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Protein

Receptor-type tyrosine-protein phosphatase C

Gene

PTPRC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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).By similarity2 Publications

Caution

It is uncertain whether Met-1 or Met-3 is the initiator.Curated

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei821SubstrateBy similarity1
Active sitei853Phosphocysteine intermediate1
Binding sitei897SubstrateBy similarity1
Active sitei1169Phosphocysteine intermediateBy similarity1

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB
  • protein tyrosine phosphatase activity Source: UniProtKB
  • transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

GO - Biological processi

  • B cell proliferation Source: UniProtKB
  • B cell receptor signaling pathway Source: UniProtKB
  • bone marrow development Source: UniProtKB
  • cell cycle phase transition Source: UniProtKB
  • cell surface receptor signaling pathway Source: ProtInc
  • defense response to virus Source: UniProtKB
  • dephosphorylation Source: UniProtKB
  • hematopoietic progenitor cell differentiation Source: UniProtKB
  • immunoglobulin biosynthetic process Source: UniProtKB
  • negative regulation of cell adhesion involved in substrate-bound cell migration Source: UniProtKB
  • negative regulation of cytokine-mediated signaling pathway Source: UniProtKB
  • negative regulation of protein kinase activity Source: UniProtKB
  • negative regulation of T cell mediated cytotoxicity Source: UniProtKB
  • neutrophil degranulation Source: Reactome
  • positive regulation of antigen receptor-mediated signaling pathway Source: UniProtKB
  • positive regulation of B cell proliferation Source: UniProtKB
  • positive regulation of hematopoietic stem cell migration Source: UniProtKB
  • positive regulation of protein kinase activity Source: UniProtKB
  • positive regulation of stem cell proliferation Source: UniProtKB
  • positive regulation of T cell proliferation Source: UniProtKB
  • protein dephosphorylation Source: UniProtKB
  • regulation of cell cycle Source: UniProtKB
  • release of sequestered calcium ion into cytosol Source: UniProtKB
  • stem cell development Source: UniProtKB
  • T cell differentiation Source: UniProtKB
  • T cell receptor signaling pathway Source: UniProtKB

Keywordsi

Molecular functionHydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiR-HSA-202427 Phosphorylation of CD3 and TCR zeta chains
R-HSA-416700 Other semaphorin interactions
R-HSA-6798695 Neutrophil degranulation
SignaLinkiP08575
SIGNORiP08575

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase CCurated (EC:3.1.3.48)
Alternative name(s):
Leukocyte common antigen
Short name:
L-CA
T200
CD_antigen: CD45
Gene namesi
Name:PTPRCImported
Synonyms:CD45
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi

Organism-specific databases

EuPathDBiHostDB:ENSG00000081237.18
HGNCiHGNC:9666 PTPRC
MIMi151460 gene
neXtProtiNX_P08575

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 577ExtracellularSequence analysisAdd BLAST552
Transmembranei578 – 598HelicalSequence analysisAdd BLAST21
Topological domaini599 – 1306CytoplasmicSequence analysisAdd BLAST708

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:608971
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021205364 – 365Missing in T(-)B(+)NK(+) SCID; associated with lack of surface expression. 1 Publication2
Multiple sclerosis (MS)1 Publication
Disease susceptibility may be associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:126200

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi853C → S: Loss of activity. Abolishes interaction with SKAP1. 1 Publication1

Keywords - Diseasei

Disease mutation, SCID

Organism-specific databases

DisGeNETi5788
MalaCardsiPTPRC
MIMi126200 phenotype
608971 phenotype
OpenTargetsiENSG00000081237
Orphaneti169157 T-B+ severe combined immunodeficiency due to CD45 deficiency
PharmGKBiPA34011

Chemistry databases

ChEMBLiCHEMBL3243

Polymorphism and mutation databases

BioMutaiPTPRC
DMDMi33112650

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Add BLAST25
ChainiPRO_000002547026 – 1306Receptor-type tyrosine-protein phosphatase CAdd BLAST1281

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi80N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi92N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi97N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi186N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi192N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi199N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi234N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi242N-linked (GlcNAc...) asparagine; atypical1 Publication1
Glycosylationi262N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi272N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi278N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi286N-linked (GlcNAc...) asparagine; atypical1 Publication1
Glycosylationi337N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi380N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi421N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi470N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi490N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi499N-linked (GlcNAc...) asparagine; atypical1 Publication1
Glycosylationi531N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei683PhosphotyrosineBy similarity1
Modified residuei975PhosphoserineCombined sources1
Modified residuei994PhosphoserineCombined sources1
Modified residuei997PhosphoserineBy similarity1
Modified residuei1001PhosphoserineBy similarity1
Modified residuei1004PhosphoserineBy similarity1
Modified residuei1005PhosphoserineBy similarity1
Modified residuei1009PhosphoserineBy similarity1
Modified residuei1299PhosphoserineCombined sources1

