Full text data of PTPRCAP
PTPRCAP
(LPAP)
[Confidence: low (only semi-automatic identification from reviews)]
Protein tyrosine phosphatase receptor type C-associated protein; PTPRC-associated protein (CD45-associated protein; CD45-AP; Lymphocyte phosphatase-associated phosphoprotein)
Protein tyrosine phosphatase receptor type C-associated protein; PTPRC-associated protein (CD45-associated protein; CD45-AP; Lymphocyte phosphatase-associated phosphoprotein)
UniProt
Q14761
ID PTCA_HUMAN Reviewed; 206 AA.
AC Q14761; B2R512; O00643; Q6I9S6;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=Protein tyrosine phosphatase receptor type C-associated protein;
DE Short=PTPRC-associated protein;
DE AltName: Full=CD45-associated protein;
DE Short=CD45-AP;
DE AltName: Full=Lymphocyte phosphatase-associated phosphoprotein;
GN Name=PTPRCAP; Synonyms=LPAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7961877;
RA Schraven B., Schoenhaut D., Bruyns E., Koretzky G., Eckerskorn C.,
RA Wallich R., Kirchgessner H., Sakorafas P., Labkovsky B., Ratnofsky S.,
RA Meuer S.;
RT "LPAP, a novel 32-kDa phosphoprotein that interacts with CD45 in human
RT lymphocytes.";
RL J. Biol. Chem. 269:29102-29111(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8954783; DOI=10.1006/geno.1996.0595;
RA Bruyns E., Mincheva A., Bruyns R.M., Kirchgessner H., Weitz S.,
RA Lichter P., Meuer S., Schraven B.;
RT "Sequence, genomic organization, and chromosomal localization of the
RT human LPAP (PTPRCAP) and mouse CD45-AP/LSM-1 genes.";
RL Genomics 38:79-83(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH CD45.
RX PubMed=8537410; DOI=10.1074/jbc.270.52.31372;
RA Bruyns E., Hendricks-Taylor L.R., Meuer S., Koretzky G.A.,
RA Schraven B.;
RT "Identification of the sites of interaction between lymphocyte
RT phosphatase-associated phosphoprotein (LPAP) and CD45.";
RL J. Biol. Chem. 270:31372-31376(1995).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- SUBUNIT: Interacts with CD45/PTPRC.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC (Potential).
CC -!- PTM: Phosphorylated on tyrosine residues.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X81422; CAA57182.1; -; mRNA.
DR EMBL; X97267; CAA65922.1; -; Genomic_DNA.
DR EMBL; CR457429; CAG33710.1; -; mRNA.
DR EMBL; AK312022; BAG34959.1; -; mRNA.
DR EMBL; BC113859; AAI13860.1; -; mRNA.
DR EMBL; BC114467; AAI14468.1; -; mRNA.
DR PIR; A55412; A55412.
DR RefSeq; NP_005599.1; NM_005608.2.
DR UniGene; Hs.155975; -.
DR ProteinModelPortal; Q14761; -.
DR IntAct; Q14761; 2.
DR MINT; MINT-1389998; -.
DR STRING; 9606.ENSP00000325589; -.
DR BindingDB; Q14761; -.
DR ChEMBL; CHEMBL4806; -.
DR PhosphoSite; Q14761; -.
DR DMDM; 22001841; -.
DR PaxDb; Q14761; -.
DR PRIDE; Q14761; -.
DR Ensembl; ENST00000326294; ENSP00000325589; ENSG00000213402.
DR GeneID; 5790; -.
DR KEGG; hsa:5790; -.
DR UCSC; uc001oli.1; human.
DR CTD; 5790; -.
DR GeneCards; GC11M067202; -.
DR H-InvDB; HIX0079400; -.
DR H-InvDB; HIX0201772; -.
DR HGNC; HGNC:9667; PTPRCAP.
DR HPA; HPA043734; -.
DR MIM; 601577; gene.
DR neXtProt; NX_Q14761; -.
DR PharmGKB; PA34012; -.
DR eggNOG; NOG87279; -.
DR HOGENOM; HOG000115756; -.
DR HOVERGEN; HBG030697; -.
DR InParanoid; Q14761; -.
DR OMA; GYYHPAR; -.
