HUL4_YEAST
ID HUL4_YEAST Reviewed; 892 AA.
AC P40985; D6VWK9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Probable E3 ubiquitin-protein ligase HUL4;
DE EC=2.3.2.26;
DE AltName: Full=HECT ubiquitin ligase 4;
DE AltName: Full=HECT-type E3 ubiquitin transferase HUL4;
GN Name=HUL4; OrderedLocusNames=YJR036C; ORFNames=J1608;
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 204508 / S288c;
RX PubMed=7668047; DOI=10.1002/yea.320110809;
RA Huang M.-E., Chuat J.-C., Galibert F.;
RT "Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA
RT genes and 14 new open reading frames including a gene most probably
RT belonging to the family of ubiquitin-protein ligases.";
RL Yeast 11:775-781(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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] OF 362-892.
RX PubMed=7957102;
RA van Gool A.J., Verhage R., Swagemakers S.M.A., van de Putte P., Brouwer J.,
RA Troelstra C., Bootsma D., Hoeijmakers J.H.J.;
RT "RAD26, the functional S. cerevisiae homolog of the Cockayne syndrome B
RT gene ERCC6.";
RL EMBO J. 13:5361-5369(1994).
RN [5]
RP GENE NAME, AND GENE DISRUPTION.
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 IDENTIFICATION IN THE TRF4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND FUNCTION OF THE TRF4 COMPLEX.
RX PubMed=15828860; DOI=10.1371/journal.pbio.0030189;
RA Vanacova S., Wolf J., Martin G., Blank D., Dettwiler S., Friedlein A.,
RA Langen H., Keith G., Keller W.;
RT "A new yeast poly(A) polymerase complex involved in RNA quality control.";
RL PLoS Biol. 3:986-997(2005).
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase, component of the TRAMP
CC (TRF4) complex which has a poly(A) RNA polymerase activity and is
CC involved in a post-transcriptional quality control mechanism limiting
CC inappropriate expression of genetic information. Polyadenylation is
CC required for the degradative activity of the exosome on several of its
CC nuclear RNA substrates. {ECO:0000269|PubMed:15828860}.
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;
CC -!- SUBUNIT: Component of the TRAMP complex (also called TRF4 complex)
CC composed of at least HUL4, MTR4, PAP2/TRF4 and either AIR1 or AIR2.
CC {ECO:0000269|PubMed:15828860}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the HUL4 family. {ECO:0000305}.
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DR EMBL; L36344; AAA88738.1; -; Genomic_DNA.
DR EMBL; Z49536; CAA89563.1; -; Genomic_DNA.
DR EMBL; X81635; CAA57291.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08825.1; -; Genomic_DNA.
DR PIR; S57055; S57055.
DR RefSeq; NP_012570.3; NM_001181694.3.
DR AlphaFoldDB; P40985; -.
DR SMR; P40985; -.
DR BioGRID; 33789; 53.
DR ComplexPortal; CPX-1678; TRAMP complex variant 4-1.
DR ComplexPortal; CPX-1679; TRAMP complex variant 4-2.
DR IntAct; P40985; 1.
DR MINT; P40985; -.
DR STRING; 4932.YJR036C; -.
DR PaxDb; P40985; -.
DR PRIDE; P40985; -.
DR EnsemblFungi; YJR036C_mRNA; YJR036C; YJR036C.
DR GeneID; 853494; -.
DR KEGG; sce:YJR036C; -.
DR SGD; S000003797; HUL4.
DR VEuPathDB; FungiDB:YJR036C; -.
DR eggNOG; KOG0941; Eukaryota.
DR GeneTree; ENSGT00940000163989; -.
DR HOGENOM; CLU_002173_5_1_1; -.
DR InParanoid; P40985; -.
DR OMA; YGNDWHI; -.
DR BioCyc; YEAST:G3O-31673-MON; -.
DR PRO; PR:P40985; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40985; protein.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0031499; C:TRAMP complex; IDA:SGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:SGD.
DR GO; GO:0016567; P:protein ubiquitination; ISS:SGD.
DR GO; GO:0000292; P:RNA fragment catabolic process; IC:ComplexPortal.
DR CDD; cd00078; HECTc; 1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
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 Nucleus; Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..892
FT /note="Probable E3 ubiquitin-protein ligase HUL4"
FT /id="PRO_0000084094"
FT DOMAIN 792..892
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 31..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 860
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT CONFLICT 362
FT /note="H -> Q (in Ref. 4; CAA57291)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="T -> M (in Ref. 4; CAA57291)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="T -> I (in Ref. 4; CAA57291)"
FT /evidence="ECO:0000305"
FT CONFLICT 514..519
FT /note="GKSVDV -> RQIRRR (in Ref. 4; CAA57291)"
FT /evidence="ECO:0000305"
FT CONFLICT 589..607
FT /note="ESSRSWFAIDPPNFDKSKG -> KKAHVHGLPLTLQILTNQR (in Ref.
FT 4; CAA57291)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="V -> A (in Ref. 4; CAA57291)"
FT /evidence="ECO:0000305"
FT CONFLICT 723..724
FT /note="KH -> ND (in Ref. 4; CAA57291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 892 AA; 103457 MW; 35EF9A8DDA92BD84 CRC64;
MVSLFDKLNA KKDGRDGSVS KELLSHSVAH TKNRLPKSGR RTSERSLAAS VKDGSCSNSK
SNKRNSSASV SGEEDKSCLI SLNCLCCGVP LRFPASITKF RCSACQVTVI VKEPEINSNL
ESSTHISCTL EGLQMVVRRC HDDLQRLKKT GILDKERKGL IFQPVITYLL DRFHDVSILN
RSFLVHDGGK NIKMLNYEVL QRFYSILSNL PTRKPYYSML CCCNDLLKRI TINKGENLQI
LQYRWLLIIL NIPTIRTCLI RDRKSKNVFE TQQIRAVSYE LAKRCIGYLS NLSTKTSQQL
IQSLRRTPTD NFSYQVEILN LYINFQFSRL LSNELSNRTA KNNVKPEDEM RSRLRRHHTT
GHEFLSTRPI SAQSNDKQGS GFTHPVNNKM KFKFFQYEED WHIHSAAKLT FIYYVANTRR
NGRGALSIQS FYNITLDFID YKQDFDHWRG VAQKTKMNQL IEEWGNSTTK KCFSFCKYPF
ILSLGIKISI MEYEIRRIME HEAEQAFLIS LDKGKSVDVY FKIKVRRDVI SHDSLRCIKE
HQGDLLKSLR IEFVNEPGID AGGLRKEWFF LLTKSLFNPM NGLFIYIKES SRSWFAIDPP
NFDKSKGKNS QLELYYLFGV VMGLAIFNST ILDLQFPKAL YKKLCSEPLS FEDYSELFPE
TSRNLIKMLN YTEDNFEDVF SLTFETTYRN NNWILNDSKS SKEYVTVELC ENGRNVPITQ
SNKHEFVMKW VEFYLEKSIE PQYNKFVSGF KRVFAECNSI KLFNSEELER LVCGDEEQTK
FDFKSLRSVT KYVGGFSDDS RAVCWFWEII ESWDYPLQKK LLQFVTASDR IPATGISTIP
FKISLLGSHD SDDLPLAHTC FNEICLWNYS SKKKLELKLL WAINESEGYG FR
