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P06800 (PTPRC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 C

EC=3.1.3.48
Alternative name(s):
Leukocyte common antigen
Short name=L-CA
Lymphocyte antigen 5
Short name=Ly-5
T200
CD_antigen=CD45
Gene names
Name:Ptprc
Synonyms:Ly-5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1291 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN By similarity. Dephosphorylates LYN, and thereby modulates LYN activity. Ref.14

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with SKAP1. Interacts with DPP4; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes By similarity. Binds GANAB and PRKCSH. Ref.13

Subcellular location

Membrane; Single-pass type I membrane protein. Membrane raft By similarity. Note: Colocalized with DPP4 in membrane rafts By similarity.

Developmental stage

Expression is restricted to the hematopoietic compartment of development.

Domain

The first PTPase domain interacts with SKAP1 By similarity.

Post-translational modification

Heavily N- and O-glycosylated.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 1/6 subfamily.

Contains 2 fibronectin type-III domains.

Contains 2 tyrosine-protein phosphatase domains.

Sequence caution

The sequence AAA39462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from mutant phenotype PubMed 12902479. Source: MGI

B cell proliferation

Inferred from mutant phenotype PubMed 8334701. Source: UniProtKB

B cell receptor signaling pathway

Inferred from mutant phenotype PubMed 8692271. Source: UniProtKB

T cell differentiation

Inferred from mutant phenotype PubMed 8334701. Source: UniProtKB

T cell proliferation

Inferred from mutant phenotype PubMed 12902479. Source: MGI

T cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

activation of MAPK activity

Inferred from mutant phenotype PubMed 9254656. Source: MGI

defense response to virus

Inferred from mutant phenotype PubMed 8334701. Source: UniProtKB

dephosphorylation

Inferred from direct assay PubMed 11201744. Source: UniProtKB

heterotypic cell-cell adhesion

Inferred from mutant phenotype PubMed 7743522. Source: MGI

leukocyte cell-cell adhesion

Inferred from mutant phenotype PubMed 7743522. Source: MGI

negative regulation of T cell mediated cytotoxicity

Inferred from mutant phenotype PubMed 9725213. Source: UniProtKB

negative regulation of cytokine-mediated signaling pathway

Inferred from direct assay PubMed 11201744. Source: UniProtKB

negative regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 7499277PubMed 8175795. Source: MGI

negative regulation of protein autophosphorylation

Inferred from mutant phenotype PubMed 7499277PubMed 8175795. Source: MGI

negative regulation of protein kinase activity

Inferred from direct assay PubMed 10970857. Source: UniProtKB

negative thymic T cell selection

Inferred from mutant phenotype PubMed 8666928. Source: MGI

peptidyl-tyrosine dephosphorylation

Inferred from direct assay PubMed 7743522PubMed 8566025. Source: GOC

positive regulation of B cell proliferation

Inferred from mutant phenotype PubMed 8566034PubMed 8666928PubMed 9015183PubMed 9254656. Source: MGI

positive regulation of MAPK cascade

Inferred from mutant phenotype PubMed 9254656. Source: MGI

positive regulation of T cell differentiation

Inferred from mutant phenotype PubMed 8666928. Source: MGI

positive regulation of T cell mediated cytotoxicity

Inferred from mutant phenotype PubMed 6233370. Source: MGI

positive regulation of T cell mediated immunity

Inferred from mutant phenotype PubMed 6233370PubMed 8566034. Source: MGI

positive regulation of T cell proliferation

Inferred from mutant phenotype PubMed 8334701. Source: UniProtKB

positive regulation of alpha-beta T cell proliferation

Inferred from mutant phenotype PubMed 7751624. Source: MGI

positive regulation of antigen receptor-mediated signaling pathway

Inferred from mutant phenotype PubMed 8692271. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 8666928. Source: MGI

positive regulation of gamma-delta T cell differentiation

Inferred from mutant phenotype PubMed 7807014. Source: MGI

positive regulation of humoral immune response mediated by circulating immunoglobulin

