Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Receptor-type tyrosine-protein phosphatase C (EC 3.1.3.48) (Leukocyte common antigen) (L-CA) (T200) (CD antigen CD45)

 PTPRC_HUMAN             Reviewed;        1306 AA.
P08575; A0A0A0MT22; A8K7W6; Q16614; Q9H0Y6; X6R433;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 3.
28-MAR-2018, entry version 207.
RecName: Full=Receptor-type tyrosine-protein phosphatase C {ECO:0000305};
EC=3.1.3.48;
AltName: Full=Leukocyte common antigen;
Short=L-CA;
AltName: Full=T200;
AltName: CD_antigen=CD45;
Flags: Precursor;
Name=PTPRC {ECO:0000312|HGNC:HGNC:9666}; Synonyms=CD45;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
TISSUE=Lymphocyte;
PubMed=2824653; DOI=10.1084/jem.166.5.1548;
Streuli M., Hall L.R., Saga Y., Schlossman S.F., Saito H.;
"Differential usage of three exons generates at least five different
mRNAs encoding human leukocyte common antigens.";
J. Exp. Med. 166:1548-1566(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
PubMed=2956090;
Ralph S.J., Thomas M.L., Morton C.C., Trowbridge I.S.;
"Structural variants of human T200 glycoprotein (leukocyte-common
antigen).";
EMBO J. 6:1251-1257(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-194.
PubMed=2531281; DOI=10.1128/MCB.9.10.4550;
Tsai A.Y.M., Streuli M., Saito H.;
"Integrity of the exon 6 sequence is essential for tissue-specific
alternative splicing of human leukocyte common antigen pre-mRNA.";
Mol. Cell. Biol. 9:4550-4555(1989).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 193-1306.
TISSUE=Placenta;
PubMed=2971730;
Hall L.R., Streuli M., Schlossman S.F., Saito H.;
"Complete exon-intron organization of the human leukocyte common
antigen (CD45) gene.";
J. Immunol. 141:2781-2787(1988).
[8]
FUNCTION.
PubMed=2845400; DOI=10.1073/pnas.85.19.7182;
Charbonneau H., Tonks N.K., Walsh K.A., Fischer E.H.;
"The leukocyte common antigen (CD45): a putative receptor-linked
protein tyrosine phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 85:7182-7186(1988).
[9]
MUTAGENESIS.
PubMed=1695146;
Streuli M., Krueger N.X., Thai T., Tang M., Saito H.;
"Distinct functional roles of the two intracellular phosphatase like
domains of the receptor-linked protein tyrosine phosphatases LCA and
LAR.";
EMBO J. 9:2399-2407(1990).
[10]
INTERACTION WITH SKAP1, MUTAGENESIS OF CYS-853, AND FUNCTION.
PubMed=11909961; DOI=10.1128/MCB.22.8.2673-2686.2002;
Wu L., Fu J., Shen S.-H.;
"SKAP55 coupled with CD45 positively regulates T-cell receptor-
mediated gene transcription.";
Mol. Cell. Biol. 22:2673-2686(2002).
[11]
INTERACTION WITH DPP4, AND SUBCELLULAR LOCATION.
PubMed=12676959; DOI=10.1074/jbc.M212978200;
Salgado F.J., Lojo J., Alonso-Lebrero J.L., Lluis C., Franco R.,
Cordero O.J., Nogueira M.;
"A role for interleukin-12 in the regulation of T cell plasma membrane
compartmentation.";
J. Biol. Chem. 278:24849-24857(2003).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-234 AND ASN-337.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-234; ASN-242; ASN-278;
ASN-286; ASN-337; ASN-421; ASN-490 AND ASN-499.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975 AND SER-1299, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL11.
PubMed=22174689; DOI=10.1371/journal.ppat.1002432;
Gabaev I., Steinbrueck L., Pokoyski C., Pich A., Stanton R.J.,
Schwinzer R., Schulz T.F., Jacobs R., Messerle M., Kay-Fedorov P.C.;
"The human cytomegalovirus UL11 protein interacts with the receptor
tyrosine phosphatase CD45, resulting in functional paralysis of T
cells.";
PLoS Pathog. 7:E1002432-E1002432(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975 AND SER-994, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 624-1233 ALONE AND IN COMPLEX
WITH PHOSPHOPEPTIDE.
