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P08575 (PTPRC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
T200
CD_antigen=CD45
Gene names
Name:PTPRC
Synonyms:CD45
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1304 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. Dephosphorylates LYN, and thereby modulates LYN activity By similarity. Ref.6 Ref.8

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Binds GANAB and PRKCSH By similarity. Interacts with SKAP1. Interacts with DPP4; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes. Ref.8 Ref.9

Subcellular location

Membrane; Single-pass type I membrane protein. Membrane raft. Note: Colocalized with DPP4 in membrane rafts. Ref.9

Domain

The first PTPase domain interacts with SKAP1.

Post-translational modification

Heavily N- and O-glycosylated.

Involvement in disease

Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID) [MIM:608971]: A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17

Multiple sclerosis (MS) [MIM:126200]: A multifactorial, inflammatory, demyelinating disease of the central nervous system. Sclerotic lesions are characterized by perivascular infiltration of monocytes and lymphocytes and appear as indurated areas in pathologic specimens (sclerosis in plaques). The pathological mechanism is regarded as an autoimmune attack of the myelin sheath, mediated by both cellular and humoral immunity. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia and bladder dysfunction. Genetic and environmental factors influence susceptibility to the disease.
Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry. Ref.16

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.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
SCID
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

B cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

T cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

T cell receptor signaling pathway

Inferred from direct assay PubMed 10358156. Source: UniProtKB

axon guidance

Traceable author statement. Source: Reactome

bone marrow development

Inferred from mutant phenotype PubMed 21911094. Source: UniProtKB

cell cycle phase transition

Inferred from mutant phenotype PubMed 1793833. Source: UniProtKB

cell surface receptor signaling pathway

Traceable author statement Ref.6. Source: ProtInc

defense response to virus

Inferred from sequence or structural similarity. Source: UniProtKB

dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

hematopoietic progenitor cell differentiation

Inferred from mutant phenotype PubMed 21911094. Source: UniProtKB

immunoglobulin biosynthetic process

Inferred from mutant phenotype PubMed 1793833. Source: UniProtKB

negative regulation of T cell mediated cytotoxicity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell adhesion involved in substrate-bound cell migration

Inferred from mutant phenotype PubMed 21911094. Source: UniProtKB

negative regulation of cytokine-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein kinase activity

Inferred from direct assay PubMed 9197241. Source: UniProtKB

peptidyl-tyrosine dephosphorylation

Inferred from direct assay PubMed 2853967. Source: GOC

positive regulation of B cell proliferation

Inferred from mutant phenotype PubMed 1793833. Source: UniProtKB

positive regulation of T cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of antigen receptor-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of hematopoietic stem cell migration

Inferred from mutant phenotype PubMed 21911094. Source: UniProtKB

positive regulation of protein kinase activity

Non-traceable author statement PubMed 15275963. Source: UniProtKB

positive regulation of stem cell proliferation

Inferred from mutant phenotype PubMed 21911094. Source: UniProtKB

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

stem cell development

Inferred from mutant phenotype PubMed 21911094. Source: UniProtKB

   Cellular_componentexternal side of plasma membrane

Inferred from direct assay PubMed 17213291. Source: MGI

extracellular vesicular exosome

Inferred from direct assay PubMed 12519789PubMed 20458337. Source: UniProt

focal adhesion

Inferred from sequence or structural similarity. 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

Traceable author statement. Source: Reactome

   Molecular_functionprotein kinase binding

Inferred from physical interaction PubMed 14625311. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay PubMed 2853967. Source: UniProtKB

transmembrane receptor protein tyrosine phosphatase activity

Traceable author statement Ref.6. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: At least 8 isoforms are produced.
Isoform 1 (identifier: P08575-1)

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: P08575-2)

The sequence of this isoform differs from the canonical sequence as follows:
     32-192: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 13041281Receptor-type tyrosine-protein phosphatase C
PRO_0000025470

Regions

Topological domain24 – 575552Extracellular Potential
Transmembrane576 – 59722Helical; Potential
Topological domain598 – 1304707Cytoplasmic Potential
Domain389 – 48193Fibronectin type-III 1
Domain482 – 57493Fibronectin type-III 2
Domain651 – 910260Tyrosine-protein phosphatase 1
Domain942 – 1226285Tyrosine-protein phosphatase 2
Region851 – 8577Substrate binding By similarity

Sites

Active site8511Phosphocysteine intermediate
Active site11671Phosphocysteine intermediate By similarity
Binding site8191Substrate By similarity
Binding site8951Substrate By similarity

