位置:首页 > 蛋白库 > HUB1_YEAST
HUB1_YEAST
ID   HUB1_YEAST              Reviewed;          73 AA.
AC   Q6Q546; D6W1K7;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Ubiquitin-like modifier HUB1;
GN   Name=HUB1; OrderedLocusNames=YNR032C-A;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [2]
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   [3]
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   [4]
RP   FUNCTION.
RX   PubMed=11923536; DOI=10.1126/science.1069989;
RA   Dittmar G.A.G., Wilkinson C.R.M., Jedrzejewski P.T., Finley D.;
RT   "Role of a ubiquitin-like modification in polarized morphogenesis.";
RL   Science 295:2442-2446(2002).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [6]
RP   STRUCTURE BY NMR.
RX   PubMed=12943364; DOI=10.1023/a:1024674220425;
RA   Ramelot T.A., Cort J.R., Yee A.A., Semesi A., Edwards A.M.,
RA   Arrowsmith C.H., Kennedy M.A.;
RT   "Solution structure of the yeast ubiquitin-like modifier protein Hub1.";
RL   J. Struct. Funct. Genomics 4:25-30(2003).
CC   -!- FUNCTION: Forms conjugate with SPH1 and HBT1. Involved in
CC       morphogenesis. {ECO:0000269|PubMed:11923536}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z71648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY558559; AAS56885.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10573.1; -; Genomic_DNA.
DR   RefSeq; NP_014430.1; NM_001184344.1.
DR   PDB; 1M94; NMR; -; A=1-73.
DR   PDB; 3PLU; X-ray; 1.40 A; A/B=1-73.
DR   PDB; 3PLV; X-ray; 1.90 A; A=1-73.
DR   PDBsum; 1M94; -.
DR   PDBsum; 3PLU; -.
DR   PDBsum; 3PLV; -.
DR   AlphaFoldDB; Q6Q546; -.
DR   BMRB; Q6Q546; -.
DR   SMR; Q6Q546; -.
DR   BioGRID; 35857; 140.
DR   IntAct; Q6Q546; 1.
DR   STRING; 4932.YNR032C-A; -.
DR   MaxQB; Q6Q546; -.
DR   PaxDb; Q6Q546; -.
DR   PRIDE; Q6Q546; -.
DR   DNASU; 855767; -.
DR   EnsemblFungi; YNR032C-A_mRNA; YNR032C-A; YNR032C-A.
DR   GeneID; 855767; -.
DR   KEGG; sce:YNR032C-A; -.
DR   SGD; S000007251; HUB1.
DR   VEuPathDB; FungiDB:YNR032C-A; -.
DR   eggNOG; KOG3493; Eukaryota.
DR   GeneTree; ENSGT00390000001945; -.
DR   HOGENOM; CLU_156193_2_0_1; -.
DR   InParanoid; Q6Q546; -.
DR   OMA; HIKLEDY; -.
DR   BioCyc; YEAST:G3O-33397-MON; -.
DR   EvolutionaryTrace; Q6Q546; -.
DR   PRO; PR:Q6Q546; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; Q6Q546; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031386; F:protein tag; IDA:SGD.
DR   GO; GO:0000753; P:cell morphogenesis involved in conjugation with cellular fusion; IMP:SGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IPI:SGD.
DR   GO; GO:0033120; P:positive regulation of RNA splicing; IMP:SGD.
DR   GO; GO:0043687; P:post-translational protein modification; IDA:SGD.
DR   GO; GO:0036211; P:protein modification process; IBA:GO_Central.
DR   InterPro; IPR039732; Hub1/Ubl5.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR13042; PTHR13042; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..73
FT                   /note="Ubiquitin-like modifier HUB1"
FT                   /id="PRO_0000114879"
FT   DOMAIN          1..73
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CONFLICT        12
FT                   /note="K -> E (in Ref. 3; AAS56885)"
FT                   /evidence="ECO:0000305"
FT   STRAND          1..7
FT                   /evidence="ECO:0007829|PDB:3PLU"
FT   TURN            9..11
FT                   /evidence="ECO:0007829|PDB:1M94"
FT   STRAND          13..19
FT                   /evidence="ECO:0007829|PDB:3PLU"
FT   HELIX           24..35
FT                   /evidence="ECO:0007829|PDB:3PLU"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:3PLU"
FT   STRAND          42..46
FT                   /evidence="ECO:0007829|PDB:3PLU"
FT   HELIX           58..60
FT                   /evidence="ECO:0007829|PDB:3PLU"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:3PLU"
SQ   SEQUENCE   73 AA;  8272 MW;  2D5EFB83483F2ABA CRC64;
     MIEVVVNDRL GKKVRVKCLA EDSVGDFKKV LSLQIGTQPN KIVLQKGGSV LKDHISLEDY
     EVHDQTNLEL YYL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024