HEL2_SCHPO
ID HEL2_SCHPO Reviewed; 732 AA.
AC Q76PD2;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=E3 ubiquitin-protein ligase hel2 {ECO:0000250|UniProtKB:Q05580};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q05580};
DE AltName: Full=Histone E3 ligase 2 {ECO:0000250|UniProtKB:Q05580};
DE AltName: Full=RING-type E3 ubiquitin transferase hel2 {ECO:0000305};
GN ORFNames=SPCC1223.01, SPCC285.18;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Probable ubiquitin-protein ligase involved in the
CC degradation-related ubiquitination of histones. Contributes to the
CC post-translational regulation of histone protein levels by
CC polyubiquitination of excess histones for subsequent degradation.
CC {ECO:0000250|UniProtKB:Q05580}.
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=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q05580};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329672; CAA20857.2; -; Genomic_DNA.
DR RefSeq; NP_588346.2; NM_001023337.2.
DR AlphaFoldDB; Q76PD2; -.
DR BioGRID; 275651; 44.
DR STRING; 4896.SPCC1223.01.1; -.
DR iPTMnet; Q76PD2; -.
DR MaxQB; Q76PD2; -.
DR PaxDb; Q76PD2; -.
DR PRIDE; Q76PD2; -.
DR EnsemblFungi; SPCC1223.01.1; SPCC1223.01.1:pep; SPCC1223.01.
DR GeneID; 2539079; -.
DR KEGG; spo:SPCC1223.01; -.
DR PomBase; SPCC1223.01; -.
DR VEuPathDB; FungiDB:SPCC1223.01; -.
DR eggNOG; KOG2231; Eukaryota.
DR HOGENOM; CLU_008515_0_0_1; -.
DR InParanoid; Q76PD2; -.
DR OMA; RMKHERC; -.
DR PhylomeDB; Q76PD2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q76PD2; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; NAS:PomBase.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISO:PomBase.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR041888; RING-HC_ZNF598/Hel2.
DR InterPro; IPR044288; ZNF598/Hel2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22938; PTHR22938; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; LIM domain; Metal-binding; Phosphoprotein; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..732
FT /note="E3 ubiquitin-protein ligase hel2"
FT /id="PRO_0000353800"
FT DOMAIN 245..315
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT ZN_FING 81..121
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 732 AA; 82700 MW; 8E5C4B10CB19AF05 CRC64;
MSPSGPNLNN KEHNRASEKK NSRTHNKKTN RNQSKEKPVS SRSVETPKNA VCLEPVGTDP
VSNVATVDAS KEEQDEDEQI CFICAEGITY SCVLPCNHRM CHVCALRLRA LYKTKECTFC
KTEWDTVLIT KDHEIDIHDV DLAKLPFQDE KLGIVYSDEH AQEESNLLLQ FNCPEDACDI
TCKGWFDLKL HAKVKHHKFF CDLCVKNKKV FTHEHTLFSK KGLTKHNEVG DQGSDLEITG
FKGHPKCEFC NTHFYDDDEL FKHCREKHER CYICDQVAGR PTHQYFKNYD SLERHFEKDH
YICRERECLE RKFVVFGTEI DLKAHQLDEH PHNFTQRELR EARRIIPQFS YDPPGASGRN
RRERTSSTPS EQSTSVNETA NSLSNLHLSR GEIAHLRQEE YVREQQARHR DFGFTLSNPA
PTSARPATST RTISRGKTRT LRNEDFPSLA EVANQNSSSA PSVPVSAPRL SGKSASRNHV
PSPPKGTKSP MASSEQAQHQ QVIDRMQKLT NYDDHKINDF KFAVSSFRGN VMPAREAVAR
ITKLVAKPHE QLSGVFNQIA NLLENKEKSR ELLEAWQEWK ILNAKDDTRI GTTNSNLLRL
KRSNRTAAQT ASVWNRIERA AAHDGPSLSA PSSSINLANI TSRPTNSSAA NTPSWGVRKA
RASALNARSE EDFPALPPST SKRISVQLGK KQARPVDSWG STPNTSSNRN SNTMGVSKKK
NGKKQTVLFH IG