PubMed=15684325; DOI=10.1084/jem.20041890;
Nam H.J., Poy F., Saito H., Frederick C.A.;
"Structural basis for the function and regulation of the receptor
protein tyrosine phosphatase CD45.";
J. Exp. Med. 201:441-452(2005).
[21]
INVOLVEMENT IN SUSCEPTIBILITY TO MS.
PubMed=11101853; DOI=10.1038/82659;
Jacobsen M., Schweer D., Ziegler A., Gaber R., Schock S.,
Schwinzer R., Wonigeit K., Lindert R.-B., Kantarci O.,
Schaefer-Klein J., Schipper H.I., Oertel W.H., Heidenreich F.,
Weinshenker B.G., Sommer N., Hemmer B.;
"A point mutation in PTPRC is associated with the development of
multiple sclerosis.";
Nat. Genet. 26:495-499(2000).
[22]
VARIANT T(-)B(+)NK(+) SCID 364-GLU--TYR-365 DEL, AND CHARACTERIZATION
OF VARIANT T(-)B(+)NK(+) SCID 364-GLU--TYR-365 DEL.
PubMed=11145714; DOI=10.4049/jimmunol.166.2.1308;
Tchilian E.Z., Wallace D.L., Wells R.S., Flower D.R., Morgan G.,
Beverley P.C.L.;
"A deletion in the gene encoding the CD45 antigen in a patient with
SCID.";
J. Immunol. 166:1308-1313(2001).
[23]
VARIANTS [LARGE SCALE ANALYSIS] ALA-230 AND ARG-865.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: 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). {ECO:0000250, ECO:0000269|PubMed:11909961,
ECO:0000269|PubMed:2845400}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- SUBUNIT: 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. {ECO:0000250,
ECO:0000269|PubMed:11909961, ECO:0000269|PubMed:12676959,
ECO:0000269|PubMed:15684325, ECO:0000269|PubMed:22174689}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1341, EBI-1341;
P41240:CSK; NbExp=3; IntAct=EBI-1341, EBI-1380630;
P35222:CTNNB1; NbExp=2; IntAct=EBI-1341, EBI-491549;
P04626:ERBB2; NbExp=2; IntAct=EBI-1341, EBI-641062;
P20701:ITGAL; NbExp=2; IntAct=EBI-1341, EBI-961214;
P06239:LCK; NbExp=7; IntAct=EBI-1341, EBI-1348;
P06240:Lck (xeno); NbExp=2; IntAct=EBI-1341, EBI-1401;
P09382:LGALS1; NbExp=2; IntAct=EBI-1341, EBI-1048875;
Q02763:TEK; NbExp=3; IntAct=EBI-1341, EBI-2257090;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12676959};
Single-pass type I membrane protein {ECO:0000269|PubMed:12676959}.
Membrane raft {ECO:0000269|PubMed:12676959}. Note=Colocalized with
DPP4 in membrane rafts.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=At least 8 isoforms are produced.;
Name=1;
IsoId=P08575-3; Sequence=Displayed;
Name=2;
IsoId=P08575-4; Sequence=VSP_059409;
-!- DOMAIN: The first PTPase domain interacts with SKAP1.
-!- PTM: Heavily N- and O-glycosylated. {ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
-!- DISEASE: 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.
{ECO:0000269|PubMed:11145714}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:11101853}. Note=Disease susceptibility may be
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Receptor class 1/6 subfamily. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAF84820.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA68269.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA68669.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=PTPRCbase; Note=PTPRC mutation db;
URL="http://structure.bmc.lu.se/idbase/PTPRCbase/";
-!- WEB RESOURCE: Name=Wikipedia; Note=CD45 entry;
URL="https://en.wikipedia.org/wiki/CD45";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y00638; CAA68669.1; ALT_INIT; mRNA.
EMBL; Y00062; CAA68269.1; ALT_INIT; mRNA.
EMBL; AK292131; BAF84820.1; ALT_INIT; mRNA.
EMBL; AL157402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL355988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF510707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91303.1; -; Genomic_DNA.
EMBL; M23492; AAD15273.2; -; Genomic_DNA.
EMBL; M23496; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23466; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23467; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23468; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23469; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23470; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23471; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23472; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23473; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23474; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23475; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23476; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23477; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23478; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23479; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23480; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23481; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23482; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23483; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23484; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23485; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23486; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23487; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23488; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23489; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23490; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23491; AAD15273.2; JOINED; Genomic_DNA.
