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Protein

Ubiquitin-conjugating enzyme E2 D1

Gene

UBE2D1

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

Functioni

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.5 Publications

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathway: protein ubiquitination

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei85 – 851Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ligase activity Source: UniProtKB-KW
  • ubiquitin conjugating enzyme activity Source: BHF-UCL
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.3.2.B6. 2681.
2.3.2.B8. 2681.
ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_12034. Signaling by BMP.
REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_150471. Separation of Sister Chromatids.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_188323. CLEC7A (Dectin-1) signaling.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6904. Phosphorylation of the APC/C.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
SignaLinkiP51668.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 D1 (EC:6.3.2.19)
Alternative name(s):
Stimulator of Fe transport
Short name:
SFT
UBC4/5 homolog
UbcH5
Ubiquitin carrier protein D1
Ubiquitin-conjugating enzyme E2(17)KB 1
Ubiquitin-conjugating enzyme E2-17 kDa 1
Ubiquitin-protein ligase D1
Gene namesi
Name:UBE2D1
Synonyms:SFT, UBC5A, UBCH5, UBCH5A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:12474. UBE2D1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • protein complex Source: MGI
  • ubiquitin ligase complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37124.

Polymorphism and mutation databases

BioMutaiUBE2D1.
DMDMi1717848.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 147147Ubiquitin-conjugating enzyme E2 D1PRO_0000082460Add
BLAST

Proteomic databases

MaxQBiP51668.
PaxDbiP51668.
PRIDEiP51668.

PTM databases

PhosphoSiteiP51668.

Expressioni

Tissue specificityi

Ubiquitous. Up-regulated in livers of iron-overloaded patients with hereditary hemochromatosis.2 Publications

Gene expression databases

BgeeiP51668.
CleanExiHS_UBE2D1.
ExpressionAtlasiP51668. baseline and differential.
GenevisibleiP51668. HS.

Organism-specific databases

HPAiHPA003920.

Interactioni

Subunit structurei

Component of a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with RNF11.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DTX2Q4ZH493EBI-743540,EBI-10192429
MID1O153444EBI-743540,EBI-2340316
MID2Q9UJV3-23EBI-743540,EBI-10172526
MKRN2Q9H0003EBI-743540,EBI-2341005
MKRN3Q130644EBI-743540,EBI-2340269
OTUB1Q96FW14EBI-743540,EBI-1058491
RNF11Q9Y3C54EBI-743540,EBI-396669
RNF111Q6ZNA45EBI-743540,EBI-2129175
RNF115Q9Y4L54EBI-743540,EBI-2129242
RNF126Q9BV686EBI-743540,EBI-357322
RNF14Q9UBS84EBI-743540,EBI-2130308
RNF5Q999425EBI-743540,EBI-348482
TRAF6Q9Y4K32EBI-743540,EBI-359276
TRIM39Q9HCM96EBI-743540,EBI-739510
XIAPP981703EBI-743540,EBI-517127
ZNRF1Q8ND254EBI-743540,EBI-2129250

Protein-protein interaction databases

BioGridi113169. 249 interactions.
DIPiDIP-44088N.
IntActiP51668. 105 interactions.
MINTiMINT-1433717.
STRINGi9606.ENSP00000363019.

Structurei

Secondary structure

147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1515Combined sources
Beta strandi21 – 266Combined sources
Beta strandi29 – 3810Combined sources
Beta strandi41 – 433Combined sources
Turni44 – 474Combined sources
Beta strandi49 – 557Combined sources
Turni58 – 614Combined sources
Beta strandi66 – 694Combined sources
Helixi87 – 893Combined sources
Turni90 – 923Combined sources
Helixi99 – 11113Combined sources
Helixi121 – 1299Combined sources
Helixi131 – 14616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C4PX-ray2.35A/B1-147[»]
2YHOX-ray2.10B/D/F/H1-147[»]
3OJ4X-ray3.40A/D1-147[»]
3PTFX-ray2.70A/B1-147[»]
4AP4X-ray2.21B/E1-147[»]
4QPLX-ray1.90B/D1-147[»]
ProteinModelPortaliP51668.
SMRiP51668. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51668.

