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VGLL4_HUMAN
ID   VGLL4_HUMAN             Reviewed;         290 AA.
AC   Q14135; B4DTS7; J3KN68; Q7L5V0; Q9BQ78;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 4.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Transcription cofactor vestigial-like protein 4;
DE            Short=Vgl-4;
GN   Name=VGLL4; Synonyms=KIAA0121;
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=Bone marrow;
RX   PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA   Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. IV. The
RT   coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 2:167-174(1995).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS; C-TERMINUS; 32 AND 113.
RA   Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 5 AND 6), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-167 (ISOFORM 4).
RC   TISSUE=Brain, Placenta, Salivary gland, 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-32.
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-32.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Lung;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-149 AND THR-153, 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   [8]
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   [9]
RP   INTERACTION WITH IRF2BP2.
RX   PubMed=20702774; DOI=10.1096/fj.10-167049;
RA   Teng A.C., Kuraitis D., Deeke S.A., Ahmadi A., Dugan S.G., Cheng B.L.,
RA   Crowson M.G., Burgon P.G., Suuronen E.J., Chen H.H., Stewart A.F.;
RT   "IRF2BP2 is a skeletal and cardiac muscle-enriched ischemia-inducible
RT   activator of VEGFA expression.";
RL   FASEB J. 24:4825-4834(2010).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; THR-153 AND SER-274, AND
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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-149 AND SER-274, AND
RP   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).
CC   -!- FUNCTION: May act as a specific coactivator for the mammalian TEFs.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TEFs (By similarity). Interacts with IRF2BP2.
CC       {ECO:0000250, ECO:0000269|PubMed:20702774}.
CC   -!- INTERACTION:
CC       Q14135; Q15562-2: TEAD2; NbExp=3; IntAct=EBI-5278589, EBI-9370956;
CC       Q14135; Q99594: TEAD3; NbExp=3; IntAct=EBI-5278589, EBI-746720;
CC       Q14135; Q15561: TEAD4; NbExp=3; IntAct=EBI-5278589, EBI-747736;
CC       Q14135; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-5278589, EBI-750109;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q14135-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14135-2; Sequence=VSP_010776;
CC       Name=3;
CC         IsoId=Q14135-3; Sequence=VSP_040213, VSP_040214;
CC       Name=4;
CC         IsoId=Q14135-4; Sequence=VSP_040212;
CC       Name=5;
CC         IsoId=Q14135-5; Sequence=VSP_040210, VSP_040216;
CC       Name=6;
CC         IsoId=Q14135-6; Sequence=VSP_040211, VSP_040215;
CC   -!- MISCELLANEOUS: [Isoform 3]: Probable target of nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the vestigial family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH03038.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=BAA09470.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D50911; BAA09470.3; ALT_INIT; mRNA.
DR   EMBL; AK130542; BAC85375.1; -; mRNA.
DR   EMBL; AK300344; BAG62089.1; -; mRNA.
DR   EMBL; AK307708; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK308761; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; DA770257; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC022001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471055; EAW64104.1; -; Genomic_DNA.
DR   EMBL; BC001514; AAH01514.2; -; mRNA.
DR   EMBL; BC003038; AAH03038.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS2606.1; -. [Q14135-1]
DR   CCDS; CCDS46754.1; -. [Q14135-4]
DR   CCDS; CCDS46755.1; -. [Q14135-6]
DR   CCDS; CCDS46756.1; -. [Q14135-5]
DR   RefSeq; NP_001121691.1; NM_001128219.2.
DR   RefSeq; NP_001121692.1; NM_001128220.2. [Q14135-6]
DR   RefSeq; NP_001121693.1; NM_001128221.2. [Q14135-5]
DR   RefSeq; NP_001271319.1; NM_001284390.1.
DR   RefSeq; NP_001271320.1; NM_001284391.1.
DR   RefSeq; NP_055482.2; NM_014667.3.
DR   AlphaFoldDB; Q14135; -.
DR   SMR; Q14135; -.
DR   BioGRID; 115039; 24.
DR   IntAct; Q14135; 16.
DR   STRING; 9606.ENSP00000404251; -.
DR   GlyGen; Q14135; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q14135; -.
DR   PhosphoSitePlus; Q14135; -.
DR   BioMuta; VGLL4; -.
DR   DMDM; 68068037; -.
DR   EPD; Q14135; -.
DR   jPOST; Q14135; -.
DR   MassIVE; Q14135; -.
DR   MaxQB; Q14135; -.
DR   PaxDb; Q14135; -.
DR   PeptideAtlas; Q14135; -.
DR   PRIDE; Q14135; -.