PIR; A46546; A46546.
RefSeq; NP_002829.3; NM_002838.4.
RefSeq; NP_563578.2; NM_080921.3.
UniGene; Hs.654514; -.
PDB; 1YGR; X-ray; 2.90 A; A/B=624-1233.
PDB; 1YGU; X-ray; 2.90 A; A/B=624-1233.
PDB; 5FMV; X-ray; 2.90 A; A/B=225-573.
PDB; 5FN6; X-ray; 3.30 A; A=225-481.
PDB; 5FN7; X-ray; 2.30 A; A/B=225-394.
PDBsum; 1YGR; -.
PDBsum; 1YGU; -.
PDBsum; 5FMV; -.
PDBsum; 5FN6; -.
PDBsum; 5FN7; -.
ProteinModelPortal; P08575; -.
SMR; P08575; -.
BioGrid; 111752; 24.
DIP; DIP-224N; -.
IntAct; P08575; 40.
MINT; P08575; -.
STRING; 9606.ENSP00000356346; -.
BindingDB; P08575; -.
ChEMBL; CHEMBL3243; -.
DEPOD; P08575; -.
iPTMnet; P08575; -.
PhosphoSitePlus; P08575; -.
SwissPalm; P08575; -.
UniCarbKB; P08575; -.
BioMuta; PTPRC; -.
DMDM; 33112650; -.
EPD; P08575; -.
MaxQB; P08575; -.
PaxDb; P08575; -.
PeptideAtlas; P08575; -.
PRIDE; P08575; -.
Ensembl; ENST00000367376; ENSP00000356346; ENSG00000081237.
Ensembl; ENST00000573477; ENSP00000461074; ENSG00000262418.
Ensembl; ENST00000573679; ENSP00000458322; ENSG00000262418.
Ensembl; ENST00000594404; ENSP00000471843; ENSG00000081237.
GeneID; 5788; -.
KEGG; hsa:5788; -.
UCSC; uc001gur.3; human.
UCSC; uc001gut.3; human.
CTD; 5788; -.
DisGeNET; 5788; -.
EuPathDB; HostDB:ENSG00000081237.18; -.
GeneCards; PTPRC; -.
HGNC; HGNC:9666; PTPRC.
HPA; HPA000440; -.
MalaCards; PTPRC; -.
MIM; 126200; phenotype.
MIM; 151460; gene.
MIM; 608971; phenotype.
neXtProt; NX_P08575; -.
OpenTargets; ENSG00000081237; -.
Orphanet; 169157; T-B+ severe combined immunodeficiency due to CD45 deficiency.
PharmGKB; PA34011; -.
eggNOG; KOG4228; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00760000118900; -.
HOGENOM; HOG000049064; -.
HOVERGEN; HBG000066; -.
InParanoid; P08575; -.
KO; K06478; -.
OMA; KHELEMS; -.
OrthoDB; EOG091G015A; -.
PhylomeDB; P08575; -.
TreeFam; TF351829; -.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-HSA-416700; Other semaphorin interactions.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SignaLink; P08575; -.
SIGNOR; P08575; -.
ChiTaRS; PTPRC; human.
EvolutionaryTrace; P08575; -.
GeneWiki; PTPRC; -.
GenomeRNAi; 5788; -.
PRO; PR:P08575; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000081237; -.
CleanEx; HS_PTPRC; -.
ExpressionAtlas; X6R433; baseline and differential.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
GO; GO:0042100; P:B cell proliferation; ISS:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0048539; P:bone marrow development; IMP:UniProtKB.
GO; GO:0044770; P:cell cycle phase transition; IMP:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:UniProtKB.
GO; GO:0002378; P:immunoglobulin biosynthetic process; IMP:UniProtKB.
GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IMP:UniProtKB.
GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; ISS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0050857; P:positive regulation of antigen receptor-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
GO; GO:2000473; P:positive regulation of hematopoietic stem cell migration; IMP:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; NAS:UniProtKB.
GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
GO; GO:0048864; P:stem cell development; IMP:UniProtKB.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.90.190.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR024739; PTP_recept_N.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR016335; Ptprc.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF12567; CD45; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF12453; PTP_N; 1.
