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KHDC4_HUMAN
ID   KHDC4_HUMAN             Reviewed;         614 AA.
AC   Q7Z7F0; O94981; Q7L7Q2; Q7Z7E9; Q8TBQ0;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=KH homology domain-containing protein 4 {ECO:0000312|HGNC:HGNC:29145};
DE   AltName: Full=Brings lots of money 7 {ECO:0000303|PubMed:19641227};
DE   AltName: Full=Pre-mRNA splicing factor protein KHDC4 {ECO:0000305};
GN   Name=KHDC4 {ECO:0000312|HGNC:HGNC:29145};
GN   Synonyms=BLOM7 {ECO:0000303|PubMed:19641227}, KIAA0907,
GN   SNORA80EHG {ECO:0000312|HGNC:HGNC:29145};
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] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBCELLULAR
RP   LOCATION, SUBUNIT, ALTERNATIVE SPLICING, DOMAIN, TISSUE SPECIFICITY,
RP   INTERACTION WITH PRPF19, AND INTERACTION WITH U2AF65 (ISOFORM 2).
RX   PubMed=19641227; DOI=10.1074/jbc.m109.036632;
RA   Grillari J., Loescher M., Denegri M., Lee K., Fortschegger K.,
RA   Eisenhaber F., Ajuh P., Lamond A.I., Katinger H., Grillari-Voglauer R.;
RT   "Blom7alpha is a novel heterogeneous nuclear ribonucleoprotein K homology
RT   domain protein involved in pre-mRNA splicing that interacts with SNEVPrp19-
RT   Pso4.";
RL   J. Biol. Chem. 284:29193-29204(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=10048485; DOI=10.1093/dnares/5.6.355;
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. XII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:355-364(1998).
RN   [3]
RP   SEQUENCE REVISION.
RA   Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC   TISSUE=Adrenal cortex, and Lymph;
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571 AND SER-572, AND
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571 AND SER-572, AND
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).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX   PubMed=23144703; DOI=10.1371/journal.pone.0047497;
RA   Loescher M., Schosserer M., Dausse E., Lee K., Ajuh P.,
RA   Grillari-Voglauer R., Lamond A.I., Toulme J.J., Grillari J.;
RT   "Inhibition of pre-mRNA splicing by a synthetic Blom7alpha-interacting
RT   small RNA.";
RL   PLoS ONE 7:E47497-E47497(2012).
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 227-338.
RG   RIKEN structural genomics initiative (RSGI);
RT   "solution structure of the KH domain in KIAA0907 protein.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: RNA-binding protein involved in pre-mRNA splicing
CC       (PubMed:19641227). Interacts with the PRP19C/Prp19 complex/NTC/Nineteen
CC       complex which is part of the spliceosome (PubMed:19641227). Involved in
CC       regulating splice site selection (PubMed:19641227). Binds
CC       preferentially RNA with A/C rich sequences and poly-C stretches
CC       (PubMed:23144703). {ECO:0000269|PubMed:19641227,
CC       ECO:0000269|PubMed:23144703}.
CC   -!- SUBUNIT: Interacts with PRPF19 (PubMed:19641227).
CC       {ECO:0000269|PubMed:19641227}.
CC   -!- SUBUNIT: [Isoform 2]: Interacts with U2AF65 (PubMed:19641227).
CC       {ECO:0000269|PubMed:19641227}.
