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Reviewed, UniProtKB/Swiss-Prot P08575 (CD45_HUMAN)

Last modified February 9, 2010. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Leukocyte common antigen
      Short name=L-CA
    EC=3.1.3.48
Alternative name(s):
    T200
    CD_antigen=CD45
Gene names
Name: PTPRC
Synonyms: CD45
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length1304 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Acts as a positive regulator of T-cell coactivation, by binding DPP4. Required for T-cell activation through the antigen receptor. 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 an dephosphorylates SKAP1 and FYN.

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

Subcellular location

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

Domain

The first PTPase domain interacts with SKAP1.

Post-translational modification

Heavily N- and O-glycosylated. Ref.13 Ref.14

Involvement in disease

Defects in PTPRC are a cause of 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. Ref.18

Genetic variations in PTPRC are involved in multiple sclerosis susceptibility (MS) [MIM:126200]. MS is a neurodegenerative disorder characterized by the gradual accumulation of focal plaques of demyelination particularly in the periventricular areas of the brain. Peripheral nerves are not affected. Onset usually in third or fourth decade with intermittent progression over an extended period. The cause is still uncertain. Ref.17

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.

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Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
SCID
   DomainRepeat
Signal
Transmembrane
   Molecular functionHydrolase
Protein phosphatase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete 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 receptor signaling pathway

Inferred from direct assay. Source: UniProtKB

defense response to virus

Inferred from sequence or structural similarity. Source: UniProtKB

immunoglobulin biosynthetic process

Inferred from mutant phenotype. Source: UniProtKB

negative regulation of T cell mediated cytotoxicity

Inferred from sequence or structural similarity. 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. Source: UniProtKB

positive regulation of B cell proliferation

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of antigen receptor-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

protein amino acid dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of S phase

Inferred from mutant phenotype. Source: UniProtKB

release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentfocal adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

integral to plasma membrane Ref.2

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionprotein kinase binding

Inferred from physical interaction. Source: UniProtKB

transmembrane receptor protein tyrosine phosphatase activity Ref.6

Traceable author statement. Source: ProtInc

Complete GO annotation...

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 13041281Leukocyte common antigen
PRO_0000025470

Regions

Topological domain24 – 575552Extracellular Potential
Transmembrane576 – 59722 Potential
Topological domain598 – 1304707Cytoplasmic Potential
Domain390 – 47889Fibronectin type-III 1
Domain482 – 57089Fibronectin type-III 2
Domain651 – 910260Tyrosine-protein phosphatase 1
Domain942 – 1226285Tyrosine-protein phosphatase 2

Sites

Active site8511Phosphocysteine intermediate
Active site11671Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue9511Phosphoserine By similarity
Modified residue9731Phosphoserine Ref.11 Ref.15
Modified residue9951Phosphoserine Ref.10
Modified residue10031Phosphoserine Ref.10
Modified residue10071Phosphoserine Ref.10
Modified residue12971Phosphoserine Ref.15
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.13 Ref.14
Glycosylation2401N-linked (GlcNAc...) Ref.14
Glycosylation2601N-linked (GlcNAc...) Potential
Glycosylation2701N-linked (GlcNAc...) Potential
Glycosylation2761N-linked (GlcNAc...) Ref.14
Glycosylation2841N-linked (GlcNAc...) Ref.14
Glycosylation3351N-linked (GlcNAc...) Ref.13 Ref.14
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation4191N-linked (GlcNAc...) Ref.14
Glycosylation4681N-linked (GlcNAc...) Potential
Glycosylation4881N-linked (GlcNAc...) Ref.14
Glycosylation4971N-linked (GlcNAc...) Ref.14
Glycosylation5291N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence32 – 192161Missing in isoform 2.
VSP_007780
Natural variant1911T → A: dbSNP rs4915154.
VAR_036860
Natural variant2281E → A in a breast cancer sample; somatic mutation. Ref.19
VAR_035653
Natural variant2941I → L: dbSNP rs2230606.
VAR_051763
Natural variant362 – 3632Missing in T(-)B(+)NK(+) SCID; associated with lack of surface expression.
VAR_021205
Natural variant4211T → I: dbSNP rs6696162.
VAR_051764
Natural variant5681H → Q: dbSNP rs12136658.
VAR_051765
Natural variant8631G → R in a breast cancer sample; somatic mutation. Ref.19
VAR_035654
Natural variant12831S → R: dbSNP rs2298872.
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

1 ................................................................................................... 1304
Helix Strand Turn

Details...

