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Protein

Receptor-type tyrosine-protein phosphatase C

Gene

PTPRC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei819SubstrateBy similarity1
Active sitei851Phosphocysteine intermediate1
Binding sitei895SubstrateBy similarity1
Active sitei1167Phosphocysteine 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
  • 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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciZFISH:HS01390-MONOMER.
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 C (EC:3.1.3.48)
Alternative name(s):
Leukocyte common antigen
Short name:
L-CA
T200
CD_antigen: CD45
Gene namesi
Name:PTPRC
Synonyms:CD45
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9666. PTPRC.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 575ExtracellularSequence analysisAdd BLAST552
Transmembranei576 – 597HelicalSequence analysisAdd BLAST22
Topological domaini598 – 1304CytoplasmicSequence analysisAdd BLAST707

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • external side of plasma membrane Source: MGI
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • membrane raft Source: UniProtKB-SubCell
  • plasma membrane Source: Reactome
Complete GO annotation...

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_021205362 – 363Missing 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
Mutagenesisi851C → S: Loss of activity. Abolishes interaction with SKAP1. 1 Publication1

Keywords - Diseasei

Disease mutation, SCID

Organism-specific databases

DisGeNETi5788.
MalaCardsiPTPRC.
MIMi126200. phenotype.
608971. phenotype.
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 – 23Add BLAST23
ChainiPRO_000002547024 – 1304Receptor-type tyrosine-protein phosphatase CAdd BLAST1281

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi78N-linked (GlcNAc...)Sequence analysis1
Glycosylationi90N-linked (GlcNAc...)Sequence analysis1
Glycosylationi95N-linked (GlcNAc...)Sequence analysis1
Glycosylationi184N-linked (GlcNAc...)Sequence analysis1
Glycosylationi190N-linked (GlcNAc...)Sequence analysis1
Glycosylationi197N-linked (GlcNAc...)Sequence analysis1
Glycosylationi232N-linked (GlcNAc...)2 Publications1
Glycosylationi240N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi260N-linked (GlcNAc...)Sequence analysis1
Glycosylationi270N-linked (GlcNAc...)Sequence analysis1
Glycosylationi276N-linked (GlcNAc...)1 Publication1
Glycosylationi284N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi335N-linked (GlcNAc...)2 Publications1
Glycosylationi378N-linked (GlcNAc...)Sequence analysis1
Glycosylationi419N-linked (GlcNAc...)1 Publication1
Glycosylationi468N-linked (GlcNAc...)Sequence analysis1
Glycosylationi488N-linked (GlcNAc...)1 Publication1
Glycosylationi497N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi529N-linked (GlcNAc...)Sequence analysis1
Modified residuei681PhosphotyrosineBy similarity1
Modified residuei973PhosphoserineCombined sources1
Modified residuei992PhosphoserineCombined sources1
Modified residuei995PhosphoserineBy similarity1
Modified residuei999PhosphoserineBy similarity1
Modified residuei1002PhosphoserineBy similarity1
Modified residuei1003PhosphoserineBy similarity1
Modified residuei1007PhosphoserineBy similarity1
Modified residuei1297PhosphoserineCombined 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.
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

WithEntry#Exp.IntActNotes
CSKP412403EBI-1341,EBI-1380630
CTNNB1P352222EBI-1341,EBI-491549
ERBB2P046262EBI-1341,EBI-641062
ITGALP207012EBI-1341,EBI-961214
LCKP062397EBI-1341,EBI-1348
LckP062402EBI-1341,EBI-1401From a different organism.
LGALS1P093822EBI-1341,EBI-1048875
TEKQ027633EBI-1341,EBI-2257090

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111752. 23 interactors.
DIPiDIP-224N.
IntActiP08575. 39 interactors.
MINTiMINT-1130341.
STRINGi9606.ENSP00000356346.

Chemistry databases

BindingDBiP08575.

