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Protein

E3 ubiquitin-protein ligase E3D

Gene

UBE3D

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase E3D (EC:6.3.2.-)
Alternative name(s):
UbcH10-binding protein with a HECT-like domain
Ubiquitin-conjugating enzyme E2C-binding protein
Gene namesi
Name:UBE3D
Synonyms:C6orf157, H10BH, UBE2CBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21381. UBE3D.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162407873.

Polymorphism and mutation databases

BioMutaiUBE3D.
DMDMi160395569.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 389388E3 ubiquitin-protein ligase E3DPRO_0000311190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Post-translational modificationi

Ubiquitinated by UBCH10 (E2 ubiquitin-conjugating enzyme).

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

EPDiQ7Z6J8.
MaxQBiQ7Z6J8.
PaxDbiQ7Z6J8.
PRIDEiQ7Z6J8.

PTM databases

iPTMnetiQ7Z6J8.

Expressioni

Gene expression databases

BgeeiQ7Z6J8.
CleanExiHS_UBE2CBP.
ExpressionAtlasiQ7Z6J8. baseline and differential.
GenevisibleiQ7Z6J8. HS.

Organism-specific databases

HPAiHPA027231.

Interactioni

Subunit structurei

Interacts with UBE2C/UbcH10 (E2 ubiquitin-conjugating enzyme). In vitro, interacts with cyclin-B.1 Publication

Protein-protein interaction databases

BioGridi124656. 18 interactions.
IntActiQ7Z6J8. 2 interactions.
STRINGi9606.ENSP00000358762.

Structurei

3D structure databases

ProteinModelPortaliQ7Z6J8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni235 – 25723Interaction with UBE2CAdd
BLAST
Regioni353 – 38937HECT-likeAdd
BLAST

Domaini

The C-terminal half (AA 188-389) is able to bind cyclin-B and shows a self-ubiquitination activity (mono-, poly, or multi-ubiquitination) in a HECT-like sequence dependent manner.

Phylogenomic databases

eggNOGiKOG4784. Eukaryota.
ENOG4111HHQ. LUCA.
GeneTreeiENSGT00390000003986.
HOVERGENiHBG056762.
InParanoidiQ7Z6J8.
OMAiTPEGCTE.
OrthoDBiEOG7288RR.
PhylomeDBiQ7Z6J8.
TreeFamiTF324684.

Family and domain databases

InterProiIPR019193. UBQ-conj_enz_E2-bd_prot.
[Graphical view]
PfamiPF09814. HECT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7Z6J8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASAAETRV FLEVRGQLQS ALLILGEPKE GGMPMNISIM PSSLQMKTPE
60 70 80 90 100
GCTEIQLPAE VRLVPSSCRG LQFVVGDGLH LRLQTQAKLG TKLISMFNQS
110 120 130 140 150
SQTQECCTFY CQSCGEVIIK DRKLLRVLPL PSENWGALVG EWCCHPDPFA
160 170 180 190 200
NKSLHPQEND CFIGDSFFLV NLRTSLWQQR PELSPVEMCC VSSDNHCKLE
210 220 230 240 250
PKANTKVICK RCKVMLGETV SSETTKFYMT EIIIQSSERS FPIIPRSWFV
260 270 280 290 300
QSVIAQCLVQ LSSARSTFRF TIQGQDDKVY ILLWLLNSDS LVIESLRNSK
310 320 330 340 350
YIKKFPLLEN TFKADSSSAW SAVKVLYQPC IKSRNEKLVS LWESDISVHP
360 370 380
LTLPSATCLE LLLILSKSNA NLPSSLRRVN SFQVAFLKM
Length:389
Mass (Da):43,657
Last modified:November 13, 2007 - v2
Checksum:i5F72BE6670863E2B
GO

Sequence cautioni

The sequence AAH53645.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI13740.2 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI15282.2 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAM28304.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti223 – 2264ETTK → ARSC in CAB70802 (PubMed:17974005).Curated
Sequence conflicti340 – 3401S → G in AAH71763 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti174 – 1741T → P.
Corresponds to variant rs12528542 [ dbSNP | Ensembl ].
VAR_037152
Natural varianti379 – 3791V → M.
Corresponds to variant rs7739323 [ dbSNP | Ensembl ].
VAR_037153