Post-translational modificationi

Heavily N- and O-glycosylated.2 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP08575
MaxQBiP08575
PaxDbiP08575
PeptideAtlasiP08575
PRIDEiP08575

PTM databases

DEPODiP08575
GlyConnecti339
iPTMnetiP08575
PhosphoSitePlusiP08575
SwissPalmiP08575
UniCarbKBiP08575

Expressioni

Gene expression databases

BgeeiENSG00000081237
CleanExiHS_PTPRC

Organism-specific databases

HPAiHPA000440

Interactioni

Subunit structurei

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. Interacts with human cytomegalovirus protein UL11.By similarity4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111752, 24 interactors
DIPiDIP-224N
IntActiP08575, 40 interactors
MINTiP08575
STRINGi9606.ENSP00000356346

Chemistry databases

BindingDBiP08575

Structurei

Secondary structure

11306
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi228 – 231Combined sources4
Turni232 – 234Combined sources3
Beta strandi237 – 242Combined sources6
Turni243 – 246Combined sources4
Beta strandi247 – 252Combined sources6
Beta strandi259 – 263Combined sources5
Helixi266 – 268Combined sources3
Beta strandi269 – 273Combined sources5
Beta strandi278 – 284Combined sources7
Beta strandi288 – 291Combined sources4
Beta strandi293 – 298Combined sources6
Helixi303 – 305Combined sources3
Beta strandi306 – 310Combined sources5
Helixi314 – 316Combined sources3
Turni317 – 319Combined sources3
Beta strandi321 – 327Combined sources7
Helixi335 – 337Combined sources3
Beta strandi338 – 344Combined sources7
Beta strandi347 – 356Combined sources10
Beta strandi364 – 373Combined sources10
Beta strandi376 – 388Combined sources13
Beta strandi396 – 401Combined sources6
Beta strandi403 – 406Combined sources4
Beta strandi408 – 413Combined sources6
Beta strandi420 – 427Combined sources8
Beta strandi429 – 438Combined sources10
Beta strandi443 – 446Combined sources4
Beta strandi454 – 470Combined sources17
Beta strandi474 – 479Combined sources6
Beta strandi489 – 499Combined sources11
Beta strandi501 – 506Combined sources6
Beta strandi518 – 541Combined sources24
Beta strandi549 – 557Combined sources9
Beta strandi566 – 571Combined sources6
Turni635 – 637Combined sources3
Helixi638 – 658Combined sources21
Beta strandi665 – 667Combined sources3
Turni670 – 672Combined sources3
Helixi675 – 680Combined sources6
Turni690 – 692Combined sources3
Beta strandi693 – 695Combined sources3
Beta strandi700 – 702Combined sources3
Turni703 – 706Combined sources4
Beta strandi707 – 713Combined sources7
Beta strandi716 – 718Combined sources3
Beta strandi722 – 725Combined sources4
Turni730 – 732Combined sources3
Helixi733 – 742Combined sources10
Beta strandi747 – 750Combined sources4
Beta strandi754 – 756Combined sources3
Beta strandi759 – 761Combined sources3
Turni769 – 771Combined sources3
Beta strandi773 – 776Combined sources4
Beta strandi779 – 788Combined sources10
Beta strandi790 – 804Combined sources15
Beta strandi809 – 816Combined sources8
Helixi828 – 838Combined sources11
Beta strandi849 – 852Combined sources4
Beta strandi854 – 857Combined sources4
Helixi858 – 871Combined sources14
Helixi873 – 876Combined sources4
Beta strandi877 – 879Combined sources3
Helixi881 – 889Combined sources9
Helixi899 – 915Combined sources17
Helixi922 – 924Combined sources3
Helixi925 – 932Combined sources8
Helixi943 – 950Combined sources8
Helixi962 – 964Combined sources3
Helixi968 – 970Combined sources3
Turni981 – 983Combined sources3
Beta strandi1020 – 1024Combined sources5
Beta strandi1031 – 1036Combined sources6
Turni1040 – 1042Combined sources3
Helixi1043 – 1052Combined sources10
Beta strandi1057 – 1060Combined sources4
Beta strandi1064 – 1066Combined sources3
Beta strandi1069 – 1072Combined sources4
Beta strandi1090 – 1095Combined sources6
Beta strandi1097 – 1107Combined sources11
Beta strandi1115 – 1122Combined sources8
Beta strandi1127 – 1129Combined sources3
Helixi1134 – 1145Combined sources12
Beta strandi1165 – 1173Combined sources9
Helixi1176 – 1191Combined sources16
Beta strandi1192 – 1194Combined sources3
Helixi1197 – 1207Combined sources11
Turni1209 – 1212Combined sources4
Helixi1215 – 1227Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YGRX-ray2.90A/B624-1233[»]
1YGUX-ray2.90A/B624-1233[»]
5FMVX-ray2.90A/B225-573[»]
5FN6X-ray3.30A225-481[»]
5FN7X-ray2.30A/B225-394[»]
ProteinModelPortaliP08575
SMRiP08575
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08575

