PTPRH_HUMAN
ID PTPRH_HUMAN Reviewed; 1115 AA.
AC Q9HD43; C9JCH2; Q15426; Q2NKN9; Q2NKP0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase H;
DE Short=R-PTP-H;
DE EC=3.1.3.48;
DE AltName: Full=Stomach cancer-associated protein tyrosine phosphatase 1;
DE Short=SAP-1;
DE AltName: Full=Transmembrane-type protein-tyrosine phosphatase type H;
DE Flags: Precursor;
GN Name=PTPRH; Synonyms=SAP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8294459; DOI=10.1016/s0021-9258(17)42137-5;
RA Matozaki T., Suzuki T., Uchida T., Inazawa J., Ariyama T., Matsuda K.,
RA Horita K., Noguchi H., Mizuno H., Sakamoto C., Kasuga M.;
RT "Molecular cloning of a human transmembrane-type protein tyrosine
RT phosphatase and its expression in gastrointestinal cancers.";
RL J. Biol. Chem. 269:2075-2081(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT LYS-823.
RX PubMed=11435690; DOI=10.1159/000056905;
RA Marneros A.G., Mehenni H., Reichenberger E., Antonarakis S.E., Krieg T.,
RA Olsen B.R.;
RT "Gene for the human transmembrane-type protein tyrosine phosphatase H
RT (PTPRH): genomic structure, fine-mapping and its exclusion as a candidate
RT for Peutz-Jeghers syndrome.";
RL Cytogenet. Cell Genet. 92:213-216(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP TYR-348.
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF ASP-986 AND CYS-1020.
RX PubMed=11278335; DOI=10.1074/jbc.m007208200;
RA Noguchi T., Tsuda M., Takeda H., Takada T., Inagaki K., Yamao T.,
RA Fukunaga K., Matozaki T., Kasuga M.;
RT "Inhibition of cell growth and spreading by stomach cancer-associated
RT protein-tyrosine phosphatase-1 (SAP-1) through dephosphorylation of
RT p130cas.";
RL J. Biol. Chem. 276:15216-15224(2001).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF CYS-1020.
RX PubMed=12101188; DOI=10.1074/jbc.m206541200;
RA Takada T., Noguchi T., Inagaki K., Hosooka T., Fukunaga K., Yamao T.,
RA Ogawa W., Matozaki T., Kasuga M.;
RT "Induction of apoptosis by stomach cancer-associated protein-tyrosine
RT phosphatase-1.";
RL J. Biol. Chem. 277:34359-34366(2002).
RN [7]
RP FUNCTION, DOMAIN, TISSUE SPECIFICITY, AND INTERACTION WITH LCK.
RX PubMed=12837766; DOI=10.1074/jbc.m300648200;
RA Ito T., Okazawa H., Maruyama K., Tomizawa K., Motegi S., Ohnishi H.,
RA Kuwano H., Kosugi A., Matozaki T.;
RT "Interaction of SAP-1, a transmembrane-type protein-tyrosine phosphatase,
RT with the tyrosine kinase Lck. Roles in regulation of T cell function.";
RL J. Biol. Chem. 278:34854-34863(2003).
RN [8]
RP SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=12879010; DOI=10.1038/sj.onc.1206588;
RA Nagano H., Noguchi T., Inagaki K., Yoon S., Matozaki T., Itoh H.,
RA Kasuga M., Hayashi Y.;
RT "Downregulation of stomach cancer-associated protein tyrosine phosphatase-1
RT (SAP-1) in advanced human hepatocellular carcinoma.";
RL Oncogene 22:4656-4663(2003).
RN [9]
RP FUNCTION, SUBUNIT, ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=15850787; DOI=10.1016/j.bbrc.2005.03.196;
RA Waelchli S., Espanel X., Hooft van Huijsduijnen R.;
RT "Sap-1/PTPRH activity is regulated by reversible dimerization.";
RL Biochem. Biophys. Res. Commun. 331:497-502(2005).