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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.

Checksum: DB4B4400F3602B3C
Show »

FASTA1,143130,898

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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: 2824653] [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: 2956090] [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: 14702039] [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: 2531281] [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: 2971730] [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: 2845400] [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: 1695146] [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: 11909961] [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: 12676959] [Abstract]
Cited for: INTERACTION WITH DPP4, SUBCELLULAR LOCATION.
[10]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-995; SER-1003 AND SER-1007, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"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: 19367720] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973, MASS SPECTROMETRY.
Tissue: T-cell.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]"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-232 AND ASN-335, MASS SPECTROMETRY.
Tissue: Liver.
[14]"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-232; ASN-240; ASN-276; ASN-284; ASN-335; ASN-419; ASN-488 AND ASN-497, MASS SPECTROMETRY.
[15]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973 AND SER-1297, MASS SPECTROMETRY.
Tissue: T-cell.
[16]"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: 15684325] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 622-1231 ALONE AND IN COMPLEX WITH PHOSPHOPEPTIDE.
[17]"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: 11101853] [Abstract]
Cited for: INVOLVEMENT IN MS SUSCEPTIBILITY.
[18]"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: 11145714] [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.
[19]"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: 16959974] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-228 AND ARG-863.
+Additional computationally mapped references.

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Web resources

PTPRCbase

PTPRC mutation db

Wikipedia

CD45 entry

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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.
IPIIPI00647613.
IPI00844079.
PIRA46546.
RefSeqNP_002829.2.
NP_563578.1.
NP_563579.1.
UniGeneHs.654514

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YGRX-ray2.90A/B622-1231[»]
1YGUX-ray2.90A/B622-1231[»]
SMRP08575. Positions 133-158, 314-564, 348-570, 562-911.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-224N.
IntActP08575. 28 interactions.
STRINGP08575.

PTM databases

GlycoSuiteDBP08575.
PhosphoSiteP08575.

Proteomic databases

PRIDEP08575.

Genome annotation databases

EnsemblENST00000271610; ENSP00000271610; ENSG00000081237; Homo sapiens. [Genome view]
ENST00000367376; ENSP00000356346; ENSG00000081237; Homo sapiens. [Genome view]
GeneID5788.
KEGGhsa:5788.
UCSCuc001gur.1. human.
uc001gut.1. human.

Organism-specific databases

CTD5788.
GeneCardsGC01P196874.
H-InvDBHIX0023611.
HGNCHGNC:9666. PTPRC.
HPACAB000052.
CAB002800.
HPA000440.
MIM126200. phenotype.
151460. gene.
608971. phenotype.
Orphanet169073. Autosomal recessive severe combined immunodeficiency T-B+NK+.
PharmGKBPA34011.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG04989.
HOVERGENP08575.
InParanoidP08575.
PhylomeDBP08575.

Enzyme and pathway databases

BRENDA3.1.3.48. 247.
Pathway_Interaction_DBbcr_5pathway. BCR signaling pathway.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
ReactomeREACT_18266. Axon guidance.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressP08575.
BgeeP08575.
CleanExHS_PTPRC.
GenevestigatorP08575.
GermOnlineENSG00000081237. Homo sapiens.

Family and domain databases

InterProIPR000387. Dual-sp/Tyr_phosphatase.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR016335. Leukocyte_common_Ag.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 1 hit.
PfamPF00041. fn3. 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]
PROSITEPS50853. FN3. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
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Entry information

Entry nameCD45_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: February 9, 2010
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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