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APMAP_HUMAN
ID   APMAP_HUMAN             Reviewed;         416 AA.
AC   Q9HDC9; A8K514; B4DXG1; Q6UVZ8; Q9GZS8; Q9NUB2;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Adipocyte plasma membrane-associated protein;
DE   AltName: Full=Protein BSCv;
GN   Name=APMAP; Synonyms=C20orf3; ORFNames=UNQ1869/PRO4305;
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).
RX   PubMed=10945474; DOI=10.1006/geno.2000.6237;
RA   Morita M., Hara Y., Tamai Y., Arakawa H., Nishimura S.;
RT   "Genomic construct and mapping of the gene for CMAP (leukocystatin/cystatin
RT   F, CST7) and identification of a proximal novel gene, BSCv (C20orf3).";
RL   Genomics 67:87-91(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Adipose tissue, and Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-416 (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [6]
RP   GLYCOSYLATION AT ASN-160 AND ASN-196.
RX   PubMed=12754519; DOI=10.1038/nbt827;
RA   Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT   "Identification and quantification of N-linked glycoproteins using
RT   hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL   Nat. Biotechnol. 21:660-666(2003).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-196.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANTS GLN-282
RP   AND TRP-374.
RX   PubMed=18513186; DOI=10.1042/bj20080503;
RA   Ilhan A., Gartner W., Nabokikh A., Daneva T., Majdic O., Cohen G.,
RA   Boehmig G.A., Base W., Hoerl W.H., Wagner L.;
RT   "Localization and characterization of the novel protein encoded by
RT   C20orf3.";
RL   Biochem. J. 414:485-495(2008).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-196.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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 THR-19, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19, AND IDENTIFICATION BY
RP   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   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Exhibits strong arylesterase activity with beta-naphthyl
CC       acetate and phenyl acetate. May play a role in adipocyte
CC       differentiation. {ECO:0000269|PubMed:18513186}.
CC   -!- INTERACTION:
CC       Q9HDC9; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-723950, EBI-18304435;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18513186}; Single-
CC       pass type II membrane protein {ECO:0000269|PubMed:18513186}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9HDC9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9HDC9-2; Sequence=VSP_036992, VSP_036993;
CC   -!- TISSUE SPECIFICITY: Liver, glomerular and tubular structures of the
CC       kidney, endothelial cells, arterial wall and pancreatic islets of
CC       Langerhans (at protein level). Found ubiquitously in adult as well as
CC       in embryonic tissues. In adult tissue, the highest expression is found
CC       in the liver, placenta and heart. Found on the cell surface of
CC       monocytes. In embryonic tissue, the highest expression levels is found
CC       in the liver and the kidney. {ECO:0000269|PubMed:18513186}.
CC   -!- SIMILARITY: Belongs to the strictosidine synthase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ89435.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB11885.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB15253.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB15578.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB033767; BAB11885.1; ALT_INIT; mRNA.
DR   EMBL; AK291129; BAF83818.1; -; mRNA.
DR   EMBL; AK301959; BAG63373.1; -; mRNA.
DR   EMBL; AL035661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC003501; AAH03501.1; -; mRNA.
DR   EMBL; AY359076; AAQ89435.1; ALT_INIT; mRNA.
DR   EMBL; AK025834; BAB15253.1; ALT_INIT; mRNA.
DR   EMBL; AK026866; BAB15578.1; ALT_INIT; mRNA.
DR   CCDS; CCDS13166.1; -. [Q9HDC9-1]
DR   RefSeq; NP_065392.1; NM_020531.2. [Q9HDC9-1]
DR   RefSeq; XP_005260820.1; XM_005260763.3. [Q9HDC9-2]
DR   AlphaFoldDB; Q9HDC9; -.
DR   SMR; Q9HDC9; -.
DR   BioGRID; 121397; 47.
DR   IntAct; Q9HDC9; 35.
DR   MINT; Q9HDC9; -.
DR   STRING; 9606.ENSP00000217456; -.
DR   GlyConnect; 797; 38 N-Linked glycans (2 sites).
DR   GlyGen; Q9HDC9; 3 sites, 44 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q9HDC9; -.
DR   MetOSite; Q9HDC9; -.
DR   PhosphoSitePlus; Q9HDC9; -.
DR   SwissPalm; Q9HDC9; -.
DR   BioMuta; APMAP; -.
DR   DMDM; 24211474; -.
DR   CPTAC; CPTAC-1280; -.
DR   CPTAC; CPTAC-648; -.
DR   EPD; Q9HDC9; -.
DR   jPOST; Q9HDC9; -.
DR   MassIVE; Q9HDC9; -.
DR   MaxQB; Q9HDC9; -.
DR   PaxDb; Q9HDC9; -.
DR   PeptideAtlas; Q9HDC9; -.
DR   PRIDE; Q9HDC9; -.
