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HSH49_YEAST
ID   HSH49_YEAST             Reviewed;         213 AA.
AC   Q99181; D6W317;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 187.
DE   RecName: Full=Protein HSH49;
GN   Name=HSH49; OrderedLocusNames=YOR319W; ORFNames=O6142;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8896266;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b<1021::aid-yea981>3.0.co;2-7;
RA   Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A.,
RA   Schweizer M.;
RT   "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome
RT   XV reveals regions of similarity to chromosomes I and XIII.";
RL   Yeast 12:1021-1031(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   INTERACTION WITH RDS3.
RX   PubMed=14517302; DOI=10.1128/mcb.23.20.7339-7349.2003;
RA   Wang Q., Rymond B.C.;
RT   "Rds3p is required for stable U2 snRNP recruitment to the splicing
RT   apparatus.";
RL   Mol. Cell. Biol. 23:7339-7349(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Possible SF3b-like factor.
CC   -!- SUBUNIT: Interacts with RDS3. {ECO:0000269|PubMed:14517302}.
CC   -!- INTERACTION:
CC       Q99181; Q02554: CUS1; NbExp=6; IntAct=EBI-8579, EBI-654;
CC       Q99181; P47093: LSM8; NbExp=3; IntAct=EBI-8579, EBI-313;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 1240 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z75227; CAA99639.1; -; Genomic_DNA.
DR   EMBL; X90565; CAA62174.1; -; Genomic_DNA.
DR   EMBL; AY558437; AAS56763.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA11083.1; -; Genomic_DNA.
DR   PIR; S58329; S58329.
DR   RefSeq; NP_014964.1; NM_001183739.1.
DR   PDB; 5GM6; EM; 3.50 A; e=1-213.
DR   PDB; 5LSB; X-ray; 2.70 A; A/C/F=2-213.
DR   PDB; 5LSL; X-ray; 1.65 A; A/B/C/D=2-100.
DR   PDB; 5NRL; EM; 7.20 A; R=1-213.
DR   PDB; 5ZWM; EM; 3.40 A; 4=1-213.
DR   PDB; 5ZWO; EM; 3.90 A; 4=1-213.
DR   PDB; 6G90; EM; 4.00 A; R=1-213.
DR   PDB; 7OQB; EM; 9.00 A; R=1-213.
DR   PDB; 7OQE; EM; 5.90 A; R=1-213.
DR   PDBsum; 5GM6; -.
DR   PDBsum; 5LSB; -.
DR   PDBsum; 5LSL; -.
DR   PDBsum; 5NRL; -.
DR   PDBsum; 5ZWM; -.
DR   PDBsum; 5ZWO; -.
DR   PDBsum; 6G90; -.
DR   PDBsum; 7OQB; -.
DR   PDBsum; 7OQE; -.
DR   AlphaFoldDB; Q99181; -.
DR   SMR; Q99181; -.
DR   BioGRID; 34705; 206.
DR   ComplexPortal; CPX-1647; SF3B complex.
DR   ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex.
DR   DIP; DIP-930N; -.
DR   IntAct; Q99181; 43.
DR   MINT; Q99181; -.
DR   STRING; 4932.YOR319W; -.
DR   CarbonylDB; Q99181; -.
DR   MaxQB; Q99181; -.
DR   PaxDb; Q99181; -.
DR   PRIDE; Q99181; -.
DR   EnsemblFungi; YOR319W_mRNA; YOR319W; YOR319W.
DR   GeneID; 854497; -.
DR   KEGG; sce:YOR319W; -.
DR   SGD; S000005846; HSH49.
DR   VEuPathDB; FungiDB:YOR319W; -.
DR   eggNOG; KOG0131; Eukaryota.
DR   GeneTree; ENSGT00870000136537; -.
DR   HOGENOM; CLU_012062_21_2_1; -.
DR   InParanoid; Q99181; -.
DR   OMA; IPGAVQH; -.
DR   BioCyc; YEAST:G3O-33799-MON; -.
DR   PRO; PR:Q99181; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q99181; protein.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR   GO; GO:0005686; C:U2 snRNP; IDA:SGD.
DR   GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR   GO; GO:0005684; C:U2-type spliceosomal complex; IPI:ComplexPortal.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR   GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR   GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IDA:SGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR   GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR   CDD; cd12334; RRM1_SF3B4; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034158; SF3B4_RRM1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   3D-structure; mRNA processing; Nucleus; Reference proteome; Repeat;
KW   RNA-binding.
FT   CHAIN           1..213
FT                   /note="Protein HSH49"
FT                   /id="PRO_0000081613"
FT   DOMAIN          9..88
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          108..185
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   STRAND          10..14
FT                   /evidence="ECO:0007829|PDB:5LSL"
FT   HELIX           22..29
FT                   /evidence="ECO:0007829|PDB:5LSL"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:5LSL"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:5LSL"
FT   TURN            44..47
FT                   /evidence="ECO:0007829|PDB:5LSL"
FT   STRAND          51..59
FT                   /evidence="ECO:0007829|PDB:5LSL"
FT   HELIX           60..70
FT                   /evidence="ECO:0007829|PDB:5LSL"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:5LSL"
FT   STRAND          82..85
FT                   /evidence="ECO:0007829|PDB:5LSL"
FT   STRAND          108..113
FT                   /evidence="ECO:0007829|PDB:5LSB"
FT   HELIX           121..129
FT                   /evidence="ECO:0007829|PDB:5LSB"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:5LSB"
FT   STRAND          139..143
FT                   /evidence="ECO:0007829|PDB:5LSB"
FT   STRAND          148..156
FT                   /evidence="ECO:0007829|PDB:5LSB"
FT   HELIX           158..168
FT                   /evidence="ECO:0007829|PDB:5LSB"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:5LSB"
FT   STRAND          176..182
FT                   /evidence="ECO:0007829|PDB:5LSB"
FT   TURN            192..195
FT                   /evidence="ECO:0007829|PDB:5LSB"
FT   HELIX           196..202
FT                   /evidence="ECO:0007829|PDB:5LSB"
SQ   SEQUENCE   213 AA;  24503 MW;  F6FC44083094B176 CRC64;
     MNYSADSGNT VYVGNIDPRI TKEQLYELFI QINPVLRIKY PKDKVLQAYQ GYAFIEFYNQ
     GDAQYAIKIM NNTVRLYDRL IKVRQVTNST GTTNLPSNIS KDMILPIAKL FIKNLADSID
     SDQLVKIFNK FGKLIREPEI FYLSNGKLKC AYVYFEDFEK ADLAIKSLNN QLVANNRITV
     DYAFKENGKG NAKYGDDVDR LLNKEALKHN MLK
 
 
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