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MYO19_HUMAN
ID   MYO19_HUMAN             Reviewed;         970 AA.
AC   Q96H55; Q59GS4; Q9H5X2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Unconventional myosin-XIX {ECO:0000303|PubMed:19932026};
DE   AltName: Full=Myosin head domain-containing protein 1 {ECO:0000312|HGNC:HGNC:26234};
GN   Name=MYO19 {ECO:0000303|PubMed:19932026, ECO:0000312|HGNC:HGNC:26234};
GN   Synonyms=MYOHD1 {ECO:0000312|HGNC:HGNC:26234};
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 2).
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-176.
RA   Mural R.J., Istrail S., Sutton G.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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=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   [6]
RP   FUNCTION, TISSUE SPECIFICITY, TARGETING REGION, AND SUBCELLULAR LOCATION.
RX   PubMed=19932026; DOI=10.1016/j.cub.2009.10.026;
RA   Quintero O.A., DiVito M.M., Adikes R.C., Kortan M.B., Case L.B., Lier A.J.,
RA   Panaretos N.S., Slater S.Q., Rengarajan M., Feliu M., Cheney R.E.;
RT   "Human Myo19 is a novel myosin that associates with mitochondria.";
RL   Curr. Biol. 19:2008-2013(2009).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-135.
RX   PubMed=23568824; DOI=10.1002/cm.21110;
RA   Adikes R.C., Unrath W.C., Yengo C.M., Quintero O.A.;
RT   "Biochemical and bioinformatic analysis of the myosin-XIX motor domain.";
RL   Cytoskeleton 70:281-295(2013).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685, 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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=25447992; DOI=10.1016/j.cub.2014.09.045;
RA   Rohn J.L., Patel J.V., Neumann B., Bulkescher J., Mchedlishvili N.,
RA   McMullan R.C., Quintero O.A., Ellenberg J., Baum B.;
RT   "Myo19 ensures symmetric partitioning of mitochondria and coupling of
RT   mitochondrial segregation to cell division.";
RL   Curr. Biol. 24:2598-2605(2014).
RN   [10]
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).
RN   [11]
RP   SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ARG-855; 882-ARG-LYS-883;
RP   ARG-915; LYS-923 AND 927-ARG-LYS-928.
RX   PubMed=27126804; DOI=10.1002/cm.21305;
RA   Hawthorne J.L., Mehta P.R., Singh P.P., Wong N.Q., Quintero O.A.;
RT   "Positively charged residues within the MYO19 MyMOMA domain are essential
RT   for proper localization of MYO19 to the mitochondrial outer membrane.";
RL   Cytoskeleton 73:286-299(2016).
RN   [12]
RP   SUBCELLULAR LOCATION.
RX   PubMed=26659663; DOI=10.1242/jcs.175349;
RA   Shneyer B.I., Usaj M., Henn A.;
RT   "Myo19 is an outer mitochondrial membrane motor and effector of starvation-
RT   induced filopodia.";
RL   J. Cell Sci. 129:543-556(2016).
CC   -!- FUNCTION: Actin-based motor molecule with ATPase activity that
CC       localizes to the mitochondrion outer membrane (PubMed:19932026,
CC       PubMed:23568824, PubMed:25447992). Motor protein that moves towards the
CC       plus-end of actin filaments (By similarity). Required for mitochondrial
CC       inheritance during mitosis (PubMed:25447992). May be involved in
CC       mitochondrial transport or positioning (PubMed:23568824).
CC       {ECO:0000250|UniProtKB:Q5SV80, ECO:0000269|PubMed:19932026,
CC       ECO:0000269|PubMed:25447992, ECO:0000305|PubMed:23568824}.
CC   -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains:
CC       interacts with myosin light chains MYL9 and MYL12B.
CC       {ECO:0000250|UniProtKB:Q5SV80}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:19932026, ECO:0000269|PubMed:23568824,
CC       ECO:0000269|PubMed:25447992, ECO:0000269|PubMed:26659663,
CC       ECO:0000269|PubMed:27126804}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:27126804}. Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:19932026}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q96H55-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96H55-2; Sequence=VSP_033402, VSP_033403;
CC       Name=3;
CC         IsoId=Q96H55-3; Sequence=VSP_033405, VSP_033406;
CC       Name=4;
CC         IsoId=Q96H55-4; Sequence=VSP_033404;
CC   -!- TISSUE SPECIFICITY: Widely expressed in multiple tissues and cell
CC       lines. {ECO:0000269|PubMed:19932026}.
CC   -!- DOMAIN: The MyMOMA (MYO19-specific mitochondrial outer membrane-
CC       association) region mediates association with the mitochondrion outer
CC       membrane via electrostatic interaction. {ECO:0000269|PubMed:19932026,
CC       ECO:0000269|PubMed:27126804}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92272.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK026518; BAB15495.1; -; mRNA.
DR   EMBL; AB209035; BAD92272.1; ALT_INIT; mRNA.
DR   EMBL; AC126327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471199; EAW57557.1; -; Genomic_DNA.
DR   EMBL; BC008900; AAH08900.1; -; mRNA.