CC -!- FUNCTION: Protein phosphatase that may contribute to contact inhibition
CC of cell growth and motility by mediating the dephosphorylation of focal
CC adhesion-associated substrates and thus negatively regulating integrin-
CC promoted signaling processes. Induces apoptotic cell death by at least
CC two distinct mechanisms: inhibition of cell survival signaling mediated
CC by PI 3-kinase, Akt, and ILK and activation of a caspase-dependent
CC proapoptotic pathway. Inhibits the basal activity of LCK and its
CC activation in response to TCR stimulation and TCR-induced activation of
CC MAP kinase and surface expression of CD69. Inhibits TCR-induced
CC tyrosine phosphorylation of LAT and ZAP70. Inhibits both basal activity
CC of DOK1 and its CD2-induced tyrosine phosphorylation. Induces
CC dephosphorylation of BCAR1, focal adhesion kinase and SRC. Reduces
CC migratory activity of activity of Jurkat cells. Reduces tyrosine
CC phosphorylation of CEACAM20 and thereby contributes to suppress the
CC intestinal immune response CEACAM20 (By similarity).
CC {ECO:0000250|UniProtKB:E9Q0N2, ECO:0000269|PubMed:11278335,
CC ECO:0000269|PubMed:12101188, ECO:0000269|PubMed:12837766,
CC ECO:0000269|PubMed:15850787}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- ACTIVITY REGULATION: Regulated by reversible dimerization. Dimerization
CC reduces its catalytic activity. {ECO:0000269|PubMed:15850787}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (Probable). Interacts with LCK
CC (PubMed:12837766). Interacts (phosphorylated form) with GRB2 (via SH2
CC domain) (By similarity). Interacts (phosphorylated form) with FYN (via
CC SH2 domain) (By similarity). Interacts (via extracellular domain) with
CC CEACAM20 (via extracellular domain); the interaction dephosphorylates
CC CEACAM20 (By similarity). {ECO:0000250|UniProtKB:E9Q0N2,
CC ECO:0000269|PubMed:12837766, ECO:0000305|PubMed:15850787}.
CC -!- INTERACTION:
CC Q9HD43; P49366: DHPS; NbExp=3; IntAct=EBI-1267176, EBI-741925;
CC Q9HD43; P00533: EGFR; NbExp=3; IntAct=EBI-1267176, EBI-297353;
CC Q9HD43; P10912: GHR; NbExp=4; IntAct=EBI-1267176, EBI-286316;
CC Q9HD43; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1267176, EBI-10171774;
CC -!- SUBCELLULAR LOCATION: Cell projection, microvillus membrane
CC {ECO:0000250|UniProtKB:E9Q0N2}; Single-pass type I membrane protein
CC {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:E9Q0N2};
CC Single-pass type I membrane protein {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:12879010}. Note=Colocalizes with CEACAM20 at the
CC apical brush border of intestinal cells.
CC {ECO:0000250|UniProtKB:E9Q0N2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9HD43-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HD43-2; Sequence=VSP_031318;
CC Name=3;
CC IsoId=Q9HD43-3; Sequence=VSP_054222;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the brain, spleen and
CC liver and at lower levels in the heart and stomach. Expressed in
CC pancreatic and colorectal cancer cells, but not in normal pancreas or
CC colon. Expression in hepatocellular carcinoma is related to the
CC differentiation status of the tumor and expression is inversely related
CC to tumor aggressiveness. {ECO:0000269|PubMed:12837766,
CC ECO:0000269|PubMed:12879010, ECO:0000269|PubMed:8294459}.
CC -!- INDUCTION: Induced at the early stage of hepatocellular carcinoma and
CC is suppressed at later stages. {ECO:0000269|PubMed:12879010}.
CC -!- DOMAIN: The extracellular domain mediates homodimerization. One or more
CC cysteines in the extracellular domain is essential for the formation of
CC dimers probably by forming a disulfide bond.
CC -!- DOMAIN: The cytoplasmic domain mediates the interaction with LCK.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 3 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03645.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D15049; BAA03645.2; ALT_FRAME; mRNA.
DR EMBL; AF275150; AAF91411.1; -; Genomic_DNA.
DR EMBL; AF275131; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275132; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275133; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275134; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275135; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275136; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275137; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275138; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275139; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275140; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275141; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275142; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275143; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275144; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275145; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275146; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275147; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275148; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AF275149; AAF91411.1; JOINED; Genomic_DNA.
DR EMBL; AC010327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC111715; AAI11716.1; -; mRNA.
DR EMBL; BC111716; AAI11717.1; -; mRNA.