Pfam; PF00102; Y_phosphatase; 2.
PIRSF; PIRSF002004; Leukocyte_common_antigen; 1.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00060; FN3; 2.
SMART; SM00194; PTPc; 2.
SMART; SM00404; PTPc_motif; 2.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF52799; SSF52799; 2.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
Polymorphism; Protein phosphatase; Reference proteome; Repeat; SCID;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 25
CHAIN 26 1306 Receptor-type tyrosine-protein
phosphatase C.
/FTId=PRO_0000025470.
TOPO_DOM 26 577 Extracellular. {ECO:0000255}.
TRANSMEM 578 598 Helical. {ECO:0000255}.
TOPO_DOM 599 1306 Cytoplasmic. {ECO:0000255}.
DOMAIN 391 483 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 484 576 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 653 912 Tyrosine-protein phosphatase 1.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
DOMAIN 944 1228 Tyrosine-protein phosphatase 2.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 853 859 Substrate binding. {ECO:0000250}.
ACT_SITE 853 853 Phosphocysteine intermediate.
ACT_SITE 1169 1169 Phosphocysteine intermediate.
{ECO:0000250}.
BINDING 821 821 Substrate. {ECO:0000250}.
BINDING 897 897 Substrate. {ECO:0000250}.
MOD_RES 683 683 Phosphotyrosine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 975 975 Phosphoserine.
{ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 994 994 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 997 997 Phosphoserine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 1001 1001 Phosphoserine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 1004 1004 Phosphoserine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 1005 1005 Phosphoserine.
{ECO:0000250|UniProtKB:P06800}.
MOD_RES 1009 1009 Phosphoserine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 1299 1299 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 262 262 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 286 286 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 380 380 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 421 421 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 470 470 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 490 490 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 499 499 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 531 531 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 34 194 Missing (in isoform 2).
/FTId=VSP_059409.
VARIANT 193 193 T -> A (in dbSNP:rs4915154).
/FTId=VAR_036860.
VARIANT 230 230 E -> A (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035653.
VARIANT 296 296 I -> L (in dbSNP:rs2230606).
/FTId=VAR_051763.
VARIANT 364 365 Missing (in T(-)B(+)NK(+) SCID;
associated with lack of surface
expression).
{ECO:0000269|PubMed:11145714}.
/FTId=VAR_021205.
VARIANT 423 423 T -> I (in dbSNP:rs6696162).
/FTId=VAR_051764.
VARIANT 570 570 H -> Q (in dbSNP:rs12136658).
/FTId=VAR_051765.
VARIANT 865 865 G -> R (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035654.
VARIANT 1285 1285 S -> R (in dbSNP:rs2298872).
/FTId=VAR_020303.
MUTAGEN 853 853 C->S: Loss of activity. Abolishes
interaction with SKAP1.
{ECO:0000269|PubMed:11909961}.
CONFLICT 652 652 L -> P (in Ref. 1; CAA68669).
{ECO:0000305}.
CONFLICT 1209 1209 P -> L (in Ref. 1; CAA68669).
{ECO:0000305}.
HELIX 228 231 {ECO:0000244|PDB:5FN7}.
TURN 232 234 {ECO:0000244|PDB:5FN7}.
STRAND 237 242 {ECO:0000244|PDB:5FN7}.
TURN 243 246 {ECO:0000244|PDB:5FN7}.
STRAND 247 252 {ECO:0000244|PDB:5FN7}.
STRAND 259 263 {ECO:0000244|PDB:5FN7}.
HELIX 266 268 {ECO:0000244|PDB:5FN7}.
STRAND 269 273 {ECO:0000244|PDB:5FN7}.
STRAND 278 284 {ECO:0000244|PDB:5FN7}.
STRAND 288 291 {ECO:0000244|PDB:5FN7}.
STRAND 293 298 {ECO:0000244|PDB:5FN7}.
HELIX 303 305 {ECO:0000244|PDB:5FN7}.
STRAND 306 310 {ECO:0000244|PDB:5FN7}.
HELIX 314 316 {ECO:0000244|PDB:5FN7}.
TURN 317 319 {ECO:0000244|PDB:5FN7}.
STRAND 321 327 {ECO:0000244|PDB:5FN7}.
HELIX 335 337 {ECO:0000244|PDB:5FN7}.
