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Ubiquitin-conjugating enzyme E2 Z (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme Z) (Uba6-specific E2 conjugating enzyme 1) (Use1) (Ubiquitin carrier protein Z) (Ubiquitin-protein ligase Z)

 UBE2Z_HUMAN             Reviewed;         354 AA.
Q9H832; A6N8M6; A6NC60; Q7L354; Q8TCM4; Q9H893;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 2.
27-SEP-2017, entry version 144.
RecName: Full=Ubiquitin-conjugating enzyme E2 Z;
EC=2.3.2.23;
AltName: Full=E2 ubiquitin-conjugating enzyme Z;
AltName: Full=Uba6-specific E2 conjugating enzyme 1;
Short=Use1;
AltName: Full=Ubiquitin carrier protein Z;
AltName: Full=Ubiquitin-protein ligase Z;
Name=UBE2Z; ORFNames=HOYS7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=17597759; DOI=10.1038/nature05902;
Jin J., Li X., Gygi S.P., Harper J.W.;
"Dual E1 activation systems for ubiquitin differentially regulate E2
enzyme charging.";
Nature 447:1135-1138(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Retinoblastoma, and Thyroid;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 109-354.
Ikeda A., Turitani K.;
"Molecular cloning of an osteocyte derived gene.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-354.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 238-354.
TISSUE=Brain, and Pancreas;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17160626; DOI=10.1007/s11033-006-9033-7;
Gu X., Zhao F., Zheng M., Fei X., Chen X., Huang S., Xie Y., Mao Y.;
"Cloning and characterization of a gene encoding the human putative
ubiquitin conjugating enzyme E2Z (UBE2Z).";
Mol. Biol. Rep. 34:183-188(2007).
[10]
FUNCTION.
PubMed=17464193;
Park K.M., Kang E., Jeon Y.-J., Kim N., Kim N.-S., Yoo H.-S.,
Yeom Y.I., Kim S.J.;
"Identification of novel regulators of apoptosis using a high-
throughput cell-based screen.";
Mol. Cells 23:170-174(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
proteins (By similarity). Specific substrate for UBA6, not charged
with ubiquitin by UBE1. May be involved in apoptosis regulation.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000269|PubMed:17464193, ECO:0000269|PubMed:17597759}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- INTERACTION:
Q96MA6:AK8; NbExp=3; IntAct=EBI-720977, EBI-8466265;
Q6NT76:HMBOX1; NbExp=3; IntAct=EBI-720977, EBI-2549423;
Q9H8W4:PLEKHF2; NbExp=3; IntAct=EBI-720977, EBI-742388;
Q04864:REL; NbExp=3; IntAct=EBI-720977, EBI-307352;
O15205:UBD; NbExp=2; IntAct=EBI-720977, EBI-6657186;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17160626}.
Nucleus {ECO:0000269|PubMed:17160626}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H832-1; Sequence=Displayed;
Name=2;
IsoId=Q9H832-2; Sequence=VSP_023747;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Highly in placenta,
pancreas, spleen and testis. {ECO:0000269|PubMed:17160626,
ECO:0000269|PubMed:17597759}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SEQUENCE CAUTION:
Sequence=AAH15890.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB14724.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; EF623992; ABR25252.1; -; mRNA.
EMBL; AK023917; BAB14724.1; ALT_INIT; mRNA.
EMBL; AK024030; BAB14789.1; -; mRNA.
EMBL; AC091133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94703.1; -; Genomic_DNA.
EMBL; BC015169; AAH15169.2; -; mRNA.
EMBL; BC015890; AAH15890.1; ALT_INIT; mRNA.
EMBL; AB025426; BAB87810.1; -; mRNA.
EMBL; CR457322; CAG33603.1; -; mRNA.
EMBL; AL713782; CAD28542.1; -; mRNA.
CCDS; CCDS11540.2; -. [Q9H832-1]
RefSeq; NP_075567.2; NM_023079.4. [Q9H832-1]
UniGene; Hs.514297; -.
PDB; 5A4P; X-ray; 2.10 A; A=1-354.
PDBsum; 5A4P; -.
DisProt; DP00953; -.
ProteinModelPortal; Q9H832; -.
SMR; Q9H832; -.
BioGrid; 122419; 35.
IntAct; Q9H832; 38.
MINT; MINT-1388629; -.
STRING; 9606.ENSP00000354201; -.
iPTMnet; Q9H832; -.
PhosphoSitePlus; Q9H832; -.
BioMuta; UBE2Z; -.
DMDM; 134035344; -.
EPD; Q9H832; -.
MaxQB; Q9H832; -.
PaxDb; Q9H832; -.
PeptideAtlas; Q9H832; -.
PRIDE; Q9H832; -.
DNASU; 65264; -.
Ensembl; ENST00000360943; ENSP00000354201; ENSG00000159202. [Q9H832-1]
GeneID; 65264; -.
KEGG; hsa:65264; -.
UCSC; uc002ioi.4; human. [Q9H832-1]
CTD; 65264; -.
DisGeNET; 65264; -.
EuPathDB; HostDB:ENSG00000159202.17; -.
GeneCards; UBE2Z; -.
HGNC; HGNC:25847; UBE2Z.
HPA; HPA007922; -.
MIM; 611362; gene.
neXtProt; NX_Q9H832; -.
OpenTargets; ENSG00000159202; -.
PharmGKB; PA142670659; -.
eggNOG; ENOG410ITJE; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00730000110680; -.
HOGENOM; HOG000233451; -.
HOVERGEN; HBG083204; -.
InParanoid; Q9H832; -.
KO; K10585; -.
OMA; YYDFYEG; -.
OrthoDB; EOG091G0K0Y; -.
PhylomeDB; Q9H832; -.
TreeFam; TF354204; -.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q9H832; -.
UniPathway; UPA00143; -.
ChiTaRS; UBE2Z; human.
GenomeRNAi; 65264; -.
PRO; PR:Q9H832; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000159202; -.
CleanEx; HS_UBE2Z; -.
ExpressionAtlas; Q9H832; baseline and differential.
Genevisible; Q9H832; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:Ensembl.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IEA:Ensembl.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; ATP-binding;
Complete proteome; Cytoplasm; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Transferase;
Ubl conjugation pathway.
CHAIN 1 354 Ubiquitin-conjugating enzyme E2 Z.
/FTId=PRO_0000280515.
ACT_SITE 188 188 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UE37}.
VAR_SEQ 1 108 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_023747.
HELIX 102 113 {ECO:0000244|PDB:5A4P}.
STRAND 119 123 {ECO:0000244|PDB:5A4P}.
STRAND 130 136 {ECO:0000244|PDB:5A4P}.
TURN 142 145 {ECO:0000244|PDB:5A4P}.
STRAND 147 153 {ECO:0000244|PDB:5A4P}.
TURN 156 159 {ECO:0000244|PDB:5A4P}.
STRAND 164 167 {ECO:0000244|PDB:5A4P}.
TURN 171 174 {ECO:0000244|PDB:5A4P}.
STRAND 185 187 {ECO:0000244|PDB:5A4P}.
HELIX 190 192 {ECO:0000244|PDB:5A4P}.
STRAND 194 198 {ECO:0000244|PDB:5A4P}.
HELIX 206 216 {ECO:0000244|PDB:5A4P}.
HELIX 221 224 {ECO:0000244|PDB:5A4P}.
TURN 226 229 {ECO:0000244|PDB:5A4P}.
HELIX 236 251 {ECO:0000244|PDB:5A4P}.
HELIX 254 257 {ECO:0000244|PDB:5A4P}.
HELIX 265 277 {ECO:0000244|PDB:5A4P}.
HELIX 279 287 {ECO:0000244|PDB:5A4P}.
HELIX 288 292 {ECO:0000244|PDB:5A4P}.
HELIX 310 325 {ECO:0000244|PDB:5A4P}.
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


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E1063r ELISA kit HR6B,RAD6 homolog B,Rad6b,Rat,Rattus norvegicus,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T


 

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