DR OrthoDB; EOG70W3GN; -.
DR PhylomeDB; Q14761; -.
DR GeneWiki; PTPRCAP; -.
DR GenomeRNAi; 5790; -.
DR NextBio; 22540; -.
DR PRO; PR:Q14761; -.
DR Bgee; Q14761; -.
DR CleanEx; HS_PTPRCAP; -.
DR Genevestigator; Q14761; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR InterPro; IPR016553; Tyr_Pase_rcpt_C-assoc_CD45-AP.
DR PANTHER; PTHR15312; PTHR15312; 1.
DR PIRSF; PIRSF009325; PTPRC-associated_protein; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 206 Protein tyrosine phosphatase receptor
FT type C-associated protein.
FT /FTId=PRO_0000097087.
FT TRANSMEM 34 54 Helical; (Potential).
FT VARIANT 128 128 G -> E (in dbSNP:rs60969594).
FT /FTId=VAR_061698.
SQ SEQUENCE 206 AA; 21196 MW; 26A9F96699BD34D5 CRC64;
MALPCTLGLG MLLALPGALG SGGSAEDSVG SSSVTVVLLL LLLLLLATGL ALAWRRLSRD
SGGYYHPARL GAALWGRTRR LLWASPPGRW LQARAELGST DNDLERQEDE QDTDYDHVAD
GGLQADPGEG EQQCGEASSP EQVPVRAEEA RDSDTEGDLV LGSPGPASAG GSAEALLSDL
HAFAGSAAWD DSARAAGGQG LHVTAL
//
ID PTCA_HUMAN Reviewed; 206 AA.
AC Q14761; B2R512; O00643; Q6I9S6;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=Protein tyrosine phosphatase receptor type C-associated protein;
DE Short=PTPRC-associated protein;
DE AltName: Full=CD45-associated protein;
DE Short=CD45-AP;
DE AltName: Full=Lymphocyte phosphatase-associated phosphoprotein;
GN Name=PTPRCAP; Synonyms=LPAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7961877;
RA Schraven B., Schoenhaut D., Bruyns E., Koretzky G., Eckerskorn C.,
RA Wallich R., Kirchgessner H., Sakorafas P., Labkovsky B., Ratnofsky S.,
RA Meuer S.;
RT "LPAP, a novel 32-kDa phosphoprotein that interacts with CD45 in human
RT lymphocytes.";
RL J. Biol. Chem. 269:29102-29111(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8954783; DOI=10.1006/geno.1996.0595;
RA Bruyns E., Mincheva A., Bruyns R.M., Kirchgessner H., Weitz S.,
RA Lichter P., Meuer S., Schraven B.;
RT "Sequence, genomic organization, and chromosomal localization of the
RT human LPAP (PTPRCAP) and mouse CD45-AP/LSM-1 genes.";
RL Genomics 38:79-83(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH CD45.
RX PubMed=8537410; DOI=10.1074/jbc.270.52.31372;
RA Bruyns E., Hendricks-Taylor L.R., Meuer S., Koretzky G.A.,
RA Schraven B.;
RT "Identification of the sites of interaction between lymphocyte
RT phosphatase-associated phosphoprotein (LPAP) and CD45.";
RL J. Biol. Chem. 270:31372-31376(1995).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- SUBUNIT: Interacts with CD45/PTPRC.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC (Potential).
CC -!- PTM: Phosphorylated on tyrosine residues.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X81422; CAA57182.1; -; mRNA.
DR EMBL; X97267; CAA65922.1; -; Genomic_DNA.
DR EMBL; CR457429; CAG33710.1; -; mRNA.
DR EMBL; AK312022; BAG34959.1; -; mRNA.
DR EMBL; BC113859; AAI13860.1; -; mRNA.
DR EMBL; BC114467; AAI14468.1; -; mRNA.
DR PIR; A55412; A55412.
DR RefSeq; NP_005599.1; NM_005608.2.
DR UniGene; Hs.155975; -.
DR ProteinModelPortal; Q14761; -.
DR IntAct; Q14761; 2.
DR MINT; MINT-1389998; -.
DR STRING; 9606.ENSP00000325589; -.
DR BindingDB; Q14761; -.
