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MET7A_HUMAN
ID   MET7A_HUMAN             Reviewed;         244 AA.
AC   Q9H8H3; Q9H7R3; Q9UHZ7; Q9Y422;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Putative methyltransferase-like protein 7A {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000305};
DE   AltName: Full=Protein AAM-B {ECO:0000303|PubMed:19773358};
DE   Flags: Precursor;
GN   Name=METTL7A; ORFNames=PRO0066, UNQ1902/PRO4348;
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].
RA   Gratchev A., Kzhyhskowska J., Utikal J., Goerdt S.;
RT   "Expression profiling of alternatively activated macrophages.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta, and Thyroid;
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 MRNA].
RC   TISSUE=Pancreas, and Placenta;
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 2-244.
RC   TISSUE=Uterus;
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] OF 14-244.
RC   TISSUE=Fetal liver;
RA   Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Liu M.,
RA   He F.;
RT   "Functional prediction of the coding sequences of 14 new genes deduced by
RT   analysis of cDNA clones from human fetal liver.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   SUBCELLULAR LOCATION, SUBUNIT, AND REGION.
RX   PubMed=18477614; DOI=10.1242/jcs.012013;
RA   Zehmer J.K., Bartz R., Liu P., Anderson R.G.W.;
RT   "Identification of a novel N-terminal hydrophobic sequence that targets
RT   proteins to lipid droplets.";
RL   J. Cell Sci. 121:1852-1860(2008).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19773358; DOI=10.1242/jcs.054700;
RA   Zehmer J.K., Bartz R., Bisel B., Liu P., Seemann J., Anderson R.G.W.;
RT   "Targeting sequences of UBXD8 and AAM-B reveal that the ER has a direct
RT   role in the emergence and regression of lipid droplets.";
RL   J. Cell Sci. 122:3694-3702(2009).
RN   [9]
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   [10]
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   [11]
RP   FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   HCV NSB4.
RX   PubMed=26185986; DOI=10.1371/journal.pone.0132839;
RA   Park E.M., Lim Y.S., Ahn B.Y., Hwang S.B.;
RT   "AAM-B Interacts with Nonstructural 4B and Regulates Hepatitis C Virus
RT   Propagation.";
RL   PLoS ONE 10:e0132839-e0132839(2015).
CC   -!- FUNCTION: Putative methyltransferase. {ECO:0000305}.
CC   -!- FUNCTION: (Microbial infection) May be involved in the assembly and
CC       release stages of hepatitis C virus (HCV) life cycle and thus play a
CC       crucial role in HCV propagation. {ECO:0000269|PubMed:26185986}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HCV non-structural
CC       protein 4B/NS4B (via C-terminal region); this interaction may promote
CC       the recruitment of NS4B in the proximity of lipid droplet.
CC       {ECO:0000269|PubMed:26185986}.
CC   -!- SUBUNIT: Self-associates. {ECO:0000269|PubMed:18477614}.
CC   -!- INTERACTION:
CC       Q9H8H3; P54252: ATXN3; NbExp=3; IntAct=EBI-1390168, EBI-946046;
CC       Q9H8H3; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-1390168, EBI-21603100;
CC       Q9H8H3; P22607: FGFR3; NbExp=3; IntAct=EBI-1390168, EBI-348399;
CC       Q9H8H3; P06396: GSN; NbExp=3; IntAct=EBI-1390168, EBI-351506;
CC       Q9H8H3; Q92993: KAT5; NbExp=3; IntAct=EBI-1390168, EBI-399080;
CC       Q9H8H3; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-1390168, EBI-11742507;
CC       Q9H8H3; O75489: NDUFS3; NbExp=3; IntAct=EBI-1390168, EBI-1224896;
CC       Q9H8H3; P62937-2: PPIA; NbExp=3; IntAct=EBI-1390168, EBI-25884072;
CC       Q9H8H3; P17252: PRKCA; NbExp=3; IntAct=EBI-1390168, EBI-1383528;
CC       Q9H8H3; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-1390168, EBI-9090795;
CC       Q9H8H3; P61981: YWHAG; NbExp=3; IntAct=EBI-1390168, EBI-359832;
CC   -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:18477614,
CC       ECO:0000269|PubMed:19773358, ECO:0000269|PubMed:26185986}. Endoplasmic
CC       reticulum {ECO:0000269|PubMed:19773358}. Membrane
CC       {ECO:0000269|PubMed:18477614}. Note=Inserted in the ER membrane and
CC       migrates from the inserted site to lipid droplet.
CC       {ECO:0000269|PubMed:18477614}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF20268.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ536233; CAD60207.1; -; mRNA.
DR   EMBL; AY358797; AAQ89157.1; -; mRNA.
DR   EMBL; AK023693; BAB14643.1; -; mRNA.
DR   EMBL; AK024409; BAB14913.1; -; mRNA.
DR   EMBL; BC004492; AAH04492.1; -; mRNA.
DR   EMBL; BC008180; AAH08180.1; -; mRNA.
