physical interaction PubMed 16973135. Source: UniProtKB

gamma-catenin binding

Inferred from direct assay PubMed 16973135. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from mutant phenotype PubMed 16973135PubMed 17360477. Source: UniProtKB

thiolester hydrolase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GRB2P629932EBI-728180,EBI-401755
Nlgn1Q99K102EBI-728180,EBI-775037From a different organism.
Nlgn2Q69ZK92EBI-728180,EBI-775065From a different organism.
Nrxn1Q9CS842EBI-728180,EBI-399696From a different organism.
Nrxn3Q6P9K92EBI-728180,EBI-7281557From a different organism.
PTPRNQ168493EBI-728180,EBI-728153

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: O14522-3)

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 1 (identifier: O14522-1)

The sequence of this isoform differs from the canonical sequence as follows:
     725-725: K → KAPMGSAQVTPGTPLCLLTT
     781-781: L → LSQR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 14411416Receptor-type tyrosine-protein phosphatase T
PRO_0000025463

Regions

Topological domain26 – 747722Extracellular Potential
Transmembrane748 – 76821Helical; Potential
Topological domain769 – 1441673Cytoplasmic Potential
Domain30 – 191162MAM
Domain193 – 28492Ig-like C2-type
Domain291 – 38494Fibronectin type-III 1
Domain389 – 48395Fibronectin type-III 2
Domain484 – 590107Fibronectin type-III 3
Domain591 – 726136Fibronectin type-III 4
Domain889 – 1143255Tyrosine-protein phosphatase 1
Domain1175 – 1437263Tyrosine-protein phosphatase 2
Region1084 – 10907Substrate binding By similarity

Sites

Active site10841Phosphocysteine intermediate By similarity
Active site13781Phosphocysteine intermediate By similarity
Binding site10521Substrate By similarity
Binding site11281Substrate By similarity

Amino acid modifications

Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation1371N-linked (GlcNAc...) Potential
Glycosylation2081N-linked (GlcNAc...) Potential
Glycosylation4211N-linked (GlcNAc...) Potential
Glycosylation5101N-linked (GlcNAc...) Potential
Glycosylation5471N-linked (GlcNAc...) Potential
Glycosylation6011N-linked (GlcNAc...) Potential
Glycosylation6541N-linked (GlcNAc...) Potential
Glycosylation6841N-linked (GlcNAc...) Potential
Disulfide bond213 ↔ 267 By similarity

Natural variations

Alternative sequence7251K → KAPMGSAQVTPGTPLCLLTT in isoform 1.
VSP_040385
Alternative sequence7811L → LSQR in isoform 1.
VSP_040386
Natural variant291A → P. Ref.1 Ref.2 Ref.4
Corresponds to variant rs2867655 [ dbSNP | Ensembl ].
VAR_028795
Natural variant741F → S in a colorectal cancer. Ref.8
VAR_020746
Natural variant761M → V.
Corresponds to variant rs17811401 [ dbSNP | Ensembl ].
VAR_028796
Natural variant2091A → T in some colorectal cancers. Ref.8
VAR_020747
Natural variant2181K → T in a gastric cancer. Ref.8
VAR_020748
Natural variant2481F → S in a colorectal cancer. Ref.8
VAR_020749
Natural variant2801Y → H in a colorectal cancer. Ref.8
VAR_020750
Natural variant3951I → V in a colorectal cancer. Ref.8
VAR_020751
Natural variant4121Y → F in a colorectal cancer. Ref.8
VAR_020752
Natural variant4531R → C in a gastric cancer. Ref.8
VAR_020753
Natural variant5101N → K in a colorectal cancer. Ref.8
VAR_020754
Natural variant6051T → M in a colorectal cancer. Ref.8
VAR_020755
Natural variant6481V → G in a colorectal cancer. Ref.8
VAR_020756
Natural variant7071A → T in a colorectal cancer. Ref.8
VAR_020757
Natural variant7071A → V in a colorectal cancer. Ref.8
VAR_020758
Natural variant7081L → P in a colorectal cancer. Ref.8
VAR_020759
Natural variant7711R → I in a lung cancer. Ref.8
VAR_020760
Natural variant9051D → G in a colorectal cancer. Ref.8
VAR_020761
Natural variant9651Q → K in a colorectal cancer; reduced phosphatase activity. Ref.8
VAR_020762
Natural variant10961A → P in a colorectal cancer. Ref.8
VAR_020763
Natural variant11061N → I in a colorectal cancer; reduced phosphatase activity. Ref.8
VAR_020764
Natural variant11901R → W in a colorectal cancer; reduced phosphatase activity. Ref.8
VAR_020765
Natural variant12131P → L in an acute myeloid leukemia sample; somatic mutation. Ref.9
VAR_054144
Natural variant12371M → L in a colorectal cancer. Ref.8
VAR_020766
Natural variant12471V → M in a colorectal cancer. Ref.8
VAR_020767
Natural variant13241R → L in a lung cancer; reduced phosphatase activity. Ref.8
VAR_020768
Natural variant13291Y → F in a colorectal cancer. Ref.8
VAR_020769
Natural variant13461T → M Found in a patient with severe intellectual disability, behavioral problems, microcephaly, congenital cardiac defect and herniation of the abdominal diaphragm; also observed in some colorectal cancers; reduced phosphatase activity; unknown pathological significance. Ref.8 Ref.10
VAR_020770