Inferred from mutant phenotype PubMed 8566034. Source: MGI

positive regulation of isotype switching to IgG isotypes

Inferred from mutant phenotype PubMed 9015183. Source: MGI

positive thymic T cell selection

Inferred from mutant phenotype PubMed 8666928. Source: MGI

protein dephosphorylation

Inferred from direct assay PubMed 9197241. Source: UniProtKB

regulation of B cell differentiation

Inferred from mutant phenotype PubMed 8666928PubMed 9254656. Source: MGI

regulation of B cell receptor signaling pathway

Inferred from mutant phenotype PubMed 7499277. Source: MGI

regulation of cell cycle

Inferred from direct assay PubMed 10970857. Source: UniProtKB

regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 7743522. Source: MGI

regulation of humoral immune response mediated by circulating immunoglobulin

Inferred from mutant phenotype PubMed 9015183. Source: MGI

release of sequestered calcium ion into cytosol

Inferred from direct assay PubMed 10508267. Source: UniProtKB

   Cellular_componentcell periphery

Inferred from direct assay PubMed 22072979. Source: MGI

external side of plasma membrane

Inferred from direct assay PubMed 10848813PubMed 10943842PubMed 11466198PubMed 12714519PubMed 12900455PubMed 14609575PubMed 14990792PubMed 15240667PubMed 15795238PubMed 15845452PubMed 15909309PubMed 16287714PubMed 16455951PubMed 16493007PubMed 17277142PubMed 17941951PubMed 18628982PubMed 18762567PubMed 19015308PubMed 19838199PubMed 19934022PubMed 20660734PubMed 20709950PubMed 21460847PubMed 21606356PubMed 24029230PubMed 61878PubMed 6610701PubMed 7477352PubMed 7477353PubMed 7589135PubMed 7630421PubMed 7688139PubMed 7751624PubMed 8041705PubMed 8043862PubMed 8552190PubMed 8566025PubMed 8666928PubMed 8788039PubMed 9208839. Source: MGI

focal adhesion

Inferred from direct assay PubMed 9197241. Source: UniProtKB

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 15128768. Source: MGI

   Molecular_functionheparan sulfate proteoglycan binding

Inferred from direct assay PubMed 8043862. Source: MGI

heparin binding

Inferred from direct assay PubMed 8043862. Source: MGI

protein binding

Inferred from physical interaction PubMed 10330160PubMed 8570203PubMed 9581568. Source: IntAct

protein kinase binding

Inferred from physical interaction PubMed 11201744. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LckP062403EBI-1672,EBI-1401

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06800-1)

Also known as: B220;

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: P06800-2)

The sequence of this isoform differs from the canonical sequence as follows:
     31-73: Missing.
Isoform 3 (identifier: P06800-3)

The sequence of this isoform differs from the canonical sequence as follows:
     31-169: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 12911268Receptor-type tyrosine-protein phosphatase C
PRO_0000025471

Regions

Topological domain24 – 564541Extracellular Potential
Transmembrane565 – 58622Helical; Potential
Topological domain587 – 1291705Cytoplasmic Potential
Domain374 – 47097Fibronectin type-III 1
Domain471 – 56696Fibronectin type-III 2
Domain640 – 899260Tyrosine-protein phosphatase 1
Domain931 – 1214284Tyrosine-protein phosphatase 2
Region840 – 8467Substrate binding By similarity

Sites

Active site8401Phosphocysteine intermediate By similarity
Active site11551Phosphocysteine intermediate By similarity
Binding site8081Substrate By similarity
Binding site8841Substrate By similarity

Amino acid modifications

Modified residue9621Phosphoserine Ref.15
Modified residue12841Phosphoserine By similarity
Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation1501N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2111N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation3111N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential
Glycosylation4161N-linked (GlcNAc...) Potential
Glycosylation4271N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Glycosylation4891N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence31 – 169139Missing in isoform 3.
VSP_012442
Alternative sequence31 – 7343Missing in isoform 2.
VSP_012441

Experimental info

Sequence conflict3001K → E in AAA39459. Ref.3
Sequence conflict3981V → A in AAA39459. Ref.3
Sequence conflict402 – 4032ES → DP in AAA39459. Ref.3
Sequence conflict4761N → T in AAA39459. Ref.3
Sequence conflict518 – 5203KYN → NTT in AAA39458. Ref.1
Sequence conflict5281V → G in AAA39458. Ref.1
Sequence conflict5561N → S in AAA39458. Ref.1
Sequence conflict5881I → S in AAA39458. Ref.1
Sequence conflict9061E → Q in AAA39458. Ref.1
Sequence conflict9311L → R in AAA39458. Ref.1
Sequence conflict9531E → G in AAA39458. Ref.1
Sequence conflict9591N → K in AAA39458. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (B220) [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: ED752FD195BA9643

FASTA1,291144,604
        10         20         30         40         50         60 
MGLWLKLLAF GFALLDTEVF VTGQTPTPSD ELSTTENALL LPQSDPLPAR TTESTPPSIS 

        70         80         90        100        110        120 
ERGNGSSETT YHPGVLSTLL PHLSPQPDSQ TPSAGGADTQ TFSSQADNPT LTPAPGGGTD 