CC   -!- INTERACTION:
CC       Q7Z7F0; Q9UHX1: PUF60; NbExp=3; IntAct=EBI-751942, EBI-1053259;
CC       Q7Z7F0; Q14498: RBM39; NbExp=3; IntAct=EBI-751942, EBI-395290;
CC       Q7Z7F0; Q14498-3: RBM39; NbExp=3; IntAct=EBI-751942, EBI-6654703;
CC       Q7Z7F0; Q15637: SF1; NbExp=5; IntAct=EBI-751942, EBI-744603;
CC       Q7Z7F0-4; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-9089060, EBI-11524452;
CC       Q7Z7F0-4; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-9089060, EBI-725606;
CC       Q7Z7F0-4; P22607: FGFR3; NbExp=3; IntAct=EBI-9089060, EBI-348399;
CC       Q7Z7F0-4; Q14957: GRIN2C; NbExp=3; IntAct=EBI-9089060, EBI-8285963;
CC       Q7Z7F0-4; P06396: GSN; NbExp=3; IntAct=EBI-9089060, EBI-351506;
CC       Q7Z7F0-4; Q9Y2W7: KCNIP3; NbExp=3; IntAct=EBI-9089060, EBI-751501;
CC       Q7Z7F0-4; P43365: MAGEA12; NbExp=3; IntAct=EBI-9089060, EBI-749530;
CC       Q7Z7F0-4; Q16656-4: NRF1; NbExp=3; IntAct=EBI-9089060, EBI-11742836;
CC       Q7Z7F0-4; P61970: NUTF2; NbExp=3; IntAct=EBI-9089060, EBI-591778;
CC       Q7Z7F0-4; Q9HB75-2: PIDD1; NbExp=3; IntAct=EBI-9089060, EBI-12326369;
CC       Q7Z7F0-4; O43741: PRKAB2; NbExp=3; IntAct=EBI-9089060, EBI-1053424;
CC       Q7Z7F0-4; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-9089060, EBI-740924;
CC       Q7Z7F0-4; P20618: PSMB1; NbExp=3; IntAct=EBI-9089060, EBI-372273;
CC       Q7Z7F0-4; Q9UHX1-2: PUF60; NbExp=10; IntAct=EBI-9089060, EBI-11529177;
CC       Q7Z7F0-4; Q9UHX1-5: PUF60; NbExp=3; IntAct=EBI-9089060, EBI-11526420;
CC       Q7Z7F0-4; Q9UHX1-6: PUF60; NbExp=3; IntAct=EBI-9089060, EBI-11085298;
CC       Q7Z7F0-4; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-9089060, EBI-2798044;
CC       Q7Z7F0-4; Q14498-3: RBM39; NbExp=3; IntAct=EBI-9089060, EBI-6654703;
CC       Q7Z7F0-4; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-9089060, EBI-372094;
CC       Q7Z7F0-4; P21673: SAT1; NbExp=3; IntAct=EBI-9089060, EBI-711613;
CC       Q7Z7F0-4; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-9089060, EBI-12023934;
CC       Q7Z7F0-4; P26368-2: U2AF2; NbExp=3; IntAct=EBI-9089060, EBI-11097439;
CC       Q7Z7F0-4; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-9089060, EBI-741480;
CC       Q7Z7F0-4; Q15696: ZRSR2; NbExp=3; IntAct=EBI-9089060, EBI-6657923;
CC       Q7Z7F0-4; B2RDP1; NbExp=3; IntAct=EBI-9089060, EBI-18956102;
CC       Q7Z7F0-4; Q9Y649; NbExp=3; IntAct=EBI-9089060, EBI-25900580;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19641227,
CC       ECO:0000269|PubMed:23144703}. Cytoplasm {ECO:0000269|PubMed:19641227}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Alpha, Blom7alpha {ECO:0000303|PubMed:19641227};
CC         IsoId=Q7Z7F0-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta, KIAA0907 {ECO:0000303|PubMed:19641227};
CC         IsoId=Q7Z7F0-2; Sequence=VSP_027242, VSP_027243;
CC       Name=3; Synonyms=Gamma;
CC         IsoId=Q7Z7F0-3; Sequence=VSP_027240, VSP_027241;
CC       Name=4;
CC         IsoId=Q7Z7F0-4; Sequence=VSP_027238, VSP_027239;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high level in skeletal
CC       muscle, kidney, heart, brain and liver. {ECO:0000269|PubMed:19641227}.
CC   -!- DOMAIN: The C-terminal part is necessary for the interaction with the
CC       PRP19C/Prp19 complex/NTC/Nineteen complex.
CC       {ECO:0000269|PubMed:19641227}.
CC   -!- DOMAIN: The KH domains mediate RNA-binding.
CC       {ECO:0000269|PubMed:23144703}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Interacts with U2AF65.
CC       {ECO:0000269|PubMed:19641227}.
CC   -!- SIMILARITY: Belongs to the KHDC4 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA74930.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY112680; AAM51855.1; -; mRNA.
DR   EMBL; AY112681; AAM51856.1; -; mRNA.
DR   EMBL; AY112682; AAM51857.1; -; mRNA.
DR   EMBL; AB020714; BAA74930.2; ALT_INIT; mRNA.