Experimental info

Sequence conflict601W → T in AAD09421. Ref.1
Sequence conflict3751P → A in AAD09421. Ref.1
Sequence conflict8671P → L in AAD09421. Ref.1

Secondary structure

............................................... 1441
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified January 11, 2011. Version 6.
Checksum: BE60F3DB2CE13539

FASTA1,441162,134
        10         20         30         40         50         60 
MASLAALALS LLLRLQLPPL PGARAQSAAG GCSFDEHYSN CGYSVALGTN GFTWEQINTW 

        70         80         90        100        110        120 
EKPMLDQAVP TGSFMMVNSS GRASGQKAHL LLPTLKENDT HCIDFHYYFS SRDRSSPGAL 

       130        140        150        160        170        180 
NVYVKVNGGP QGNPVWNVSG VVTEGWVKAE LAISTFWPHF YQVIFESVSL KGHPGYIAVD 

       190        200        210        220        230        240 
EVRVLAHPCR KAPHFLRLQN VEVNVGQNAT FQCIAGGKWS QHDKLWLQQW NGRDTALMVT 

       250        260        270        280        290        300 
RVVNHRRFSA TVSVADTAQR SVSKYRCVIR SDGGSGVSNY AELIVKEPPT PIAPPELLAV 

       310        320        330        340        350        360 
GATYLWIKPN ANSIIGDGPI ILKEVEYRTT TGTWAETHIV DSPNYKLWHL DPDVEYEIRV 

       370        380        390        400        410        420 
LLTRPGEGGT GPPGPPLTTR TKCADPVHGP QNVEIVDIRA RQLTLQWEPF GYAVTRCHSY 

       430        440        450        460        470        480 
NLTVQYQYVF NQQQYEAEEV IQTSSHYTLR GLRPFMTIRL RLLLSNPEGR MESEELVVQT 

       490        500        510        520        530        540 
EEDVPGAVPL ESIQGGPFEE KIYIQWKPPN ETNGVITLYE INYKAVGSLD PSADLSSQRG 

       550        560        570        580        590        600 
KVFKLRNETH HLFVGLYPGT TYSFTIKAST AKGFGPPVTT RIATKISAPS MPEYDTDTPL 

       610        620        630        640        650        660 
NETDTTITVM LKPAQSRGAP VSVYQLVVKE ERLQKSRRAA DIIECFSVPV SYRNASSLDS 

       670        680        690        700        710        720 
LHYFAAELKP ANLPVTQPFT VGDNKTYNGY WNPPLSPLKS YSIYFQALSK ANGETKINCV 

       730        740        750        760        770        780 
RLATKGASTQ NSNTVEPEKQ VDNTVKMAGV IAGLLMFIII LLGVMLTIKR RRNAYSYSYY 

       790        800        810        820        830        840 
LKLAKKQKET QSGAQREMGP VASADKPTTK LSASRNDEGF SSSSQDVNGF TDGSRGELSQ 

       850        860        870        880        890        900 
PTLTIQTHPY RTCDPVEMSY PRDQFQPAIR VADLLQHITQ MKRGQGYGFK EEYEALPEGQ 

       910        920        930        940        950        960 
TASWDTAKED ENRNKNRYGN IISYDHSRVR LLVLDGDPHS DYINANYIDG YHRPRHYIAT 

       970        980        990       1000       1010       1020 
QGPMQETVKD FWRMIWQENS ASIVMVTNLV EVGRVKCVRY WPDDTEVYGD IKVTLIETEP 

      1030       1040       1050       1060       1070       1080 
LAEYVIRTFT VQKKGYHEIR ELRLFHFTSW PDHGVPCYAT GLLGFVRQVK FLNPPEAGPI 

      1090       1100       1110       1120       1130       1140 
VVHCSAGAGR TGCFIAIDTM LDMAENEGVV DIFNCVRELR AQRVNLVQTE EQYVFVHDAI 