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP51668.
KOiK06689.
OMAiHIYKSDR.
OrthoDBiEOG7PCJGX.
PhylomeDBiP51668.
TreeFamiTF101108.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51668-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALKRIQKEL SDLQRDPPAH CSAGPVGDDL FHWQATIMGP PDSAYQGGVF
60 70 80 90 100
FLTVHFPTDY PFKPPKIAFT TKIYHPNINS NGSICLDILR SQWSPALTVS
110 120 130 140
KVLLSICSLL CDPNPDDPLV PDIAQIYKSD KEKYNRHARE WTQKYAM
Length:147
Mass (Da):16,602
Last modified:October 1, 1996 - v1
Checksum:i2E96FD0179EE119D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78140 mRNA. Translation: CAA55019.1.
AF257220 mRNA. Translation: AAM81086.1.
AJ272367 mRNA. Translation: CAC82177.1.
AK291901 mRNA. Translation: BAF84590.1.
AJ293565 Genomic DNA. Translation: CAC82097.1.
BT007041 mRNA. Translation: AAP35690.1.
AC016396 Genomic DNA. No translation available.
AC023170 Genomic DNA. No translation available.
CH471083 Genomic DNA. Translation: EAW54169.1.
BC005980 mRNA. Translation: AAH05980.1.
BC015997 mRNA. Translation: AAH15997.1.
AF020761 mRNA. No translation available.
CCDSiCCDS7252.1.
PIRiI39202.
RefSeqiNP_003329.1. NM_003338.4.
UniGeneiHs.129683.

Genome annotation databases

EnsembliENST00000373910; ENSP00000363019; ENSG00000072401.
GeneIDi7321.
KEGGihsa:7321.
UCSCiuc001jke.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78140 mRNA. Translation: CAA55019.1.
AF257220 mRNA. Translation: AAM81086.1.
AJ272367 mRNA. Translation: CAC82177.1.
AK291901 mRNA. Translation: BAF84590.1.
AJ293565 Genomic DNA. Translation: CAC82097.1.
BT007041 mRNA. Translation: AAP35690.1.
AC016396 Genomic DNA. No translation available.
AC023170 Genomic DNA. No translation available.
CH471083 Genomic DNA. Translation: EAW54169.1.
BC005980 mRNA. Translation: AAH05980.1.
BC015997 mRNA. Translation: AAH15997.1.
AF020761 mRNA. No translation available.
CCDSiCCDS7252.1.
PIRiI39202.
RefSeqiNP_003329.1. NM_003338.4.
UniGeneiHs.129683.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C4PX-ray2.35A/B1-147[»]
2YHOX-ray2.10B/D/F/H1-147[»]
3OJ4X-ray3.40A/D1-147[»]
3PTFX-ray2.70A/B1-147[»]
4AP4X-ray2.21B/E1-147[»]
4QPLX-ray1.90B/D1-147[»]
ProteinModelPortaliP51668.
SMRiP51668. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113169. 249 interactions.
DIPiDIP-44088N.
IntActiP51668. 105 interactions.
MINTiMINT-1433717.
STRINGi9606.ENSP00000363019.

PTM databases

PhosphoSiteiP51668.

Polymorphism and mutation databases

BioMutaiUBE2D1.
DMDMi1717848.

Proteomic databases

MaxQBiP51668.
PaxDbiP51668.
PRIDEiP51668.

Protocols and materials databases

DNASUi7321.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373910; ENSP00000363019; ENSG00000072401.
GeneIDi7321.
KEGGihsa:7321.
UCSCiuc001jke.2. human.

