ID   UBE2Z_RAT               Reviewed;         356 AA.
AC   Q3B7D1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   27-MAR-2024, entry version 123.
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=Uba6-specific E2 conjugating enzyme 1;
DE            Short=Use1;
DE   AltName: Full=Ubiquitin carrier protein Z;
DE   AltName: Full=Ubiquitin-protein ligase Z;
GN   Name=Ube2z;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Specific substrate for UBA6, not charged with ubiquitin by
CC       UBE1. May be involved in apoptosis regulation. {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: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=AAI07664.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC107663; AAI07664.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001032732.2; NM_001037643.2.
DR   AlphaFoldDB; Q3B7D1; -.
DR   SMR; Q3B7D1; -.
DR   STRING; 10116.ENSRNOP00000052365; -.
DR   iPTMnet; Q3B7D1; -.
DR   PhosphoSitePlus; Q3B7D1; -.
DR   jPOST; Q3B7D1; -.
DR   PaxDb; 10116-ENSRNOP00000052365; -.
DR   Ensembl; ENSRNOT00000055500.3; ENSRNOP00000052365.2; ENSRNOG00000006868.5.
DR   Ensembl; ENSRNOT00055056747; ENSRNOP00055046851; ENSRNOG00055032813.
DR   Ensembl; ENSRNOT00060044869; ENSRNOP00060037217; ENSRNOG00060025874.
DR   Ensembl; ENSRNOT00065030188; ENSRNOP00065023983; ENSRNOG00065017993.
DR   GeneID; 303478; -.
DR   KEGG; rno:303478; -.
DR   UCSC; RGD:1308347; rat.
DR   AGR; RGD:1308347; -.
DR   CTD; 65264; -.
DR   RGD; 1308347; Ube2z.
DR   eggNOG; KOG0895; Eukaryota.
DR   GeneTree; ENSGT00940000159091; -.
DR   HOGENOM; CLU_025097_2_0_1; -.
DR   InParanoid; Q3B7D1; -.
DR   OMA; CFDYHSL; -.
DR   OrthoDB; 5311053at2759; -.
DR   PhylomeDB; Q3B7D1; -.
DR   TreeFam; TF354204; -.
DR   Reactome; R-RNO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q3B7D1; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000006868; Expressed in jejunum and 19 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0060090; F:molecular adaptor activity; ISO:RGD.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:RGD.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:RGD.
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.
DR   Genevisible; Q3B7D1; RN.
PE   1: Evidence at protein level;
KW   Apoptosis; ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..356
FT                   /note="Ubiquitin-conjugating enzyme E2 Z"
FT                   /id="PRO_0000280517"
FT   DOMAIN          101..255
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        190
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UE37"
SQ   SEQUENCE   356 AA;  38352 MW;  3C77B50527A30676 CRC64;
     MAESPTEEAA TATAGAGAAG PGASGVAGVV GVSGSGGGFG PPFLPDVWAA AAAAGGAGGP
     GSGLAPLPGL PPSAAAHGAA LLSHWDPTLS SDWDGERTAP QCLLRIKRDI MSIYKEPPPG
     MFVVPDTVDM TKIHALITGP FDTPYEGGFF LFVFRCPPDY PIHPPRVKLM TTGNNTVRFN
     PNFYRNGKVC LSILGTWTGP AWSPAQSISS VLISIQSLMT ENPYHNEPGF EQERHPGDSK
     NYNECIRHET IRVAVCDMME GKCPCPEPLR GVMEKSFLEY YDFYEVACKD RLHLQGQTMQ
     DPFGEKRGHF DYQSLLMRLG LIRQKVLERL HNENAEMDSD SSSSGTETDL HGSLRV
//