      1150       1160       1170       1180       1190       1200 
LEACLCGNTA IPVCEFRSLY YNISRLDPQT NSSQIKDEFQ TLNIVTPRVR PEDCSIGLLP 

      1210       1220       1230       1240       1250       1260 
RNHDKNRSMD VLPLDRCLPF LISVDGESSN YINAALMDSH KQPAAFVVTQ HPLPNTVADF 

      1270       1280       1290       1300       1310       1320 
WRLVFDYNCS SVVMLNEMDT AQFCMQYWPE KTSGCYGPIQ VEFVSADIDE DIIHRIFRIC 

      1330       1340       1350       1360       1370       1380 
NMARPQDGYR IVQHLQYIGW PAYRDTPPSK RSLLKVVRRL EKWQEQYDGR EGRTVVHCLN 

      1390       1400       1410       1420       1430       1440 
GGGRSGTFCA ICSVCEMIQQ QNIIDVFHIV KTLRNNKSNM VETLEQYKFV YEVALEYLSS 


F 

« Hide

Isoform 1 [UniParc].

Checksum: 531E33DF9040F4B5
Show »

FASTA1,463164,346

References

« Hide 'large scale' references
[1]"Identification and characterization of RPTP rho, a novel RPTP mu/kappa-like receptor protein tyrosine phosphatase whose expression is restricted to the central nervous system."
McAndrew P.E., Frostholm A., White R.A., Rotter A., Burghes A.H.M.
Brain Res. Mol. Brain Res. 56:9-21(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, VARIANT PRO-29.
[2]"Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins."
Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N.
DNA Res. 4:53-59(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT PRO-29.
Tissue: Brain.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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), VARIANT PRO-29.
[5]"Genomic organization and alternative splicing of the human and mouse RPTPrho genes."
Besco J.A., Frostholm A., Popesco M.C., Burghes A.H.M., Rotter A.
BMC Genomics 2:1-1(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[6]Erratum
Besco J.A., Frostholm A., Popesco M.C., Burghes A.H.M., Rotter A.
BMC Genomics 2:5-5(2001) [PubMed] [Europe PMC] [Abstract]
[7]"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 (1.8 ANGSTROMS) OF 868-1151.
[8]"Mutational analysis of the tyrosine phosphatome in colorectal cancers."
Wang Z., Shen D., Parsons D.W., Bardelli A., Sager J., Szabo S., Ptak J., Silliman N., Peters B.A., van der Heijden M.S., Parmigiani G., Yan H., Wang T.-L., Riggins G., Powell S.M., Willson J.K.V., Markowitz S., Kinzler K.W., Vogelstein B., Velculescu V.E.
Science 304:1164-1166(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-74; THR-209; THR-218; SER-248; HIS-280; VAL-395; PHE-412; CYS-453; LYS-510; MET-605; GLY-648; THR-707; VAL-707; PRO-708; ILE-771; GLY-905; LYS-965; PRO-1096; ILE-1106; TRP-1190; LEU-1237; MET-1247; LEU-1324; PHE-1329 AND MET-1346, TISSUE SPECIFICITY.
[9]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. expand/collapse author list , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K.
Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-1213.
[10]"Identification of pathogenic gene variants in small families with intellectually disabled siblings by exome sequencing."
Schuurs-Hoeijmakers J.H., Vulto-van Silfhout A.T., Vissers L.E., van de Vondervoort I.I., van Bon B.W., de Ligt J., Gilissen C., Hehir-Kwa J.Y., Neveling K., del Rosario M., Hira G., Reitano S., Vitello A., Failla P., Greco D., Fichera M., Galesi O., Kleefstra T. expand/collapse author list , Greally M.T., Ockeloen C.W., Willemsen M.H., Bongers E.M., Janssen I.M., Pfundt R., Veltman J.A., Romano C., Willemsen M.A., van Bokhoven H., Brunner H.G., de Vries B.B., de Brouwer A.P.
J. Med. Genet. 50:802-811(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MET-1346.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF043644 mRNA. Translation: AAD09421.2.
AB006621 mRNA. Translation: BAA22952.2. Different initiation.
AL021395 expand/collapse EMBL AC list , AL022239, AL024473, AL031656, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI19981.1.
AL021395 expand/collapse EMBL AC list , AL022239, AL024473, AL031656, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI19983.1. Sequence problems.
AL022239 expand/collapse EMBL AC list , AL021395, AL024473, AL031656, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI20437.1.
AL022239 expand/collapse EMBL AC list , AL021395, AL024473, AL031656, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI20439.1. Sequence problems.
AL024473 expand/collapse EMBL AC list , AL021395, AL022239, AL031656, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI22489.1.
AL024473 expand/collapse EMBL AC list , AL021395, AL022239, AL031656, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI22491.1. Sequence problems.
AL031656 expand/collapse EMBL AC list , AL021395, AL022239, AL024473, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI19877.1.
AL031656 expand/collapse EMBL AC list , AL021395, AL022239, AL024473, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI19879.1. Sequence problems.
AL035459 expand/collapse EMBL AC list , AL021395, AL022239, AL024473, AL031656, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI22909.1.
AL035459 expand/collapse EMBL AC list , AL021395, AL022239, AL024473, AL031656, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI22911.1. Sequence problems.
AL049812 expand/collapse EMBL AC list , AL021395, AL022239, AL024473, AL031656, AL035459, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI19251.1. Sequence problems.
AL049812 expand/collapse EMBL AC list , AL022239, AL031656, AL021395, AL024473, AL035459, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI19253.1.
AL121763 expand/collapse EMBL AC list , AL021395, AL022239, AL024473, AL031656, AL035459, AL049812, AL136461, Z93942 Genomic DNA. Translation: CAI23310.1.
AL121763 expand/collapse EMBL AC list , AL021395, AL022239, AL024473, AL031656, AL035459, AL049812, AL136461, Z93942 Genomic DNA. Translation: CAI23312.1. Sequence problems.
AL136461 expand/collapse EMBL AC list , AL021395, AL022239, AL024473, AL031656, AL035459, AL049812, AL121763, Z93942 Genomic DNA. Translation: CAH72553.1.
AL136461 expand/collapse EMBL AC list , AL021395, AL022239, AL024473, AL031656, AL035459, AL049812, AL121763, Z93942 Genomic DNA. Translation: CAH72555.1. Sequence problems.
Z93942 expand/collapse EMBL AC list , AL021395, AL022239, AL024473, AL031656, AL035459, AL049812, AL121763, AL136461 Genomic DNA. Translation: CAI19865.1.
Z93942 expand/collapse EMBL AC list , AL021395, AL022239, AL024473, AL031656, AL035459, AL049812, AL121763, AL136461 Genomic DNA. Translation: CAI19867.1. Sequence problems.
AL031676 Genomic DNA. No translation available.
AL035666 Genomic DNA. No translation available.
AL109826 Genomic DNA. No translation available.
AL117374 Genomic DNA. No translation available.
AL359695 Genomic DNA. No translation available.
BC153300 mRNA. Translation: AAI53301.1.
RefSeqNP_008981.4. NM_007050.5.
NP_573400.3. NM_133170.3.
UniGeneHs.526879.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OOQX-ray1.80A/B868-1151[»]
ProteinModelPortalO14522.
SMRO14522. Positions 29-591, 866-1441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116296. 1 interaction.
DIPDIP-33967N.
IntActO14522. 12 interactions.
MINTMINT-1350261.