STRAND 338 344 {ECO:0000244|PDB:5FN7}.
STRAND 347 356 {ECO:0000244|PDB:5FN7}.
STRAND 364 373 {ECO:0000244|PDB:5FN7}.
STRAND 376 388 {ECO:0000244|PDB:5FN7}.
STRAND 396 401 {ECO:0000244|PDB:5FMV}.
STRAND 403 406 {ECO:0000244|PDB:5FMV}.
STRAND 408 413 {ECO:0000244|PDB:5FMV}.
STRAND 420 427 {ECO:0000244|PDB:5FMV}.
STRAND 429 438 {ECO:0000244|PDB:5FMV}.
STRAND 443 446 {ECO:0000244|PDB:5FMV}.
STRAND 454 470 {ECO:0000244|PDB:5FMV}.
STRAND 474 479 {ECO:0000244|PDB:5FMV}.
STRAND 489 499 {ECO:0000244|PDB:5FMV}.
STRAND 501 506 {ECO:0000244|PDB:5FMV}.
STRAND 518 541 {ECO:0000244|PDB:5FMV}.
STRAND 549 557 {ECO:0000244|PDB:5FMV}.
STRAND 566 571 {ECO:0000244|PDB:5FMV}.
TURN 635 637 {ECO:0000244|PDB:1YGR}.
HELIX 638 658 {ECO:0000244|PDB:1YGR}.
STRAND 665 667 {ECO:0000244|PDB:1YGR}.
TURN 670 672 {ECO:0000244|PDB:1YGR}.
HELIX 675 680 {ECO:0000244|PDB:1YGR}.
TURN 690 692 {ECO:0000244|PDB:1YGR}.
STRAND 693 695 {ECO:0000244|PDB:1YGR}.
STRAND 700 702 {ECO:0000244|PDB:1YGR}.
TURN 703 706 {ECO:0000244|PDB:1YGR}.
STRAND 707 713 {ECO:0000244|PDB:1YGR}.
STRAND 716 718 {ECO:0000244|PDB:1YGR}.
STRAND 722 725 {ECO:0000244|PDB:1YGR}.
TURN 730 732 {ECO:0000244|PDB:1YGR}.
HELIX 733 742 {ECO:0000244|PDB:1YGR}.
STRAND 747 750 {ECO:0000244|PDB:1YGR}.
STRAND 754 756 {ECO:0000244|PDB:1YGR}.
STRAND 759 761 {ECO:0000244|PDB:1YGR}.
TURN 769 771 {ECO:0000244|PDB:1YGR}.
STRAND 773 776 {ECO:0000244|PDB:1YGR}.
STRAND 779 788 {ECO:0000244|PDB:1YGR}.
STRAND 790 804 {ECO:0000244|PDB:1YGR}.
STRAND 809 816 {ECO:0000244|PDB:1YGR}.
HELIX 828 838 {ECO:0000244|PDB:1YGR}.
STRAND 849 852 {ECO:0000244|PDB:1YGR}.
STRAND 854 857 {ECO:0000244|PDB:1YGR}.
HELIX 858 871 {ECO:0000244|PDB:1YGR}.
HELIX 873 876 {ECO:0000244|PDB:1YGR}.
STRAND 877 879 {ECO:0000244|PDB:1YGR}.
HELIX 881 889 {ECO:0000244|PDB:1YGR}.
HELIX 899 915 {ECO:0000244|PDB:1YGR}.
HELIX 922 924 {ECO:0000244|PDB:1YGR}.
HELIX 925 932 {ECO:0000244|PDB:1YGR}.
HELIX 943 950 {ECO:0000244|PDB:1YGR}.
HELIX 962 964 {ECO:0000244|PDB:1YGR}.
HELIX 968 970 {ECO:0000244|PDB:1YGR}.
TURN 981 983 {ECO:0000244|PDB:1YGR}.
STRAND 1020 1024 {ECO:0000244|PDB:1YGR}.
STRAND 1031 1036 {ECO:0000244|PDB:1YGR}.
TURN 1040 1042 {ECO:0000244|PDB:1YGR}.
HELIX 1043 1052 {ECO:0000244|PDB:1YGR}.
STRAND 1057 1060 {ECO:0000244|PDB:1YGR}.
STRAND 1064 1066 {ECO:0000244|PDB:1YGR}.