       130        140        150        160        170        180 
PPGVPGERTV PGTIPADTAF PVDTPSLARN SSAASPTHTS NVSTTDISSG ASLTTLTPST 

       190        200        210        220        230        240 
LGLASTDPPS TTIATTTKQT CAAMFGNITV NYTYESSNQT FKADLKDVQN AKCGNEDCEN 

       250        260        270        280        290        300 
VLNNLEECSQ IKNISVSNDS CAPATTIDLY VPPGTDKFSL HDCTPKEKAN TSICLEWKTK 

       310        320        330        340        350        360 
NLDFRKCNSD NISYVLHCEP ENNTKCIRRN TFIPERCQLD NLRAQTNYTC VAEILYRGVK 

       370        380        390        400        410        420 
LVKNVINVQT DLGIPETPKP SCGDPAARKT LVSWPEPVSK PESASKPHGY VLCYKNNSEK 

       430        440        450        460        470        480 
CKSLPNNVTS FEVESLKPYK YYEVSLLAYV NGKIQRNGTA EKCNFHTKAD RPDKVNGMKT 

       490        500        510        520        530        540 
SRPTDNSINV TCGPPYETNG PKTFYILVVR SGGSFVTKYN KTNCQFYVDN LYYSTDYEFL 

       550        560        570        580        590        600 
VSFHNGVYEG DSVIRNESTN FNAKALIIFL VFLIIVTSIA LLVVLYKIYD LRKKRSSNLD 

       610        620        630        640        650        660 
EQQELVERDD EKQLMDVEPI HSDILLETYK RKIADEGRLF LAEFQSIPRV FSKFPIKDAR 

       670        680        690        700        710        720 
KPHNQNKNRY VDILPYDYNR VELSEINGDA GSTYINASYI DGFKEPRKYI AAQGPRDETV 

       730        740        750        760        770        780 
DDFWRMIWEQ KATVIVMVTR CEEGNRNKCA EYWPSMEEGT RAFKDIVVTI NDHKRCPDYI 

       790        800        810        820        830        840 
IQKLNVAHKK EKATGREVTH IQFTSWPDHG VPEDPHLLLK LRRRVNAFSN FFSGPIVVHC 

       850        860        870        880        890        900 
SAGVGRTGTY IGIDAMLEGL EAEGKVDVYG YVVKLRRQRC LMVQVEAQYI LIHQALVEYN 

       910        920        930        940        950        960 
QFGETEVNLS ELHSCLHNMK KRDPPSDPSP LEAEYQRLPS YRSWRTQHIG NQEENKKKNR 

       970        980        990       1000       1010       1020 
NSNVVPYDFN RVPLKHELEM SKESEPESDE SSDDDSDSEE TSKYINASFV MSYWKPEMMI 

      1030       1040       1050       1060       1070       1080 
AAQGPLKETI GDFWQMIFQR KVKVIVMLTE LVNGDQEVCA QYWGEGKQTY GDMEVEMKDT 

      1090       1100       1110       1120       1130       1140 
NRASAYTLRT FELRHSKRKE PRTVYQYQCT TWKGEELPAE PKDLVSMIQD LKQKLPKASP 

      1150       1160       1170       1180       1190       1200 
EGMKYHKHAS ILVHCRDGSQ QTGLFCALFN LLESAETEDV VDVFQVVKSL RKARPGVVCS 

      1210       1220       1230       1240       1250       1260 
YEQYQFLYDI IASIYPAQNG QVKKTNSQDK IEFHNEVDGG KQDANCVRPD GPLNKAQEDS 

      1270       1280       1290 
RGVGTPEPTN SAEEPEHAAN GSASPAPTQS S 

« Hide

Isoform 2 [UniParc].

Checksum: D08281C0463EA174
Show »

FASTA1,248140,040
Isoform 3 [UniParc].

Checksum: F1AA6650E654CAAB
Show »

