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XIRP1_HUMAN
ID   XIRP1_HUMAN             Reviewed;        1843 AA.
AC   Q702N8; A0JP25; A4QPE2; Q68DF2; Q6ZTR3; Q702N9; Q8IVN7; Q8N1N3; Q8N904;
AC   Q8TCG7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Xin actin-binding repeat-containing protein 1;
DE   AltName: Full=Cardiomyopathy-associated protein 1;
GN   Name=XIRP1; Synonyms=CMYA1, XIN;
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 B), FUNCTION, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH F-ACTIN.
RC   TISSUE=Skeletal muscle;
RX   PubMed=15454575; DOI=10.1242/jcs.01406;
RA   Pacholsky D., Vakeel P., Himmel M., Loewe T., Stradal T., Rottner K.,
RA   Fuerst D.O., van der Ven P.F.M.;
RT   "Xin repeats define a novel actin-binding motif.";
RL   J. Cell Sci. 117:5257-5268(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), ALTERNATIVE SPLICING (ISOFORMS B
RP   AND C), TISSUE SPECIFICITY, AND INTERACTION WITH FLNC AND VASP.
RC   TISSUE=Skeletal muscle;
RX   PubMed=16631741; DOI=10.1016/j.yexcr.2006.03.015;
RA   van der Ven P.F.M., Ehler E., Vakeel P., Eulitz S., Schenk J.A.,
RA   Milting H., Micheel B., Fuerst D.O.;
RT   "Unusual splicing events result in distinct Xin isoforms that associate
RT   differentially with filamin c and Mena/VASP.";
RL   Exp. Cell Res. 312:2154-2167(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RA   Luo J., Liu M., Wu X.;
RT   "A novel human gene, hXin, specifically expressed in human heart and
RT   skeletal muscle.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 444-1843 (ISOFORM A).
RC   TISSUE=Heart, Tongue, and Trachea;
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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] (ISOFORM B), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 570-1623 (ISOFORM A), AND VARIANT ARG-346.
RC   TISSUE=Liver, and Skeletal muscle;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), AND VARIANT ARG-1604.
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1554-1843.
RA   Trevisan S., Lanfranchi G.;
RT   "Study of a muscle specific transcript.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   VARIANTS [LARGE SCALE ANALYSIS] HIS-929 AND LYS-1634.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Protects actin filaments from depolymerization.
CC       {ECO:0000269|PubMed:15454575}.
CC   -!- SUBUNIT: Interacts with CTNNB1 (By similarity). Interacts with F-actin,
CC       FLNC and VASP. {ECO:0000250, ECO:0000269|PubMed:15454575,
CC       ECO:0000269|PubMed:16631741}.
CC   -!- INTERACTION:
CC       Q702N8; Q14315: FLNC; NbExp=4; IntAct=EBI-7851194, EBI-489954;
CC       Q702N8; P50552: VASP; NbExp=5; IntAct=EBI-7851194, EBI-748201;
CC   -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:15454575}.
CC       Note=Colocalizes with actin stress fibers.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=A;
CC         IsoId=Q702N8-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q702N8-2; Sequence=VSP_030844, VSP_030845;
CC       Name=C;
CC         IsoId=Q702N8-3; Sequence=VSP_030843;
CC   -!- TISSUE SPECIFICITY: Isoform A, isoform B and isoform C are expressed in
CC       heart. {ECO:0000269|PubMed:16631741}.
CC   -!- DOMAIN: Xin repeats bind F-actin.
CC   -!- MISCELLANEOUS: 'Xin' means 'heart' in Chinese.
CC   -!- SIMILARITY: Belongs to the Xin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00721}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC86519.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAC81057.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAD28459.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ626899; CAF25191.1; -; mRNA.
DR   EMBL; AJ626900; CAF25192.1; -; mRNA.
DR   EMBL; AY375160; AAQ64003.1; -; mRNA.
DR   EMBL; AK095941; BAC04655.1; -; mRNA.
DR   EMBL; AK096421; BAC04783.1; -; mRNA.
DR   EMBL; AK126299; BAC86519.1; ALT_INIT; mRNA.
DR   EMBL; AL713648; CAD28459.1; ALT_INIT; mRNA.
DR   EMBL; CR749430; CAH18268.1; -; mRNA.
DR   EMBL; BC127119; AAI27120.1; -; mRNA.
DR   EMBL; BC139782; AAI39783.1; -; mRNA.