DR   ProteomicsDB; 59833; -. [Q14135-1]
DR   ProteomicsDB; 59834; -. [Q14135-2]
DR   ProteomicsDB; 59835; -. [Q14135-3]
DR   ProteomicsDB; 59836; -. [Q14135-4]
DR   ProteomicsDB; 59837; -. [Q14135-5]
DR   ProteomicsDB; 59838; -. [Q14135-6]
DR   Antibodypedia; 26100; 164 antibodies from 24 providers.
DR   DNASU; 9686; -.
DR   Ensembl; ENST00000424529.6; ENSP00000402878.2; ENSG00000144560.16. [Q14135-5]
DR   Ensembl; ENST00000451674.6; ENSP00000416615.2; ENSG00000144560.16. [Q14135-6]
DR   GeneID; 9686; -.
DR   KEGG; hsa:9686; -.
DR   UCSC; uc010hdv.3; human. [Q14135-1]
DR   CTD; 9686; -.
DR   DisGeNET; 9686; -.
DR   GeneCards; VGLL4; -.
DR   HGNC; HGNC:28966; VGLL4.
DR   HPA; ENSG00000144560; Low tissue specificity.
DR   MIM; 618692; gene.
DR   neXtProt; NX_Q14135; -.
DR   OpenTargets; ENSG00000144560; -.
DR   PharmGKB; PA128394553; -.
DR   VEuPathDB; HostDB:ENSG00000144560; -.
DR   eggNOG; ENOG502QTV3; Eukaryota.
DR   GeneTree; ENSGT00390000003282; -.
DR   HOGENOM; CLU_085402_0_0_1; -.
DR   InParanoid; Q14135; -.
DR   OrthoDB; 1275581at2759; -.
DR   PhylomeDB; Q14135; -.
DR   PathwayCommons; Q14135; -.
DR   SignaLink; Q14135; -.
DR   BioGRID-ORCS; 9686; 20 hits in 1083 CRISPR screens.
DR   ChiTaRS; VGLL4; human.
DR   GenomeRNAi; 9686; -.
DR   Pharos; Q14135; Tbio.
DR   PRO; PR:Q14135; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q14135; protein.
DR   Bgee; ENSG00000144560; Expressed in tibia and 215 other tissues.
DR   ExpressionAtlas; Q14135; baseline and differential.
DR   Genevisible; Q14135; HS.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0001223; F:transcription coactivator binding; IBA:GO_Central.
DR   GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; ISS:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR   GO; GO:0035331; P:negative regulation of hippo signaling; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR006627; TDU_repeat.
DR   InterPro; IPR028184; VGLL4.
DR   PANTHER; PTHR17604; PTHR17604; 1.
DR   Pfam; PF15245; VGLL4; 1.
DR   SMART; SM00711; TDU; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..290
FT                   /note="Transcription cofactor vestigial-like protein 4"
FT                   /id="PRO_0000191351"
FT   REGION          17..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         153
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         274
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..84
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040210"
FT   VAR_SEQ         1..80
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040211"
FT   VAR_SEQ         1..31
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_010776"
FT   VAR_SEQ         1..22
FT                   /note="METPLDVLSRAASLVHADDEKR -> MLFMKMDLLNYQYLDKMNNNIGILCY
FT                   EG (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040212"
FT   VAR_SEQ         22..41
FT                   /note="REAALRGEPRMQTLPVASAL -> PSPGNLLEMQNRSPRCGTDD (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040213"
FT   VAR_SEQ         42..290
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040214"
FT   VAR_SEQ         81..85
FT                   /note="FNPHL -> MIKVR (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040215"
FT   VAR_SEQ         85
FT                   /note="L -> M (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040216"
FT   VARIANT         32
FT                   /note="M -> I (in dbSNP:rs2276749)"
FT                   /evidence="ECO:0000269|PubMed:16641997, ECO:0000269|Ref.5"
FT                   /id="VAR_024689"
SQ   SEQUENCE   290 AA;  30948 MW;  A5EA4C167CC8F0B4 CRC64;
     METPLDVLSR AASLVHADDE KREAALRGEP RMQTLPVASA LSSHRTGPPP ISPSKRKFSM
     EPGDEDLDCD NDHVSKMSRI FNPHLNKTAN GDCRRDPRER SRSPIERAVA PTMSLHGSHL
     YTSLPSLGLE QPLALTKNSL DASRPAGLSP TLTPGERQQN RPSVITCASA GARNCNLSHC
     PIAHSGCAAP GPASYRRPPS AATTCDPVVE EHFRRSLGKN YKEPEPAPNS VSITGSVDDH
     FAKALGDTWL QIKAAKDGAS SSPESASRRG QPASPSAHMV SHSHSPSVVS
 
 
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