Amino acid modifications

Modified residue9731Phosphoserine Ref.10 Ref.13
Modified residue12971Phosphoserine Ref.13
Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation901N-linked (GlcNAc...) Potential
Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation2321N-linked (GlcNAc...) Ref.11 Ref.12
Glycosylation2401N-linked (GlcNAc...); atypical Ref.12
Glycosylation2601N-linked (GlcNAc...) Potential
Glycosylation2701N-linked (GlcNAc...) Potential
Glycosylation2761N-linked (GlcNAc...) Ref.12
Glycosylation2841N-linked (GlcNAc...); atypical Ref.12
Glycosylation3351N-linked (GlcNAc...) Ref.11 Ref.12
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation4191N-linked (GlcNAc...) Ref.12
Glycosylation4681N-linked (GlcNAc...) Potential
Glycosylation4881N-linked (GlcNAc...) Ref.12
Glycosylation4971N-linked (GlcNAc...); atypical Ref.12
Glycosylation5291N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence32 – 192161Missing in isoform 2.
VSP_007780
Natural variant1911T → A.
Corresponds to variant rs4915154 [ dbSNP | Ensembl ].
VAR_036860
Natural variant2281E → A in a breast cancer sample; somatic mutation. Ref.18
VAR_035653
Natural variant2941I → L.
Corresponds to variant rs2230606 [ dbSNP | Ensembl ].
VAR_051763
Natural variant362 – 3632Missing in T(-)B(+)NK(+) SCID; associated with lack of surface expression.
VAR_021205
Natural variant4211T → I.
Corresponds to variant rs6696162 [ dbSNP | Ensembl ].
VAR_051764
Natural variant5681H → Q.
Corresponds to variant rs12136658 [ dbSNP | Ensembl ].
VAR_051765
Natural variant8631G → R in a breast cancer sample; somatic mutation. Ref.18
VAR_035654
Natural variant12831S → R.
Corresponds to variant rs2298872 [ dbSNP | Ensembl ].
VAR_020303

Experimental info

Mutagenesis8511C → S: Loss of activity. Abolishes interaction with SKAP1. Ref.8
Sequence conflict6501L → P in CAA68669. Ref.1
Sequence conflict12071P → L in CAA68669. Ref.1

Secondary structure

................................................................................................... 1304
Helix Strand Turn

Details...

Sequences

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

Last modified July 19, 2003. Version 2.
Checksum: A08FC22D6069BAF7

FASTA1,304147,254
        10         20         30         40         50         60 
MYLWLKLLAF GFAFLDTEVF VTGQSPTPSP TGLTTAKMPS VPLSSDPLPT HTTAFSPAST 

        70         80         90        100        110        120 
FERENDFSET TTSLSPDNTS TQVSPDSLDN ASAFNTTGVS SVQTPHLPTH ADSQTPSAGT 

       130        140        150        160        170        180 
DTQTFSGSAA NAKLNPTPGS NAISDVPGER STASTFPTDP VSPLTTTLSL AHHSSAALPA 

       190        200        210        220        230        240 
RTSNTTITAN TSDAYLNASE TTTLSPSGSA VISTTTIATT PSKPTCDEKY ANITVDYLYN 

       250        260        270        280        290        300 
KETKLFTAKL NVNENVECGN NTCTNNEVHN LTECKNASVS ISHNSCTAPD KTLILDVPPG 

       310        320        330        340        350        360 
VEKFQLHDCT QVEKADTTIC LKWKNIETFT CDTQNITYRF QCGNMIFDNK EIKLENLEPE 

       370        380        390        400        410        420 
HEYKCDSEIL YNNHKFTNAS KIIKTDFGSP GEPQIIFCRS EAAHQGVITW NPPQRSFHNF 

       430        440        450        460        470        480 
TLCYIKETEK DCLNLDKNLI KYDLQNLKPY TKYVLSLHAY IIAKVQRNGS AAMCHFTTKS 

       490        500        510        520        530        540 
APPSQVWNMT VSMTSDNSMH VKCRPPRDRN GPHERYHLEV EAGNTLVRNE SHKNCDFRVK 

       550        560        570        580        590        600 
DLQYSTDYTF KAYFHNGDYP GEPFILHHST SYNSKALIAF LAFLIIVTSI ALLVVLYKIY 

       610        620        630        640        650        660 
DLHKKRSCNL DEQQELVERD DEKQLMNVEP IHADILLETY KRKIADEGRL FLAEFQSIPR 