Structurei

Secondary structure

11304
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi226 – 229Combined sources4
Turni230 – 232Combined sources3
Beta strandi235 – 240Combined sources6
Turni241 – 244Combined sources4
Beta strandi245 – 250Combined sources6
Beta strandi257 – 261Combined sources5
Helixi264 – 266Combined sources3
Beta strandi267 – 271Combined sources5
Beta strandi276 – 282Combined sources7
Beta strandi286 – 289Combined sources4
Beta strandi291 – 296Combined sources6
Helixi301 – 303Combined sources3
Beta strandi304 – 308Combined sources5
Helixi312 – 314Combined sources3
Turni315 – 317Combined sources3
Beta strandi319 – 325Combined sources7
Helixi333 – 335Combined sources3
Beta strandi336 – 342Combined sources7
Beta strandi345 – 354Combined sources10
Beta strandi362 – 371Combined sources10
Beta strandi374 – 386Combined sources13
Beta strandi394 – 399Combined sources6
Beta strandi401 – 404Combined sources4
Beta strandi406 – 411Combined sources6
Beta strandi418 – 425Combined sources8
Beta strandi427 – 436Combined sources10
Beta strandi441 – 444Combined sources4
Beta strandi452 – 468Combined sources17
Beta strandi472 – 477Combined sources6
Beta strandi487 – 497Combined sources11
Beta strandi499 – 504Combined sources6
Beta strandi516 – 539Combined sources24
Beta strandi547 – 555Combined sources9
Beta strandi564 – 569Combined sources6
Turni633 – 635Combined sources3
Helixi636 – 656Combined sources21
Beta strandi663 – 665Combined sources3
Turni668 – 670Combined sources3
Helixi673 – 678Combined sources6
Turni688 – 690Combined sources3
Beta strandi691 – 693Combined sources3
Beta strandi698 – 700Combined sources3
Turni701 – 704Combined sources4
Beta strandi705 – 711Combined sources7
Beta strandi714 – 716Combined sources3
Beta strandi720 – 723Combined sources4
Turni728 – 730Combined sources3
Helixi731 – 740Combined sources10
Beta strandi745 – 748Combined sources4
Beta strandi752 – 754Combined sources3
Beta strandi757 – 759Combined sources3
Turni767 – 769Combined sources3
Beta strandi771 – 774Combined sources4
Beta strandi777 – 786Combined sources10
Beta strandi788 – 802Combined sources15
Beta strandi807 – 814Combined sources8
Helixi826 – 836Combined sources11
Beta strandi847 – 850Combined sources4
Beta strandi852 – 855Combined sources4
Helixi856 – 869Combined sources14
Helixi871 – 874Combined sources4
Beta strandi875 – 877Combined sources3
Helixi879 – 887Combined sources9
Helixi897 – 913Combined sources17
Helixi920 – 922Combined sources3
Helixi923 – 930Combined sources8
Helixi941 – 948Combined sources8
Helixi960 – 962Combined sources3
Helixi966 – 968Combined sources3
Turni979 – 981Combined sources3
Beta strandi1018 – 1022Combined sources5
Beta strandi1029 – 1034Combined sources6
Turni1038 – 1040Combined sources3
Helixi1041 – 1050Combined sources10
Beta strandi1055 – 1058Combined sources4
Beta strandi1062 – 1064Combined sources3
Beta strandi1067 – 1070Combined sources4
Beta strandi1088 – 1093Combined sources6
Beta strandi1095 – 1105Combined sources11
Beta strandi1113 – 1120Combined sources8
Beta strandi1125 – 1127Combined sources3
Helixi1132 – 1143Combined sources12
Beta strandi1163 – 1171Combined sources9
Helixi1174 – 1189Combined sources16
Beta strandi1190 – 1192Combined sources3
Helixi1195 – 1205Combined sources11
Turni1207 – 1210Combined sources4
Helixi1213 – 1225Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YGRX-ray2.90A/B622-1231[»]
1YGUX-ray2.90A/B622-1231[»]
5FMVX-ray2.90A/B223-571[»]
5FN6X-ray3.30A223-479[»]
5FN7X-ray2.30A/B223-392[»]
ProteinModelPortaliP08575.
SMRiP08575.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08575.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini389 – 481Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST93
Domaini482 – 574Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST93
Domaini651 – 910Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd BLAST260
Domaini942 – 1226Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd BLAST285

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni851 – 857Substrate bindingBy similarity7

Domaini

The first PTPase domain interacts with SKAP1.

Sequence similaritiesi

Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4228. Eukaryota.
COG5599. LUCA.
HOGENOMiHOG000049064.
HOVERGENiHBG000066.
InParanoidiP08575.
KOiK06478.
OrthoDBiEOG091G015A.
PhylomeDBiP08575.
TreeFamiTF351829.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.60.40.10. 2 hits.
3.90.190.10. 2 hits.
InterProiIPR003961. FN3_dom.
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.
[Graphical view]
PfamiPF12567. CD45. 1 hit.
PF00041. fn3. 2 hits.
PF12453. PTP_N. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PIRSFiPIRSF002004. Leukocyte_common_antigen. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 2 hits.
SM00194. PTPc. 2 hits.
SM00404. PTPc_motif. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEiPS50853. FN3. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]