STRAND 1069 1072 {ECO:0000244|PDB:1YGR}.
STRAND 1090 1095 {ECO:0000244|PDB:1YGR}.
STRAND 1097 1107 {ECO:0000244|PDB:1YGR}.
STRAND 1115 1122 {ECO:0000244|PDB:1YGR}.
STRAND 1127 1129 {ECO:0000244|PDB:1YGR}.
HELIX 1134 1145 {ECO:0000244|PDB:1YGR}.
STRAND 1165 1173 {ECO:0000244|PDB:1YGR}.
HELIX 1176 1191 {ECO:0000244|PDB:1YGR}.
STRAND 1192 1194 {ECO:0000244|PDB:1YGR}.
HELIX 1197 1207 {ECO:0000244|PDB:1YGR}.
TURN 1209 1212 {ECO:0000244|PDB:1YGR}.
HELIX 1215 1227 {ECO:0000244|PDB:1YGR}.
SEQUENCE 1306 AA; 147486 MW; 6E942E2BF6B17AC5 CRC64;
MTMYLWLKLL AFGFAFLDTE VFVTGQSPTP SPTGLTTAKM PSVPLSSDPL PTHTTAFSPA
STFERENDFS ETTTSLSPDN TSTQVSPDSL DNASAFNTTG VSSVQTPHLP THADSQTPSA
GTDTQTFSGS AANAKLNPTP GSNAISDVPG ERSTASTFPT DPVSPLTTTL SLAHHSSAAL
PARTSNTTIT ANTSDAYLNA SETTTLSPSG SAVISTTTIA TTPSKPTCDE KYANITVDYL
YNKETKLFTA KLNVNENVEC GNNTCTNNEV HNLTECKNAS VSISHNSCTA PDKTLILDVP
PGVEKFQLHD CTQVEKADTT ICLKWKNIET FTCDTQNITY RFQCGNMIFD NKEIKLENLE
PEHEYKCDSE ILYNNHKFTN ASKIIKTDFG SPGEPQIIFC RSEAAHQGVI TWNPPQRSFH
NFTLCYIKET EKDCLNLDKN LIKYDLQNLK PYTKYVLSLH AYIIAKVQRN GSAAMCHFTT
KSAPPSQVWN MTVSMTSDNS MHVKCRPPRD RNGPHERYHL EVEAGNTLVR NESHKNCDFR
VKDLQYSTDY TFKAYFHNGD YPGEPFILHH STSYNSKALI AFLAFLIIVT SIALLVVLYK
IYDLHKKRSC NLDEQQELVE RDDEKQLMNV EPIHADILLE TYKRKIADEG RLFLAEFQSI
PRVFSKFPIK EARKPFNQNK NRYVDILPYD YNRVELSEIN GDAGSNYINA SYIDGFKEPR
KYIAAQGPRD ETVDDFWRMI WEQKATVIVM VTRCEEGNRN KCAEYWPSME EGTRAFGDVV
VKINQHKRCP DYIIQKLNIV NKKEKATGRE VTHIQFTSWP DHGVPEDPHL LLKLRRRVNA
FSNFFSGPIV VHCSAGVGRT GTYIGIDAML EGLEAENKVD VYGYVVKLRR QRCLMVQVEA
QYILIHQALV EYNQFGETEV NLSELHPYLH NMKKRDPPSE PSPLEAEFQR LPSYRSWRTQ
HIGNQEENKS KNRNSNVIPY DYNRVPLKHE LEMSKESEHD SDESSDDDSD SEEPSKYINA
SFIMSYWKPE VMIAAQGPLK ETIGDFWQMI FQRKVKVIVM LTELKHGDQE ICAQYWGEGK
QTYGDIEVDL KDTDKSSTYT LRVFELRHSK RKDSRTVYQY QYTNWSVEQL PAEPKELISM
IQVVKQKLPQ KNSSEGNKHH KSTPLLIHCR DGSQQTGIFC ALLNLLESAE TEEVVDIFQV
VKALRKARPG MVSTFEQYQF LYDVIASTYP AQNGQVKKNN HQEDKIEFDN EVDKVKQDAN
CVNPLGAPEK LPEAKEQAEG SEPTSGTEGP EHSVNGPASP ALNQGS


Related products :

Catalog number Product name Quantity
E1030h ELISA CD45,Homo sapiens,Human,L-CA,Leukocyte common antigen,PTPRC,Receptor-type tyrosine-protein phosphatase C,T200 96T
U1030h CLIA CD45,Homo sapiens,Human,L-CA,Leukocyte common antigen,PTPRC,Receptor-type tyrosine-protein phosphatase C,T200 96T
E1030h ELISA kit CD45,Homo sapiens,Human,L-CA,Leukocyte common antigen,PTPRC,Receptor-type tyrosine-protein phosphatase C,T200 96T
E1030m ELISA L-CA,Leukocyte common antigen,Ly-5,Ly-5,Lymphocyte antigen 5,Mouse,Mus musculus,Ptprc,Receptor-type tyrosine-protein phosphatase C,T200 96T
