P61077 (UB2D3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 D3
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein D3
Ubiquitin-conjugating enzyme E2(17)KB 3
Ubiquitin-conjugating enzyme E2-17 kDa 3
Ubiquitin-protein ligase D3

Gene names

Name:	UBE2D3
Synonyms:	UBC5C, UBCH5C

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	147 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction By similarity. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex; when Cullin is neddylated, the interaction between the E2 and the SCF complex is strengthened. Interacts with DAPK3. Interacts with BRCA1; the DNA damage checkpoint promotes the association with BRCA1 after ionizing radiation. Interacts non-covalently with ubiquitin. Ref.14 Ref.15 Ref.18 Ref.24
Subcellular location	Cell membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein Ref.17.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Apoptosis DNA damage DNA repair Ubl conjugation pathway
Cellular component	Cell membrane Endosome Membrane
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway Traceable author statement. Source: Reactome DNA repair Inferred from electronic annotation. Source: UniProtKB-KW apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Traceable author statement. Source: Reactome negative regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: Reactome negative regulation of type I interferon production Traceable author statement. Source: Reactome proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.21. Source: UniProtKB protein K11-linked ubiquitination Inferred from direct assay Ref.20. Source: UniProtKB protein K48-linked ubiquitination Inferred from direct assay Ref.20. Source: UniProtKB protein monoubiquitination Inferred from direct assay Ref.21. Source: UniProtKB regulation of transcription from RNA polymerase II promoter in response to hypoxia Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay PubMed 14765125PubMed 16522193Ref.20Ref.21Ref.23. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RNF11	Q9Y3C5	3	EBI-348268,EBI-396669
RNF126	Q9BV68	3	EBI-348268,EBI-357322
RNF43	Q68DV7	2	EBI-348268,EBI-1647060
RNF5	Q99942	3	EBI-348268,EBI-348482
TRAF6	Q9Y4K3	2	EBI-348268,EBI-359276
XIAP	P98170	2	EBI-348268,EBI-517127
ZNRF1	Q8ND25	3	EBI-348268,EBI-2129250

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P61077-1)

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: P61077-2)

The sequence of this isoform differs from the canonical sequence as follows:
     134-147: YNRISREWTQKYAM → YNRLAREWTEKYAML

Isoform 3 (identifier: P61077-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MALKRINK → MLSNRKCLSK

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 147

147

Ubiquitin-conjugating enzyme E2 D3

PRO_0000082466

Sites

Active site

85

1

Glycyl thioester intermediate By similarity

Amino acid modifications

Disulfide bond

21 ↔ 107

Ref.25

Natural variations

Alternative sequence

1 – 8

8

MALKRINK → MLSNRKCLSK in isoform 3.

VSP_038096

Alternative sequence

134 – 147

14

YNRIS…QKYAM → YNRLAREWTEKYAML in isoform 2.

VSP_038097

Experimental info

Mutagenesis

77

1

N → S: Activity is restricted HECT-type and not RING-containing E3 ubiquitin-protein ligases. Exhibits ubiquitin transfer with ARIH1 and PARK2. Ref.23

Mutagenesis

85

1

C → A: Loss of function. Ref.8

Mutagenesis

87

1

D → E or P: Has intermediate lysine reactivity. Ref.23

Mutagenesis

87

1

D → K: Abolishes affect lysine reactivity. Ref.23

Mutagenesis

87

1

D → N: Does not affect lysine reactivity. Ref.23

Mutagenesis

117

1

D → H: Strongly impairs lysine reactivity but retains some ability to transfer ubiquitin to BRCA1. Ref.23

Sequence conflict

50

1

Missing in DB045280. Ref.3

Sequence conflict

123

1

I → L in AAH66917. Ref.7

Sequence conflict

137

1

I → V in CAG33197. Ref.3

Sequence conflict

147

1

M → I in CAG33197. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

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.

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147

Helix Strand Turn

Details...