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini391 – 483Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST93
Domaini484 – 576Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST93
Domaini653 – 912Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd BLAST260
Domaini944 – 1228Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd BLAST285

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni853 – 859Substrate bindingBy similarity7

Domaini

The first PTPase domain interacts with SKAP1.

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4228 Eukaryota
COG5599 LUCA
GeneTreeiENSGT00760000118900
HOGENOMiHOG000049064
HOVERGENiHBG000066
InParanoidiP08575
KOiK06478
OMAiKHELEMS
OrthoDBiEOG091G015A
PhylomeDBiP08575
TreeFamiTF351829

Family and domain databases

CDDicd00063 FN3, 2 hits
Gene3Di2.60.40.10, 2 hits
3.90.190.10, 2 hits
InterProiView protein in InterPro
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR013783 Ig-like_fold
IPR029021 Prot-tyrosine_phosphatase-like
IPR024739 PTP_recept_N
IPR000242 PTPase_domain
IPR016335 Ptprc
IPR016130 Tyr_Pase_AS
IPR003595 Tyr_Pase_cat
IPR000387 TYR_PHOSPHATASE_dom
PfamiView protein in Pfam
PF12567 CD45, 1 hit
PF00041 fn3, 2 hits
PF12453 PTP_N, 1 hit
PF00102 Y_phosphatase, 2 hits
PIRSFiPIRSF002004 Leukocyte_common_antigen, 1 hit
PRINTSiPR00700 PRTYPHPHTASE
SMARTiView protein in SMART
SM00060 FN3, 2 hits
SM00194 PTPc, 2 hits
SM00404 PTPc_motif, 2 hits
SUPFAMiSSF49265 SSF49265, 1 hit
SSF52799 SSF52799, 2 hits
PROSITEiView protein in PROSITE
PS50853 FN3, 2 hits
PS00383 TYR_PHOSPHATASE_1, 1 hit
PS50056 TYR_PHOSPHATASE_2, 2 hits
PS50055 TYR_PHOSPHATASE_PTP, 2 hits

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: At least 8 isoforms are produced.
Isoform 1 (identifier: P08575-3) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTMYLWLKLL AFGFAFLDTE VFVTGQSPTP SPTGLTTAKM PSVPLSSDPL
60 70 80 90 100
PTHTTAFSPA STFERENDFS ETTTSLSPDN TSTQVSPDSL DNASAFNTTG
110 120 130 140 150
VSSVQTPHLP THADSQTPSA GTDTQTFSGS AANAKLNPTP GSNAISDVPG
160 170 180 190 200
ERSTASTFPT DPVSPLTTTL SLAHHSSAAL PARTSNTTIT ANTSDAYLNA
210 220 230 240 250
SETTTLSPSG SAVISTTTIA TTPSKPTCDE KYANITVDYL YNKETKLFTA
260 270 280 290 300
KLNVNENVEC GNNTCTNNEV HNLTECKNAS VSISHNSCTA PDKTLILDVP
310 320 330 340 350
PGVEKFQLHD CTQVEKADTT ICLKWKNIET FTCDTQNITY RFQCGNMIFD
360 370 380 390 400
NKEIKLENLE PEHEYKCDSE ILYNNHKFTN ASKIIKTDFG SPGEPQIIFC
410 420 430 440 450
RSEAAHQGVI TWNPPQRSFH NFTLCYIKET EKDCLNLDKN LIKYDLQNLK
460 470 480 490 500
PYTKYVLSLH AYIIAKVQRN GSAAMCHFTT KSAPPSQVWN MTVSMTSDNS
510 520 530 540 550
MHVKCRPPRD RNGPHERYHL EVEAGNTLVR NESHKNCDFR VKDLQYSTDY
560 570 580 590 600
TFKAYFHNGD YPGEPFILHH STSYNSKALI AFLAFLIIVT SIALLVVLYK
610 620 630 640 650
IYDLHKKRSC NLDEQQELVE RDDEKQLMNV EPIHADILLE TYKRKIADEG
660 670 680 690 700
RLFLAEFQSI PRVFSKFPIK EARKPFNQNK NRYVDILPYD YNRVELSEIN
710 720 730 740 750
GDAGSNYINA SYIDGFKEPR KYIAAQGPRD ETVDDFWRMI WEQKATVIVM
760 770 780 790 800
VTRCEEGNRN KCAEYWPSME EGTRAFGDVV VKINQHKRCP DYIIQKLNIV
810 820 830 840 850
NKKEKATGRE VTHIQFTSWP DHGVPEDPHL LLKLRRRVNA FSNFFSGPIV
860 870 880 890 900
VHCSAGVGRT GTYIGIDAML EGLEAENKVD VYGYVVKLRR QRCLMVQVEA
910 920 930 940 950
QYILIHQALV EYNQFGETEV NLSELHPYLH NMKKRDPPSE PSPLEAEFQR
960 970 980 990 1000
LPSYRSWRTQ HIGNQEENKS KNRNSNVIPY DYNRVPLKHE LEMSKESEHD
1010 1020 1030 1040 1050
SDESSDDDSD SEEPSKYINA SFIMSYWKPE VMIAAQGPLK ETIGDFWQMI
1060 1070 1080 1090 1100
FQRKVKVIVM LTELKHGDQE ICAQYWGEGK QTYGDIEVDL KDTDKSSTYT
1110 1120 1130 1140 1150
LRVFELRHSK RKDSRTVYQY QYTNWSVEQL PAEPKELISM IQVVKQKLPQ
1160 1170 1180 1190 1200
KNSSEGNKHH KSTPLLIHCR DGSQQTGIFC ALLNLLESAE TEEVVDIFQV
1210 1220 1230 1240 1250
VKALRKARPG MVSTFEQYQF LYDVIASTYP AQNGQVKKNN HQEDKIEFDN
1260 1270 1280 1290 1300
EVDKVKQDAN CVNPLGAPEK LPEAKEQAEG SEPTSGTEGP EHSVNGPASP

