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R3HD2_HUMAN
ID   R3HD2_HUMAN             Reviewed;         976 AA.
AC   Q9Y2K5; B7ZL65; Q2M1T9; Q3ZCT5;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 3.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=R3H domain-containing protein 2;
GN   Name=R3HDM2; Synonyms=KIAA1002;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:63-70(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 321-976 (ISOFORM 1).
RC   TISSUE=Brain, and Testis;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-853, AND IDENTIFICATION BY
RP   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).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-330; SER-349 AND
RP   SER-855, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [10]
RP   STRUCTURE BY NMR OF 147-257.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the R3H domain from human.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- INTERACTION:
CC       Q9Y2K5; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-948428, EBI-10173507;
CC       Q9Y2K5; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-948428, EBI-3867333;
CC       Q9Y2K5; Q0VD86: INCA1; NbExp=3; IntAct=EBI-948428, EBI-6509505;
CC       Q9Y2K5; Q15323: KRT31; NbExp=3; IntAct=EBI-948428, EBI-948001;
CC       Q9Y2K5; O76011: KRT34; NbExp=3; IntAct=EBI-948428, EBI-1047093;
CC       Q9Y2K5; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-948428, EBI-11959885;
CC       Q9Y2K5; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-948428, EBI-11749135;
CC       Q9Y2K5; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-948428, EBI-10172290;
CC       Q9Y2K5; P60410: KRTAP10-8; NbExp=5; IntAct=EBI-948428, EBI-10171774;
CC       Q9Y2K5; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-948428, EBI-11953334;
CC       Q9Y2K5; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-948428, EBI-10241252;
CC       Q9Y2K5; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-948428, EBI-739863;
CC       Q9Y2K5; A8MW99: MEI4; NbExp=3; IntAct=EBI-948428, EBI-19944212;
CC       Q9Y2K5; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-948428, EBI-22310682;
CC       Q9Y2K5; O43610: SPRY3; NbExp=3; IntAct=EBI-948428, EBI-12290641;
CC       Q9Y2K5; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-948428, EBI-5235829;
CC       Q9Y2K5-2; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-10326419, EBI-946029;
CC       Q9Y2K5-2; Q92567: FAM168A; NbExp=3; IntAct=EBI-10326419, EBI-7957930;
CC       Q9Y2K5-2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-10326419, EBI-10171774;
CC       Q9Y2K5-2; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-10326419, EBI-751260;
CC       Q9Y2K5-2; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-10326419, EBI-945833;
CC       Q9Y2K5-2; Q93062: RBPMS; NbExp=3; IntAct=EBI-10326419, EBI-740322;
CC       Q9Y2K5-2; Q04864: REL; NbExp=3; IntAct=EBI-10326419, EBI-307352;
CC       Q9Y2K5-2; O43609: SPRY1; NbExp=3; IntAct=EBI-10326419, EBI-3866665;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9Y2K5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y2K5-2; Sequence=VSP_026087, VSP_026088;
CC       Name=3;
CC         IsoId=Q9Y2K5-3; Sequence=VSP_057391, VSP_057392;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI04996.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAI12227.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA76846.2; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB023219; BAA76846.2; ALT_FRAME; mRNA.
DR   EMBL; AC126614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC137834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC041857; AAH41857.1; -; mRNA.
DR   EMBL; BC104995; AAI04996.2; ALT_INIT; mRNA.
DR   EMBL; BC112226; AAI12227.2; ALT_INIT; mRNA.
DR   EMBL; BC143605; AAI43606.1; -; mRNA.
DR   CCDS; CCDS8937.2; -. [Q9Y2K5-1]
DR   RefSeq; NP_001317050.1; NM_001330121.1.
DR   RefSeq; NP_001317051.1; NM_001330122.1.
DR   RefSeq; NP_001317052.1; NM_001330123.1.
DR   RefSeq; NP_055740.3; NM_014925.4. [Q9Y2K5-1]
DR   RefSeq; XP_016874520.1; XM_017019031.1. [Q9Y2K5-3]
DR   RefSeq; XP_016874521.1; XM_017019032.1.
DR   RefSeq; XP_016874522.1; XM_017019033.1.