DR ChEMBL; CHEMBL4806; -.
DR PhosphoSite; Q14761; -.
DR DMDM; 22001841; -.
DR PaxDb; Q14761; -.
DR PRIDE; Q14761; -.
DR Ensembl; ENST00000326294; ENSP00000325589; ENSG00000213402.
DR GeneID; 5790; -.
DR KEGG; hsa:5790; -.
DR UCSC; uc001oli.1; human.
DR CTD; 5790; -.
DR GeneCards; GC11M067202; -.
DR H-InvDB; HIX0079400; -.
DR H-InvDB; HIX0201772; -.
DR HGNC; HGNC:9667; PTPRCAP.
DR HPA; HPA043734; -.
DR MIM; 601577; gene.
DR neXtProt; NX_Q14761; -.
DR PharmGKB; PA34012; -.
DR eggNOG; NOG87279; -.
DR HOGENOM; HOG000115756; -.
DR HOVERGEN; HBG030697; -.
DR InParanoid; Q14761; -.
DR OMA; GYYHPAR; -.
DR OrthoDB; EOG70W3GN; -.
DR PhylomeDB; Q14761; -.
DR GeneWiki; PTPRCAP; -.
DR GenomeRNAi; 5790; -.
DR NextBio; 22540; -.
DR PRO; PR:Q14761; -.
DR Bgee; Q14761; -.
DR CleanEx; HS_PTPRCAP; -.
DR Genevestigator; Q14761; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR InterPro; IPR016553; Tyr_Pase_rcpt_C-assoc_CD45-AP.
DR PANTHER; PTHR15312; PTHR15312; 1.
DR PIRSF; PIRSF009325; PTPRC-associated_protein; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 206 Protein tyrosine phosphatase receptor
FT type C-associated protein.
FT /FTId=PRO_0000097087.
FT TRANSMEM 34 54 Helical; (Potential).
FT VARIANT 128 128 G -> E (in dbSNP:rs60969594).
FT /FTId=VAR_061698.
SQ SEQUENCE 206 AA; 21196 MW; 26A9F96699BD34D5 CRC64;
MALPCTLGLG MLLALPGALG SGGSAEDSVG SSSVTVVLLL LLLLLLATGL ALAWRRLSRD
SGGYYHPARL GAALWGRTRR LLWASPPGRW LQARAELGST DNDLERQEDE QDTDYDHVAD
GGLQADPGEG EQQCGEASSP EQVPVRAEEA RDSDTEGDLV LGSPGPASAG GSAEALLSDL
HAFAGSAAWD DSARAAGGQG LHVTAL
//
MIM
601577
*RECORD*
*FIELD* NO
601577
*FIELD* TI
*601577 PROTEIN-TYROSINE PHOSPHATASE, RECEPTOR-TYPE, C POLYPEPTIDE-ASSOCIATED
PROTEIN; PTPRCAP
read more;;PTPRC-ASSOCIATED PROTEIN;;
LYMPHOCYTE PHOSPHATASE-ASSOCIATED PHOSPHOPROTEIN; LPAP
*FIELD* TX
CLONING
The tyrosine phosphatase CD45 (151460) plays a key role in lymphocyte
activation. Its expression is required for proximal signaling events
following triggering of the T- and B-cell antigen receptors in human and
mouse, and in T cells, the enzymatic phosphatase activity of CD45 is
required to link the T cell receptor/CD3 complex to the intracellular
signaling machinery. Schraven et al. (1994) described the cDNA and
protein sequence of a 32-kD transmembrane phosphoprotein, which they
called LPAP (lymphocyte phosphatase associated phosphoprotein), that
noncovalently interacts with CD45 in human lymphocytes. The interaction
of LPAP and CD45 is mediated by the transmembrane regions of both
molecules and seems to be required for stable protein expression of
LPAP. The mouse homolog is a 30-kD transmembrane protein.
GENE STRUCTURE
Bruyns et al. (1996) isolated and sequenced genomic clones of the human
and mouse genes. Both genes span 3 kb and consist of 2 exons that are
separated by a 1.2-kb intron. The promoter regions do not contain TATA
boxes, but possess consensus transcriptional initiator sequences that
had also been described for other TATA-less genes.