ALNQGS
Length:1,306
Mass (Da):147,486
Last modified:March 28, 2018 - v3
Checksum:i6E942E2BF6B17AC5
GO
Isoform 2 (identifier: P08575-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     34-194: Missing.

Show »
Length:1,145
Mass (Da):131,130
Checksum:iD3CB364EF4243384
GO

Sequence cautioni

The sequence BAF84820 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA68269 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA68669 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti652L → P in CAA68669 (PubMed:2824653).Curated1
Sequence conflicti1209P → L in CAA68669 (PubMed:2824653).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036860193T → A. Corresponds to variant dbSNP:rs4915154EnsemblClinVar.1
Natural variantiVAR_035653230E → A in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_051763296I → L. Corresponds to variant dbSNP:rs2230606EnsemblClinVar.1
Natural variantiVAR_021205364 – 365Missing in T(-)B(+)NK(+) SCID; associated with lack of surface expression. 1 Publication2
Natural variantiVAR_051764423T → I. Corresponds to variant dbSNP:rs6696162EnsemblClinVar.1
Natural variantiVAR_051765570H → Q. Corresponds to variant dbSNP:rs12136658EnsemblClinVar.1
Natural variantiVAR_035654865G → R in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0203031285S → R. Corresponds to variant dbSNP:rs2298872Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05940934 – 194Missing in isoform 2. Add BLAST161

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00638 mRNA Translation: CAA68669.1 Different initiation.
Y00062 mRNA Translation: CAA68269.1 Different initiation.
AK292131 mRNA Translation: BAF84820.1 Different initiation.
AL157402 Genomic DNA No translation available.
AL355988 Genomic DNA No translation available.
KF510707 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW91303.1
M23492
, 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
CCDSiCCDS1397.2 [P08575-3]
CCDS1398.2 [P08575-4]
PIRiA46546
RefSeqiNP_002829.3, NM_002838.4 [P08575-3]
NP_563578.2, NM_080921.3 [P08575-4]
UniGeneiHs.654514

Genome annotation databases

EnsembliENST00000348564; ENSP00000306782; ENSG00000081237 [P08575-4]
ENST00000442510; ENSP00000411355; ENSG00000081237 [P08575-3]
ENST00000573477; ENSP00000461074; ENSG00000262418
ENST00000573679; ENSP00000458322; ENSG00000262418
GeneIDi5788
KEGGihsa:5788
UCSCiuc061fse.1 human [P08575-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPTPRC_HUMAN
AccessioniPrimary (citable) accession number: P08575
Secondary accession number(s): A0A0A0MT22
, A8K7W6, Q16614, Q9H0Y6, X6R433
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: March 28, 2018
Last modified: May 23, 2018
This is version 209 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

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