PTM databases

PhosphoSiteO14522.

Proteomic databases

PaxDbO14522.
PRIDEO14522.

Protocols and materials databases

DNASU11122.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373187; ENSP00000362283; ENSG00000196090. [O14522-3]
GeneID11122.
KEGGhsa:11122.
UCSCuc002xkg.3. human. [O14522-3]
uc010ggj.3. human. [O14522-1]

Organism-specific databases

CTD11122.
GeneCardsGC20M040701.
HGNCHGNC:9682. PTPRT.
HPAHPA017336.
MIM608712. gene.
neXtProtNX_O14522.
PharmGKBPA34027.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOVERGENHBG062785.
InParanoidO14522.
KOK13297.
OMATHPYRTC.
OrthoDBEOG70KGNP.
PhylomeDBO14522.
TreeFamTF312900.

Enzyme and pathway databases

SignaLinkO14522.

Gene expression databases

ArrayExpressO14522.
BgeeO14522.
GenevestigatorO14522.

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

EvolutionaryTraceO14522.
GeneWikiPTPRT.
GenomeRNAi11122.
NextBio42270.
PROO14522.
SOURCESearch...

Entry information

Entry namePTPRT_HUMAN
AccessionPrimary (citable) accession number: O14522
Secondary accession number(s): A8E4R6 expand/collapse secondary AC list , O43655, O75664, Q5W0X9, Q5W0Y1, Q9BR24, Q9BR28, Q9H0Y8, Q9NTL1, Q9NU72, Q9UBD2, Q9UJL7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 130 of the entry and version 6 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 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 20

Human chromosome 20: entries, gene names and cross-references to MIM