DR   EMBL; AL050159; CAB43300.1; -; mRNA.
DR   EMBL; AF113007; AAF20268.1; ALT_INIT; mRNA.
DR   CCDS; CCDS8804.1; -.
DR   PIR; T08785; T08785.
DR   RefSeq; NP_054752.3; NM_014033.3.
DR   RefSeq; XP_006719395.1; XM_006719332.1.
DR   AlphaFoldDB; Q9H8H3; -.
DR   SMR; Q9H8H3; -.
DR   BioGRID; 117366; 358.
DR   IntAct; Q9H8H3; 19.
DR   MINT; Q9H8H3; -.
DR   STRING; 9606.ENSP00000448785; -.
DR   iPTMnet; Q9H8H3; -.
DR   PhosphoSitePlus; Q9H8H3; -.
DR   SwissPalm; Q9H8H3; -.
DR   BioMuta; METTL7A; -.
DR   DMDM; 74761529; -.
DR   CPTAC; CPTAC-238; -.
DR   CPTAC; CPTAC-239; -.
DR   EPD; Q9H8H3; -.
DR   jPOST; Q9H8H3; -.
DR   MassIVE; Q9H8H3; -.
DR   MaxQB; Q9H8H3; -.
DR   PaxDb; Q9H8H3; -.
DR   PeptideAtlas; Q9H8H3; -.
DR   PRIDE; Q9H8H3; -.
DR   ProteomicsDB; 81213; -.
DR   Antibodypedia; 2699; 240 antibodies from 26 providers.
DR   DNASU; 25840; -.
DR   Ensembl; ENST00000332160.5; ENSP00000331787.4; ENSG00000185432.12.
DR   Ensembl; ENST00000547104.1; ENSP00000447542.1; ENSG00000185432.12.
DR   Ensembl; ENST00000548553.1; ENSP00000448785.1; ENSG00000185432.12.
DR   GeneID; 25840; -.
DR   KEGG; hsa:25840; -.
DR   MANE-Select; ENST00000332160.5; ENSP00000331787.4; NM_014033.4; NP_054752.3.
DR   UCSC; uc001rxb.3; human.
DR   CTD; 25840; -.
DR   DisGeNET; 25840; -.
DR   GeneCards; METTL7A; -.
DR   HGNC; HGNC:24550; METTL7A.
DR   HPA; ENSG00000185432; Tissue enhanced (liver).
DR   MIM; 618338; gene.
DR   neXtProt; NX_Q9H8H3; -.
DR   OpenTargets; ENSG00000185432; -.
DR   PharmGKB; PA128394635; -.
DR   VEuPathDB; HostDB:ENSG00000185432; -.
DR   eggNOG; KOG4300; Eukaryota.
DR   GeneTree; ENSGT00940000154786; -.
DR   InParanoid; Q9H8H3; -.
DR   OMA; VWYLLFD; -.
DR   OrthoDB; 1178802at2759; -.
DR   PhylomeDB; Q9H8H3; -.
DR   TreeFam; TF331790; -.
DR   PathwayCommons; Q9H8H3; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; Q9H8H3; -.
DR   BioGRID-ORCS; 25840; 52 hits in 1075 CRISPR screens.
DR   ChiTaRS; METTL7A; human.
DR   GenomeRNAi; 25840; -.
DR   Pharos; Q9H8H3; Tbio.
DR   PRO; PR:Q9H8H3; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9H8H3; protein.
DR   Bgee; ENSG00000185432; Expressed in bronchial epithelial cell and 207 other tissues.
DR   ExpressionAtlas; Q9H8H3; baseline and differential.
DR   Genevisible; Q9H8H3; HS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR   GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Host-virus interaction; Lipid droplet; Membrane;
KW   Methyltransferase; Reference proteome; Signal; Transferase.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..244
FT                   /note="Putative methyltransferase-like protein 7A"
FT                   /id="PRO_0000251921"
FT   REGION          1..28
FT                   /note="Targeting to lipid droplets"
FT                   /evidence="ECO:0000269|PubMed:18477614"
FT   VARIANT         134
FT                   /note="A -> T (in dbSNP:rs28372674)"
FT                   /id="VAR_050296"
FT   CONFLICT        39
FT                   /note="F -> L (in Ref. 3; BAB14913)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   244 AA;  28319 MW;  6967783BAB2348BE CRC64;
     MELTIFILRL AIYILTFPLY LLNFLGLWSW ICKKWFPYFL VRFTVIYNEQ MASKKRELFS
     NLQEFAGPSG KLSLLEVGCG TGANFKFYPP GCRVTCIDPN PNFEKFLIKS IAENRHLQFE
     RFVVAAGENM HQVADGSVDV VVCTLVLCSV KNQERILREV CRVLRPGGAF YFMEHVAAEC
     STWNYFWQQV LDPAWHLLFD GCNLTRESWK ALERASFSKL KLQHIQAPLS WELVRPHIYG
     YAVK
 
 
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