DR   EMBL; AJ271461; CAC81057.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS2683.1; -. [Q702N8-1]
DR   CCDS; CCDS56245.1; -. [Q702N8-2]
DR   CCDS; CCDS87065.1; -. [Q702N8-3]
DR   RefSeq; NP_001185550.1; NM_001198621.2. [Q702N8-2]
DR   RefSeq; NP_919269.2; NM_194293.2. [Q702N8-1]
DR   RefSeq; XP_005264966.1; XM_005264909.3. [Q702N8-1]
DR   AlphaFoldDB; Q702N8; -.
DR   SMR; Q702N8; -.
DR   BioGRID; 127921; 18.
DR   ELM; Q702N8; -.
DR   IntAct; Q702N8; 6.
DR   MINT; Q702N8; -.
DR   STRING; 9606.ENSP00000343140; -.
DR   GlyGen; Q702N8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q702N8; -.
DR   PhosphoSitePlus; Q702N8; -.
DR   BioMuta; XIRP1; -.
DR   DMDM; 74712579; -.
DR   EPD; Q702N8; -.
DR   jPOST; Q702N8; -.
DR   MassIVE; Q702N8; -.
DR   PaxDb; Q702N8; -.
DR   PeptideAtlas; Q702N8; -.
DR   PRIDE; Q702N8; -.
DR   ProteomicsDB; 68504; -. [Q702N8-1]
DR   ProteomicsDB; 68505; -. [Q702N8-2]
DR   ProteomicsDB; 68506; -. [Q702N8-3]
DR   Antibodypedia; 12167; 80 antibodies from 21 providers.
DR   DNASU; 165904; -.
DR   Ensembl; ENST00000340369.4; ENSP00000343140.3; ENSG00000168334.9. [Q702N8-1]
DR   Ensembl; ENST00000396251.1; ENSP00000379550.1; ENSG00000168334.9. [Q702N8-2]
DR   Ensembl; ENST00000421646.1; ENSP00000391645.1; ENSG00000168334.9. [Q702N8-3]
DR   GeneID; 165904; -.
DR   KEGG; hsa:165904; -.
DR   MANE-Select; ENST00000340369.4; ENSP00000343140.3; NM_194293.4; NP_919269.2.
DR   UCSC; uc003cji.4; human. [Q702N8-1]
DR   CTD; 165904; -.
DR   DisGeNET; 165904; -.
DR   GeneCards; XIRP1; -.
DR   HGNC; HGNC:14301; XIRP1.
DR   HPA; ENSG00000168334; Group enriched (heart muscle, skeletal muscle).
DR   MIM; 609777; gene.
DR   neXtProt; NX_Q702N8; -.
DR   OpenTargets; ENSG00000168334; -.
DR   PharmGKB; PA162409336; -.
DR   VEuPathDB; HostDB:ENSG00000168334; -.
DR   eggNOG; ENOG502QTAC; Eukaryota.
DR   GeneTree; ENSGT00530000063779; -.
DR   HOGENOM; CLU_280589_0_0_1; -.
DR   InParanoid; Q702N8; -.
DR   OMA; DGIYTAH; -.
DR   OrthoDB; 34408at2759; -.
DR   PhylomeDB; Q702N8; -.
DR   TreeFam; TF330745; -.
DR   PathwayCommons; Q702N8; -.
DR   SignaLink; Q702N8; -.
DR   BioGRID-ORCS; 165904; 5 hits in 1065 CRISPR screens.
DR   ChiTaRS; XIRP1; human.
DR   GenomeRNAi; 165904; -.
DR   Pharos; Q702N8; Tbio.
DR   PRO; PR:Q702N8; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q702N8; protein.
DR   Bgee; ENSG00000168334; Expressed in left ventricle myocardium and 119 other tissues.
DR   Genevisible; Q702N8; HS.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR   GO; GO:0032091; P:negative regulation of protein binding; IMP:UniProtKB.
DR   InterPro; IPR012510; Actin-binding_Xin_repeat.
DR   InterPro; IPR030072; XIRP1/XIRP2.
DR   PANTHER; PTHR22591; PTHR22591; 2.
DR   Pfam; PF08043; Xin; 9.
DR   PROSITE; PS51389; XIN; 17.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cell junction; Coiled coil;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1843
FT                   /note="Xin actin-binding repeat-containing protein 1"
FT                   /id="PRO_0000316983"
FT   REPEAT          89..104
FT                   /note="Xin 1"
FT   REPEAT          121..136
FT                   /note="Xin 2"
FT   REPEAT          151..166
FT                   /note="Xin 3"
FT   REPEAT          186..201
FT                   /note="Xin 4"
FT   REPEAT          226..241
FT                   /note="Xin 5"
FT   REPEAT          264..279
FT                   /note="Xin 6"
FT   REPEAT          302..317
FT                   /note="Xin 7"
FT   REPEAT          340..355
FT                   /note="Xin 8"
FT   REPEAT          376..391
FT                   /note="Xin 9"
FT   REPEAT          436..451
FT                   /note="Xin 10"
FT   REPEAT          507..522
FT                   /note="Xin 11"
FT   REPEAT          545..560
FT                   /note="Xin 12"
FT   REPEAT          589..604
FT                   /note="Xin 13"
FT   REPEAT          621..636
FT                   /note="Xin 14"
FT   REPEAT          654..669
FT                   /note="Xin 15"
FT   REPEAT          691..706
FT                   /note="Xin 16"
FT   REPEAT          723..738
FT                   /note="Xin 17"
FT   REGION          1..54
FT                   /note="Interaction with VASP"
FT                   /evidence="ECO:0000269|PubMed:16631741"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..632
FT                   /note="Interaction with CTNNB1"
FT                   /evidence="ECO:0000250"
FT   REGION          564..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          943..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1063..1205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1238..1277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1289..1471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1561..1696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1685..1843
FT                   /note="Interaction with FLNC"
FT                   /evidence="ECO:0000269|PubMed:16631741"
FT   COILED          1462..1490
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        21..35
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..579
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1063..1106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1250..1264
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1296..1314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1318..1346
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1393..1443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1585..1620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1634..1650
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1662..1684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70373"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70373"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70373"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         332
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70373"
FT   VAR_SEQ         1..1317
FT                   /note="Missing (in isoform C)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_030843"
FT   VAR_SEQ         1120..1121
FT                   /note="VS -> LL (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:15454575,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_030844"
FT   VAR_SEQ         1122..1843
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:15454575,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_030845"
FT   VARIANT         3
FT                   /note="D -> N (in dbSNP:rs2271488)"
FT                   /id="VAR_038439"
FT   VARIANT         346
FT                   /note="Q -> R (in dbSNP:rs6805248)"
FT                   /evidence="ECO:0000269|PubMed:17974005"
FT                   /id="VAR_038440"
FT   VARIANT         551
FT                   /note="R -> Q (in dbSNP:rs34121641)"
FT                   /id="VAR_038441"
FT   VARIANT         695
FT                   /note="R -> C (in dbSNP:rs60540208)"
FT                   /id="VAR_061722"
FT   VARIANT         776