E1030m ELISA kit L-CA,Leukocyte common antigen,Ly-5,Ly-5,Lymphocyte antigen 5,Mouse,Mus musculus,Ptprc,Receptor-type tyrosine-protein phosphatase C,T200 96T
U1030m CLIA L-CA,Leukocyte common antigen,Ly-5,Ly-5,Lymphocyte antigen 5,Mouse,Mus musculus,Ptprc,Receptor-type tyrosine-protein phosphatase C,T200 96T
E1030r ELISA L-CA,Leukocyte common antigen,Ptprc,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase C,T200 96T
E1030r ELISA kit L-CA,Leukocyte common antigen,Ptprc,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase C,T200 96T
U1030r CLIA L-CA,Leukocyte common antigen,Ptprc,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase C,T200 96T
EIAAB33112 LAR-PTP2,Leukocyte common antigen-related protein-tyrosine phosphatase 2,Ptprs,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase S,Receptor-type tyrosine-protein phosphatase sigma,R-PTP
EIAAB33084 LAR,Lar,Leukocyte common antigen related,Ptprf,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase F
EIAAB33085 LAR,Lar,Leukocyte common antigen related,Mouse,Mus musculus,Ptprf,Receptor-type tyrosine-protein phosphatase F
15-288-21465 Leukocyte common antigen - EC 3.1.3.48; L-CA; CD45 antigen; T200 Polyclonal 0.05 mg
15-288-21465 Leukocyte common antigen - EC 3.1.3.48; L-CA; CD45 antigen; T200 Polyclonal 0.1 mg
10-782-55092 Leukocyte common antigen - EC 3.1.3.48; L-CA; CD45 antigen; T200 N_A 0.01 mg
10-782-55092 Leukocyte common antigen - EC 3.1.3.48; L-CA; CD45 antigen; T200 N_A 0.005 mg
10-782-55092 Leukocyte common antigen - EC 3.1.3.48; L-CA; CD45 antigen; T200 N_A 0.001 mg
10-782-55092 Leukocyte common antigen - EC 3.1.3.48; L-CA; CD45 antigen; T200 N_A 0.02 mg
EIAAB33086 Homo sapiens,Human,LAR,LAR,Leukocyte common antigen related,PTPRF,Receptor-type tyrosine-protein phosphatase F
15-288-21469 Receptor-type tyrosine-protein phosphatase F - EC 3.1.3.48; LAR protein; Leukocyte antigen related Polyclonal 0.05 mg
15-288-21469 Receptor-type tyrosine-protein phosphatase F - EC 3.1.3.48; LAR protein; Leukocyte antigen related Polyclonal 0.1 mg
10-054-165004 DEP1 (1024-1306) HUMAN - EC 3.1.3.48; Protein-tyrosine phosphatase eta; R-PTP-eta; HPTP eta; Protein-tyrosine phosphatase receptor type J; Density-enhanced phosphatase 1; DEP-1; CD148 antigen 0.02 mg
10-054-165001 PTPbeta (1675-1996) HUMAN - EC 3.1.3.48; Protein-tyrosine phosphatase eta; R-PTP-eta; HPTP eta; Protein-tyrosine phosphatase receptor type J; Density-enhanced phosphatase 1; DEP-1; CD148 antigen 0.02 mg
MA-CD45-6 Anti-human CD45 (Leukocyte Common Antigen) IgG fraction (monoclonal) 200
MA-CD45-6 Anti_human CD45 (Leukocyte Common Antigen) IgG fraction (monoclonal) 200 µg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur