UBC4_SCHPO
ID UBC4_SCHPO Reviewed; 147 AA.
AC P46595;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 4;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 4;
DE AltName: Full=Ubiquitin carrier protein 4;
DE AltName: Full=Ubiquitin-protein ligase 4;
GN Name=ubc4; ORFNames=SPBC119.02;
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 [MRNA].
RX PubMed=7698660; DOI=10.1016/0378-1119(94)00926-j;
RA Damagnez V., Rolfe M., Cottarel G.;
RT "Schizosaccharomyces pombe and Candida albicans cDNA homologues of the
RT Saccharomyces cerevisiae UBC4 gene.";
RL Gene 155:137-138(1995).
RN [2]
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).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Mediates the selective degradation of short-lived and
CC abnormal proteins. Mediates ubiquitination of PEX5.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; L37384; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CU329671; CAA17917.1; -; Genomic_DNA.
DR PIR; T39300; T39300.
DR RefSeq; NP_595283.1; NM_001021190.2.
DR PDB; 4II2; X-ray; 2.20 A; C=1-147.
DR PDBsum; 4II2; -.
DR AlphaFoldDB; P46595; -.
DR SMR; P46595; -.
DR BioGRID; 276621; 19.
DR IntAct; P46595; 1.
DR STRING; 4896.SPBC119.02.1; -.
DR iPTMnet; P46595; -.
DR MaxQB; P46595; -.
DR PaxDb; P46595; -.
DR PRIDE; P46595; -.
DR EnsemblFungi; SPBC119.02.1; SPBC119.02.1:pep; SPBC119.02.
DR GeneID; 2540083; -.
DR KEGG; spo:SPBC119.02; -.
DR PomBase; SPBC119.02; ubc4.
DR VEuPathDB; FungiDB:SPBC119.02; -.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; P46595; -.
DR OMA; VHFTTRI; -.
DR PhylomeDB; P46595; -.
DR Reactome; R-SPO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-SPO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-SPO-9033241; Peroxisomal protein import.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P46595; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:PomBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:PomBase.
DR GO; GO:0032933; P:SREBP signaling pathway; IMP:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..147
FT /note="Ubiquitin-conjugating enzyme E2 4"
FT /id="PRO_0000082569"
FT DOMAIN 1..147
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT HELIX 2..14
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 58..62
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 131..145
FT /evidence="ECO:0007829|PDB:4II2"
SQ SEQUENCE 147 AA; 16476 MW; 3E8BADFF494A91EB CRC64;
MALKRINREL ADLGKDPPSS CSAGPVGDDL FHWQATIMGP ADSPYAGGVF FLSIHFPTDY
PFKPPKVNFT TRIYHPNINS NGSICLDILR DQWSPALTIS KVLLSICSLL TDPNPDDPLV
PEIAHVYKTD RSRYELSARE WTRKYAI
