HUL5_YEAST
ID HUL5_YEAST Reviewed; 910 AA.
AC P53119; D6VU08;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=E3 ubiquitin-protein ligase HUL5 {ECO:0000305};
DE EC=2.3.2.26 {ECO:0000269|PubMed:17190603, ECO:0000269|PubMed:21983566};
GN Name=HUL5 {ECO:0000303|PubMed:9858558, ECO:0000312|SGD:S000003109};
GN OrderedLocusNames=YGL141W {ECO:0000312|SGD:S000003109};
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=9046099;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<177::aid-yea62>3.0.co;2-2;
RA Voet M., Defoor E., Verhasselt P., Riles L., Robben J., Volckaert G.;
RT "The sequence of a nearly unclonable 22.8 kb segment on the left arm
RT chromosome VII from Saccharomyces cerevisiae reveals ARO2, RPL9A, TIP1,
RT MRF1 genes and six new open reading frames.";
RL Yeast 13:177-182(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 GENE NAME, AND DISRUPTION PHENOTYPE.
RX PubMed=9858558; DOI=10.1128/mcb.19.1.342;
RA Wang G., Yang J., Huibregtse J.M.;
RT "Functional domains of the rsp5 ubiquitin-protein ligase.";
RL Mol. Cell. Biol. 19:342-352(1999).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, ACTIVE SITE, AND MUTAGENESIS OF
RP CYS-878.
RX PubMed=17190603; DOI=10.1016/j.cell.2006.09.051;
RA Crosas B., Hanna J., Kirkpatrick D.S., Zhang D.P., Tone Y., Hathaway N.A.,
RA Buecker C., Leggett D.S., Schmidt M., King R.W., Gygi S.P., Finley D.;
RT "Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin
RT ligase and deubiquitinating activities.";
RL Cell 127:1401-1413(2006).
RN [9]
RP FUNCTION, INTERACTION WITH THE 19S PROTEASOME, ACTIVE SITE, AND MUTAGENESIS
RP OF CYS-878.
RX PubMed=20008553; DOI=10.1128/mcb.00909-09;
RA Aviram S., Kornitzer D.;
RT "The ubiquitin ligase Hul5 promotes proteasomal processivity.";
RL Mol. Cell. Biol. 30:985-994(2010).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PATHWAY, ACTIVE SITE,
RP AND MUTAGENESIS OF CYS-878.
RX PubMed=21983566; DOI=10.1038/ncb2343;
RA Fang N.N., Ng A.H., Measday V., Mayor T.;
RT "Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and
RT turnover of cytosolic misfolded proteins.";
RL Nat. Cell Biol. 13:1344-1352(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Non-essential E3 ubiquitin-protein ligase that specifically
CC catalyzes 'Lys-29'- and 'Lys-48'-linked polyubiquitin chains (By
CC similarity). Accepts ubiquitin from an E2 ubiquitin-conjugating enzyme
CC in the form of a thioester and then directly transfers the ubiquitin to
CC targeted substrates (By similarity). Associates with the proteasome and
CC promotes elongation of ubiquitin chains on substrates bound to the
CC proteasome (PubMed:17190603). Elongation of ubiquitin chains on
CC substrates bound to the proteasome promotes proteasomal processivity
CC (PubMed:20008553). Also promotes ubiquitin elongation of 26S proteasome
CC subunit RPN10 (PubMed:17190603). Involved in the stress response
CC required to maintain cell fitness following heat-shock: acts by
CC mediating ubiquitination of cytosolic misfolded proteins, leading to
CC their subsequent degradation (PubMed:21983566).
CC {ECO:0000250|UniProtKB:Q15386, ECO:0000269|PubMed:17190603,
CC ECO:0000269|PubMed:20008553, ECO:0000269|PubMed:21983566}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000269|PubMed:17190603,
CC ECO:0000269|PubMed:21983566};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:17190603, ECO:0000269|PubMed:21983566}.
CC -!- SUBUNIT: Interacts with 19S proteasomes. {ECO:0000269|PubMed:20008553}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21983566,
CC ECO:0000305|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:21983566}.
CC -!- DISRUPTION PHENOTYPE: Cells are viable. {ECO:0000269|PubMed:9858558}.
CC -!- MISCELLANEOUS: Present with 3120 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UBE3C family. {ECO:0000305}.
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DR EMBL; X99960; CAA68221.1; -; Genomic_DNA.
DR EMBL; Z72663; CAA96853.1; -; Genomic_DNA.
DR EMBL; AY723811; AAU09728.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07969.1; -; Genomic_DNA.
DR PIR; S64155; S64155.
DR RefSeq; NP_011374.1; NM_001181006.1.
DR AlphaFoldDB; P53119; -.
DR SMR; P53119; -.
DR BioGRID; 33111; 82.
DR DIP; DIP-6349N; -.
DR IntAct; P53119; 4.
DR MINT; P53119; -.
DR STRING; 4932.YGL141W; -.
DR iPTMnet; P53119; -.
DR MaxQB; P53119; -.
DR PaxDb; P53119; -.
DR PRIDE; P53119; -.
DR EnsemblFungi; YGL141W_mRNA; YGL141W; YGL141W.
DR GeneID; 852736; -.
DR KEGG; sce:YGL141W; -.
DR SGD; S000003109; HUL5.
DR VEuPathDB; FungiDB:YGL141W; -.
DR eggNOG; KOG0942; Eukaryota.
DR GeneTree; ENSGT00940000156321; -.
DR HOGENOM; CLU_002173_2_3_1; -.
DR InParanoid; P53119; -.
DR OMA; EMFNSVE; -.
DR BioCyc; YEAST:G3O-30636-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P53119; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53119; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IDA:SGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:SGD.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IDA:UniProtKB.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; IMP:SGD.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR CDD; cd00078; HECTc; 1.
DR InterPro; IPR044611; E3B/C.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR45700; PTHR45700; 2.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..910
FT /note="E3 ubiquitin-protein ligase HUL5"
FT /id="PRO_0000084095"
FT DOMAIN 810..910
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 878
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104,
FT ECO:0000305|PubMed:17190603, ECO:0000305|PubMed:20008553,
FT ECO:0000305|PubMed:21983566"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 878
FT /note="C->A: Abolishes E3 ubiquitin-protein ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:17190603,
FT ECO:0000269|PubMed:20008553, ECO:0000269|PubMed:21983566"
SQ SEQUENCE 910 AA; 105566 MW; 8DB832A48A81CD19 CRC64;
MLNFTGQTRR RNVNLGNRTR NSKKDLLEKA KRERERRAQD KLKEDASKTI QKSIRRHFSN
VRLFKNTFTS SQLVHMIPAY GGKLIYYISQ YDLQQLLKLS HNFLSSYPNS LGNRQLLSLL
KLYQDDALVA ETLSDLNMDC PTVDEFLDSL SVYLCRASFL SYSSASKLAD VIEAWEVMHS
SASISIFSIS IGSYEKRPFA LQFYCILAER NLLPQLINTN PILWDNMAKT YSHCSKGGQK
NIAKLLIPNF NNHIAPSVLR SDNDYVLKFY EKAFIDEVIA TTANYVSDED HVKNLMCYIA
SSPNQSCKNS VLITLLSNKD FVRRLSWEFF HTKFNASKTE AHPLFSVLAQ LIDMHLLIST
DRELLDYNSV IPIEELKKFT STLKDFTFRQ YWELPKSERN PMLKEAVPLL SKVYERDSRL
HFLSTENNPT YWENSEKQFL NLRFYEELQE YEDLYREHLE EESDEDMEKE IDLDKERPPL
KSLLLNKMKK RLKSSLRFRK LEILLELPFF IPFEERVDLF YMFIALDKKR LSLDDDHNLI
NMFTPWASTG MRKQSAIISR DNVLEDAFNA FNSIGERFKA SLDVTFINEF GEEAGIDGGG
ITKEFLTTVS DEGFKDPKHE LFRTNDRYEL YPSVVYDATK LKYIWFLGKV VGKCLYEHVL
IDVSFADFFL KKLLNYSNGF LSSFSDLGSY DSVLYNNLIK LLNMTTDEIK SLDLTFEIDE
PESSAKVVDL IPNGSKTYVT KDNVLLYVTK VTDYKLNKRC FKPVSAFHGG LSVIIAPHWM
EMFNSIELQM LISGERDNID LDDLKSNTEY GGYKEEDQTI VDFWEVLNEF KFEEKLNFLK
FVTSVPQAPL QGFKALDPKF GIRNAGTEKY RLPTASTCVN LLKLPDYRNK TILREKLLYA
INSGARFDLS
