UBE2Z_MOUSE
ID UBE2Z_MOUSE Reviewed; 356 AA.
AC Q3UE37; A2A6M3; Q3TFZ8; Q3U618; Q7TMY6; Q8BVL2; Q9DAU4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
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; Synonyms=D11Moh35;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, Placenta, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-356.
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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=AAH54412.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB24097.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC37014.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK005524; BAB24097.1; ALT_INIT; mRNA.
DR EMBL; AK077793; BAC37014.1; ALT_FRAME; mRNA.
DR EMBL; AK149770; BAE29074.1; -; mRNA.
DR EMBL; AK153328; BAE31907.1; -; mRNA.
DR EMBL; AK168942; BAE40750.1; -; mRNA.
DR EMBL; AL603682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054412; AAH54412.1; ALT_INIT; mRNA.
DR CCDS; CCDS36289.1; -.
DR RefSeq; NP_758504.3; NM_172300.3.
DR AlphaFoldDB; Q3UE37; -.
DR SMR; Q3UE37; -.
DR BioGRID; 234504; 5.
DR IntAct; Q3UE37; 1.
DR MINT; Q3UE37; -.
DR STRING; 10090.ENSMUSP00000098097; -.
DR iPTMnet; Q3UE37; -.
DR PhosphoSitePlus; Q3UE37; -.
DR EPD; Q3UE37; -.
DR MaxQB; Q3UE37; -.
DR PaxDb; Q3UE37; -.
DR PeptideAtlas; Q3UE37; -.
DR PRIDE; Q3UE37; -.
DR ProteomicsDB; 298405; -.
DR Antibodypedia; 2025; 205 antibodies from 29 providers.
DR DNASU; 268470; -.
DR Ensembl; ENSMUST00000100528; ENSMUSP00000098097; ENSMUSG00000014349.
DR GeneID; 268470; -.
DR KEGG; mmu:268470; -.
DR UCSC; uc007lbd.2; mouse.
DR CTD; 65264; -.
DR MGI; MGI:1343160; Ube2z.
DR VEuPathDB; HostDB:ENSMUSG00000014349; -.
DR eggNOG; KOG0895; Eukaryota.
DR GeneTree; ENSGT00940000159091; -.
DR HOGENOM; CLU_025097_2_0_1; -.
DR InParanoid; Q3UE37; -.
DR OMA; ACPEALW; -.
DR OrthoDB; 1404665at2759; -.
DR PhylomeDB; Q3UE37; -.
DR TreeFam; TF354204; -.
DR Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 268470; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Ube2z; mouse.
DR PRO; PR:Q3UE37; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3UE37; protein.
DR Bgee; ENSMUSG00000014349; Expressed in placenta labyrinth and 260 other tissues.
DR Genevisible; Q3UE37; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:0061631; F:ubiquitin conjugating enzyme activity; IMP:MGI.
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:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IGI:MGI.
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 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_0000280516"
FT DOMAIN 101..255
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..23
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:0007744|PubMed:21183079"
FT CONFLICT 7
FT /note="E -> D (in Ref. 1; BAC37014)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="A -> S (in Ref. 1; BAC37014)"
FT /evidence="ECO:0000305"
FT CONFLICT 16..17
FT /note="AG -> SW (in Ref. 1; BAC37014)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="P -> H (in Ref. 1; BAC37014)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="P -> R (in Ref. 1; BAC37014)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="D -> E (in Ref. 1; BAC37014)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="E -> G (in Ref. 1; BAE29074)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 38368 MW; 15FB00E9988B0A6D CRC64;
MAESPTEEAA TATAGAGAAG PGSSGVAGVV 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