FT                   /note="R -> W (in dbSNP:rs9823779)"
FT                   /id="VAR_061723"
FT   VARIANT         929
FT                   /note="L -> H (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_038442"
FT   VARIANT         965
FT                   /note="H -> P (in dbSNP:rs11711871)"
FT                   /id="VAR_038443"
FT   VARIANT         1046
FT                   /note="P -> A (in dbSNP:rs35649793)"
FT                   /id="VAR_038444"
FT   VARIANT         1061
FT                   /note="A -> V (in dbSNP:rs35795536)"
FT                   /id="VAR_061724"
FT   VARIANT         1604
FT                   /note="G -> R (in dbSNP:rs3732383)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_038445"
FT   VARIANT         1608
FT                   /note="A -> V (in dbSNP:rs34810344)"
FT                   /id="VAR_038446"
FT   VARIANT         1634
FT                   /note="R -> K (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs768911526)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_038447"
FT   VARIANT         1707
FT                   /note="Q -> H (in dbSNP:rs34053674)"
FT                   /id="VAR_061725"
FT   VARIANT         1724
FT                   /note="I -> V (in dbSNP:rs9827576)"
FT                   /id="VAR_038448"
FT   CONFLICT        21
FT                   /note="D -> G (in Ref. 5; CAH18268)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="I -> T (in Ref. 5; CAH18268)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        274
FT                   /note="E -> G (in Ref. 5; CAH18268)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        754
FT                   /note="Q -> P (in Ref. 5; CAH18268)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        813
FT                   /note="G -> R (in Ref. 5; CAH18268)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1556
FT                   /note="K -> R (in Ref. 4; BAC04783)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1843 AA;  198561 MW;  41A5CC13FE1955CB CRC64;
     MADTQTQVAP TPTMRMATAE DLPLPPPPAL EDLPLPPPKE SFSKFHQQRQ ASELRRLYRH
     IHPELRKNLA EAVAEDLAEV LGSEEPTEGD VQCMRWIFEN WRLDAIGEHE RPAAKEPVLC
     GDVQATSRKF EEGSFANSTD QEPTRPQPGG GDVRAARWLF ETKPLDELTG QAKELEATVR
     EPAASGDVQG TRMLFETRPL DRLGSRPSLQ EQSPLELRSE IQELKGDVKK TVKLFQTEPL
     CAIQDAEGAI HEVKAACREE IQSNAVRSAR WLFETRPLDA INQDPSQVRV IRGISLEEGA
     RPDVSATRWI FETQPLDAIR EILVDEKDFQ PSPDLIPPGP DVQQQQHLFE TRALDTLKGD
     EEAGAEAPPK EEVVPGDVRS TLWLFETKPL DAFRDKVQVG HLQRVDPQDG EGHLSSDSSS
     ALPFSQSAPQ RDELKGDVKT FKNLFETLPL DSIGQGEVLA HGSPSREEGT DSAGQAQGIG
     SPVYAMQDSK GRLHALTSVS REQIVGGDVQ GYRWMFETQP LDQLGRSPST IDVVRGITRQ
     EVVAGDVGTA RWLFETQPLE MIHQREQQER QKEEGKSQGD PQPEAPPKGD VQTIRWLFET
     CPMSELAEKQ GSEVTDPTAK AEAQSCTWMF KPQPVDRPVG SREQHLQVSQ VPAGERQTDR
     HVFETEPLQA SGRPCGRRPV RYCSRVEIPS GQVSRQKEVF QALEAGKKEE QEPRVIAGSI
     PAGSVHKFTW LFENCPMGSL AAESIQGGNL LEEQPMSPSG NRMQESQETA AEGTLRTLHA
     TPGILHHGGI LMEARGPGEL CLAKYVLSGT GQGHPYIRKE ELVSGELPRI ICQVLRRPDV
     DQQGLLVQED PTGQLQLKPL RLPTPGSSGN IEDMDPELQQ LLACGLGTSV ARTGLVMQET
     EQGLVALTAY SLQPRLTSKA SERSSVQLLA SCIDKGDLSG LHSLRWEPPA DPSPVPASEG
     AQSLHPTESI IHVPPLDPSM GMGHLRASGA TPCPPQAIGK AVPLAGEAAA PAQLQNTEKQ
     EDSHSGQKGM AVLGKSEGAT TTPPGPGAPD LLAAMQSLRM ATAEAQSLHQ QVLNKHKQGP
     TPTATSNPIQ DGLRKAGATQ SNIRPGGGSD PRIPAAPRKV SREEQALPRG LPGGWVTIQD
     GIYTAHPVRT FDPPGGVQLS QREPQSRHRE TALSVQAPRP LQGGPGQSTG PGREEPGGCT
     QMAWGPPGKA MAEVCPGGLQ AAETTLKTAP LGRHILASGP QAAGASPHPH NAFVPPPPTL
     PAAVTGPDFP AGAHRAEDSI QQASEPLKDP LLHSHSSPAG QRTPGGSQTK TPKLDPTMPP
     KKKPQLPPKP AHLTQSHPPQ RLPKPLPLSP SFSSEVGQRE HQRGERDTAI PQPAKVPTTV
     DQGHIPLARC PSGHSQPSLQ HGLSTTAPRP TKNQATGSNA QSSEPPKLNA LNHDPTSPQW
     GPGPSGEQPM EGSHQGAPES PDSLQRNQKE LQGLLNQVQA LEKEAASSVD VQALRRLFEA
     VPQLGGAAPQ APAAHQKPEA SVEQAFGELT RVSTEVAQLK EQTLARLLDI EEAVHKALSS
     MSSLQPEASA RGHFQGPPKD HSAHKISVTV SSSARPSGSG QEVGGQTAVK NQAKVECHTE
     AQSQVKIRNH TEARGHTAST APSTRRQETS REYLCPPRVL PSSRDSPSSP TFISIQSATR
     KPLETPSFKG NPDVSVKSTQ LAQDIGQALL HQKGVQDKTG KKDITQCSVQ PEPAPPSASP
     LPRGWQKSVL ELQTGPGSSQ HYGAMRTVTE QYEEVDQFGN TVLMSSTTVT EQAEPPRNPG
     SHLGLHASPL LRQFLHSPAG FSSDLTEAET VQVSCSYSQP AAQ
 
 
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