Entry euk: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   10-MAY-2017, entry version 116.
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;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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,
CC       ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
CC       enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
CC       = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
CC       ubiquitin-conjugating enzyme]-L-cysteine.
CC       {ECO:0000250|UniProtKB:P15731, ECO:0000255|PROSITE-
CC       ProRule:PRU00388}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:P15731, ECO:0000255|PROSITE-
CC       ProRule:PRU00388}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CU329670; CAB54826.1; -; Genomic_DNA.
DR   PIR; T37559; T37559.
DR   RefSeq; NP_594859.1; NM_001020288.2.
DR   ProteinModelPortal; Q9UTN8; -.
DR   SMR; Q9UTN8; -.
DR   BioGrid; 278063; 13.
DR   MaxQB; Q9UTN8; -.
DR   PRIDE; Q9UTN8; -.
DR   EnsemblFungi; SPAC1250.03.1; SPAC1250.03.1:pep; SPAC1250.03.
DR   GeneID; 2541565; -.
DR   KEGG; spo:SPAC1250.03; -.
DR   EuPathDB; FungiDB:SPAC1250.03; -.
DR   PomBase; SPAC1250.03; ubc14.
DR   HOGENOM; HOG000233455; -.
DR   InParanoid; Q9UTN8; -.
DR   OMA; KTAREYT; -.
DR   OrthoDB; EOG092C50OL; -.
DR   PhylomeDB; Q9UTN8; -.
DR   Reactome; R-SPO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9UTN8; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO: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; UBIQUITIN_CONJUGAT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Nucleotide-binding;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN         1    155       Ubiquitin-conjugating enzyme E2 14.
FT                                /FTId=PRO_0000361053.
FT   ACT_SITE     91     91       Glycyl thioester intermediate.
FT                                {ECO:0000250|UniProtKB:P15731,
FT                                ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        10    143       iprf:UBIQUITIN_CONJUGAT_2 [T]
FT   MYHIT        11    148       ipfam:UQ_con [T]
SQ   SEQUENCE   155 AA;  17743 MW;  76E66013E5C2BE05 CRC64;
     MASASPSSSR RLTKEYSDLR EHPIPDIRVN LVDDNLFHWA CTALGPSDSV YAGGKFHFSL
     KFPLDYPFQP PTIEFTTRIY HPNFDSEGNV CLAILKQQVF KPSIKLRSVL EQILQLLREP
     NPDDPLVASI AEQYRNDRPS FDKIARDYVE QFAKS
//