DR   CCDS; CCDS45654.1; -. [Q96H55-4]
DR   CCDS; CCDS54112.1; -. [Q96H55-1]
DR   CCDS; CCDS59283.1; -. [Q96H55-2]
DR   RefSeq; NP_001028752.1; NM_001033580.2. [Q96H55-2]
DR   RefSeq; NP_001157207.1; NM_001163735.1. [Q96H55-1]
DR   RefSeq; NP_079385.2; NM_025109.5. [Q96H55-4]
DR   AlphaFoldDB; Q96H55; -.
DR   SMR; Q96H55; -.
DR   BioGRID; 123161; 285.
DR   IntAct; Q96H55; 188.
DR   MINT; Q96H55; -.
DR   STRING; 9606.ENSP00000479518; -.
DR   iPTMnet; Q96H55; -.
DR   PhosphoSitePlus; Q96H55; -.
DR   BioMuta; MYO19; -.
DR   DMDM; 189083208; -.
DR   EPD; Q96H55; -.
DR   jPOST; Q96H55; -.
DR   MassIVE; Q96H55; -.
DR   MaxQB; Q96H55; -.
DR   PaxDb; Q96H55; -.
DR   PeptideAtlas; Q96H55; -.
DR   PRIDE; Q96H55; -.
DR   ProteomicsDB; 76702; -. [Q96H55-1]
DR   ProteomicsDB; 76703; -. [Q96H55-2]
DR   ProteomicsDB; 76704; -. [Q96H55-3]
DR   ProteomicsDB; 76705; -. [Q96H55-4]
DR   Antibodypedia; 73086; 151 antibodies from 24 providers.
DR   DNASU; 80179; -.
DR   Ensembl; ENST00000610930.4; ENSP00000478437.1; ENSG00000278259.5. [Q96H55-4]
DR   Ensembl; ENST00000610992.4; ENSP00000480125.1; ENSG00000278259.5. [Q96H55-3]
DR   Ensembl; ENST00000613929.2; ENSP00000478355.1; ENSG00000278372.4. [Q96H55-4]
DR   Ensembl; ENST00000614623.5; ENSP00000479518.1; ENSG00000278259.5. [Q96H55-1]
DR   Ensembl; ENST00000618519.4; ENSP00000480242.1; ENSG00000278372.4. [Q96H55-1]
DR   Ensembl; ENST00000621344.4; ENSP00000477559.1; ENSG00000278259.5. [Q96H55-2]
DR   Ensembl; ENST00000633264.1; ENSP00000487617.1; ENSG00000278372.4. [Q96H55-3]
DR   Ensembl; ENST00000633938.1; ENSP00000488204.1; ENSG00000278372.4. [Q96H55-2]
DR   GeneID; 80179; -.
DR   KEGG; hsa:80179; -.
DR   MANE-Select; ENST00000614623.5; ENSP00000479518.1; NM_001163735.2; NP_001157207.1.
DR   UCSC; uc032fdu.2; human. [Q96H55-1]
DR   CTD; 80179; -.
DR   DisGeNET; 80179; -.
DR   GeneCards; MYO19; -.
DR   HGNC; HGNC:26234; MYO19.
DR   HPA; ENSG00000278259; Low tissue specificity.
DR   MIM; 617379; gene.
DR   neXtProt; NX_Q96H55; -.
DR   OpenTargets; ENSG00000278259; -.
DR   PharmGKB; PA162396512; -.
DR   VEuPathDB; HostDB:ENSG00000278259; -.
DR   eggNOG; KOG0160; Eukaryota.
DR   GeneTree; ENSGT00940000157382; -.
DR   HOGENOM; CLU_000192_7_4_1; -.
DR   InParanoid; Q96H55; -.
DR   OMA; CQLMDDA; -.
DR   OrthoDB; 311886at2759; -.
DR   PhylomeDB; Q96H55; -.
DR   TreeFam; TF328771; -.
DR   PathwayCommons; Q96H55; -.
DR   Reactome; R-HSA-9013419; RHOT2 GTPase cycle.
DR   Reactome; R-HSA-9013425; RHOT1 GTPase cycle.
DR   SignaLink; Q96H55; -.
DR   BioGRID-ORCS; 80179; 14 hits in 1070 CRISPR screens.
DR   ChiTaRS; MYO19; human.
DR   GenomeRNAi; 80179; -.
DR   Pharos; Q96H55; Tbio.
DR   PRO; PR:Q96H55; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q96H55; protein.
DR   Bgee; ENSG00000278259; Expressed in skin of leg and 171 other tissues.
DR   ExpressionAtlas; Q96H55; baseline and differential.
DR   Genevisible; Q96H55; HS.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0032027; F:myosin light chain binding; IEA:Ensembl.
DR   GO; GO:0060002; F:plus-end directed microfilament motor activity; IEA:Ensembl.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0034642; P:mitochondrion migration along actin filament; IDA:MGI.
DR   GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR   GO; GO:0090140; P:regulation of mitochondrial fission; IMP:UniProtKB.
