ID   UBE2Z_XENTR             Reviewed;         313 AA.
AC   Q66KB0;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 Z;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme Z;
DE   AltName: Full=Ubiquitin carrier protein Z;
DE   AltName: Full=Ubiquitin-protein ligase Z;
GN   Name=ube2z;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. May be involved in apoptosis regulation.
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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H832}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9H832}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH80480.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC080480; AAH80480.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001007969.2; NM_001007968.2.
DR   AlphaFoldDB; Q66KB0; -.
DR   SMR; Q66KB0; -.
DR   STRING; 8364.ENSXETP00000050856; -.
DR   PaxDb; 8364-ENSXETP00000049362; -.
DR   DNASU; 493338; -.
DR   Ensembl; ENSXETT00000112553; ENSXETP00000108780; ENSXETG00000043685.
DR   Ensembl; ENSXETT00000117564; ENSXETP00000105723; ENSXETG00000043685.
DR   GeneID; 493338; -.
DR   KEGG; xtr:493338; -.
DR   AGR; Xenbase:XB-GENE-990986; -.
DR   CTD; 65264; -.
DR   Xenbase; XB-GENE-990986; ube2z.
DR   eggNOG; KOG0895; Eukaryota.
DR   InParanoid; Q66KB0; -.
DR   OMA; CFDYHSL; -.
DR   OrthoDB; 5311053at2759; -.
DR   Reactome; R-XTR-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008143; Chromosome 10.
DR   Bgee; ENSXETG00000022817; Expressed in egg cell and 14 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR46116; (E3-INDEPENDENT) E2 UBIQUITIN-CONJUGATING ENZYME; 1.
DR   PANTHER; PTHR46116:SF26; UBIQUITIN-CONJUGATING ENZYME E2 Z; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..313
FT                   /note="Ubiquitin-conjugating enzyme E2 Z"
FT                   /id="PRO_0000280520"
FT   DOMAIN          58..212
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          283..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        147
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ   SEQUENCE   313 AA;  35077 MW;  DB57158992D65819 CRC64;
     MAESPAAEAI ILPGAAAGGG VLPHLSGLQA PGTSPLTTSS VWDPTASADW DNERASNQCV
     LRIKRDIMSI YKEPPPGMFV VPDPHDMTKI HALITGPFDT PYEGGFFLFL FRCPPDYPIH
     PPRVKLMTTG NNTVRFNPNF YRNGKVCLSI LGTWTGPAWS PAQSLSSVLI SIQSLMTENP
     YHNEPGFEQE RHSGDSKNYN ECIRHETIRV AVCEMLEGKC QCPDALRSVM EKSFMEYYDF
     YEAVCKDRFH LQGQNMQDPF GEKRGHFDYQ SLLSRLQTIH QRVREKHRKE TVDIDSDSSS
     SETETDTQGS SNP
//