DR CCDS; CCDS33110.1; -. [Q9HD43-1]
DR CCDS; CCDS54321.1; -. [Q9HD43-3]
DR PIR; A49724; A49724.
DR RefSeq; NP_001154912.2; NM_001161440.2. [Q9HD43-3]
DR RefSeq; NP_002833.4; NM_002842.4. [Q9HD43-1]
DR AlphaFoldDB; Q9HD43; -.
DR SMR; Q9HD43; -.
DR IntAct; Q9HD43; 26.
DR MINT; Q9HD43; -.
DR STRING; 9606.ENSP00000365528; -.
DR DEPOD; PTPRH; -.
DR GlyGen; Q9HD43; 10 sites.
DR iPTMnet; Q9HD43; -.
DR PhosphoSitePlus; Q9HD43; -.
DR BioMuta; PTPRH; -.
DR DMDM; 296452983; -.
DR MassIVE; Q9HD43; -.
DR PaxDb; Q9HD43; -.
DR PeptideAtlas; Q9HD43; -.
DR PRIDE; Q9HD43; -.
DR ProteomicsDB; 81830; -. [Q9HD43-1]
DR ProteomicsDB; 81831; -. [Q9HD43-2]
DR ProteomicsDB; 9594; -.
DR Antibodypedia; 33039; 92 antibodies from 17 providers.
DR DNASU; 5794; -.
DR Ensembl; ENST00000263434.5; ENSP00000263434.4; ENSG00000080031.10. [Q9HD43-3]
DR Ensembl; ENST00000376350.8; ENSP00000365528.2; ENSG00000080031.10. [Q9HD43-1]
DR GeneID; 5794; -.
DR KEGG; hsa:5794; -.
DR MANE-Select; ENST00000376350.8; ENSP00000365528.2; NM_002842.5; NP_002833.4.
DR UCSC; uc002qjq.4; human. [Q9HD43-1]
DR CTD; 5794; -.
DR DisGeNET; 5794; -.
DR GeneCards; PTPRH; -.
DR HGNC; HGNC:9672; PTPRH.
DR HPA; ENSG00000080031; Tissue enhanced (gallbladder, intestine, stomach).
DR MIM; 602510; gene.
DR neXtProt; NX_Q9HD43; -.
DR OpenTargets; ENSG00000080031; -.
DR PharmGKB; PA34017; -.
DR VEuPathDB; HostDB:ENSG00000080031; -.
DR eggNOG; KOG0791; Eukaryota.
DR GeneTree; ENSGT00940000162227; -.
DR HOGENOM; CLU_001541_2_0_1; -.
DR InParanoid; Q9HD43; -.
DR OMA; QNLTYWV; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q9HD43; -.
DR TreeFam; TF351926; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q9HD43; -.
DR SignaLink; Q9HD43; -.
DR SIGNOR; Q9HD43; -.
DR ChiTaRS; PTPRH; human.
DR Pharos; Q9HD43; Tbio.
DR PRO; PR:Q9HD43; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9HD43; protein.
DR Bgee; ENSG00000080031; Expressed in jejunal mucosa and 149 other tissues.
DR Genevisible; Q9HD43; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; IPI:ARUK-UCL.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00063; FN3; 7.
DR Gene3D; 2.60.40.10; -; 7.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR028855; R-PTP-H.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR19134:SF297; PTHR19134:SF297; 4.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 7.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF49265; SSF49265; 4.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50853; FN3; 7.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cell membrane; Cell projection; Cytoplasm;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1115
FT /note="Receptor-type tyrosine-protein phosphatase H"
FT /id="PRO_0000318950"
FT TOPO_DOM 28..754
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 776..1115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..121
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 122..209
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 210..299
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 300..387
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 388..477
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 478..563
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 564..666
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 665..749
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 820..1079
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 1020
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT MOD_RES 1094
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:E9Q0N2"
FT MOD_RES 1102
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:E9Q0N2"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 84..261
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031318"
FT VAR_SEQ 126..303
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054222"
FT VARIANT 232
FT /note="D -> N (in dbSNP:rs55870162)"
FT /id="VAR_061762"
FT VARIANT 243
FT /note="V -> I (in dbSNP:rs45535035)"
FT /id="VAR_061763"
FT VARIANT 348
FT /note="H -> Y (in dbSNP:rs2288515)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038918"
FT VARIANT 543
FT /note="L -> F (in dbSNP:rs16986309)"
FT /id="VAR_038919"
FT VARIANT 781
FT /note="K -> N (in dbSNP:rs2288523)"
FT /id="VAR_038920"
FT VARIANT 823
FT /note="E -> K (in dbSNP:rs890870)"
FT /evidence="ECO:0000269|PubMed:11435690"
FT /id="VAR_038921"
FT VARIANT 831
FT /note="G -> D (in dbSNP:rs36092369)"
FT /id="VAR_061764"
FT VARIANT 1076
FT /note="I -> V (in dbSNP:rs2288419)"
FT /id="VAR_038922"
FT MUTAGEN 986
FT /note="D->A: Loss of activity. Acts as a dominant negative
FT mutant."