FASTA1,152130,622

References

« Hide 'large scale' references
[1]"Sequences of Ly-5 cDNA: isoform-related diversity of Ly-5 mRNA."
Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.
Proc. Natl. Acad. Sci. U.S.A. 83:6940-6944(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[2]Erratum
Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.
Proc. Natl. Acad. Sci. U.S.A. 84:1991-1991(1987)
Cited for: SEQUENCE REVISION.
[3]"Comparison of mouse Ly5a and Ly5b leucocyte common antigen alleles."
Zebedee S.L., Barritt D.S., Raschke W.C.
Dev. Immunol. 1:243-254(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: BALB/c.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"Alternative use of 5' exons in the specification of Ly-5 isoforms distinguishing hematopoietic cell lineages."
Saga Y., Tung J.-S., Shen F.-W.W., Boyse E.A.
Proc. Natl. Acad. Sci. U.S.A. 84:5364-5368(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-226 (ISOFORM 2).
[6]"Organization of the Ly-5 gene."
Saga Y., Tung J.-S., Shen F.-W.W., Pancoast T.C., Boyse E.A.
Mol. Cell. Biol. 8:4889-4895(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[7]"Sequence conservation in potential regulatory regions of the mouse and human leukocyte common antigen gene."
Johnson N.A., Meyer C.M., Pingel J.T., Thomas M.L.
J. Biol. Chem. 264:6220-6229(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[8]"Cloning of Ly-5 cDNA."
Shen F.-W., Saga Y., Litman G., Freeman G., Tung J.-S., Cantor H., Boyse E.A.
Proc. Natl. Acad. Sci. U.S.A. 82:7360-7363(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-263 (ISOFORM 3).
Tissue: T-cell.
[9]"Structural features of Ly-5 glycoproteins of the mouse and counterparts in other mammals."
Tung J.-S., Saga Y., Boyse E.A.
Immunogenetics 28:271-277(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-73.
[10]"Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification."
Yi T., Cleveland J.L., Ihle J.N.
Blood 78:2222-2228(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 730-838.
[11]"Cloned murine T200 (Ly-5) cDNA reveals multiple transcripts within B- and T-lymphocyte lineages."
Raschke W.C.
Proc. Natl. Acad. Sci. U.S.A. 84:161-165(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 961-1291.
[12]"High sequence conservation between rat (T200) and mouse (Ly-5) leukocyte common antigens."
Gonez L.J., Walker I.D., Sandrin M.S., McKenzie I.F.
Immunogenetics 25:263-266(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[13]"Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II."
Arendt C.W., Ostergaard H.L.
J. Biol. Chem. 272:13117-13125(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GANAB AND PRKCSH.
[14]"CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells."
Katagiri T., Ogimoto M., Hasegawa K., Arimura Y., Mitomo K., Okada M., Clark M.R., Mizuno K., Yakura H.
J. Immunol. 163:1321-1326(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14342 mRNA. Translation: AAA39458.1.
M92933 mRNA. Translation: AAA39459.1.
AC122903 Genomic DNA. No translation available.
AC159278 Genomic DNA. No translation available.
M17320 mRNA. Translation: AAA60449.1.
M23354 Genomic DNA. Translation: AAA39462.1. Different initiation.
M22456 Genomic DNA. Translation: AAB46374.1.
M11934 mRNA. Translation: AAA39461.1.
M23241 Genomic DNA. Translation: AAA39460.1.
M15174 mRNA. Translation: AAA40161.1.
PIRA23329.
A28334.
A28335.
I57644.
UniGeneMm.391573.

3D structure databases

ProteinModelPortalP06800.
SMRP06800. Positions 612-1216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202493. 3 interactions.
IntActP06800. 8 interactions.
MINTMINT-188397.
STRING10090.ENSMUSP00000074352.

Chemistry

GuidetoPHARMACOLOGY1852.

PTM databases

PhosphoSiteP06800.

Proteomic databases

MaxQBP06800.
PaxDbP06800.
PRIDEP06800.

Protocols and materials databases

DNASU19264.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027645; ENSMUSP00000027645; ENSMUSG00000026395. [P06800-1]
ENSMUST00000112036; ENSMUSP00000107667; ENSMUSG00000026395. [P06800-3]
UCSCuc007cvf.2. mouse. [P06800-1]
uc007cvh.2. mouse. [P06800-3]

Organism-specific databases

MGIMGI:97810. Ptprc.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00680000099951.
HOVERGENHBG000066.
OrthoDBEOG7XSTCW.
TreeFamTF351829.

Gene expression databases

ArrayExpressP06800.
BgeeP06800.
CleanExMM_PTPRC.
GenevestigatorP06800.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
3.90.190.10. 2 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR016335. Leukocyte_common_ag.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR024739. PTP_recept_N.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF12567. CD45. 1 hit.
PF12453. PTP_N. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PIRSFPIRSF002004. Leukocyte_common_antigen. 1 hit.
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 2 hits.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
SSF52799. SSF52799. 2 hits.
PROSITEPS50853. FN3. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio296132.
PROP06800.
SOURCESearch...

Entry information

Entry namePTPRC_MOUSE
AccessionPrimary (citable) accession number: P06800
Secondary accession number(s): E9QLT5 expand/collapse secondary AC list , Q61812, Q61813, Q61814, Q61815, Q78EF1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot