Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P62837

- UB2D2_HUMAN

UniProt

P62837 - UB2D2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ubiquitin-conjugating enzyme E2 D2

Gene

UBE2D2

Organism
Homo sapiens (Human)
Status
Reviewed - 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 autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection. Essential for viral activation of IRF3.9 Publications

Catalytic activityi

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

Pathwayi

Sites

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

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. cellular response to hypoxia Source: Reactome
  3. innate immune response Source: Reactome
  4. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  5. protein K48-linked ubiquitination Source: UniProtKB
  6. protein polyubiquitination Source: BHF-UCL
  7. protein ubiquitination Source: BHF-UCL
  8. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  9. toll-like receptor 3 signaling pathway Source: Reactome
  10. toll-like receptor 4 signaling pathway Source: Reactome
  11. toll-like receptor signaling pathway Source: Reactome
  12. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  13. ubiquitin-dependent protein catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP62837.
UniPathwayiUPA00143.

Protein family/group databases

TCDBi3.A.20.1.1. the peroxisomal protein importer (ppi) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 D2 (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein D2
Ubiquitin-conjugating enzyme E2(17)KB 2
Ubiquitin-conjugating enzyme E2-17 kDa 2
Ubiquitin-protein ligase D2
p53-regulated ubiquitin-conjugating enzyme 1
Gene namesi
Name:UBE2D2
Synonyms:PUBC1, UBC4, UBC5B, UBCH4, UBCH5B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:12475. UBE2D2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. protein complex Source: MGI
  5. ubiquitin ligase complex Source: BHF-UCL
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631K → A or E: Strongly reduced interaction with CNTO4. 1 Publication
Mutagenesisi85 – 851C → A: Catalytically inactive. Loss of ability to promote FBXW2-mediated GCM1 ubiquitination. Inhibition of TNF-alpha-induced degradation of NFKBIA. 3 Publications

Organism-specific databases

PharmGKBiPA37125.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 147147Ubiquitin-conjugating enzyme E2 D2PRO_0000082462Add
BLAST

Proteomic databases

PaxDbiP62837.
PRIDEiP62837.

PTM databases

PhosphoSiteiP62837.

Expressioni

Gene expression databases

BgeeiP62837.
CleanExiHS_UBE2D2.
ExpressionAtlasiP62837. baseline and differential.
GenevestigatoriP62837.

Organism-specific databases

HPAiHPA003920.

Interactioni

Subunit structurei

Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex. Interacts with CNOT4 (via RING domain). Interacts with E3 ubiquitin-protein ligases CBLC, PJA1 and PJA2. Interacts with PDZRN3.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MDM4O151512EBI-347677,EBI-398437
ospGQ99PZ63EBI-347677,EBI-9316527From a different organism.
OTUB1Q96FW15EBI-347677,EBI-1058491
RNF11Q9Y3C55EBI-347677,EBI-396669
RNF43Q68DV72EBI-347677,EBI-1647060
RNF5Q999423EBI-347677,EBI-348482
TRAF6Q9Y4K32EBI-347677,EBI-359276
XIAPP981702EBI-347677,EBI-517127
ZNRF1Q8ND254EBI-347677,EBI-2129250

Protein-protein interaction databases

BioGridi113170. 214 interactions.
DIPiDIP-29267N.
IntActiP62837. 100 interactions.
MINTiMINT-1035011.
STRINGi9606.ENSP00000381717.

Structurei

Secondary structure

147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1515Combined sources
Beta strandi19 – 2810Combined sources
Beta strandi32 – 387Combined sources
Beta strandi41 – 433Combined sources
Turni44 – 474Combined sources
Beta strandi49 – 557Combined sources
Turni58 – 614Combined sources
Beta strandi66 – 716Combined sources
Beta strandi76 – 783Combined sources
Beta strandi82 – 843Combined sources
Helixi87 – 893Combined sources
Turni90 – 923Combined sources
Helixi99 – 11113Combined sources
Beta strandi115 – 1173Combined sources
Helixi121 – 1299Combined sources
Helixi131 – 14515Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UR6NMR-A1-147[»]
1W4UNMR-A1-147[»]
2CLWX-ray1.94A/B/C/D1-147[»]
2ESKX-ray1.36A1-147[»]
2ESOX-ray1.50A1-147[»]
2ESPX-ray1.52A1-147[»]
2ESQX-ray1.44A1-147[»]
3A33X-ray2.20A1-147[»]
3JVZX-ray3.30A/B2-147[»]
3JW0X-ray3.10A/B2-147[»]
3L1YX-ray1.60A1-147[»]
3TGDX-ray1.80A1-147[»]
3ZNIX-ray2.21C/G/K/O2-147[»]
4A49X-ray2.21B1-147[»]
4A4BX-ray2.79C1-147[»]
4A4CX-ray2.70C1-147[»]
4AUQX-ray2.18A/D1-147[»]
4DDGX-ray3.30A/B/C/J/K/L1-147[»]
4LDTX-ray1.90C1-147[»]
ProteinModelPortaliP62837.
SMRiP62837. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62837.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP62837.
KOiK06689.
OMAiNDLGRDP.
OrthoDBiEOG7PCJGX.
PhylomeDBiP62837.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P62837-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF
60 70 80 90 100
FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS
110 120 130 140
KVLLSICSLL CDPNPDDPLV PEIARIYKTD REKYNRIARE WTQKYAM
Length:147
Mass (Da):16,735
Last modified:August 16, 2004 - v1
Checksum:iC942BE7853CBC355
GO
Isoform 2 (identifier: P62837-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Note: No experimental confirmation available.

Show »
Length:118
Mass (Da):13,635
Checksum:iCC29567199FE8084
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti128 – 1281K → Q in AAC41750. (PubMed:7724550)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929Missing in isoform 2. 1 PublicationVSP_045180Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U39317 mRNA. Translation: AAA91460.1.
L40146 Genomic DNA. Translation: AAC41750.1.
AY651263 mRNA. Translation: AAX35690.1.
AF317220 mRNA. Translation: AAK93958.1.
AK001311 mRNA. Translation: BAG50891.1.
AK001428 mRNA. Translation: BAG50911.1.
AC010378 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW62095.1.
CH471062 Genomic DNA. Translation: EAW62096.1.
CH471062 Genomic DNA. Translation: EAW62097.1.
BC033349 mRNA. Translation: AAH33349.1.
CCDSiCCDS43369.1. [P62837-1]
CCDS47275.1. [P62837-2]
PIRiI59365.
RefSeqiNP_003330.1. NM_003339.2. [P62837-1]
NP_862821.1. NM_181838.1. [P62837-2]
UniGeneiHs.108332.

Genome annotation databases

EnsembliENST00000398733; ENSP00000381717; ENSG00000131508. [P62837-1]
ENST00000398734; ENSP00000381718; ENSG00000131508. [P62837-1]
ENST00000505548; ENSP00000424941; ENSG00000131508. [P62837-2]
ENST00000511725; ENSP00000429613; ENSG00000131508. [P62837-2]
GeneIDi7322.
KEGGihsa:7322.
UCSCiuc003leq.3. human. [P62837-1]

Polymorphism databases

DMDMi51338685.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U39317 mRNA. Translation: AAA91460.1 .
L40146 Genomic DNA. Translation: AAC41750.1 .
AY651263 mRNA. Translation: AAX35690.1 .
AF317220 mRNA. Translation: AAK93958.1 .
AK001311 mRNA. Translation: BAG50891.1 .
AK001428 mRNA. Translation: BAG50911.1 .
AC010378 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW62095.1 .
CH471062 Genomic DNA. Translation: EAW62096.1 .
CH471062 Genomic DNA. Translation: EAW62097.1 .
BC033349 mRNA. Translation: AAH33349.1 .
CCDSi CCDS43369.1. [P62837-1 ]
CCDS47275.1. [P62837-2 ]
PIRi I59365.
RefSeqi NP_003330.1. NM_003339.2. [P62837-1 ]
NP_862821.1. NM_181838.1. [P62837-2 ]
UniGenei Hs.108332.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UR6 NMR - A 1-147 [» ]
1W4U NMR - A 1-147 [» ]
2CLW X-ray 1.94 A/B/C/D 1-147 [» ]
2ESK X-ray 1.36 A 1-147 [» ]
2ESO X-ray 1.50 A 1-147 [» ]
2ESP X-ray 1.52 A 1-147 [» ]
2ESQ X-ray 1.44 A 1-147 [» ]
3A33 X-ray 2.20 A 1-147 [» ]
3JVZ X-ray 3.30 A/B 2-147 [» ]
3JW0 X-ray 3.10 A/B 2-147 [» ]
3L1Y X-ray 1.60 A 1-147 [» ]
3TGD X-ray 1.80 A 1-147 [» ]
3ZNI X-ray 2.21 C/G/K/O 2-147 [» ]
4A49 X-ray 2.21 B 1-147 [» ]
4A4B X-ray 2.79 C 1-147 [» ]
4A4C X-ray 2.70 C 1-147 [» ]
4AUQ X-ray 2.18 A/D 1-147 [» ]
4DDG X-ray 3.30 A/B/C/J/K/L 1-147 [» ]
4LDT X-ray 1.90 C 1-147 [» ]
ProteinModelPortali P62837.
SMRi P62837. Positions 1-147.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113170. 214 interactions.
DIPi DIP-29267N.
IntActi P62837. 100 interactions.
MINTi MINT-1035011.
STRINGi 9606.ENSP00000381717.

Protein family/group databases

TCDBi 3.A.20.1.1. the peroxisomal protein importer (ppi) family.

PTM databases

PhosphoSitei P62837.

Polymorphism databases

DMDMi 51338685.

Proteomic databases

PaxDbi P62837.
PRIDEi P62837.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000398733 ; ENSP00000381717 ; ENSG00000131508 . [P62837-1 ]
ENST00000398734 ; ENSP00000381718 ; ENSG00000131508 . [P62837-1 ]
ENST00000505548 ; ENSP00000424941 ; ENSG00000131508 . [P62837-2 ]
ENST00000511725 ; ENSP00000429613 ; ENSG00000131508 . [P62837-2 ]
GeneIDi 7322.
KEGGi hsa:7322.
UCSCi uc003leq.3. human. [P62837-1 ]

Organism-specific databases

CTDi 7322.
GeneCardsi GC05P138920.
H-InvDB HIX0019025.
HIX0028451.
HGNCi HGNC:12475. UBE2D2.
HPAi HPA003920.
MIMi 602962. gene.
neXtProti NX_P62837.
PharmGKBi PA37125.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00760000119012.
HOGENOMi HOG000233455.
HOVERGENi HBG063308.
InParanoidi P62837.
KOi K06689.
OMAi NDLGRDP.
OrthoDBi EOG7PCJGX.
PhylomeDBi P62837.
TreeFami TF101108.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki P62837.

Miscellaneous databases

EvolutionaryTracei P62837.
GeneWikii UBE2D2.
GenomeRNAii 7322.
NextBioi 28630.
PROi P62837.
SOURCEi Search...

Gene expression databases

Bgeei P62837.
CleanExi HS_UBE2D2.
ExpressionAtlasi P62837. baseline and differential.
Genevestigatori P62837.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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).
    Tissue: Peripheral blood lymphocyte.
  2. "Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP)."
    Rolfe M., Beer-Romero P., Glass S., Eckstein J., Berdo I., Theodoras A., Pagano M., Draetta G.
    Proc. Natl. Acad. Sci. U.S.A. 92:3264-3268(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Humoral detection of leukaemia-associated antigens in presentation acute myeloid leukaemia."
    Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S., Wells J.W., Banham A.H., Mufti G.J.
    Biochem. Biophys. Res. Commun. 335:1293-1304(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  4. "Cloning and identification of a p53-regulated ubiquitin-conjugating enzyme, PUBC1."
    Yin Y.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  5. "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 1).
    Tissue: Teratocarcinoma.
  6. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Testis.
  9. Lubec G., Afjehi-Sadat L.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 73-90, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  10. "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.
  11. "SCF(beta-TRCP) and phosphorylation dependent ubiquitination of I kappa B alpha catalyzed by Ubc3 and Ubc4."
    Strack P., Caligiuri M., Pelletier M., Boisclair M., Theodoras A., Beer-Romero P., Glass S., Parsons T., Copeland R.A., Auger K.R., Benfield P., Brizuela L., Rolfe M.
    Oncogene 19:3529-3536(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCF COMPLEX.
  12. "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain."
    Yu P., Chen Y., Tagle D.A., Cai T.
    Genomics 79:869-874(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PJA1 AND PJA2.
  13. Cited for: FUNCTION.
  14. "An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair."
    Winkler G.S., Albert T.K., Dominguez C., Legtenberg Y.I., Boelens R., Timmers H.T.
    J. Mol. Biol. 337:157-165(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CNOT4, MUTAGENESIS OF LYS-63.
  15. "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.
  16. "Ubiquitin-conjugating enzyme UBE2D2 is responsible for FBXW2 (F-box and WD repeat domain containing 2)-mediated human GCM1 (glial cell missing homolog 1) ubiquitination and degradation."
    Chiang M.H., Chen L.F., Chen H.
    Biol. Reprod. 79:914-920(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-85.
  17. "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.
  18. "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: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  19. "Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity."
    Zeng W., Sun L., Jiang X., