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MYH15_HUMAN
ID   MYH15_HUMAN             Reviewed;        1946 AA.
AC   Q9Y2K3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 5.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Myosin-15;
DE   AltName: Full=Myosin heavy chain 15;
GN   Name=MYH15; Synonyms=KIAA1000;
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], AND VARIANT TYR-504.
RC   TISSUE=Brain;
RX   PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:63-70(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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   [3]
RP   IDENTIFICATION.
RX   PubMed=11919279; DOI=10.1093/oxfordjournals.molbev.a004093;
RA   Desjardins P.R., Burkman J.M., Shrager J.B., Allmond L.A., Stedman H.H.;
RT   "Evolutionary implications of three novel members of the human sarcomeric
RT   myosin heavy chain gene family.";
RL   Mol. Biol. Evol. 19:375-393(2002).
RN   [4]
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).
CC   -!- FUNCTION: Muscle contraction. {ECO:0000250}.
CC   -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC       chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC       regulatory light chain subunits (MLC-2). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC       myofibrils.
CC   -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC       of a 28-residue repeat pattern composed of 4 heptapeptides,
CC       characteristic for alpha-helical coiled coils. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000305}.
CC   -!- CAUTION: Represents a conventional myosin. This protein should not be
CC       confused with the unconventional myosin-15 (MYO15). {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA76844.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB023217; BAA76844.3; ALT_INIT; mRNA.
DR   EMBL; AC069499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_055796.1; NM_014981.1.
DR   RefSeq; XP_011510861.1; XM_011512559.2.
DR   AlphaFoldDB; Q9Y2K3; -.
DR   SMR; Q9Y2K3; -.
DR   BioGRID; 116637; 12.
DR   IntAct; Q9Y2K3; 5.
DR   STRING; 9606.ENSP00000273353; -.
DR   CarbonylDB; Q9Y2K3; -.
DR   iPTMnet; Q9Y2K3; -.
DR   PhosphoSitePlus; Q9Y2K3; -.
DR   BioMuta; MYH15; -.
DR   DMDM; 296439498; -.
DR   jPOST; Q9Y2K3; -.
DR   MassIVE; Q9Y2K3; -.
DR   PaxDb; Q9Y2K3; -.
DR   PeptideAtlas; Q9Y2K3; -.
DR   PRIDE; Q9Y2K3; -.
DR   ProteomicsDB; 85823; -.
DR   Antibodypedia; 46526; 66 antibodies from 21 providers.
DR   DNASU; 22989; -.
DR   Ensembl; ENST00000273353.5; ENSP00000273353.4; ENSG00000144821.11.
DR   GeneID; 22989; -.
DR   KEGG; hsa:22989; -.
DR   UCSC; uc003dxa.1; human.
DR   CTD; 22989; -.
DR   DisGeNET; 22989; -.
DR   GeneCards; MYH15; -.
DR   HGNC; HGNC:31073; MYH15.
DR   HPA; ENSG00000144821; Tissue enhanced (brain, retina, tongue).
DR   MIM; 609929; gene.
DR   neXtProt; NX_Q9Y2K3; -.
DR   PharmGKB; PA134958635; -.
DR   VEuPathDB; HostDB:ENSG00000144821; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   HOGENOM; CLU_000192_8_1_1; -.
DR   InParanoid; Q9Y2K3; -.
DR   OMA; RKQQCAI; -.
DR   OrthoDB; 47111at2759; -.
DR   PhylomeDB; Q9Y2K3; -.
DR   TreeFam; TF314375; -.
DR   PathwayCommons; Q9Y2K3; -.
DR   SignaLink; Q9Y2K3; -.
DR   BioGRID-ORCS; 22989; 10 hits in 1069 CRISPR screens.
DR   ChiTaRS; MYH15; human.
DR   GeneWiki; MYH15; -.
DR   GenomeRNAi; 22989; -.
DR   Pharos; Q9Y2K3; Tbio.
DR   PRO; PR:Q9Y2K3; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9Y2K3; protein.
DR   Bgee; ENSG00000144821; Expressed in paraflocculus and 103 other tissues.
DR   Genevisible; Q9Y2K3; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR   GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR   GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   Gene3D; 1.20.5.370; -; 5.
DR   Gene3D; 2.30.30.360; -; 1.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014751; XRCC4-like_C.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW   Methylation; Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW   Reference proteome; Thick filament.
FT   CHAIN           1..1946
FT                   /note="Myosin-15"
FT                   /id="PRO_0000274233"
FT   DOMAIN          49..99
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT   DOMAIN          103..790
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          793..822
FT                   /note="IQ"
FT   REGION          667..689
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          769..783
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   COILED          853..1946
FT                   /evidence="ECO:0000255"
FT   BINDING         196..203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         147
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         454
FT                   /note="R -> Q (in dbSNP:rs4299484)"
FT                   /id="VAR_030235"
FT   VARIANT         504
FT                   /note="H -> Y (in dbSNP:rs9868484)"
FT                   /evidence="ECO:0000269|PubMed:10231032"
FT                   /id="VAR_030236"
FT   VARIANT         949
FT                   /note="T -> I (in dbSNP:rs12638212)"
FT                   /id="VAR_030237"
FT   VARIANT         1125
FT                   /note="T -> A (in dbSNP:rs3900940)"
FT                   /id="VAR_030238"
FT   VARIANT         1467
FT                   /note="D -> N (in dbSNP:rs1078456)"
FT                   /id="VAR_046376"
SQ   SEQUENCE   1946 AA;  224619 MW;  6CCE1836B64FC9C9 CRC64;
     MVESCLLTFR AFFWWIALIK MDLSDLGEAA AFLRRSEAEL LLLQATALDG KKKCWIPDGE
     NAYIEAEVKG SEDDGTVIVE TADGESLSIK EDKIQQMNPP EFEMIEDMAM LTHLNEASVL
     HTLKRRYGQW MIYTYSGLFC VTINPYKWLP VYQKEVMAAY KGKRRSEAPP HIFAVANNAF
     QDMLHNRENQ SILFTGESGA GKTVNSKHII QYFATIAAMI ESRKKQGALE DQIMQANTIL
     EAFGNAKTLR NDNSSRFGKF IRMHFGARGM LSSVDIDIYL LEKSRVIFQQ AGERNYHIFY
     QILSGQKELH DLLLVSANPS DFHFCSCGAV TVESLDDAEE LLATEQAMDI LGFLPDEKYG
     CYKLTGAIMH FGNMKFKQKP REEQLEADGT ENADKAAFLM GINSSELVKC LIHPRIKVGN
     EYVTRGQTIE QVTCAVGALS KSMYERMFKW LVARINRALD AKLSRQFFIG ILDITGFEIL
     EYNSLEQLCI NFTNEKLQQF FNWHMFVLEQ EEYKKESIEW VSIGFGLDLQ ACIDLIEKPM
     GILSILEEEC MFPKATDLTF KTKLFDNHFG KSVHLQKPKP DKKKFEAHFE LVHYAGVVPY
     NISGWLEKNK DLLNETVVAV FQKSSNRLLA SLFENYMSTD SAIPFGEKKR KKGASFQTVA
     SLHKENLNKL MTNLKSTAPH FVRCINPNVN KIPGILDPYL VLQQLRCNGV LEGTRICREG
     FPNRLQYADF KQRYCILNPR TFPKSKFVSS RKAAEELLGS LEIDHTQYRF GITKVFFKAG
     FLGQLEAIRD ERLSKVFTLF QARAQGKLMR IKFQKILEER DALILIQWNI RAFMAVKNWP
     WMRLFFKIKP LVKSSEVGEE VAGLKEECAQ LQKALEKSEF QREELKAKQV SLTQEKNDLI
     LQLQAEQETL ANVEEQCEWL IKSKIQLEAR VKELSERVEE EEEINSELTA RGRKLEDECF
     ELKKEIDDLE TMLVKSEKEK RTTEHKVKNL TEEVEFLNED ISKLNRAAKV VQEAHQQTLD
     DLHMEEEKLS SLSKANLKLE QQVDELEGAL EQERKARMNC ERELHKLEGN LKLNRESMEN
     LESSQRHLAE ELRKKELELS QMNSKVENEK GLVAQLQKTV KELQTQIKDL KEKLEAERTT
     RAKMERERAD LTQDLADLNE RLEEVGGSSL AQLEITKKQE TKFQKLHRDM EEATLHFETT
     SASLKKRHAD SLAELEGQVE NLQQVKQKLE KDKSDLQLEV DDLLTRVEQM TRAKANAEKL
     CTLYEERLHE ATAKLDKVTQ LANDLAAQKT KLWSESGEFL RRLEEKEALI NQLSREKSNF
     TRQIEDLRGQ LEKETKSQSA LAHALQKAQR DCDLLREQYE EEQEVKAELH RTLSKVNAEM
     VQWRMKYENN VIQRTEDLED AKKELAIRLQ EAAEAMGVAN ARNASLERAR HQLQLELGDA
     LSDLGKVRSA AARLDQKQLQ SGKALADWKQ KHEESQALLD ASQKEVQALS TELLKLKNTY
     EESIVGQETL RRENKNLQEE ISNLTNQVRE GTKNLTEMEK VKKLIEEEKT EVQVTLEETE
     GALERNESKI LHFQLELLEA KAELERKLSE KDEEIENFRR KQQCTIDSLQ SSLDSEAKSR
     IEVTRLKKKM EEDLNEMELQ LSCANRQVSE ATKSLGQLQI QIKDLQMQLD DSTQLNSDLK
     EQVAVAERRN SLLQSELEDL RSLQEQTERG RRLSEEELLE ATERINLFYT QNTSLLSQKK
     KLEADVARMQ KEAEEVVQEC QNAEEKAKKA AIEAANLSEE LKKKQDTIAH LERTRENMEQ
     TITDLQKRLA EAEQMALMGS RKQIQKLESR VRELEGELEG EIRRSAEAQR GARRLERCIK
     ELTYQAEEDK KNLSRMQTQM DKLQLKVQNY KQQVEVAETQ ANQYLSKYKK QQHELNEVKE
     RAEVAESQVN KLKIKAREFG KKVQEE
 
 
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