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P08575

- PTPRC_HUMAN

UniProt

P08575 - PTPRC_HUMAN

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Protein

Receptor-type tyrosine-protein phosphatase C

Gene

PTPRC

Organism
Homo sapiens (Human)
Status
Reviewed - 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 similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei819 – 8191SubstrateBy similarity
Active sitei851 – 8511Phosphocysteine intermediate
Binding sitei895 – 8951SubstrateBy similarity
Active sitei1167 – 11671Phosphocysteine intermediateBy similarity

GO - Molecular functioni

  1. protein kinase binding Source: UniProtKB
  2. protein tyrosine phosphatase activity Source: UniProtKB
  3. transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

GO - Biological processi

  1. axon guidance Source: Reactome
  2. B cell proliferation Source: UniProtKB
  3. B cell receptor signaling pathway Source: UniProtKB
  4. bone marrow development Source: UniProtKB
  5. cell cycle phase transition Source: UniProtKB
  6. cell surface receptor signaling pathway Source: ProtInc
  7. defense response to virus Source: UniProtKB
  8. dephosphorylation Source: UniProtKB
  9. hematopoietic progenitor cell differentiation Source: UniProtKB
  10. immunoglobulin biosynthetic process Source: UniProtKB
  11. negative regulation of cell adhesion involved in substrate-bound cell migration Source: UniProtKB
  12. negative regulation of cytokine-mediated signaling pathway Source: UniProtKB
  13. negative regulation of protein kinase activity Source: UniProtKB
  14. negative regulation of T cell mediated cytotoxicity Source: UniProtKB
  15. peptidyl-tyrosine dephosphorylation Source: GOC
  16. positive regulation of antigen receptor-mediated signaling pathway Source: UniProtKB
  17. positive regulation of B cell proliferation Source: UniProtKB
  18. positive regulation of hematopoietic stem cell migration Source: UniProtKB
  19. positive regulation of protein kinase activity Source: UniProtKB
  20. positive regulation of stem cell proliferation Source: UniProtKB
  21. positive regulation of T cell proliferation Source: UniProtKB
  22. protein dephosphorylation Source: UniProtKB
  23. regulation of cell cycle Source: UniProtKB
  24. release of sequestered calcium ion into cytosol Source: UniProtKB
  25. stem cell development Source: UniProtKB
  26. T cell differentiation Source: UniProtKB
  27. T cell receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiREACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_19200. Other semaphorin interactions.
SignaLinkiP08575.

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
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:9666. PTPRC.

Subcellular locationi

Membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Membrane raft 1 Publication
Note: Colocalized with DPP4 in membrane rafts.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 575552ExtracellularSequence AnalysisAdd
BLAST
Transmembranei576 – 59722HelicalSequence AnalysisAdd
BLAST
Topological domaini598 – 1304707CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. external side of plasma membrane Source: MGI
  2. extracellular vesicular exosome Source: UniProt
  3. focal adhesion Source: UniProtKB
  4. integral component of plasma membrane Source: UniProtKB
  5. membrane Source: UniProtKB
  6. 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) [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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti362 – 3632Missing in T(-)B(+)NK(+) SCID; associated with lack of surface expression. 1 Publication
VAR_021205
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.1 Publication
Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi851 – 8511C → S: Loss of activity. Abolishes interaction with SKAP1. 1 Publication

Keywords - Diseasei

Disease mutation, SCID

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 13041281Receptor-type tyrosine-protein phosphatase CPRO_0000025470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi90 – 901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi232 – 2321N-linked (GlcNAc...)2 Publications
Glycosylationi240 – 2401N-linked (GlcNAc...); atypical1 Publication
Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi276 – 2761N-linked (GlcNAc...)1 Publication
Glycosylationi284 – 2841N-linked (GlcNAc...); atypical1 Publication
Glycosylationi335 – 3351N-linked (GlcNAc...)2 Publications
Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi419 – 4191N-linked (GlcNAc...)1 Publication
Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi488 – 4881N-linked (GlcNAc...)1 Publication
Glycosylationi497 – 4971N-linked (GlcNAc...); atypical1 Publication
Glycosylationi529 – 5291N-linked (GlcNAc...)Sequence Analysis
Modified residuei973 – 9731Phosphoserine2 Publications
Modified residuei1297 – 12971Phosphoserine1 Publication

Post-translational modificationi

Heavily N- and O-glycosylated.2 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP08575.
PaxDbiP08575.
PRIDEiP08575.

PTM databases

PhosphoSiteiP08575.
UniCarbKBiP08575.

Expressioni

Gene expression databases

BgeeiP08575.
CleanExiHS_PTPRC.
GenevestigatoriP08575.

Organism-specific databases

HPAiCAB000052.
CAB002800.
CAB056154.
HPA000440.

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.By similarity3 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

Protein-protein interaction databases

BioGridi111752. 24 interactions.
DIPiDIP-224N.
IntActiP08575. 39 interactions.
MINTiMINT-1130341.
STRINGi9606.ENSP00000356346.

Structurei

Secondary structure

1
1304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni633 – 6353Combined sources
Helixi636 – 65621Combined sources
Beta strandi663 – 6653Combined sources
Turni668 – 6703Combined sources
Helixi673 – 6786Combined sources
Turni688 – 6903Combined sources
Beta strandi691 – 6933Combined sources
Beta strandi698 – 7003Combined sources
Turni701 – 7044Combined sources
Beta strandi705 – 7117Combined sources
Beta strandi714 – 7163Combined sources
Beta strandi720 – 7234Combined sources
Turni728 – 7303Combined sources
Helixi731 – 74010Combined sources
Beta strandi745 – 7484Combined sources
Beta strandi752 – 7543Combined sources
Beta strandi757 – 7593Combined sources
Turni767 – 7693Combined sources
Beta strandi771 – 7744Combined sources
Beta strandi777 – 78610Combined sources
Beta strandi788 – 80215Combined sources
Beta strandi807 – 8148Combined sources
Helixi826 – 83611Combined sources
Beta strandi847 – 8504Combined sources
Beta strandi852 – 8554Combined sources
Helixi856 – 86914Combined sources
Helixi871 – 8744Combined sources
Beta strandi875 – 8773Combined sources
Helixi879 – 8879Combined sources
Helixi897 – 91317Combined sources
Helixi920 – 9223Combined sources
Helixi923 – 9308Combined sources
Helixi941 – 9488Combined sources
Helixi960 – 9623Combined sources
Helixi966 – 9683Combined sources
Turni979 – 9813Combined sources
Beta strandi1018 – 10225Combined sources
Beta strandi1029 – 10346Combined sources
Turni1038 – 10403Combined sources
Helixi1041 – 105010Combined sources
Beta strandi1055 – 10584Combined sources
Beta strandi1062 – 10643Combined sources
Beta strandi1067 – 10704Combined sources
Beta strandi1088 – 10936Combined sources
Beta strandi1095 – 110511Combined sources
Beta strandi1113 – 11208Combined sources
Beta strandi1125 – 11273Combined sources
Helixi1132 – 114312Combined sources
Beta strandi1163 – 11719Combined sources
Helixi1174 – 118916Combined sources
Beta strandi1190 – 11923Combined sources
Helixi1195 – 120511Combined sources
Turni1207 – 12104Combined sources
Helixi1213 – 122513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YGRX-ray2.90A/B622-1231[»]
1YGUX-ray2.90A/B622-1231[»]
ProteinModelPortaliP08575.
SMRiP08575. Positions 391-469, 498-562, 623-1228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08575.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini389 – 48193Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini482 – 57493Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini651 – 910260Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
BLAST
Domaini942 – 1226285Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni851 – 8577Substrate bindingBy similarity