DR   GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR   CDD; cd14880; MYSc_Myo19; 1.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036035; MYSc_Myo19.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Motor protein;
KW   Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..970
FT                   /note="Unconventional myosin-XIX"
FT                   /id="PRO_0000332969"
FT   DOMAIN          35..758
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          759..779
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          783..812
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          602..624
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   REGION          824..970
FT                   /note="MyMOMA region"
FT                   /evidence="ECO:0000269|PubMed:19932026,
FT                   ECO:0000269|PubMed:27126804"
FT   BINDING         132..139
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   MOD_RES         685
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         300..317
FT                   /note="LAGLLHLGNIQFAASEDE -> RRKATPLKFGRDDGQPFA (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_033402"
FT   VAR_SEQ         318..970
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_033403"
FT   VAR_SEQ         439..638
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033404"
FT   VAR_SEQ         636
FT                   /note="V -> A (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_033405"
FT   VAR_SEQ         637..970
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_033406"
FT   VARIANT         176
FT                   /note="N -> S (in dbSNP:rs2306595)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_043018"
FT   VARIANT         203
FT                   /note="Q -> H (in dbSNP:rs9890918)"
FT                   /id="VAR_043019"
FT   VARIANT         475
FT                   /note="L -> I (in dbSNP:rs7217346)"
FT                   /id="VAR_043020"
FT   MUTAGEN         135
FT                   /note="G->R: Rigor-like phenotype due to disruption of ATP-
FT                   binding. Does not affect localization to mitochondrion."
FT                   /evidence="ECO:0000269|PubMed:23568824"
FT   MUTAGEN         855
FT                   /note="R->A: Does not affect localization to mitochondrion
FT                   outer membrane."
FT                   /evidence="ECO:0000269|PubMed:27126804"
FT   MUTAGEN         882..883
FT                   /note="RK->AA: Abolishes localization to mitochondrion
FT                   outer membrane."
FT                   /evidence="ECO:0000269|PubMed:27126804"
FT   MUTAGEN         915
FT                   /note="R->A: Does not affect localization to mitochondrion
FT                   outer membrane."
FT                   /evidence="ECO:0000269|PubMed:27126804"
FT   MUTAGEN         923
FT                   /note="K->A: Does not affect localization to mitochondrion
FT                   outer membrane."
FT                   /evidence="ECO:0000269|PubMed:27126804"
FT   MUTAGEN         927..928
FT                   /note="RK->AA: Does not affect localization to
FT                   mitochondrion outer membrane."
FT                   /evidence="ECO:0000269|PubMed:27126804"
SQ   SEQUENCE   970 AA;  109135 MW;  3AB15AD901BE7407 CRC64;
     MLQQVNGHNP GSDGQAREYL REDLQEFLGG EVLLYKLDDL TRVNPVTLET VLRCLQARYM
     ADTFYTNAGC TLVALNPFKP VPQLYSPELM REYHAAPQPQ KLKPHVFTVG EQTYRNVKSL
     IEPVNQSIVV SGESGAGKTW TSRCLMKFYA VVATSPASWE SHKIAERIEQ RILNSNPVME
     AFGNACTLRN NNSSRFGKFI QLQLNRAQQM TGAAVQTYLL EKTRVACQAS SERNFHIFYQ
     ICKGASEDER LQWHLPEGAA FSWLPNPERS LEEDCFEVTR EAMLHLGIDT PTQNNIFKVL
     AGLLHLGNIQ FAASEDEAQP CQPMDDAKYS VRTAASLLGL PEDVLLEMVQ IRTIRAGRQQ
     QVFRKPCARA ECDTRRDCLA KLIYARLFDW LVSVINSSIC ADTDSWTTFI GLLDVYGFES
     FPDNSLEQLC INYANEKLQQ HFVAHYLRAQ QEEYAVEGLE WSFINYQDNQ PCLDLIEGSP
     ISICSLINEE CRLNRPSSAA QLQTRIETAL AGSPCLGHNK LSREPSFIVV HYAGPVRYHT
     AGLVEKNKDP IPPELTRLLQ QSQDPLLMGL FPTNPKEKTQ EEPPGQSRAP VLTVVSKFKA
     SLEQLLQVLH STTPHYIRCI KPNSQGQAQT FLQEEVLSQL EACGLVETIH ISAAGFPIRV
     SHRNFVERYK LLRRLHPCTS SGPDSPYPAK GLPEWCPHSE EATLEPLIQD ILHTLPVLTQ
     AAAITGDSAE AMPAPMHCGR TKVFMTDSML ELLECGRARV LEQCARCIQG GWRRHRHREQ
     ERQWRAVMLI QAAIRSWLTR KHIQRLHAAA TVIKRAWQKW RIRMACLAAK ELDGVEEKHF
     SQAPCSLSTS PLQTRLLEAI IRLWPLGLVL ANTAMGVGSF QRKLVVWACL QLPRGSPSSY
     TVQTAQDQAG VTSIRALPQG SIKFHCRKSP LRYADICPEP SPYSITGFNQ ILLERHRLIH
     VTSSAFTGLG
 
 
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