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P06800

- PTPRC_MOUSE

UniProt

P06800 - PTPRC_MOUSE

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Protein

Receptor-type tyrosine-protein phosphatase C

Gene

Ptprc

Organism
Mus musculus (Mouse)
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 (By similarity). Dephosphorylates LYN, and thereby modulates LYN activity.By similarity1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei808 – 8081SubstrateBy similarity
Active sitei840 – 8401Phosphocysteine intermediateBy similarity
Binding sitei884 – 8841SubstrateBy similarity
Active sitei1155 – 11551Phosphocysteine intermediateBy similarity

GO - Molecular functioni

  1. heparan sulfate proteoglycan binding Source: MGI
  2. heparin binding Source: MGI
  3. protein kinase binding Source: UniProtKB
  4. protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. activation of MAPK activity Source: MGI
  2. B cell differentiation Source: MGI
  3. B cell proliferation Source: UniProtKB
  4. B cell receptor signaling pathway Source: UniProtKB
  5. bone marrow development Source: Ensembl
  6. cell cycle phase transition Source: Ensembl
  7. defense response to virus Source: UniProtKB
  8. dephosphorylation Source: UniProtKB
  9. hematopoietic progenitor cell differentiation Source: Ensembl
  10. heterotypic cell-cell adhesion Source: MGI
  11. immunoglobulin biosynthetic process Source: Ensembl
  12. leukocyte cell-cell adhesion Source: MGI
  13. negative regulation of cell adhesion involved in substrate-bound cell migration Source: Ensembl
  14. negative regulation of cytokine-mediated signaling pathway Source: UniProtKB
  15. negative regulation of peptidyl-tyrosine phosphorylation Source: MGI
  16. negative regulation of protein autophosphorylation Source: MGI
  17. negative regulation of protein kinase activity Source: UniProtKB
  18. negative regulation of T cell mediated cytotoxicity Source: UniProtKB
  19. negative thymic T cell selection Source: MGI
  20. peptidyl-tyrosine dephosphorylation Source: GOC
  21. positive regulation of alpha-beta T cell proliferation Source: MGI
  22. positive regulation of antigen receptor-mediated signaling pathway Source: UniProtKB
  23. positive regulation of B cell proliferation Source: MGI
  24. positive regulation of extrinsic apoptotic signaling pathway Source: MGI
  25. positive regulation of gamma-delta T cell differentiation Source: MGI
  26. positive regulation of hematopoietic stem cell migration Source: Ensembl
  27. positive regulation of humoral immune response mediated by circulating immunoglobulin Source: MGI
  28. positive regulation of isotype switching to IgG isotypes Source: MGI
  29. positive regulation of MAPK cascade Source: MGI
  30. positive regulation of stem cell proliferation Source: Ensembl
  31. positive regulation of T cell differentiation Source: MGI
  32. positive regulation of T cell mediated cytotoxicity Source: MGI
  33. positive regulation of T cell mediated immunity Source: MGI
  34. positive regulation of T cell proliferation Source: UniProtKB
  35. positive thymic T cell selection Source: MGI
  36. protein dephosphorylation Source: UniProtKB
  37. regulation of B cell differentiation Source: MGI
  38. regulation of B cell receptor signaling pathway Source: MGI
  39. regulation of cell cycle Source: UniProtKB
  40. regulation of extrinsic apoptotic signaling pathway Source: MGI
  41. regulation of humoral immune response mediated by circulating immunoglobulin Source: MGI
  42. release of sequestered calcium ion into cytosol Source: UniProtKB
  43. response to gamma radiation Source: Ensembl
  44. stem cell development Source: Ensembl
  45. T cell differentiation Source: UniProtKB
  46. T cell proliferation Source: MGI
  47. T cell receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiREACT_216080. Phosphorylation of CD3 and TCR zeta chains.
REACT_231928. Other semaphorin interactions.

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
Lymphocyte antigen 5
Short name:
Ly-5
T200
CD_antigen: CD45
Gene namesi
Name:Ptprc
Synonyms:Ly-5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:97810. Ptprc.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 564541ExtracellularSequence AnalysisAdd
BLAST
Transmembranei565 – 58622HelicalSequence AnalysisAdd
BLAST
Topological domaini587 – 1291705CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell periphery Source: MGI
  2. external side of plasma membrane Source: MGI
  3. extracellular vesicular exosome Source: Ensembl
  4. focal adhesion Source: UniProtKB
  5. integral component of plasma membrane Source: UniProtKB
  6. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 12911268Receptor-type tyrosine-protein phosphatase CPRO_0000025471Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi489 – 4891N-linked (GlcNAc...)Sequence Analysis
Modified residuei962 – 9621Phosphoserine1 Publication
Modified residuei1284 – 12841PhosphoserineBy similarity

Post-translational modificationi

Heavily N- and O-glycosylated.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP06800.
PaxDbiP06800.
PRIDEiP06800.

PTM databases

PhosphoSiteiP06800.

Expressioni

Developmental stagei

Expression is restricted to the hematopoietic compartment of development.

Gene expression databases

BgeeiP06800.
CleanExiMM_PTPRC.
ExpressionAtlasiP06800. baseline and differential.
GenevestigatoriP06800.

Interactioni

Subunit structurei

Interacts with SKAP1. Interacts with DPP4; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes (By similarity). Binds GANAB and PRKCSH.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
LckP062403EBI-1672,EBI-1401

Protein-protein interaction databases

BioGridi202493. 3 interactions.
IntActiP06800. 8 interactions.
MINTiMINT-188397.
STRINGi10090.ENSMUSP00000074352.

Structurei

3D structure databases

ProteinModelPortaliP06800.
SMRiP06800. Positions 612-1216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini374 – 47097Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini471 – 56696Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini640 – 899260Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
BLAST
Domaini931 – 1214284Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni840 – 8467Substrate bindingBy similarity

Domaini

The first PTPase domain interacts with SKAP1.By similarity

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.
HOVERGENiHBG000066.
InParanoidiP06800.
OrthoDBiEOG7XSTCW.
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.
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.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P06800-1) [UniParc]FASTAAdd to Basket

Also known as: B220

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
MGLWLKLLAF GFALLDTEVF VTGQTPTPSD ELSTTENALL LPQSDPLPAR
60 70 80 90 100
TTESTPPSIS ERGNGSSETT YHPGVLSTLL PHLSPQPDSQ TPSAGGADTQ
110 120 130 140 150
TFSSQADNPT LTPAPGGGTD PPGVPGERTV PGTIPADTAF PVDTPSLARN
160 170 180 190 200
SSAASPTHTS NVSTTDISSG ASLTTLTPST LGLASTDPPS TTIATTTKQT
210 220 230 240 250
CAAMFGNITV NYTYESSNQT FKADLKDVQN AKCGNEDCEN VLNNLEECSQ
260 270 280 290 300
IKNISVSNDS CAPATTIDLY VPPGTDKFSL HDCTPKEKAN TSICLEWKTK
310 320 330 340 350
NLDFRKCNSD NISYVLHCEP ENNTKCIRRN TFIPERCQLD NLRAQTNYTC
360 370 380 390 400
VAEILYRGVK LVKNVINVQT DLGIPETPKP SCGDPAARKT LVSWPEPVSK
410 420 430 440 450
PESASKPHGY VLCYKNNSEK CKSLPNNVTS FEVESLKPYK YYEVSLLAYV
460 470 480 490 500
NGKIQRNGTA EKCNFHTKAD RPDKVNGMKT SRPTDNSINV TCGPPYETNG
510 520 530 540 550
PKTFYILVVR SGGSFVTKYN KTNCQFYVDN LYYSTDYEFL VSFHNGVYEG
560 570 580 590 600
DSVIRNESTN FNAKALIIFL VFLIIVTSIA LLVVLYKIYD LRKKRSSNLD
610 620 630 640 650
EQQELVERDD EKQLMDVEPI HSDILLETYK RKIADEGRLF LAEFQSIPRV
660 670 680 690 700
FSKFPIKDAR KPHNQNKNRY VDILPYDYNR VELSEINGDA GSTYINASYI
710 720 730 740 750
DGFKEPRKYI AAQGPRDETV DDFWRMIWEQ KATVIVMVTR CEEGNRNKCA
760 770 780 790 800
EYWPSMEEGT RAFKDIVVTI NDHKRCPDYI IQKLNVAHKK EKATGREVTH
810 820 830 840 850
IQFTSWPDHG VPEDPHLLLK LRRRVNAFSN FFSGPIVVHC SAGVGRTGTY
860 870 880 890 900
IGIDAMLEGL EAEGKVDVYG YVVKLRRQRC LMVQVEAQYI LIHQALVEYN
910 920 930 940 950
QFGETEVNLS ELHSCLHNMK KRDPPSDPSP LEAEYQRLPS YRSWRTQHIG
960 970 980 990 1000
NQEENKKKNR NSNVVPYDFN RVPLKHELEM SKESEPESDE SSDDDSDSEE
1010 1020 1030 1040 1050
TSKYINASFV MSYWKPEMMI AAQGPLKETI GDFWQMIFQR KVKVIVMLTE
1060 1070 1080 1090 1100
LVNGDQEVCA QYWGEGKQTY GDMEVEMKDT NRASAYTLRT FELRHSKRKE
1110 1120 1130 1140 1150
PRTVYQYQCT TWKGEELPAE PKDLVSMIQD LKQKLPKASP EGMKYHKHAS
1160 1170 1180 1190 1200
ILVHCRDGSQ QTGLFCALFN LLESAETEDV VDVFQVVKSL RKARPGVVCS
1210 1220 1230 1240 1250
YEQYQFLYDI IASIYPAQNG QVKKTNSQDK IEFHNEVDGG KQDANCVRPD
1260 1270 1280 1290
GPLNKAQEDS RGVGTPEPTN SAEEPEHAAN GSASPAPTQS S
Length:1,291
Mass (Da):144,604
Last modified:July 27, 2011 - v3
Checksum:iED752FD195BA9643
GO
Isoform 2 (identifier: P06800-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     31-73: Missing.

Show »
Length:1,248
Mass (Da):140,040
Checksum:iD08281C0463EA174
GO
Isoform 3 (identifier: P06800-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     31-169: Missing.

Show »
Length:1,152
Mass (Da):130,622
Checksum:iF1AA6650E654CAAB
GO

Sequence cautioni

The sequence AAA39462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3001K → E in AAA39459. (PubMed:1822988)Curated
Sequence conflicti398 – 3981V → A in AAA39459. (PubMed:1822988)Curated
Sequence conflicti402 – 4032ES → DP in AAA39459. (PubMed:1822988)Curated
Sequence conflicti476 – 4761N → T in AAA39459. (PubMed:1822988)Curated
Sequence conflicti518 – 5203KYN → NTT in AAA39458. (PubMed:2944116)Curated
Sequence conflicti528 – 5281V → G in AAA39458. (PubMed:2944116)Curated
Sequence conflicti556 – 5561N → S in AAA39458. (PubMed:2944116)Curated
Sequence conflicti588 – 5881I → S in AAA39458. (PubMed:2944116)Curated
Sequence conflicti906 – 9061E → Q in AAA39458. (PubMed:2944116)Curated
Sequence conflicti931 – 9311L → R in AAA39458. (PubMed:2944116)Curated
Sequence conflicti953 – 9531E → G in AAA39458. (PubMed:2944116)Curated
Sequence conflicti959 – 9591N → K in AAA39458. (PubMed:2944116)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei31 – 169139Missing in isoform 3. 2 PublicationsVSP_012442Add
BLAST
Alternative sequencei31 – 7343Missing in isoform 2. 1 PublicationVSP_012441Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14342 mRNA. Translation: AAA39458.1.
M92933 mRNA. Translation: AAA39459.1.
AC122903 Genomic DNA. No translation available.
AC159278 Genomic DNA. No translation available.
M17320 mRNA. Translation: AAA60449.1.
M23354 Genomic DNA. Translation: AAA39462.1. Different initiation.
M22456 Genomic DNA. Translation: AAB46374.1.
M11934 mRNA. Translation: AAA39461.1.
M23241 Genomic DNA. Translation: AAA39460.1.
M15174 mRNA. Translation: AAA40161.1.
PIRiA23329.
A28334.
A28335.
I57644.
UniGeneiMm.391573.

Genome annotation databases

UCSCiuc007cvf.2. mouse. [P06800-1]
uc007cvh.2. mouse. [P06800-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14342 mRNA. Translation: AAA39458.1 .
M92933 mRNA. Translation: AAA39459.1 .
AC122903 Genomic DNA. No translation available.
AC159278 Genomic DNA. No translation available.
M17320 mRNA. Translation: AAA60449.1 .
M23354 Genomic DNA. Translation: AAA39462.1 . Different initiation.
M22456 Genomic DNA. Translation: AAB46374.1 .
M11934 mRNA. Translation: AAA39461.1 .
M23241 Genomic DNA. Translation: AAA39460.1 .
M15174 mRNA. Translation: AAA40161.1 .
PIRi A23329.
A28334.
A28335.
I57644.
UniGenei Mm.391573.