DR   EMBL; AL355388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC027182; AAH27182.1; -; mRNA.
DR   EMBL; BC062637; AAH62637.1; -; mRNA.
DR   CCDS; CCDS30885.1; -. [Q7Z7F0-1]
DR   RefSeq; NP_055764.2; NM_014949.3. [Q7Z7F0-1]
DR   PDB; 2YQR; NMR; -; A=227-338.
DR   PDBsum; 2YQR; -.
DR   AlphaFoldDB; Q7Z7F0; -.
DR   SMR; Q7Z7F0; -.
DR   BioGRID; 116555; 51.
DR   IntAct; Q7Z7F0; 40.
DR   MINT; Q7Z7F0; -.
DR   STRING; 9606.ENSP00000357304; -.
DR   iPTMnet; Q7Z7F0; -.
DR   PhosphoSitePlus; Q7Z7F0; -.
DR   BioMuta; KHDC4; -.
DR   DMDM; 74750236; -.
DR   EPD; Q7Z7F0; -.
DR   jPOST; Q7Z7F0; -.
DR   MassIVE; Q7Z7F0; -.
DR   MaxQB; Q7Z7F0; -.
DR   PaxDb; Q7Z7F0; -.
DR   PeptideAtlas; Q7Z7F0; -.
DR   PRIDE; Q7Z7F0; -.
DR   ProteomicsDB; 69525; -. [Q7Z7F0-1]
DR   ProteomicsDB; 69526; -. [Q7Z7F0-2]
DR   ProteomicsDB; 69527; -. [Q7Z7F0-3]
DR   ProteomicsDB; 69528; -. [Q7Z7F0-4]
DR   Antibodypedia; 1657; 90 antibodies from 21 providers.
DR   DNASU; 22889; -.
DR   Ensembl; ENST00000368319.3; ENSP00000357302.3; ENSG00000132680.11. [Q7Z7F0-3]
DR   Ensembl; ENST00000368320.7; ENSP00000357303.3; ENSG00000132680.11. [Q7Z7F0-2]
DR   Ensembl; ENST00000368321.8; ENSP00000357304.3; ENSG00000132680.11. [Q7Z7F0-1]
DR   GeneID; 22889; -.
DR   KEGG; hsa:22889; -.
DR   MANE-Select; ENST00000368321.8; ENSP00000357304.3; NM_014949.4; NP_055764.2.
DR   UCSC; uc001fmi.2; human. [Q7Z7F0-1]
DR   CTD; 22889; -.
DR   DisGeNET; 22889; -.
DR   GeneCards; KHDC4; -.
DR   HGNC; HGNC:29145; KHDC4.
DR   HPA; ENSG00000132680; Low tissue specificity.
DR   MIM; 619370; gene.
DR   neXtProt; NX_Q7Z7F0; -.
DR   OpenTargets; ENSG00000132680; -.
DR   PharmGKB; PA142671618; -.
DR   VEuPathDB; HostDB:ENSG00000132680; -.
DR   eggNOG; KOG1960; Eukaryota.
DR   GeneTree; ENSGT00510000047412; -.
DR   HOGENOM; CLU_032219_1_0_1; -.
DR   InParanoid; Q7Z7F0; -.
DR   OMA; MSFCGTQ; -.
DR   OrthoDB; 633868at2759; -.
DR   PhylomeDB; Q7Z7F0; -.
DR   PathwayCommons; Q7Z7F0; -.
DR   SignaLink; Q7Z7F0; -.
DR   BioGRID-ORCS; 22889; 36 hits in 1082 CRISPR screens.
DR   ChiTaRS; KIAA0907; human.
DR   EvolutionaryTrace; Q7Z7F0; -.
DR   GenomeRNAi; 22889; -.
DR   Pharos; Q7Z7F0; Tdark.
DR   PRO; PR:Q7Z7F0; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q7Z7F0; protein.
DR   Bgee; ENSG00000132680; Expressed in tibia and 207 other tissues.
DR   Genevisible; Q7Z7F0; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0006376; P:mRNA splice site selection; IDA:UniProtKB.
DR   Gene3D; 3.30.1370.10; -; 2.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR031121; RIK/BLOM7.
DR   PANTHER; PTHR15744; PTHR15744; 1.
