Reviewed, UniProtKB/Swiss-Prot Q9Y2X8 (UB2D4_HUMAN)

Names and origin

Protein names

Recommended name:
    Ubiquitin-conjugating enzyme E2 D4
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase D4
    Ubiquitin carrier protein D4
    HBUCE1

Gene names

Name:

UBE2D4

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	147 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.
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW post-translational protein modification Inferred from electronic annotation. Source: InterPro regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct ubiquitin-protein ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DTX2	Q86UW9	1	EBI-745527,EBI-740376

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 147	147	Ubiquitin-conjugating enzyme E2 D4		PRO_0000270202
Sites
	Active site	85	1	Glycyl thioester intermediate By similarity
Amino acid modifications
	Modified residue	144	1	N6-acetyllysine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q9Y2X8-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 5F91A2C6BC667254	FASTA	147	16,649
	10 20 30 40 50 60 MALKRIQKEL TDLQRDPPAQ CSAGPVGDDL FHWQATIMGP NDSPYQGGVF FLTIHFPTDY 70 80 90 100 110 120 PFKPPKVAFT TKIYHPNINS NGSICLDILR SQWSPALTVS KVLLSICSLL CDPNPDDPLV 130 140 PEIAHTYKAD REKYNRLARE WTQKYAM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and screening of two ubiquitin conjugation enzymes." Li G., Jin J., Hu S., Li W., Yuan J., Qiang B. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed: 12690205] [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 (JUL-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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[6]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-144, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF125044 mRNA. Translation: AAD31180.1. AK001446 mRNA. Translation: BAA91697.1. CH236951 Genomic DNA. Translation: EAL24010.1. CH471073 Genomic DNA. Translation: EAW94182.1. BC004104 mRNA. Translation: AAH04104.1.
IPI	IPI00006475.
RefSeq	NP_057067.1.
UniGene	Hs.19196
3D structure databases
HSSP	HSSP built from PDB template 1Z2U based on UniProtKB P35129.
SMR	Q9Y2X8. Positions 1-147.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y2X8. 56 interactions.
STRING	Q9Y2X8.
Proteomic databases
PRIDE	Q9Y2X8.
Genome annotation databases
Ensembl	ENST00000222402; ENSP00000222402; ENSG00000078967; Homo sapiens. [Genome view]
GeneID	51619.
KEGG	hsa:51619.
UCSC	uc003tja.1. human.
Organism-specific databases
CTD	51619.
GeneCards	GC07P043932.
HGNC	HGNC:21647. UBE2D4.
HPA	HPA003920.
PharmGKB	PA134954568.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG756483.
HOVERGEN	Q9Y2X8.
InParanoid	Q9Y2X8.
OMA	PEIAHMC.
OrthoDB	EOG9GXJ67.
PhylomeDB	Q9Y2X8.
Enzyme and pathway databases
BRENDA	6.3.2.19. 247.
Gene expression databases
ArrayExpress	Q9Y2X8.
Bgee	Q9Y2X8.
CleanEx	HS_UBE2D4.
Genevestigator	Q9Y2X8.
Family and domain databases
InterPro	IPR016135. UBQ-conjugat/RWD-like. IPR000608. UBQ-conjugat_E2. [Graphical view]
Gene3D	G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
SMART	SM00212. UBCc. 1 hit. [Graphical view]
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	55531.

Entry information

Entry name

UB2D4_HUMAN

Accession

Primary (citable) accession number: Q9Y2X8
Secondary accession number(s): A4D1V0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	November 1, 1999
Last modified:	January 19, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.