UBE2Z_HUMAN
ID UBE2Z_HUMAN Reviewed; 354 AA.
AC Q9H832; A6N8M6; A6NC60; Q7L354; Q8TCM4; Q9H893;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 173.
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; ORFNames=HOYS7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17597759; DOI=10.1038/nature05902;
RA Jin J., Li X., Gygi S.P., Harper J.W.;
RT "Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme
RT charging.";
RL Nature 447:1135-1138(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Retinoblastoma, and Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-354.
RA Ikeda A., Turitani K.;
RT "Molecular cloning of an osteocyte derived gene.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-354.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 238-354.
RC TISSUE=Brain, and Pancreas;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17160626; DOI=10.1007/s11033-006-9033-7;
RA Gu X., Zhao F., Zheng M., Fei X., Chen X., Huang S., Xie Y., Mao Y.;
RT "Cloning and characterization of a gene encoding the human putative
RT ubiquitin conjugating enzyme E2Z (UBE2Z).";
RL Mol. Biol. Rep. 34:183-188(2007).
RN [10]
RP FUNCTION.
RX PubMed=17464193;
RA Park K.M., Kang E., Jeon Y.-J., Kim N., Kim N.-S., Yoo H.-S., Yeom Y.I.,
RA Kim S.J.;
RT "Identification of novel regulators of apoptosis using a high-throughput
RT cell-based screen.";
RL Mol. Cells 23:170-174(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins (By similarity). Specific substrate for UBA6, not charged with
CC ubiquitin by UBE1. May be involved in apoptosis regulation.
CC {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:17464193,
CC ECO:0000269|PubMed:17597759}.
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 -!- INTERACTION:
CC Q9H832; Q96MA6: AK8; NbExp=3; IntAct=EBI-720977, EBI-8466265;
CC Q9H832; P49368: CCT3; NbExp=3; IntAct=EBI-720977, EBI-356673;
CC Q9H832; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-720977, EBI-739467;
CC Q9H832; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-720977, EBI-2549423;
CC Q9H832; Q0VD86: INCA1; NbExp=3; IntAct=EBI-720977, EBI-6509505;
CC Q9H832; Q9Y2H5: PLEKHA6; NbExp=3; IntAct=EBI-720977, EBI-1171228;
CC Q9H832; Q9H8W4: PLEKHF2; NbExp=9; IntAct=EBI-720977, EBI-742388;
CC Q9H832; Q04864: REL; NbExp=3; IntAct=EBI-720977, EBI-307352;
CC Q9H832; O75382: TRIM3; NbExp=3; IntAct=EBI-720977, EBI-2129889;
CC Q9H832; O15205: UBD; NbExp=2; IntAct=EBI-720977, EBI-6657186;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17160626}. Nucleus
CC {ECO:0000269|PubMed:17160626}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H832-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H832-2; Sequence=VSP_023747;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly in placenta, pancreas,
CC spleen and testis. {ECO:0000269|PubMed:17160626,
CC ECO:0000269|PubMed:17597759}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15890.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14724.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EF623992; ABR25252.1; -; mRNA.
DR EMBL; AK023917; BAB14724.1; ALT_INIT; mRNA.
DR EMBL; AK024030; BAB14789.1; -; mRNA.
DR EMBL; AC091133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94703.1; -; Genomic_DNA.
DR EMBL; BC015169; AAH15169.2; -; mRNA.
DR EMBL; BC015890; AAH15890.1; ALT_INIT; mRNA.
DR EMBL; AB025426; BAB87810.1; -; mRNA.
DR EMBL; CR457322; CAG33603.1; -; mRNA.
DR EMBL; AL713782; CAD28542.1; -; mRNA.
DR CCDS; CCDS11540.2; -. [Q9H832-1]
DR RefSeq; NP_075567.2; NM_023079.4. [Q9H832-1]
DR PDB; 5A4P; X-ray; 2.10 A; A=1-354.
DR PDBsum; 5A4P; -.
DR AlphaFoldDB; Q9H832; -.
DR SMR; Q9H832; -.
DR BioGRID; 122419; 72.
DR IntAct; Q9H832; 40.
DR MINT; Q9H832; -.
DR STRING; 9606.ENSP00000354201; -.
DR GlyGen; Q9H832; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H832; -.
DR PhosphoSitePlus; Q9H832; -.
DR BioMuta; UBE2Z; -.
DR DMDM; 134035344; -.
DR EPD; Q9H832; -.
DR jPOST; Q9H832; -.
DR MassIVE; Q9H832; -.
DR MaxQB; Q9H832; -.
DR PaxDb; Q9H832; -.
DR PeptideAtlas; Q9H832; -.
DR PRIDE; Q9H832; -.
DR ProteomicsDB; 81173; -. [Q9H832-1]
DR ProteomicsDB; 81174; -. [Q9H832-2]
DR Antibodypedia; 2025; 205 antibodies from 29 providers.
DR DNASU; 65264; -.
DR Ensembl; ENST00000360943.10; ENSP00000354201.5; ENSG00000159202.18. [Q9H832-1]
DR GeneID; 65264; -.
DR KEGG; hsa:65264; -.
DR MANE-Select; ENST00000360943.10; ENSP00000354201.5; NM_023079.5; NP_075567.2.
DR UCSC; uc002ioi.4; human. [Q9H832-1]
DR CTD; 65264; -.
DR DisGeNET; 65264; -.
DR GeneCards; UBE2Z; -.
DR HGNC; HGNC:25847; UBE2Z.
DR HPA; ENSG00000159202; Low tissue specificity.
DR MIM; 611362; gene.
DR neXtProt; NX_Q9H832; -.
DR OpenTargets; ENSG00000159202; -.
DR PharmGKB; PA142670659; -.
DR VEuPathDB; HostDB:ENSG00000159202; -.
DR eggNOG; KOG0895; Eukaryota.
DR GeneTree; ENSGT00940000159091; -.
DR HOGENOM; CLU_025097_2_0_1; -.
DR InParanoid; Q9H832; -.
DR OMA; ACPEALW; -.
DR OrthoDB; 1404665at2759; -.
DR PhylomeDB; Q9H832; -.
DR TreeFam; TF354204; -.
DR BRENDA; 2.3.2.23; 2681.
DR PathwayCommons; Q9H832; -.
DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9H832; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 65264; 85 hits in 1082 CRISPR screens.
DR ChiTaRS; UBE2Z; human.
DR GenomeRNAi; 65264; -.
DR Pharos; Q9H832; Tbio.
DR PRO; PR:Q9H832; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9H832; protein.
DR Bgee; ENSG00000159202; Expressed in islet of Langerhans and 203 other tissues.
DR ExpressionAtlas; Q9H832; baseline and differential.
DR Genevisible; Q9H832; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR CDD; cd00195; UBCc; 1.
DR DisProt; DP00953; -.
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 3D-structure; Alternative splicing; Apoptosis; ATP-binding; Cytoplasm;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..354
FT /note="Ubiquitin-conjugating enzyme E2 Z"
FT /id="PRO_0000280515"
FT DOMAIN 99..253
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UE37"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023747"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:5A4P"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:5A4P"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:5A4P"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:5A4P"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:5A4P"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:5A4P"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:5A4P"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:5A4P"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5A4P"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:5A4P"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:5A4P"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:5A4P"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:5A4P"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:5A4P"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:5A4P"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:5A4P"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:5A4P"
FT HELIX 279..287
FT /evidence="ECO:0007829|PDB:5A4P"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:5A4P"
FT HELIX 310..325
FT /evidence="ECO:0007829|PDB:5A4P"
SQ SEQUENCE 354 AA; 38210 MW; 5AFC148BD8D31356 CRC64;
MAESPTEEAA TAGAGAAGPG ASSVAGVVGV SGSGGGFGPP FLPDVWAAAA AAGGAGGPGS
GLAPLPGLPP SAAAHGAALL SHWDPTLSSD WDGERTAPQC LLRIKRDIMS IYKEPPPGMF
VVPDTVDMTK IHALITGPFD TPYEGGFFLF VFRCPPDYPI HPPRVKLMTT GNNTVRFNPN
FYRNGKVCLS ILGTWTGPAW SPAQSISSVL ISIQSLMTEN PYHNEPGFEQ ERHPGDSKNY
NECIRHETIR VAVCDMMEGK CPCPEPLRGV MEKSFLEYYD FYEVACKDRL HLQGQTMQDP
FGEKRGHFDY QSLLMRLGLI RQKVLERLHN ENAEMDSDSS SSGTETDLHG SLRV