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: P08575-1) [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
MYLWLKLLAF GFAFLDTEVF VTGQSPTPSP TGLTTAKMPS VPLSSDPLPT
60 70 80 90 100
HTTAFSPAST FERENDFSET TTSLSPDNTS TQVSPDSLDN ASAFNTTGVS
110 120 130 140 150
SVQTPHLPTH ADSQTPSAGT DTQTFSGSAA NAKLNPTPGS NAISDVPGER
160 170 180 190 200
STASTFPTDP VSPLTTTLSL AHHSSAALPA RTSNTTITAN TSDAYLNASE
210 220 230 240 250
TTTLSPSGSA VISTTTIATT PSKPTCDEKY ANITVDYLYN KETKLFTAKL
260 270 280 290 300
NVNENVECGN NTCTNNEVHN LTECKNASVS ISHNSCTAPD KTLILDVPPG
310 320 330 340 350
VEKFQLHDCT QVEKADTTIC LKWKNIETFT CDTQNITYRF QCGNMIFDNK
360 370 380 390 400
EIKLENLEPE HEYKCDSEIL YNNHKFTNAS KIIKTDFGSP GEPQIIFCRS
410 420 430 440 450
EAAHQGVITW NPPQRSFHNF TLCYIKETEK DCLNLDKNLI KYDLQNLKPY
460 470 480 490 500
TKYVLSLHAY IIAKVQRNGS AAMCHFTTKS APPSQVWNMT VSMTSDNSMH
510 520 530 540 550
VKCRPPRDRN GPHERYHLEV EAGNTLVRNE SHKNCDFRVK DLQYSTDYTF
560 570 580 590 600
KAYFHNGDYP GEPFILHHST SYNSKALIAF LAFLIIVTSI ALLVVLYKIY
610 620 630 640 650
DLHKKRSCNL DEQQELVERD DEKQLMNVEP IHADILLETY KRKIADEGRL
660 670 680 690 700
FLAEFQSIPR VFSKFPIKEA RKPFNQNKNR YVDILPYDYN RVELSEINGD
710 720 730 740 750
AGSNYINASY IDGFKEPRKY IAAQGPRDET VDDFWRMIWE QKATVIVMVT
760 770 780 790 800
RCEEGNRNKC AEYWPSMEEG TRAFGDVVVK INQHKRCPDY IIQKLNIVNK
810 820 830 840 850
KEKATGREVT HIQFTSWPDH GVPEDPHLLL KLRRRVNAFS NFFSGPIVVH
860 870 880 890 900
CSAGVGRTGT YIGIDAMLEG LEAENKVDVY GYVVKLRRQR CLMVQVEAQY
910 920 930 940 950
ILIHQALVEY NQFGETEVNL SELHPYLHNM KKRDPPSEPS PLEAEFQRLP
960 970 980 990 1000
SYRSWRTQHI GNQEENKSKN RNSNVIPYDY NRVPLKHELE MSKESEHDSD
1010 1020 1030 1040 1050
ESSDDDSDSE EPSKYINASF IMSYWKPEVM IAAQGPLKET IGDFWQMIFQ
1060 1070 1080 1090 1100
RKVKVIVMLT ELKHGDQEIC AQYWGEGKQT YGDIEVDLKD TDKSSTYTLR
1110 1120 1130 1140 1150
VFELRHSKRK DSRTVYQYQY TNWSVEQLPA EPKELISMIQ VVKQKLPQKN
1160 1170 1180 1190 1200
SSEGNKHHKS TPLLIHCRDG SQQTGIFCAL LNLLESAETE EVVDIFQVVK
1210 1220 1230 1240 1250
ALRKARPGMV STFEQYQFLY DVIASTYPAQ NGQVKKNNHQ EDKIEFDNEV
1260 1270 1280 1290 1300
DKVKQDANCV NPLGAPEKLP EAKEQAEGSE PTSGTEGPEH SVNGPASPAL

NQGS
Length:1,304
Mass (Da):147,254
Last modified:July 19, 2003 - v2
Checksum:iA08FC22D6069BAF7
GO
Isoform 2 (identifier: P08575-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,143
Mass (Da):130,898
Checksum:iDB4B4400F3602B3C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti650L → P in CAA68669 (PubMed:2824653).Curated1
Sequence conflicti1207P → L in CAA68669 (PubMed:2824653).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036860191T → A.Corresponds to variant rs4915154dbSNPEnsembl.1
Natural variantiVAR_035653228E → A in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_051763294I → L.Corresponds to variant rs2230606dbSNPEnsembl.1
Natural variantiVAR_021205362 – 363Missing in T(-)B(+)NK(+) SCID; associated with lack of surface expression. 1 Publication2
Natural variantiVAR_051764421T → I.Corresponds to variant rs6696162dbSNPEnsembl.1
Natural variantiVAR_051765568H → Q.Corresponds to variant rs12136658dbSNPEnsembl.1
Natural variantiVAR_035654863G → R in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0203031283S → R.Corresponds to variant rs2298872dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00778032 – 192Missing in isoform 2. 2 PublicationsAdd BLAST161

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00638 mRNA. Translation: CAA68669.1.
Y00062 mRNA. Translation: CAA68269.1.
AK292131 mRNA. Translation: BAF84820.1.
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.
PIRiA46546.
RefSeqiNP_002829.3. NM_002838.4.
NP_563578.2. NM_080921.3.
UniGeneiHs.654514.

