UBC14_SCHPO
ID UBC14_SCHPO Reviewed; 155 AA.
AC Q9UTN8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 14 {ECO:0000250|UniProtKB:P15731, ECO:0000312|EMBL:CAB54826.1};
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 14;
DE AltName: Full=Ubiquitin carrier protein 14 {ECO:0000250|UniProtKB:P15731};
DE AltName: Full=Ubiquitin-protein ligase 14 {ECO:0000250|UniProtKB:P15731};
GN Name=ubc14; ORFNames=SPAC1250.03;
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).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Mediates the selective degradation of short-lived and
CC abnormal proteins. {ECO:0000250|UniProtKB:P15731, ECO:0000255|PROSITE-
CC 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:0000250|UniProtKB:P15731, ECO:0000255|PROSITE-
CC ProRule:PRU00388};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:P15731, 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; CU329670; CAB54826.1; -; Genomic_DNA.
DR PIR; T37559; T37559.
DR RefSeq; NP_594859.1; NM_001020288.2.
DR AlphaFoldDB; Q9UTN8; -.
DR SMR; Q9UTN8; -.
DR BioGRID; 278063; 15.
DR STRING; 4896.SPAC1250.03.1; -.
DR MaxQB; Q9UTN8; -.
DR PaxDb; Q9UTN8; -.
DR EnsemblFungi; SPAC1250.03.1; SPAC1250.03.1:pep; SPAC1250.03.
DR GeneID; 2541565; -.
DR KEGG; spo:SPAC1250.03; -.
DR PomBase; SPAC1250.03; ubc14.
DR VEuPathDB; FungiDB:SPAC1250.03; -.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; Q9UTN8; -.
DR OMA; HPNITND; -.
DR PhylomeDB; Q9UTN8; -.
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:Q9UTN8; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; ISS:PomBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:PomBase.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..155
FT /note="Ubiquitin-conjugating enzyme E2 14"
FT /id="PRO_0000361053"
FT DOMAIN 7..154
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 91
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P15731,
FT ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 155 AA; 17743 MW; 76E66013E5C2BE05 CRC64;
MASASPSSSR RLTKEYSDLR EHPIPDIRVN LVDDNLFHWA CTALGPSDSV YAGGKFHFSL
KFPLDYPFQP PTIEFTTRIY HPNFDSEGNV CLAILKQQVF KPSIKLRSVL EQILQLLREP
NPDDPLVASI AEQYRNDRPS FDKIARDYVE QFAKS