Q9H832 (UBE2Z_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 Z
EC=6.3.2.19

Alternative name(s):
Uba6-specific E2 conjugating enzyme 1
Short name=Use1
Ubiquitin carrier protein Z
Ubiquitin-protein ligase Z

Gene names

Name:	UBE2Z
ORF Names:	HOYS7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.10
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subcellular location	Cytoplasm. Nucleus Ref.9.
Tissue specificity	Widely expressed. Highly in placenta, pancreas, spleen and testis. Ref.1 Ref.9
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.
Sequence caution	The sequence AAH15890.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB14724.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H832-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9H832-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 354	354	Ubiquitin-conjugating enzyme E2 Z		PRO_0000280515
Sites
	Active site	188	1	Glycyl thioester intermediate By similarity
Amino acid modifications
	Modified residue	337	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 108	108	Missing in isoform 2.		VSP_023747

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 20, 2007. Version 2. Checksum: 5AFC148BD8D31356	FASTA	354	38,210
	10 20 30 40 50 60 MAESPTEEAA TAGAGAAGPG ASSVAGVVGV SGSGGGFGPP FLPDVWAAAA AAGGAGGPGS 70 80 90 100 110 120 GLAPLPGLPP SAAAHGAALL SHWDPTLSSD WDGERTAPQC LLRIKRDIMS IYKEPPPGMF 130 140 150 160 170 180 VVPDTVDMTK IHALITGPFD TPYEGGFFLF VFRCPPDYPI HPPRVKLMTT GNNTVRFNPN 190 200 210 220 230 240 FYRNGKVCLS ILGTWTGPAW SPAQSISSVL ISIQSLMTEN PYHNEPGFEQ ERHPGDSKNY 250 260 270 280 290 300 NECIRHETIR VAVCDMMEGK CPCPEPLRGV MEKSFLEYYD FYEVACKDRL HLQGQTMQDP 310 320 330 340 350 FGEKRGHFDY QSLLMRLGLI RQKVLERLHN ENAEMDSDSS SSGTETDLHG SLRV
	Isoform 2 [UniParc]. Checksum: A0AE68FB9430ACDB	FASTA	246	28,075
	10 20 30 40 50 60 MSIYKEPPPG MFVVPDTVDM TKIHALITGP FDTPYEGGFF LFVFRCPPDY PIHPPRVKLM 70 80 90 100 110 120 TTGNNTVRFN PNFYRNGKVC LSILGTWTGP AWSPAQSISS VLISIQSLMT ENPYHNEPGF 130 140 150 160 170 180 EQERHPGDSK NYNECIRHET IRVAVCDMME GKCPCPEPLR GVMEKSFLEY YDFYEVACKD 190 200 210 220 230 240 RLHLQGQTMQ DPFGEKRGHF DYQSLLMRLG LIRQKVLERL HNENAEMDSD SSSSGTETDL HGSLRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging." Jin J., Li X., Gygi S.P., Harper J.W. Nature 447:1135-1138(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Retinoblastoma and Thyroid.
[3]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." 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. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin.
[6]	"Molecular cloning of an osteocyte derived gene." Ikeda A., Turitani K. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 109-354.
[7]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-354.
[8]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 238-354. Tissue: Brain and Pancreas.
[9]	"Cloning and characterization of a gene encoding the human putative ubiquitin conjugating enzyme E2Z (UBE2Z)." Gu X., Zhao F., Zheng M., Fei X., Chen X., Huang S., Xie Y., Mao Y. Mol. Biol. Rep. 34:183-188(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[10]	"Identification of novel regulators of apoptosis using a high-throughput cell-based screen." Park K.M., Kang E., Jeon Y.-J., Kim N., Kim N.-S., Yoo H.-S., Yeom Y.I., Kim S.J. Mol. Cells 23:170-174(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	EF623992 mRNA. Translation: ABR25252.1. AK023917 mRNA. Translation: BAB14724.1. Different initiation. AK024030 mRNA. Translation: BAB14789.1. AC091133 Genomic DNA. No translation available. CH471109 Genomic DNA. Translation: EAW94703.1. BC015169 mRNA. Translation: AAH15169.2. BC015890 mRNA. Translation: AAH15890.1. Different initiation. AB025426 mRNA. Translation: BAB87810.1. CR457322 mRNA. Translation: CAG33603.1. AL713782 mRNA. Translation: CAD28542.1.
IPI	IPI00011996. IPI00829749.
RefSeq	NP_075567.2. NM_023079.4.
UniGene	Hs.514297.
3D structure databases
HSSP	HSSP built from PDB template 1PZV based on UniProtKB P34477.
ProteinModelPortal	Q9H832.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H832. 29 interactions.
MINT	MINT-1388629.
STRING	9606.ENSP00000354201.
PTM databases
PhosphoSite	Q9H832.
Polymorphism databases
DMDM	134035344.
Proteomic databases
PaxDb	Q9H832.
PRIDE	Q9H832.
Protocols and materials databases
DNASU	65264.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000360943; ENSP00000354201; ENSG00000159202.
GeneID	65264.
KEGG	hsa:65264.
UCSC	uc002ioi.3. human.
Organism-specific databases
CTD	65264.
GeneCards	GC17P046985.
HGNC	HGNC:25847. UBE2Z.
HPA	HPA007922.
MIM	611362. gene.
neXtProt	NX_Q9H832.
PharmGKB	PA142670659.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5078.
HOGENOM	HOG000233451.
HOVERGEN	HBG083204.
InParanoid	Q9H832.
KO	K10585.
OMA	AVMANMS.
OrthoDB	EOG4ZCT54.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q9H832.
Bgee	Q9H832.
CleanEx	HS_UBE2Z.
Genevestigator	Q9H832.
Family and domain databases
Gene3D	3.10.110.10. 1 hit.
InterPro	IPR000608. UBQ-conjugat_E2. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view]
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
SUPFAM	SSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. False negative. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	65264.
NextBio	67390.
SOURCE	Search...

Entry information

Entry name

UBE2Z_HUMAN

Accession

Primary (citable) accession number: Q9H832
Secondary accession number(s): A6N8M6 , A6NC60, Q7L354, Q8TCM4, Q9H893

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	March 20, 2007
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.