Genome annotation databases

EnsembliENST00000367376; ENSP00000356346; ENSG00000081237.
ENST00000573477; ENSP00000461074; ENSG00000262418.
ENST00000573679; ENSP00000458322; ENSG00000262418.
ENST00000594404; ENSP00000471843; ENSG00000081237.
GeneIDi5788.
KEGGihsa:5788.
UCSCiuc061fse.1. human. [P08575-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

PTPRCbase

PTPRC mutation db

Wikipedia

CD45 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00638 mRNA. Translation: CAA68669.1.
Y00062 mRNA. Translation: CAA68269.1.
AK292131 mRNA. Translation: BAF84820.1.
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.
PIRiA46546.
RefSeqiNP_002829.3. NM_002838.4.
NP_563578.2. NM_080921.3.
UniGeneiHs.654514.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YGRX-ray2.90A/B622-1231[»]
1YGUX-ray2.90A/B622-1231[»]
5FMVX-ray2.90A/B223-571[»]
5FN6X-ray3.30A223-479[»]
5FN7X-ray2.30A/B223-392[»]
ProteinModelPortaliP08575.
SMRiP08575.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111752. 23 interactors.
DIPiDIP-224N.
IntActiP08575. 39 interactors.
MINTiMINT-1130341.
STRINGi9606.ENSP00000356346.

Chemistry databases

BindingDBiP08575.
ChEMBLiCHEMBL3243.

PTM databases

DEPODiP08575.
iPTMnetiP08575.
PhosphoSitePlusiP08575.
SwissPalmiP08575.
UniCarbKBiP08575.

Polymorphism and mutation databases

BioMutaiPTPRC.
DMDMi33112650.

Proteomic databases

EPDiP08575.
MaxQBiP08575.
PaxDbiP08575.
PeptideAtlasiP08575.
PRIDEiP08575.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367376; ENSP00000356346; ENSG00000081237.
ENST00000573477; ENSP00000461074; ENSG00000262418.
ENST00000573679; ENSP00000458322; ENSG00000262418.
ENST00000594404; ENSP00000471843; ENSG00000081237.
GeneIDi5788.
KEGGihsa:5788.
UCSCiuc061fse.1. human. [P08575-1]

Organism-specific databases

CTDi5788.
DisGeNETi5788.
GeneCardsiPTPRC.
HGNCiHGNC:9666. PTPRC.
HPAiHPA000440.
MalaCardsiPTPRC.
MIMi126200. phenotype.
151460. gene.
608971. phenotype.
neXtProtiNX_P08575.
Orphaneti169157. T-B+ severe combined immunodeficiency due to CD45 deficiency.
PharmGKBiPA34011.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4228. Eukaryota.
COG5599. LUCA.
HOGENOMiHOG000049064.
HOVERGENiHBG000066.
InParanoidiP08575.
KOiK06478.
OrthoDBiEOG091G015A.
PhylomeDBiP08575.
TreeFamiTF351829.

Enzyme and pathway databases

BioCyciZFISH:HS01390-MONOMER.
ReactomeiR-HSA-202427. Phosphorylation of CD3 and TCR zeta chains.
R-HSA-416700. Other semaphorin interactions.
R-HSA-6798695. Neutrophil degranulation.
SignaLinkiP08575.
SIGNORiP08575.

Miscellaneous databases

ChiTaRSiPTPRC. human.
EvolutionaryTraceiP08575.
GeneWikiiPTPRC.
GenomeRNAii5788.
PROiP08575.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000081237.
CleanExiHS_PTPRC.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.60.40.10. 2 hits.
3.90.190.10. 2 hits.
InterProiIPR003961. FN3_dom.
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.
[Graphical view]
PfamiPF12567. CD45. 1 hit.
PF00041. fn3. 2 hits.
PF12453. PTP_N. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PIRSFiPIRSF002004. Leukocyte_common_antigen. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 2 hits.
SM00194. PTPc. 2 hits.
SM00404. PTPc_motif. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEiPS50853. FN3. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPTPRC_HUMAN
AccessioniPrimary (citable) accession number: P08575
Secondary accession number(s): A8K7W6, Q16614, Q9H0Y6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 19, 2003
Last modified: November 30, 2016
This is version 198 of the entry and version 2 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.