Organism-specific databases

CTDi7321.
GeneCardsiGC10P060094.
HGNCiHGNC:12474. UBE2D1.
HPAiHPA003920.
MIMi602961. gene.
neXtProtiNX_P51668.
PharmGKBiPA37124.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP51668.
KOiK06689.
OMAiHIYKSDR.
OrthoDBiEOG7PCJGX.
PhylomeDBiP51668.
TreeFamiTF101108.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B6. 2681.
2.3.2.B8. 2681.
ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_12034. Signaling by BMP.
REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_150471. Separation of Sister Chromatids.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_188323. CLEC7A (Dectin-1) signaling.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6904. Phosphorylation of the APC/C.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
SignaLinkiP51668.

Miscellaneous databases

ChiTaRSiUBE2D1. human.
EvolutionaryTraceiP51668.
GeneWikiiUBE2D1.
GenomeRNAii7321.
NextBioi28626.
PROiP51668.
SOURCEiSearch...

Gene expression databases

BgeeiP51668.
CleanExiHS_UBE2D1.
ExpressionAtlasiP51668. baseline and differential.
GenevisibleiP51668. HS.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53."
    Scheffner M., Huibregtse J.M., Howley P.M.
    Proc. Natl. Acad. Sci. U.S.A. 91:8797-8801(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "UbcH5A, a member of human E2 ubiquitin-conjugating enzymes, is closely related to SFT, a stimulator of iron transport, and is up-regulated in hereditary hemochromatosis."
    Gehrke S.G., Riedel H.-D., Herrmann T., Hadaschik B., Bents K., Veltkamp C., Stremmel W.
    Blood 101:3288-3293(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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].
    Tissue: Skeletal muscle.
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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].
    Tissue: Bone marrow and Skin.
  8. "Functional expression cloning and characterization of SFT, a stimulator of Fe transport."
    Gutierrez J.A., Yu J., Rivera S., Wessling-Resnick M.
    J. Cell Biol. 139:895-905(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 134-147, TISSUE SPECIFICITY.
  9. Erratum
    Gutierrez J.A., Yu J., Rivera S., Wessling-Resnick M.
    J. Cell Biol. 147:205-205(1999)
  10. "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses."
    Matsuzawa S., Reed J.C.
    Mol. Cell 7:915-926(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT OF A COMPLEX WITH SIAH1; CACYBP; SKP1; APC AND TBL1X.
  11. "The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase."
    Subramaniam V., Li H., Wong M.J., Kitching R., Attisano L., Wrana J., Zubovits J., Burger A.M., Seth A.K.
    Br. J. Cancer 89:1538-1544(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF11.
  12. "Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology."
    Windheim M., Peggie M., Cohen P.
    Biochem. J. 409:723-729(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but enters the nucleus upon cellular exposure to nitric oxide."
    Espinosa A., Oke V., Elfving A., Nyberg F., Covacu R., Wahren-Herlenius M.
    Exp. Cell Res. 314:3605-3613(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "Members of the E2D (UbcH5) family mediate the ubiquitination of the conserved cysteine of Pex5p, the peroxisomal import receptor."
    Grou C.P., Carvalho A.F., Pinto M.P., Wiese S., Piechura H., Meyer H.E., Warscheid B., Sa-Miranda C., Azevedo J.E.
    J. Biol. Chem. 283:14190-14197(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases."
    Pabarcus M.K., Hoe N., Sadeghi S., Patterson C., Wiertz E., Correia M.A.
    Arch. Biochem. Biophys. 483:66-74(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3."
    Zeng W., Xu M., Liu S., Sun L., Chen Z.J.
    Mol. Cell 36:315-325(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "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.
  18. "The IDOL-UBE2D complex mediates sterol-dependent degradation of the LDL receptor."
    Zhang L., Fairall L., Goult B.T., Calkin A.C., Hong C., Millard C.J., Tontonoz P., Schwabe J.W.
    Genes Dev. 25:1262-1274(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MYLIP.

Entry informationi

Entry nameiUB2D1_HUMAN
AccessioniPrimary (citable) accession number: P51668
Secondary accession number(s): A6NLF6, A8K786
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 149 of the entry and version 1 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

Caution

PubMed:9362508 cloned and sequenced SFT which consisted of UBE2D1 last coding exon along with intronic sequences on the 5'-end of this exon. A function in iron transport has been described.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.