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SNU71_YEAS7
ID   SNU71_YEAS7             Reviewed;         620 AA.
AC   A6ZV04;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=U1 small nuclear ribonucleoprotein component SNU71;
GN   Name=SNU71; ORFNames=SCY_2237;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Component of the U1 snRNP particle, which recognizes and
CC       binds the 5'-splice site of pre-mRNA. Together with other non-snRNP
CC       factors, U1 snRNP forms the spliceosomal commitment complex, that
CC       targets pre-mRNA to the splicing pathway (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the U1 snRNP particle, a subcomplex of the
CC       spliceosome. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNU71 family. {ECO:0000305}.
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DR   EMBL; AAFW02000102; EDN61612.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZV04; -.
DR   SMR; A6ZV04; -.
DR   PRIDE; A6ZV04; -.
DR   EnsemblFungi; EDN61612; EDN61612; SCY_2237.
DR   HOGENOM; CLU_031562_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR002483; PWI_dom.
DR   SMART; SM00311; PWI; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Ribonucleoprotein; RNA-binding; Spliceosome.
FT   CHAIN           1..620
FT                   /note="U1 small nuclear ribonucleoprotein component SNU71"
FT                   /id="PRO_0000333461"
FT   REGION          58..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          296..385
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        246..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..353
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         512
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53207"
FT   MOD_RES         514
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53207"
SQ   SEQUENCE   620 AA;  71397 MW;  ABB8C0F67BF993D4 CRC64;
     MRDIVFVSPQ LYLSSQEGWK SDSAKSGFIP ILKNDLQRFQ DSLKHIVDAR NSLSETLLNS
     KDDGSIHNSD QNTGLNKDKE ASIADNNSAN KCATSSSRYQ ELKQFLPISL DQQIHTVSLQ
     GVSSSFSRGQ IESLLDHCLN LALTETQSNS ALKVEAWSSF SSFLDTQDIF IRFSKVDEDE
     AFVNTLNYCK ALFAFIRKLH EDFKIELHLD LNTKEYVEDR TGTIPSVKPE KASEFYSVFK
     NIEDQTDERN SKKEQLDDSS TQYKVDTNTL SDLPSDALDQ LCKDIIEFRT KVVSIEKEKK
     MKSTYEESRR QRHQMQKVFD QIRKNHSGAK GSANTEEEDT NMEDEDEEDD TEDDLALEKR
     KEERDLEESN RRYEDMLHQL HSNTEPKIKS IRADIMSAEN YEEHLEKNRS LYLKELLHLA
     NDVHYDHHRS FKEQEERRDE EDRAKNGNAK ELAPIQLSDG KAISAGKAAA ITLPEGTVKS
     ENYNADKNVS ESSEHVKIKF DFKKAIDHSV ESSSEDEGYR ESELPPTKPS ERSAAEDRLP
     FTADELNIRL TNLKESRYVD ELVREFLGVY EDELVEYILE NIRVNQSKQA LLNELRETFD
     EDGETIADRL WSRKEFRLGT
 
 
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