Helix

1 – 15

15

Beta strand

21 – 26

6

Beta strand

32 – 38

7

Beta strand

41 – 43

3

Turn

44 – 47

4

Beta strand

49 – 55

7

Turn

58 – 61

4

Beta strand

66 – 69

4

Helix

87 – 89

3

Turn

90 – 92

3

Helix

99 – 111

13

Helix

121 – 129

9

Helix

131 – 145

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 26, 2004. Version 1. Checksum: ADD74A8A708EFEE3	FASTA	147	16,687
	10 20 30 40 50 60 MALKRINKEL SDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY 70 80 90 100 110 120 PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV 130 140 PEIARIYKTD RDKYNRISRE WTQKYAM
	Isoform 2 [UniParc]. Checksum: E73DC194DB6D4EFE	FASTA	148	16,785
	10 20 30 40 50 60 MALKRINKEL SDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY 70 80 90 100 110 120 PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV 130 140 PEIARIYKTD RDKYNRLARE WTEKYAML
	Isoform 3 [UniParc]. Checksum: F20F36FCD312444A	FASTA	149	16,893
	10 20 30 40 50 60 MLSNRKCLSK ELSDLARDPP AQCSAGPVGD DMFHWQATIM GPNDSPYQGG VFFLTIHFPT 70 80 90 100 110 120 DYPFKPPKVA FTTRIYHPNI NSNGSICLDI LRSQWSPALT ISKVLLSICS LLCDPNPDDP 130 140 LVPEIARIYK TDRDKYNRIS REWTQKYAM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a family of closely related human ubiquitin conjugating enzymes." Jensen J.P., Bates P.W., Yang M., Vierstra R.D., Weissman A.M. J. Biol. Chem. 270:30408-30414(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Genome sequencing of the chromosome 4q region implicated in human hepatocellular carcinoma pathogenesis." Chang H.-M., Tsai S.-F. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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] (ISOFORMS 2 AND 3). Tissue: Chondrocyte and Testis.
[4]	"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] (ISOFORM 1).
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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].
[7]	"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: Brain and Placenta.
[8]	"Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha." Gonen H., Bercovich B., Orian A., Carrano A., Takizawa C., Yamanaka K., Pagano M., Iwai K., Ciechanover A. J. Biol. Chem. 274:14823-14830(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-85.
[9]	"CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein." Murata S., Minami Y., Minami M., Chiba T., Tanaka K. EMBO Rep. 2:1133-1138(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Mammalian Numb is a target protein of Mdm2, ubiquitin ligase." Yogosawa S., Miyauchi Y., Honda R., Tanaka H., Yasuda H. Biochem. Biophys. Res. Commun. 302:869-872(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53." Rajendra R., Malegaonkar D., Pungaliya P., Marshall H., Rasheed Z., Brownell J., Liu L.F., Lutzker S., Saleem A., Rubin E.H. J. Biol. Chem. 279:36440-36444(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Regulation of p53 by the ubiquitin-conjugating enzymes UbcH5B/C in vivo." Saville M.K., Sparks A., Xirodimas D.P., Wardrop J., Stevenson L.F., Bourdon J.C., Woods Y.L., Lane D.P. J. Biol. Chem. 279:42169-42181(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"The poxvirus p28 virulence factor is an E3 ubiquitin ligase." Huang J., Huang Q., Zhou X., Shen M.M., Yen A., Yu S.X., Dong G., Qu K., Huang P., Anderson E.M., Daniel-Issakani S., Buller R.M., Payan D.G., Lu H.H. J. Biol. Chem. 279:54110-54116(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA damage sites." Polanowska J., Martin J.S., Garcia-Muse T., Petalcorin M.I.R., Boulton S.J. EMBO J. 25:2178-2188(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BRCA1, FUNCTION.
[15]	"Physical and functional interactions between ZIP kinase and UbcH5." Ohbayashi N., Okada K., Kawakami S., Togi S., Sato N., Ikeda O., Kamitani S., Muromoto R., Sekine Y., Kawai T., Akira S., Matsuda T. Biochem. Biophys. Res. Commun. 372:708-712(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DAPK3, FUNCTION.
[16]	"PCNA is ubiquitinated by RNF8." Zhang S., Chea J., Meng X., Zhou Y., Lee E.Y.C., Lee M.Y.W.T. Cell Cycle 7:3399-3404(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation." Umebayashi K., Stenmark H., Yoshimori T. Mol. Biol. Cell 19:3454-3462(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]	"Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation." Saha A., Deshaies R.J. Mol. Cell 32:21-31(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCF COMPLEX.
[19]	"Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions." Kubori T., Hyakutake A., Nagai H. Mol. Microbiol. 67:1307-1319(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines." David Y., Ziv T., Admon A., Navon A. J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[21]	"Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate." Wu K., Kovacev J., Pan Z.Q. Mol. Cell 37:784-796(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[22]	"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].
[23]	"UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids." Wenzel D.M., Lissounov A., Brzovic P.S., Klevit R.E. Nature 474:105-108(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASN-77; ASP-87 AND ASP-117.
[24]	"A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination." Brzovic P.S., Lissounov A., Christensen D.E., Hoyt D.W., Klevit R.E. Mol. Cell 21:873-880(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2-147 IN COMPLEX WITH THE BRCA1/BARD1 RING-DOMAIN HETERODIMER, INTERACTION WITH BRCA1.
[25]	"Crystal structure of UBCH5C." Nakanishi M., Teshima N., Mizushima T., Murata S., Tanaka K., Yamane T. Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-147, DISULFIDE BOND.
[26]	"Crystal structure of the U-Box domain of human e4b ubiquitin ligase in complex with UBCH5C E2 ubiquitin conjugating enzyme." Benirschke R., Thompson J.R., Mer G. Submitted (MAY-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (3.17 ANGSTROMS) OF 1-147 IN COMPLEX WITH U-BOX DOMAIN OF UBE4B.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U39318 mRNA. Translation: AAA91461.1.
AF213884 Genomic DNA. Translation: AAF35234.1.
AK095822 mRNA. Translation: BAC04632.1.
DB045280 mRNA. No translation available.
CR456916 mRNA. Translation: CAG33197.1.
AC018797 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX06138.1.
CH471057 Genomic DNA. Translation: EAX06143.1.
BC003395 mRNA. Translation: AAH03395.1.
BC037894 mRNA. Translation: AAH37894.1.
BC066917 mRNA. Translation: AAH66917.1.

IPI

IPI00026965.
IPI00375142.
IPI00749013.

RefSeq

NP_003331.1. NM_003340.5.
NP_871615.1. NM_181886.2.
NP_871616.1. NM_181887.1.
NP_871617.1. NM_181888.2.
NP_871618.1. NM_181889.1.
NP_871619.1. NM_181890.1.
NP_871620.1. NM_181891.1.
NP_871621.1. NM_181892.2.
NP_871622.1. NM_181893.1.

UniGene

Hs.518773.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X23	X-ray	1.85	A/B/C/D	1-147	[»]
2FUH	NMR	-	A	2-147	[»]
3L1Z	X-ray	3.17	A	1-147	[»]
3RPG	X-ray	2.65	A	2-147	[»]
3UGB	X-ray	2.35	A	1-147	[»]

ProteinModelPortal

P61077.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29062N.

IntAct

P61077. 79 interactions.

MINT

MINT-1032046.

STRING

9606.ENSP00000349722.

PTM databases

PhosphoSite

P61077.

Polymorphism databases

DMDM

46577654.

Proteomic databases

PRIDE

P61077.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000321805; ENSP00000318494; ENSG00000109332.
ENST00000338145; ENSP00000337208; ENSG00000109332.
ENST00000343106; ENSP00000345285; ENSG00000109332.
ENST00000349311; ENSP00000344069; ENSG00000109332.
ENST00000357194; ENSP00000349722; ENSG00000109332.
ENST00000394801; ENSP00000378280; ENSG00000109332.
ENST00000394803; ENSP00000378282; ENSG00000109332.
ENST00000394804; ENSP00000378283; ENSG00000109332.
ENST00000453744; ENSP00000396901; ENSG00000109332.

GeneID

7323.

KEGG

hsa:7323.

UCSC

uc003hwi.3. human.
uc003hwk.3. human.
uc003hwq.3. human.

Organism-specific databases

CTD

7323.

GeneCards

GC04M103717.

HGNC

HGNC:12476. UBE2D3.

HPA

HPA003920.

MIM

602963. gene.

neXtProt

NX_P61077.

PharmGKB

PA37126.

GenAtlas

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Phylogenomic databases

HOVERGEN

HBG063308.

KO

K06689.

OMA

DMSKDPP.

OrthoDB

EOG4RR6JK.

Enzyme and pathway databases

Pathway_Interaction_DB

bard1pathway. BARD1 signaling events.
nfkappabcanonicalpathway. Canonical NF-kappaB pathway.

Reactome

REACT_107772. Immune System.
REACT_111102. Signal Transduction.
REACT_120956. Cellular responses to stress.
REACT_6900. Immune System.
REACT_71. Gene Expression.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

P61077.

Bgee

P61077.

CleanEx

HS_UBE2D3.

Genevestigator

P61077.

GermOnline

ENSG00000109332. Homo sapiens.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
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. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

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Other

ChiTaRS

UBE2D3. human.

EvolutionaryTrace

P61077.

GenomeRNAi

7323.

NextBio

28636.

SOURCE

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Entry information

Entry name

UB2D3_HUMAN

Accession

Primary (citable) accession number: P61077
Secondary accession number(s): A6NJ93 , A6NJB1, A6NM99, P47986, Q6IB88, Q6NXS4, Q8N924

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	April 26, 2004
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 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.