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MTFR1_HUMAN
ID   MTFR1_HUMAN             Reviewed;         333 AA.
AC   Q15390; E7EP84; Q6IB94; Q7Z669; Q86XH5; Q8IVD7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Mitochondrial fission regulator 1;
DE   AltName: Full=Chondrocyte protein with a poly-proline region;
DE   Flags: Precursor;
GN   Name=MTFR1; Synonyms=CHPPR, FAM54A2, KIAA0009;
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 GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung, 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-333 (ISOFORM 2).
RC   TISSUE=Liver;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-333 (ISOFORM 1).
RC   TISSUE=Bone marrow;
RX   PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA   Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA   Nagase T., Seki N., Ishikawa K., Tabata S.;
RT   "Prediction of the coding sequences of unidentified human genes. I. The
RT   coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT   randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL   DNA Res. 1:27-35(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-333 (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP   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-119, AND IDENTIFICATION BY
RP   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-119, AND IDENTIFICATION BY
RP   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, 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).
CC   -!- FUNCTION: May play a role in mitochondrial aerobic respiration. May
CC       also regulate mitochondrial organization and fission (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q15390; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-724207, EBI-517508;
CC       Q15390; Q17RD7: SYT16; NbExp=3; IntAct=EBI-724207, EBI-10238936;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Note=May be
CC       associated with the inner and the outer mitochondrial membrane.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q15390-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15390-2; Sequence=VSP_046765;
CC   -!- SIMILARITY: Belongs to the MTFR1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA02798.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC055822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC036116; AAH36116.1; -; mRNA.
DR   EMBL; BC043498; AAH43498.1; -; mRNA.
DR   EMBL; BX537854; CAD97862.1; -; mRNA.
DR   EMBL; D13634; BAA02798.1; ALT_INIT; mRNA.
DR   EMBL; CR456910; CAG33191.1; -; mRNA.
DR   CCDS; CCDS55240.1; -. [Q15390-2]
DR   CCDS; CCDS6182.1; -. [Q15390-1]
DR   RefSeq; NP_001139310.1; NM_001145838.1. [Q15390-2]
DR   RefSeq; NP_055452.3; NM_014637.3. [Q15390-1]
DR   AlphaFoldDB; Q15390; -.
DR   SMR; Q15390; -.
DR   BioGRID; 115008; 63.
DR   IntAct; Q15390; 24.
DR   MINT; Q15390; -.
DR   STRING; 9606.ENSP00000262146; -.
DR   iPTMnet; Q15390; -.
DR   PhosphoSitePlus; Q15390; -.
DR   BioMuta; MTFR1; -.
DR   DMDM; 73920234; -.
DR   EPD; Q15390; -.
DR   jPOST; Q15390; -.
DR   MassIVE; Q15390; -.
DR   MaxQB; Q15390; -.
DR   PaxDb; Q15390; -.
DR   PeptideAtlas; Q15390; -.
DR   PRIDE; Q15390; -.
DR   ProteomicsDB; 17303; -.
DR   ProteomicsDB; 60560; -. [Q15390-1]
DR   Antibodypedia; 11925; 120 antibodies from 23 providers.
DR   DNASU; 9650; -.
DR   Ensembl; ENST00000262146.9; ENSP00000262146.4; ENSG00000066855.16. [Q15390-1]
DR   Ensembl; ENST00000458689.2; ENSP00000391502.2; ENSG00000066855.16. [Q15390-2]
DR   GeneID; 9650; -.
DR   KEGG; hsa:9650; -.
DR   MANE-Select; ENST00000262146.9; ENSP00000262146.4; NM_014637.4; NP_055452.3.
DR   UCSC; uc003xvm.3; human. [Q15390-1]
DR   CTD; 9650; -.
DR   GeneCards; MTFR1; -.
DR   HGNC; HGNC:29510; MTFR1.
DR   HPA; ENSG00000066855; Low tissue specificity.
DR   MIM; 619414; gene.
DR   neXtProt; NX_Q15390; -.
DR   OpenTargets; ENSG00000066855; -.
DR   PharmGKB; PA142671305; -.
DR   VEuPathDB; HostDB:ENSG00000066855; -.
DR   eggNOG; ENOG502QSSN; Eukaryota.
DR   GeneTree; ENSGT00950000183215; -.
DR   HOGENOM; CLU_059135_0_0_1; -.
DR   InParanoid; Q15390; -.
DR   OMA; KKPEIPN; -.
DR   OrthoDB; 1485791at2759; -.
DR   PhylomeDB; Q15390; -.
DR   TreeFam; TF331404; -.
DR   PathwayCommons; Q15390; -.
DR   SignaLink; Q15390; -.
DR   BioGRID-ORCS; 9650; 12 hits in 1045 CRISPR screens.
DR   ChiTaRS; MTFR1; human.
DR   GenomeRNAi; 9650; -.
DR   Pharos; Q15390; Tbio.
DR   PRO; PR:Q15390; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q15390; protein.
DR   Bgee; ENSG00000066855; Expressed in secondary oocyte and 202 other tissues.
DR   ExpressionAtlas; Q15390; baseline and differential.
DR   Genevisible; Q15390; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; ISS:UniProtKB.
DR   GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR   InterPro; IPR007972; Mtfr1.
DR   PANTHER; PTHR14215; PTHR14215; 1.
DR   Pfam; PF05308; Mito_fiss_reg; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..48
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..333
FT                   /note="Mitochondrial fission regulator 1"
FT                   /id="PRO_0000096622"
FT   REGION          177..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..304
FT                   /note="Necessary and sufficient to promote mitochondrial
FT                   fission"
FT                   /evidence="ECO:0000250"
FT   REGION          288..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          137..169
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        182..198
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         23..55
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_046765"
FT   CONFLICT        135
FT                   /note="L -> R (in Ref. 1; AAH36116)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   333 AA;  37000 MW;  ED8025FCF1B44827 CRC64;
     MLGWIKRLIR MVFQQVGVSM QSVLWSRKPY GSSRSIVRKI GTNLSLIQCP RVQFQINSHA
     TEWSPSHPGE DAVASFADVG WVAKEEGECS ARLRTEVRSR PPLQDDLLFF EKAPSRQISL
     PDLSQEEPQL KTPALANEEA LQKICALENE LAALRAQIAK IVTQQEQQNL TAGDLDSTTF
     GTIPPHPPPP PPPLPPPALG LHQSTSAVDL IKERREKRAN AGKTLVKNNP KKPEMPNMLE
     ILKEMNSVKL RSVKRSEQDV KPKPVDATDP AALIAEALKK KFAYRYRSDS QDEVEKGIPK
     SESEATSERV LFGPHMLKPT GKMKALIENV SDS
 
 
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