       670        680        690        700        710        720 
VFSKFPIKEA RKPFNQNKNR YVDILPYDYN RVELSEINGD AGSNYINASY IDGFKEPRKY 

       730        740        750        760        770        780 
IAAQGPRDET VDDFWRMIWE QKATVIVMVT RCEEGNRNKC AEYWPSMEEG TRAFGDVVVK 

       790        800        810        820        830        840 
INQHKRCPDY IIQKLNIVNK KEKATGREVT HIQFTSWPDH GVPEDPHLLL KLRRRVNAFS 

       850        860        870        880        890        900 
NFFSGPIVVH CSAGVGRTGT YIGIDAMLEG LEAENKVDVY GYVVKLRRQR CLMVQVEAQY 

       910        920        930        940        950        960 
ILIHQALVEY NQFGETEVNL SELHPYLHNM KKRDPPSEPS PLEAEFQRLP SYRSWRTQHI 

       970        980        990       1000       1010       1020 
GNQEENKSKN RNSNVIPYDY NRVPLKHELE MSKESEHDSD ESSDDDSDSE EPSKYINASF 

      1030       1040       1050       1060       1070       1080 
IMSYWKPEVM IAAQGPLKET IGDFWQMIFQ RKVKVIVMLT ELKHGDQEIC AQYWGEGKQT 

      1090       1100       1110       1120       1130       1140 
YGDIEVDLKD TDKSSTYTLR VFELRHSKRK DSRTVYQYQY TNWSVEQLPA EPKELISMIQ 

      1150       1160       1170       1180       1190       1200 
VVKQKLPQKN SSEGNKHHKS TPLLIHCRDG SQQTGIFCAL LNLLESAETE EVVDIFQVVK 

      1210       1220       1230       1240       1250       1260 
ALRKARPGMV STFEQYQFLY DVIASTYPAQ NGQVKKNNHQ EDKIEFDNEV DKVKQDANCV 

      1270       1280       1290       1300 
NPLGAPEKLP EAKEQAEGSE PTSGTEGPEH SVNGPASPAL NQGS 

« Hide

Isoform 2 [UniParc].

Checksum: DB4B4400F3602B3C
Show »

FASTA1,143130,898

References

« Hide 'large scale' references
[1]"Differential usage of three exons generates at least five different mRNAs encoding human leukocyte common antigens."
Streuli M., Hall L.R., Saga Y., Schlossman S.F., Saito H.
J. Exp. Med. 166:1548-1566(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
Tissue: Lymphocyte.
[2]"Structural variants of human T200 glycoprotein (leukocyte-common antigen)."
Ralph S.J., Thomas M.L., Morton C.C., Trowbridge I.S.
EMBO J. 6:1251-1257(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Synovium.
[4]"Integrity of the exon 6 sequence is essential for tissue-specific alternative splicing of human leukocyte common antigen pre-mRNA."
Tsai A.Y.M., Streuli M., Saito H.
Mol. Cell. Biol. 9:4550-4555(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-192.
[5]"Complete exon-intron organization of the human leukocyte common antigen (CD45) gene."
Hall L.R., Streuli M., Schlossman S.F., Saito H.
J. Immunol. 141:2781-2787(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-1304.
Tissue: Placenta.
[6]"The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase."
Charbonneau H., Tonks N.K., Walsh K.A., Fischer E.H.
Proc. Natl. Acad. Sci. U.S.A. 85:7182-7186(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR."
Streuli M., Krueger N.X., Thai T., Tang M., Saito H.
EMBO J. 9:2399-2407(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[8]"SKAP55 coupled with CD45 positively regulates T-cell receptor-mediated gene transcription."
Wu L., Fu J., Shen S.-H.
Mol. Cell. Biol. 22:2673-2686(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP1, MUTAGENESIS OF CYS-851, FUNCTION.
[9]"A role for interleukin-12 in the regulation of T cell plasma membrane compartmentation."
Salgado F.J., Lojo J., Alonso-Lebrero J.L., Lluis C., Franco R., Cordero O.J., Nogueira M.
J. Biol. Chem. 278:24849-24857(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DPP4, SUBCELLULAR LOCATION.
[10]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[11]"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-232 AND ASN-335.
Tissue: Liver.
[12]"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-232; ASN-240; ASN-276; ASN-284; ASN-335; ASN-419; ASN-488 AND ASN-497.
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973 AND SER-1297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45."
Nam H.J., Poy F., Saito H., Frederick C.A.
J. Exp. Med. 201:441-452(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 622-1231 ALONE AND IN COMPLEX WITH PHOSPHOPEPTIDE.
[16]"A point mutation in PTPRC is associated with the development of multiple sclerosis."
Jacobsen M., Schweer D., Ziegler A., Gaber R., Schock S., Schwinzer R., Wonigeit K., Lindert R.-B., Kantarci O., Schaefer-Klein J., Schipper H.I., Oertel W.H., Heidenreich F., Weinshenker B.G., Sommer N., Hemmer B.
Nat. Genet. 26:495-499(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO MS.
[17]"A deletion in the gene encoding the CD45 antigen in a patient with SCID."
Tchilian E.Z., Wallace D.L., Wells R.S., Flower D.R., Morgan G., Beverley P.C.L.
J. Immunol. 166:1308-1313(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT T(-)B(+)NK(+) SCID 362-GLU-TYR-363 DEL, CHARACTERIZATION OF VARIANT T(-)B(+)NK(+) SCID 362-GLU-TYR-363 DEL.
[18]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-228 AND ARG-863.
+Additional computationally mapped references.