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB126062 mRNA. Translation: BAD01604.1.
AK298205 mRNA. Translation: BAG60475.1.
AL034377
, AL139333, AL357121, AL355613 Genomic DNA. Translation: CAM28304.1. Sequence problems.
AL139333
, AL034377, AL357121, AL355613 Genomic DNA. Translation: CAI15282.2. Sequence problems.
AL357121
, AL034377, AL139333, AL355613 Genomic DNA. Translation: CAI13740.2. Sequence problems.
CH471051 Genomic DNA. Translation: EAW48681.1.
BC053645 mRNA. Translation: AAH53645.1. Different initiation.
BC071763 mRNA. Translation: AAH71763.1.
BC101512 mRNA. Translation: AAI01513.1.
BC101538 mRNA. Translation: AAI01539.1.
AL137544 mRNA. Translation: CAB70802.1.
CCDSiCCDS34491.1.
PIRiT46387.
RefSeqiNP_001291366.1. NM_001304437.1.
NP_944602.1. NM_198920.2.
UniGeneiHs.148609.

Genome annotation databases

EnsembliENST00000369747; ENSP00000358762; ENSG00000118420.
GeneIDi90025.
KEGGihsa:90025.
UCSCiuc003pjp.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB126062 mRNA. Translation: BAD01604.1.
AK298205 mRNA. Translation: BAG60475.1.
AL034377
, AL139333, AL357121, AL355613 Genomic DNA. Translation: CAM28304.1. Sequence problems.
AL139333
, AL034377, AL357121, AL355613 Genomic DNA. Translation: CAI15282.2. Sequence problems.
AL357121
, AL034377, AL139333, AL355613 Genomic DNA. Translation: CAI13740.2. Sequence problems.
CH471051 Genomic DNA. Translation: EAW48681.1.
BC053645 mRNA. Translation: AAH53645.1. Different initiation.
BC071763 mRNA. Translation: AAH71763.1.
BC101512 mRNA. Translation: AAI01513.1.
BC101538 mRNA. Translation: AAI01539.1.
AL137544 mRNA. Translation: CAB70802.1.
CCDSiCCDS34491.1.
PIRiT46387.
RefSeqiNP_001291366.1. NM_001304437.1.
NP_944602.1. NM_198920.2.
UniGeneiHs.148609.

3D structure databases

ProteinModelPortaliQ7Z6J8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124656. 18 interactions.
IntActiQ7Z6J8. 2 interactions.
STRINGi9606.ENSP00000358762.

PTM databases

iPTMnetiQ7Z6J8.

Polymorphism and mutation databases

BioMutaiUBE3D.
DMDMi160395569.

Proteomic databases

EPDiQ7Z6J8.
MaxQBiQ7Z6J8.
PaxDbiQ7Z6J8.
PRIDEiQ7Z6J8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369747; ENSP00000358762; ENSG00000118420.
GeneIDi90025.
KEGGihsa:90025.
UCSCiuc003pjp.4. human.

Organism-specific databases

CTDi90025.
GeneCardsiUBE3D.
H-InvDBHIX0006033.
HGNCiHGNC:21381. UBE3D.
HPAiHPA027231.
MIMi612495. gene.
neXtProtiNX_Q7Z6J8.
PharmGKBiPA162407873.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4784. Eukaryota.
ENOG4111HHQ. LUCA.
GeneTreeiENSGT00390000003986.
HOVERGENiHBG056762.
InParanoidiQ7Z6J8.
OMAiTPEGCTE.
OrthoDBiEOG7288RR.
PhylomeDBiQ7Z6J8.
TreeFamiTF324684.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GenomeRNAii90025.
PROiQ7Z6J8.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z6J8.
CleanExiHS_UBE2CBP.
ExpressionAtlasiQ7Z6J8. baseline and differential.
GenevisibleiQ7Z6J8. HS.

Family and domain databases

InterProiIPR019193. UBQ-conj_enz_E2-bd_prot.
[Graphical view]
PfamiPF09814. HECT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel UbcH10-binding protein facilitates the ubiquitinylation of cyclin B in vitro."
    Kobirumaki F., Miyauchi Y., Fukami K., Tanaka H.
    J. Biochem. 137:133-139(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH UBE2C AND CYCLIN-B, FUNCTION.
    Tissue: Cervix carcinoma.
  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].
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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].
    Tissue: Blood and Bone marrow.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-226.
    Tissue: Testis.
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBE3D_HUMAN
AccessioniPrimary (citable) accession number: Q7Z6J8
Secondary accession number(s): B4DP63
, Q5T4W2, Q6IPR4, Q75UG0, Q9NT42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: June 8, 2016
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.