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

eggNOGiCOG5599.
HOGENOMiHOG000049064.
HOVERGENiHBG000066.
InParanoidiP08575.
KOiK06478.
OMAiKANTSIC.
PhylomeDBiP08575.
TreeFamiTF351829.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
3.90.190.10. 2 hits.
InterProiIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR016335. Leukocyte_common_ag.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR024739. PTP_recept_N.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF12567. CD45. 1 hit.
PF00041. fn3. 2 hits.
PF12453. PTP_N. 2 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PIRSFiPIRSF002004. Leukocyte_common_antigen. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 2 hits.
SM00194. PTPc. 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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti650 – 6501L → P in CAA68669. (PubMed:2824653)Curated
Sequence conflicti1207 – 12071P → L in CAA68669. (PubMed:2824653)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti191 – 1911T → A.
Corresponds to variant rs4915154 [ dbSNP | Ensembl ].
VAR_036860
Natural varianti228 – 2281E → A in a breast cancer sample; somatic mutation. 1 Publication
VAR_035653
Natural varianti294 – 2941I → L.
Corresponds to variant rs2230606 [ dbSNP | Ensembl ].
VAR_051763
Natural varianti362 – 3632Missing in T(-)B(+)NK(+) SCID; associated with lack of surface expression. 1 Publication
VAR_021205
Natural varianti421 – 4211T → I.
Corresponds to variant rs6696162 [ dbSNP | Ensembl ].
VAR_051764
Natural varianti568 – 5681H → Q.
Corresponds to variant rs12136658 [ dbSNP | Ensembl ].
VAR_051765
Natural varianti863 – 8631G → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_035654
Natural varianti1283 – 12831S → R.
Corresponds to variant rs2298872 [ dbSNP | Ensembl ].
VAR_020303

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei32 – 192161Missing in isoform 2. 2 PublicationsVSP_007780Add
BLAST

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.

Polymorphism databases

DMDMi33112650.

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 .
PIRi A46546.
RefSeqi NP_002829.3. NM_002838.4.
NP_563578.2. NM_080921.3.
UniGenei Hs.654514.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YGR X-ray 2.90 A/B 622-1231 [» ]
1YGU X-ray 2.90 A/B 622-1231 [» ]
ProteinModelPortali P08575.
SMRi P08575. Positions 391-469, 498-562, 623-1228.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111752. 24 interactions.
DIPi DIP-224N.
IntActi P08575. 39 interactions.
MINTi MINT-1130341.
STRINGi 9606.ENSP00000356346.

Chemistry

BindingDBi P08575.
ChEMBLi CHEMBL3243.
GuidetoPHARMACOLOGYi 1852.

PTM databases

PhosphoSitei P08575.
UniCarbKBi P08575.

Polymorphism databases

DMDMi 33112650.

Proteomic databases

MaxQBi P08575.
PaxDbi P08575.
PRIDEi P08575.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367376 ; ENSP00000356346 ; ENSG00000081237 .
ENST00000573477 ; ENSP00000461074 ; ENSG00000262418 .
ENST00000573679 ; ENSP00000458322 ; ENSG00000262418 .
ENST00000594404 ; ENSP00000471843 ; ENSG00000081237 .
GeneIDi 5788.
KEGGi hsa:5788.

Organism-specific databases

CTDi 5788.
GeneCardsi GC01P198607.
HGNCi HGNC:9666. PTPRC.
HPAi CAB000052.
CAB002800.
CAB056154.
HPA000440.
MIMi 126200. phenotype.
151460. gene.
608971. phenotype.
neXtProti NX_P08575.
Orphaneti 169157. T-B+ severe combined immunodeficiency due to CD45 deficiency.
PharmGKBi PA34011.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
HOGENOMi HOG000049064.
HOVERGENi HBG000066.
InParanoidi P08575.
KOi K06478.
OMAi KANTSIC.
PhylomeDBi P08575.
TreeFami TF351829.

Enzyme and pathway databases

Reactomei REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_19200. Other semaphorin interactions.
SignaLinki P08575.

Miscellaneous databases

ChiTaRSi PTPRC. human.
EvolutionaryTracei P08575.
GeneWikii PTPRC.
GenomeRNAii 5788.
NextBioi 22518.
PROi P08575.
SOURCEi Search...

Gene expression databases

Bgeei P08575.
CleanExi HS_PTPRC.
Genevestigatori P08575.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
3.90.190.10. 2 hits.
InterProi IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR016335. Leukocyte_common_ag.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR024739. PTP_recept_N.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF12567. CD45. 1 hit.
PF00041. fn3. 2 hits.
PF12453. PTP_N. 2 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view ]
PIRSFi PIRSF002004. Leukocyte_common_antigen. 1 hit.
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM00060. FN3. 2 hits.
SM00194. PTPc. 2 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEi PS50853. FN3. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-228 AND ARG-863.

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 26, 2014
This is version 177 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

External Data

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