Web resources

PTPRCbase

PTPRC mutation db

Wikipedia

CD45 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00638 mRNA. Translation: CAA68669.1.
Y00062 mRNA. Translation: CAA68269.1.
AK292131 mRNA. Translation: BAF84820.1.
M23492 expand/collapse EMBL AC list , M23496, M23466, M23467, M23468, M23469, M23470, M23471, M23472, M23473, M23474, M23475, M23476, M23477, M23478, M23479, M23480, M23481, M23482, M23483, M23484, M23485, M23486, M23487, M23488, M23489, M23490, M23491 Genomic DNA. Translation: AAD15273.2.
PIRA46546.
RefSeqNP_002829.3. NM_002838.4.
NP_563578.2. NM_080921.3.
UniGeneHs.654514.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YGRX-ray2.90A/B622-1231[»]
1YGUX-ray2.90A/B622-1231[»]
ProteinModelPortalP08575.
SMRP08575. Positions 349-462, 623-1228.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111752. 24 interactions.
DIPDIP-224N.
IntActP08575. 39 interactions.
MINTMINT-1130341.
STRING9606.ENSP00000356346.

Chemistry

BindingDBP08575.
ChEMBLCHEMBL3243.
GuidetoPHARMACOLOGY1852.

PTM databases

PhosphoSiteP08575.
UniCarbKBP08575.

Polymorphism databases

DMDM33112650.

Proteomic databases

PaxDbP08575.
PRIDEP08575.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367376; ENSP00000356346; ENSG00000081237. [P08575-1]
ENST00000573477; ENSP00000461074; ENSG00000262418. [P08575-2]
ENST00000573679; ENSP00000458322; ENSG00000262418. [P08575-1]
ENST00000594404; ENSP00000471843; ENSG00000081237. [P08575-2]
GeneID5788.
KEGGhsa:5788.

Organism-specific databases

CTD5788.
GeneCardsGC01P198607.
HGNCHGNC:9666. PTPRC.
HPACAB000052.
CAB002800.
CAB056154.
HPA000440.
MIM126200. phenotype.
151460. gene.
608971. phenotype.
neXtProtNX_P08575.
Orphanet169157. T-B+ severe combined immunodeficiency due to CD45 deficiency.
PharmGKBPA34011.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000049064.
HOVERGENHBG000066.
InParanoidP08575.
KOK06478.
OMAEPEHSAN.
PhylomeDBP08575.
TreeFamTF351829.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_6900. Immune System.
SignaLinkP08575.

Gene expression databases

ArrayExpressP08575.
BgeeP08575.
CleanExHS_PTPRC.
GenevestigatorP08575.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR016335. Leukocyte_common_ag.
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.
PF00041. fn3. 2 hits.
PF12453. PTP_N. 2 hits.
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. 1 hit.
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

ChiTaRSPTPRC. human.
EvolutionaryTraceP08575.
GeneWikiPTPRC.
GenomeRNAi5788.
NextBio22518.
PROP08575.
SOURCESearch...

Entry information

Entry namePTPRC_HUMAN
AccessionPrimary (citable) accession number: P08575
Secondary accession number(s): A8K7W6, Q16614, Q9H0Y6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 19, 2003
Last modified: April 16, 2014
This is version 170 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human 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 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries