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MSH6_CHICK
ID   MSH6_CHICK              Reviewed;        1337 AA.
AC   E1BYJ2;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=DNA mismatch repair protein Msh6 {ECO:0000250|UniProtKB:P54276};
GN   Name=MSH6 {ECO:0000250|UniProtKB:P52701};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl;
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=23314153; DOI=10.1093/nar/gks1470;
RA   Campo V.A., Patenaude A.M., Kaden S., Horb L., Firka D., Jiricny J.,
RA   Di Noia J.M.;
RT   "MSH6- or PMS2-deficiency causes re-replication in DT40 B cells, but it has
RT   little effect on immunoglobulin gene conversion or on repair of AID-
RT   generated uracils.";
RL   Nucleic Acids Res. 41:3032-3046(2013).
CC   -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC       (MMR). Involved in B cell growth by positively regulating B cell
CC       proliferation and controlling replication efficiency. Controls cell
CC       cycle to prevent re-replication and defects in DNA damage-induced G2
CC       checkpoint. Doesn't seem to counteract or control the immunoglobulin
CC       gene conversion (Ig GC) and to contribute to guanine/uracil mismatch
CC       repair. {ECO:0000269|PubMed:23314153}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52701}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC       {ECO:0000305}.
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DR   EMBL; AADN03003073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E1BYJ2; -.
DR   SMR; E1BYJ2; -.
DR   STRING; 9031.ENSGALP00000038835; -.
DR   PaxDb; E1BYJ2; -.
DR   VEuPathDB; HostDB:geneid_421291; -.
DR   eggNOG; KOG0217; Eukaryota.
DR   HOGENOM; CLU_002472_1_3_1; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0032301; C:MutSalpha complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0030983; F:mismatched DNA binding; IBA:GO_Central.
DR   GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:UniProtKB.
DR   GO; GO:0032876; P:negative regulation of DNA endoreduplication; IMP:UniProtKB.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
DR   Gene3D; 3.30.420.110; -; 1.
DR   Gene3D; 3.40.1170.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR   InterPro; IPR017261; DNA_mismatch_repair_MutS/MSH.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR   InterPro; IPR036678; MutS_con_dom_sf.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000313; PWWP_dom.
DR   PANTHER; PTHR11361; PTHR11361; 1.
DR   Pfam; PF01624; MutS_I; 1.
DR   Pfam; PF05188; MutS_II; 1.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF05190; MutS_IV; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF48334; SSF48334; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53150; SSF53150; 1.
DR   SUPFAM; SSF55271; SSF55271; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR   PROSITE; PS50812; PWWP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA-binding; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..1337
FT                   /note="DNA mismatch repair protein Msh6"
FT                   /id="PRO_0000436927"
FT   DOMAIN          68..130
FT                   /note="PWWP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT   REGION          170..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..189
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..270
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1111..1118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1337 AA;  149891 MW;  812A3FC936697810 CRC64;
     MMSASNLSVI HEVLLVLLNH QRINLPYENL EASLSRMLFL SSFVQEVVQV PIPCNVSANR
     SVSGVYSPGD LVWAKMEGYP WWPCLIYNHP TEGTIVRGKG SSARIHVQFF DVSPTRGWVS
     IKYLRPYKGS SDREVLKGGM FYSMKPEIKK AMELADDAMS KDKTKRLELA VCSEPSDTEE
     AEEEEMEQMS GSASGDSDDS NSEEDVKGNK RVPNRGSAIK AKRRRVLDSD SDRDGSDVEF
     KPDVKEASSE EASSGVDENE ATDVETDEES IEESPIKVPS KRKRGNVSKP SKRSSLENEH
     SEAPKRAAPV SLEAKSKLTL FAAPENFESQ ANACSGGTNG FAAWEHEKLE WLQEGKKKDA
     HRRRQNHPDY DPCTLYVPED YLNKCTPGMR RWWQLKSQNF DAVICYKVGK FYELYHMDAV
     TGVNELGLIF MKGSWAHSGF PETAFGRFSA ILVQKGYKIA RVEQTETPEM MEARCKATAH
     TTKFDKVVRR EICRIITKGT QTYSIIDCDP TENHNKYLLC VKEKEDSSGQ RVYGVCFVDT
     SVGKFYVGQF SDDRHCSRFR TLVAHYTPVQ VLFEKGNLTV DTQKILKGSL ISCIQEGLIS
     GSQFWSASKT LKVLLEEEYF KENQNTESGC VLPSVIKSLT SESDSLGLTP GENSELALSA
     LGGIVFYLKK CLIDQELLSL ANFEKYIPVD ADNAKTVSSS NFFARTDRRM VLDGVTLMNL
     EVLQNGTNGT TEGTLLERID SCCTPFGKRL LKQWLCAPLC NPTSINDRLD AVEDLLAVPA
     KLTEITEHLK KLPDLERLLS KIHSIGSPLK SQNHPDSRAI FYEEIKYSKK KIADFLSALE
     GFKVMNEIVD AMEEVASDFK SQVLKQLVTR KAKHPDGRFP DLSAELKRWD TAFDHNQARK
     TGVITPKAGF DPDYDKALQD IKTVEEDFRT YLDKQRKLLG LKSVLYWGTG KNRYQMEIPE
     TATSRNLPEE YELKSTRKGY KRYWTKEIEK MLAELINAEE RRDAALKDCM RRLFYNFDKN
     SQDWQTAVQC IAVLDVLMSL ANYSQDGDGP LCRPVILLPV DSAPPFLELK NARHPCITKT
     FFGDDFIPND IVIGSKDEDG GSEASCVLVT GPNMGGKSTL MRQAGLLVIM AQLGCYVPAE
     VCRLTPIDRV FTRLGASDRI MSGESTFFVE LSETSSILQH ATEHSLVLVD ELGRGTATFD
     GTAIASAVVR ELAENIKCRT LFSTHYHSLV EDYSGSAAVR LGHMACMVEN ESEDPSQETI
     TFLYKFIEGA CPKSYGFNAA RLADIPEEII QKGHRKAKEF EKKTMSLRIF RFLCRVVDGV
     THDANAVGKL TTMLSHL
 
 
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