FT /evidence="ECO:0000269|PubMed:11278335"
FT MUTAGEN 1020
FT /note="C->S: Loss of activity. No induction of apoptosis."
FT /evidence="ECO:0000269|PubMed:11278335,
FT ECO:0000269|PubMed:12101188"
FT CONFLICT 294
FT /note="A -> T (in Ref. 1; BAA03645)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="E -> G (in Ref. 1; BAA03645)"
FT /evidence="ECO:0000305"
FT CONFLICT 951
FT /note="G -> D (in Ref. 4; AAI11716)"
FT /evidence="ECO:0000305"
FT CONFLICT 1109
FT /note="Q -> K (in Ref. 4; AAI11716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1115 AA; 122353 MW; 4E6C1DF86DCFB26C CRC64;
MAGAGGGLGV WGNLVLLGLC SWTGARAPAP NPGRNLTVET QTTSSISLSW EVPDGLDSQN
SNYWVQCTGD GGTTETRNTT ATNVTVDGLG PGSLYTCSVW VEKDGVNSSV GTVTTATAPN
PVRNLRVEAQ TNSSIALTWE VPDGPDPQNS TYGVEYTGDG GRAGTRSTAH TNITVDGLEP
GCLYAFSMWV GKNGINSSRE TRNATTAHNP VRNLRVEAQT TSSISLSWEV PDGTDPQNST
YCVQCTGDGG RTETRNTTDT RVTVDGLGPG SLYTCSVWVE KDGVNSSVEI VTSATAPNPV
RNLTVEAQTN SSIALTWEVP DGPDPQNSTY GVEYTGDGGR AGTRSTAHTN ITVDRLEPGC
LYVFSVWVGK NGINSSRETR NATTAPNPVR NLHMETQTNS SIALCWEVPD GPYPQDYTYW
VEYTGDGGGT ETRNTTNTSV TAERLEPGTL YTFSVWAEKN GARGSRQNVS ISTVPNAVTS
LSKQDWTNST IALRWTAPQG PGQSSYSYWV SWVREGMTDP RTQSTSGTDI TLKELEAGSL
YHLTVWAERN EVRGYNSTLT AATAPNEVTD LQNETQTKNS VMLWWKAPGD PHSQLYVYWV
QWASKGHPRR GQDPQANWVN QTSRTNETWY KVEALEPGTL YNFTVWAERN DVASSTQSLC
ASTYPDTVTI TSCVSTSAGY GVNLIWSCPQ GGYEAFELEV GGQRGSQDRS SCGEAVSVLG
LGPARSYPAT ITTIWDGMKV VSHSVVCHTE SAGVIAGAFV GILLFLILVG LLIFFLKRRN
KKKQQKPELR DLVFSSPGDI PAEDFADHVR KNERDSNCGF ADEYQQLSLV GHSQSQMVAS
ASENNAKNRY RNVLPYDWSR VPLKPIHEEP GSDYINASFM PGLWSPQEFI ATQGPLPQTV
GDFWRLVWEQ QSHTLVMLTN CMEAGRVKCE HYWPLDSQPC THGHLRVTLV GEEVMENWTV
RELLLLQVEE QKTLSVRQFH YQAWPDHGVP SSPDTLLAFW RMLRQWLDQT MEGGPPIVHC
SAGVGRTGTL IALDVLLRQL QSEGLLGPFS FVRKMRESRP LMVQTEAQYV FLHQCILRFL
QQSAQAPAEK EVPYEDVENL IYENVAAIQA HKLEV