DR   ProteomicsDB; 81851; -. [Q9HDC9-1]
DR   ProteomicsDB; 81852; -. [Q9HDC9-2]
DR   Antibodypedia; 2012; 300 antibodies from 22 providers.
DR   DNASU; 57136; -.
DR   Ensembl; ENST00000217456.3; ENSP00000217456.2; ENSG00000101474.12. [Q9HDC9-1]
DR   GeneID; 57136; -.
DR   KEGG; hsa:57136; -.
DR   MANE-Select; ENST00000217456.3; ENSP00000217456.2; NM_020531.3; NP_065392.1.
DR   UCSC; uc002wty.4; human. [Q9HDC9-1]
DR   CTD; 57136; -.
DR   DisGeNET; 57136; -.
DR   GeneCards; APMAP; -.
DR   HGNC; HGNC:13238; APMAP.
DR   HPA; ENSG00000101474; Tissue enhanced (liver).
DR   MIM; 615884; gene.
DR   neXtProt; NX_Q9HDC9; -.
DR   OpenTargets; ENSG00000101474; -.
DR   PharmGKB; PA25745; -.
DR   VEuPathDB; HostDB:ENSG00000101474; -.
DR   eggNOG; KOG1520; Eukaryota.
DR   GeneTree; ENSGT00440000039984; -.
DR   HOGENOM; CLU_023267_0_0_1; -.
DR   InParanoid; Q9HDC9; -.
DR   OMA; ERLWENQ; -.
DR   OrthoDB; 757814at2759; -.
DR   PhylomeDB; Q9HDC9; -.
DR   TreeFam; TF316475; -.
DR   PathwayCommons; Q9HDC9; -.
DR   SignaLink; Q9HDC9; -.
DR   BioGRID-ORCS; 57136; 8 hits in 1077 CRISPR screens.
DR   ChiTaRS; APMAP; human.
DR   GeneWiki; C20orf3; -.
DR   GenomeRNAi; 57136; -.
DR   Pharos; Q9HDC9; Tbio.
DR   PRO; PR:Q9HDC9; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9HDC9; protein.
DR   Bgee; ENSG00000101474; Expressed in cerebellar vermis and 201 other tissues.
DR   ExpressionAtlas; Q9HDC9; baseline and differential.
DR   Genevisible; Q9HDC9; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0004064; F:arylesterase activity; IDA:UniProtKB.
DR   GO; GO:0016844; F:strictosidine synthase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 2.120.10.30; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR018119; Strictosidine_synth_cons-reg.
DR   Pfam; PF03088; Str_synth; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Glycoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..416
FT                   /note="Adipocyte plasma membrane-associated protein"
FT                   /id="PRO_0000205945"
FT   TOPO_DOM        2..40
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..416
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         19
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754519,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754519,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218"
FT   VAR_SEQ         283..289
FT                   /note="RVYVSGL -> SSLVKRR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036992"
FT   VAR_SEQ         290..416
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036993"
FT   VARIANT         65
FT                   /note="I -> V (in dbSNP:rs12242)"
FT                   /id="VAR_014128"
FT   VARIANT         282
FT                   /note="R -> Q (in dbSNP:rs35097515)"
FT                   /evidence="ECO:0000269|PubMed:18513186"
FT                   /id="VAR_055039"
FT   VARIANT         374
FT                   /note="R -> W (in dbSNP:rs28364786)"
FT                   /evidence="ECO:0000269|PubMed:18513186"
FT                   /id="VAR_055040"
FT   CONFLICT        12
FT                   /note="P -> A (in Ref. 2; BAG63373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="E -> G (in Ref. 2; BAF83818)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="D -> G (in Ref. 2; BAF83818)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="V -> A (in Ref. 2; BAF83818)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   416 AA;  46480 MW;  C88E2DF2DF6093C4 CRC64;
     MSEADGLRQR RPLRPQVVTD DDGQAPEAKD GSSFSGRVFR VTFLMLAVSL TVPLLGAMML
     LESPIDPQPL SFKEPPLLLG VLHPNTKLRQ AERLFENQLV GPESIAHIGD VMFTGTADGR
     VVKLENGEIE TIARFGSGPC KTRDDEPVCG RPLGIRAGPN GTLFVADAYK GLFEVNPWKR
     EVKLLLSSET PIEGKNMSFV NDLTVTQDGR KIYFTDSSSK WQRRDYLLLV MEGTDDGRLL
     EYDTVTREVK VLLDQLRFPN GVQLSPAEDF VLVAETTMAR IRRVYVSGLM KGGADLFVEN
     MPGFPDNIRP SSSGGYWVGM STIRPNPGFS MLDFLSERPW IKRMIFKLFS QETVMKFVPR
     YSLVLELSDS GAFRRSLHDP DGLVATYISE VHEHDGHLYL GSFRSPFLCR LSLQAV
 
 
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