MAPPING
By fluorescence in situ hybridization, Bruyns et al. (1996) mapped the
human LPAP gene to chromosome 11q13, distal to the BCL1 breakpoint
(168461) at 11q13.3, and the mouse homolog to chromosome 19B.
*FIELD* RF
1. Bruyns, E.; Mincheva, A.; Bruyns, R. M.; Kirchgessner, H.; Weitz,
S.; Lichter, P.; Meuer, S.; Schraven, B.: Sequence, genomic organization,
and chromosomal localization of the human LPAP (PTPRCAP) and mouse
CD45-AP/LSM-1 genes. Genomics 38: 79-83, 1996.
2. Schraven, B.; Schoenhaut, D.; Bruyns, E.; Koretzky, G.; Eckerskorn,
C.; Wallich, R.; Kirchgessner, H.; Sakorafas, P.; Labkovsky, B.; Ratnofsky,
S.; Meuer, S.: LPAP, a novel 32-kDa phosphoprotein that interacts
with CD45 in human lymphocytes. J. Biol. Chem. 269: 29102-29111,
1994.
*FIELD* CD
Victor A. McKusick: 12/13/1996
*FIELD* ED
carol: 12/06/2001
carol: 7/16/1998
jenny: 1/14/1997
jenny: 12/20/1996
mark: 12/16/1996
*RECORD*
*FIELD* NO
601577
*FIELD* TI
*601577 PROTEIN-TYROSINE PHOSPHATASE, RECEPTOR-TYPE, C POLYPEPTIDE-ASSOCIATED
PROTEIN; PTPRCAP
read more;;PTPRC-ASSOCIATED PROTEIN;;
LYMPHOCYTE PHOSPHATASE-ASSOCIATED PHOSPHOPROTEIN; LPAP
*FIELD* TX
CLONING
The tyrosine phosphatase CD45 (151460) plays a key role in lymphocyte
activation. Its expression is required for proximal signaling events
following triggering of the T- and B-cell antigen receptors in human and
mouse, and in T cells, the enzymatic phosphatase activity of CD45 is
required to link the T cell receptor/CD3 complex to the intracellular
signaling machinery. Schraven et al. (1994) described the cDNA and
protein sequence of a 32-kD transmembrane phosphoprotein, which they
called LPAP (lymphocyte phosphatase associated phosphoprotein), that
noncovalently interacts with CD45 in human lymphocytes. The interaction
of LPAP and CD45 is mediated by the transmembrane regions of both
molecules and seems to be required for stable protein expression of
LPAP. The mouse homolog is a 30-kD transmembrane protein.
GENE STRUCTURE
Bruyns et al. (1996) isolated and sequenced genomic clones of the human
and mouse genes. Both genes span 3 kb and consist of 2 exons that are
separated by a 1.2-kb intron. The promoter regions do not contain TATA
boxes, but possess consensus transcriptional initiator sequences that
had also been described for other TATA-less genes.
MAPPING
By fluorescence in situ hybridization, Bruyns et al. (1996) mapped the
human LPAP gene to chromosome 11q13, distal to the BCL1 breakpoint
(168461) at 11q13.3, and the mouse homolog to chromosome 19B.
*FIELD* RF
1. Bruyns, E.; Mincheva, A.; Bruyns, R. M.; Kirchgessner, H.; Weitz,
S.; Lichter, P.; Meuer, S.; Schraven, B.: Sequence, genomic organization,
and chromosomal localization of the human LPAP (PTPRCAP) and mouse
CD45-AP/LSM-1 genes. Genomics 38: 79-83, 1996.
2. Schraven, B.; Schoenhaut, D.; Bruyns, E.; Koretzky, G.; Eckerskorn,
C.; Wallich, R.; Kirchgessner, H.; Sakorafas, P.; Labkovsky, B.; Ratnofsky,
S.; Meuer, S.: LPAP, a novel 32-kDa phosphoprotein that interacts
with CD45 in human lymphocytes. J. Biol. Chem. 269: 29102-29111,
1994.
*FIELD* CD
Victor A. McKusick: 12/13/1996
*FIELD* ED
carol: 12/06/2001
carol: 7/16/1998
jenny: 1/14/1997
jenny: 12/20/1996
mark: 12/16/1996