DR   PDB; 1WHR; NMR; -; A=147-257.
DR   PDBsum; 1WHR; -.
DR   AlphaFoldDB; Q9Y2K5; -.
DR   BMRB; Q9Y2K5; -.
DR   SMR; Q9Y2K5; -.
DR   BioGRID; 116532; 124.
DR   IntAct; Q9Y2K5; 33.
DR   STRING; 9606.ENSP00000317903; -.
DR   GlyGen; Q9Y2K5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y2K5; -.
DR   PhosphoSitePlus; Q9Y2K5; -.
DR   BioMuta; R3HDM2; -.
DR   DMDM; 148887413; -.
DR   EPD; Q9Y2K5; -.
DR   jPOST; Q9Y2K5; -.
DR   MassIVE; Q9Y2K5; -.
DR   MaxQB; Q9Y2K5; -.
DR   PaxDb; Q9Y2K5; -.
DR   PeptideAtlas; Q9Y2K5; -.
DR   PRIDE; Q9Y2K5; -.
DR   ProteomicsDB; 7212; -.
DR   ProteomicsDB; 85824; -. [Q9Y2K5-1]
DR   ProteomicsDB; 85825; -. [Q9Y2K5-2]
DR   Antibodypedia; 28556; 50 antibodies from 16 providers.
DR   DNASU; 22864; -.
DR   Ensembl; ENST00000347140.7; ENSP00000317903.6; ENSG00000179912.21. [Q9Y2K5-1]
DR   Ensembl; ENST00000358907.6; ENSP00000351784.2; ENSG00000179912.21. [Q9Y2K5-1]
DR   Ensembl; ENST00000441731.6; ENSP00000408536.2; ENSG00000179912.21. [Q9Y2K5-3]
DR   GeneID; 22864; -.
DR   KEGG; hsa:22864; -.
DR   UCSC; uc001sns.3; human. [Q9Y2K5-1]
DR   UCSC; uc001snu.3; human.
DR   CTD; 22864; -.
DR   DisGeNET; 22864; -.
DR   GeneCards; R3HDM2; -.
DR   HGNC; HGNC:29167; R3HDM2.
DR   HPA; ENSG00000179912; Low tissue specificity.
DR   neXtProt; NX_Q9Y2K5; -.
DR   OpenTargets; ENSG00000179912; -.
DR   PharmGKB; PA143485590; -.
DR   VEuPathDB; HostDB:ENSG00000179912; -.
DR   eggNOG; KOG2953; Eukaryota.
DR   GeneTree; ENSGT00940000155609; -.
DR   InParanoid; Q9Y2K5; -.
DR   OrthoDB; 137913at2759; -.
DR   PhylomeDB; Q9Y2K5; -.
DR   TreeFam; TF315915; -.
DR   PathwayCommons; Q9Y2K5; -.
DR   SignaLink; Q9Y2K5; -.
DR   BioGRID-ORCS; 22864; 15 hits in 1078 CRISPR screens.
DR   ChiTaRS; R3HDM2; human.
DR   EvolutionaryTrace; Q9Y2K5; -.
DR   GenomeRNAi; 22864; -.
DR   Pharos; Q9Y2K5; Tdark.
DR   PRO; PR:Q9Y2K5; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9Y2K5; protein.
DR   Bgee; ENSG00000179912; Expressed in Brodmann (1909) area 10 and 207 other tissues.
DR   ExpressionAtlas; Q9Y2K5; baseline and differential.
DR   Genevisible; Q9Y2K5; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   Gene3D; 3.30.1370.50; -; 1.
DR   InterPro; IPR001374; R3H_dom.
DR   InterPro; IPR036867; R3H_dom_sf.
DR   InterPro; IPR024771; SUZ.
DR   Pfam; PF01424; R3H; 1.
DR   SMART; SM00393; R3H; 1.
DR   SUPFAM; SSF82708; SSF82708; 1.
DR   PROSITE; PS51061; R3H; 1.