DR   SUPFAM; SSF54791; SSF54791; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..614
FT                   /note="KH homology domain-containing protein 4"
FT                   /id="PRO_0000296669"
FT   DOMAIN          100..180
FT                   /note="KH 1"
FT                   /evidence="ECO:0000305|PubMed:23144703"
FT   DOMAIN          235..317
FT                   /note="KH 2"
FT                   /evidence="ECO:0000305|PubMed:23144703"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..549
FT                   /note="Required for nuclear retention"
FT                   /evidence="ECO:0000269|PubMed:23144703"
FT   REGION          567..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..456
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         571
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332"
FT   MOD_RES         572
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332"
FT   VAR_SEQ         228..241
FT                   /note="MHYVQDKLFVGLEH -> VCFGEGSLIALSFL (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_027238"
FT   VAR_SEQ         242..614
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_027239"
FT   VAR_SEQ         338..378
FT                   /note="GYTQPSAISSVPPQPPYYPSNGYQSGYPVVPPPQQPVQPPY -> AASSTSL
FT                   RSTKHSATSCFISTWSLAGITYWSPTCANTIPDNTSAASS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:19641227"
FT                   /id="VSP_027240"
FT   VAR_SEQ         379..614
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:19641227"
FT                   /id="VSP_027241"
FT   VAR_SEQ         549..564
FT                   /note="DYPAKKMKTTEKGFGL -> GECDIAGGTGEWLRLV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10048485,
FT                   ECO:0000303|PubMed:19641227"
FT                   /id="VSP_027242"
FT   VAR_SEQ         565..614
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10048485,
FT                   ECO:0000303|PubMed:19641227"
FT                   /id="VSP_027243"
FT   STRAND          231..236
FT                   /evidence="ECO:0007829|PDB:2YQR"
FT   TURN            244..246
FT                   /evidence="ECO:0007829|PDB:2YQR"
FT   HELIX           248..252
FT                   /evidence="ECO:0007829|PDB:2YQR"
FT   HELIX           255..257
FT                   /evidence="ECO:0007829|PDB:2YQR"
FT   HELIX           258..267
FT                   /evidence="ECO:0007829|PDB:2YQR"
FT   STRAND          270..276
FT                   /evidence="ECO:0007829|PDB:2YQR"
FT   TURN            283..285
FT                   /evidence="ECO:0007829|PDB:2YQR"
FT   STRAND          290..292
FT                   /evidence="ECO:0007829|PDB:2YQR"
FT   STRAND          294..301
FT                   /evidence="ECO:0007829|PDB:2YQR"
FT   HELIX           302..330
FT                   /evidence="ECO:0007829|PDB:2YQR"
SQ   SEQUENCE   614 AA;  64845 MW;  61968993DA061561 CRC64;
     MSAGSATHPG AGGRRSKWDQ PAPAPLLFLP PAAPGGEVTS SGGSPGGTTA APSGALDAAA
     AVAAKINAML MAKGKLKPTQ NASEKLQAPG KGLTSNKSKD DLVVAEVEIN DVPLTCRNLL
     TRGQTQDEIS RLSGAAVSTR GRFMTTEEKA KVGPGDRPLY LHVQGQTREL VDRAVNRIKE
     IITNGVVKAA TGTSPTFNGA TVTVYHQPAP IAQLSPAVSQ KPPFQSGMHY VQDKLFVGLE
     HAVPTFNVKE KVEGPGCSYL QHIQIETGAK VFLRGKGSGC IEPASGREAF EPMYIYISHP
     KPEGLAAAKK LCENLLQTVH AEYSRFVNQI NTAVPLPGYT QPSAISSVPP QPPYYPSNGY
     QSGYPVVPPP QQPVQPPYGV PSIVPPAVSL APGVLPALPT GVPPVPTQYP ITQVQPPAST
     GQSPMGGPFI PAAPVKTALP AGPQPQPQPQ PPLPSQPQAQ KRRFTEELPD ERESGLLGYQ
     HGPIHMTNLG TGFSSQNEIE GAGSKPASSS GKERERDRQL MPPPAFPVTG IKTESDERNG
     SGTLTGSHDY PAKKMKTTEK GFGLVAYAAD SSDEEEEHGG HKNASSFPQG WSLGYQYPSS
     QPRAKQQMPF WMAP
 
 
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