3D structure databases

ProteinModelPortali P06800.
SMRi P06800. Positions 612-1216.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202493. 3 interactions.
IntActi P06800. 8 interactions.
MINTi MINT-188397.
STRINGi 10090.ENSMUSP00000074352.

Chemistry

GuidetoPHARMACOLOGYi 1852.

PTM databases

PhosphoSitei P06800.

Proteomic databases

MaxQBi P06800.
PaxDbi P06800.
PRIDEi P06800.

Protocols and materials databases

DNASUi 19264.
Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi uc007cvf.2. mouse. [P06800-1 ]
uc007cvh.2. mouse. [P06800-3 ]

Organism-specific databases

MGIi MGI:97810. Ptprc.

Phylogenomic databases

eggNOGi COG5599.
HOVERGENi HBG000066.
InParanoidi P06800.
OrthoDBi EOG7XSTCW.
TreeFami TF351829.

Enzyme and pathway databases

Reactomei REACT_216080. Phosphorylation of CD3 and TCR zeta chains.
REACT_231928. Other semaphorin interactions.

Miscellaneous databases

NextBioi 296132.
PROi P06800.
SOURCEi Search...

Gene expression databases

Bgeei P06800.
CleanExi MM_PTPRC.
ExpressionAtlasi P06800. baseline and differential.
Genevestigatori P06800.

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.
PF12453. PTP_N. 1 hit.
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. 2 hits.
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. "Sequences of Ly-5 cDNA: isoform-related diversity of Ly-5 mRNA."
    Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.
    Proc. Natl. Acad. Sci. U.S.A. 83:6940-6944(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  2. Erratum
    Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.
    Proc. Natl. Acad. Sci. U.S.A. 84:1991-1991(1987)
    Cited for: SEQUENCE REVISION.
  3. "Comparison of mouse Ly5a and Ly5b leucocyte common antigen alleles."
    Zebedee S.L., Barritt D.S., Raschke W.C.
    Dev. Immunol. 1:243-254(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/c.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "Alternative use of 5' exons in the specification of Ly-5 isoforms distinguishing hematopoietic cell lineages."
    Saga Y., Tung J.-S., Shen F.-W.W., Boyse E.A.
    Proc. Natl. Acad. Sci. U.S.A. 84:5364-5368(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-226 (ISOFORM 2).
  6. "Organization of the Ly-5 gene."
    Saga Y., Tung J.-S., Shen F.-W.W., Pancoast T.C., Boyse E.A.
    Mol. Cell. Biol. 8:4889-4895(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
  7. "Sequence conservation in potential regulatory regions of the mouse and human leukocyte common antigen gene."
    Johnson N.A., Meyer C.M., Pingel J.T., Thomas M.L.
    J. Biol. Chem. 264:6220-6229(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-263 (ISOFORM 3).
    Tissue: T-cell.
  9. "Structural features of Ly-5 glycoproteins of the mouse and counterparts in other mammals."
    Tung J.-S., Saga Y., Boyse E.A.
    Immunogenetics 28:271-277(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-73.
  10. "Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification."
    Yi T., Cleveland J.L., Ihle J.N.
    Blood 78:2222-2228(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 730-838.
  11. "Cloned murine T200 (Ly-5) cDNA reveals multiple transcripts within B- and T-lymphocyte lineages."
    Raschke W.C.
    Proc. Natl. Acad. Sci. U.S.A. 84:161-165(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 961-1291.
  12. "High sequence conservation between rat (T200) and mouse (Ly-5) leukocyte common antigens."
    Gonez L.J., Walker I.D., Sandrin M.S., McKenzie I.F.
    Immunogenetics 25:263-266(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  13. "Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II."
    Arendt C.W., Ostergaard H.L.
    J. Biol. Chem. 272:13117-13125(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GANAB AND PRKCSH.
  14. "CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells."
    Katagiri T., Ogimoto M., Hasegawa K., Arimura Y., Mitomo K., Okada M., Clark M.R., Mizuno K., Yakura H.
    J. Immunol. 163:1321-1326(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPTPRC_MOUSE
AccessioniPrimary (citable) accession number: P06800
Secondary accession number(s): E9QLT5
, Q61812, Q61813, Q61814, Q61815, Q78EF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3