DR   PROSITE; PS51673; SUZ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..976
FT                   /note="R3H domain-containing protein 2"
FT                   /id="PRO_0000050787"
FT   DOMAIN          169..232
FT                   /note="R3H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT   DOMAIN          233..310
FT                   /note="SUZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01009"
FT   REGION          32..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..780
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80TM6"
FT   MOD_RES         330
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80TM6"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         853
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         855
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         856
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80TM6"
FT   MOD_RES         860
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80TM6"
FT   VAR_SEQ         1..339
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_057391"
FT   VAR_SEQ         1..295
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026087"
FT   VAR_SEQ         296..298
FT                   /note="QIF -> MIT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026088"
FT   VAR_SEQ         434
FT                   /note="Q -> QPVPALQPSPQPVQFSPSSCPQVLLPVSPPQQYNM (in isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_057392"
FT   VARIANT         35
FT                   /note="T -> A (in dbSNP:rs11832661)"
FT                   /id="VAR_059713"
FT   CONFLICT        359
FT                   /note="G -> S (in Ref. 3; AAH41857)"
FT                   /evidence="ECO:0000305"
FT   HELIX           154..164
FT                   /evidence="ECO:0007829|PDB:1WHR"
FT   TURN            166..168
FT                   /evidence="ECO:0007829|PDB:1WHR"
FT   HELIX           169..184
FT                   /evidence="ECO:0007829|PDB:1WHR"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:1WHR"
FT   HELIX           198..211
FT                   /evidence="ECO:0007829|PDB:1WHR"
FT   STRAND          215..217
FT                   /evidence="ECO:0007829|PDB:1WHR"
FT   STRAND          222..227
FT                   /evidence="ECO:0007829|PDB:1WHR"
FT   HELIX           239..241
FT                   /evidence="ECO:0007829|PDB:1WHR"
SQ   SEQUENCE   976 AA;  106999 MW;  D626918F71E0F815 CRC64;
     MSNSNTTQET LEIMKESEKK LVEESVNKNK FISKTPSKEE IEKECEDTSL RQETQRRTSN
     HGHARKRAKS NSKLKLVRSL AVCEESSTPF ADGPLETQDI IQLHISCPSD KEEEKSTKDV
     SEKEDKDKNK EKIPRKMLSR DSSQEYTDST GIDLHEFLVN TLKKNPRDRM MLLKLEQEIL
     EFINDNNNQF KKFPQMTSYH RMLLHRVAAY FGMDHNVDQT GKAVIINKTS NTRIPEQRFS
     EHIKDEKNTE FQQRFILKRD DASMDRDDNQ TGQNGYLNDI RLSKEAFSSS SHKRRQIFRG
     NREGLSRTSS SRQSSTDSEL KSLEPRPWSS TDSDGSVRSM RPPVTKASSF SGISILTRGD
     SIGSSKGGSA GRISRPGMAL GAPEVCNQVT SSQSVRGLLP CTAQQQQQQQ QQQLPALPPT
     PQQQPPLNNH MISQADDLSN PFGQMSLSRQ GSTEAADPSA ALFQTPLISQ HPQQTSFIMA
     STGQPLPTSN YSTSSHAPPT QQVLPPQGYM QPPQQIQVSY YPPGQYPNSN QQYRPLSHPV
     AYSPQRGQQL PQPSQQPGLQ PMMPNQQQAA YQGMIGVQQP QNQGLLSSQR SSMGGQMQGL
     VVQYTPLPSY QVPVGSDSQN VVQPPFQQPM LVPVSQSVQG GLPAAGVPVY YSMIPPAQQN
     GTSPSVGFLQ PPGSEQYQMP QSPSPCSPPQ MPQQYSGVSP SGPGVVVMQL NVPNGPQPPQ
     NPSMVQWSHC KYYSMDQRGQ KPGDLYSPDS SPQANTQMSS SPVTSPTQSP APSPVTSLSS
     VCTGLSPLPV LTQFPRPGGP AQGDGRYSLL GQPLQYNLSI CPPLLHGQST YTVHQGQSGL
     KHGNRGKRQA LKSASTDLGT ADVVLGRVLE VTDLPEGITR TEADKLFTQL AMSGAKIQWL
     KDAQGLPGGG GGDNSGTAEN GRHSDLAALY TIVAVFPSPL AAQNASLRLN NSVSRFKLRM
     AKKNYDLRIL ERASSQ
 
 
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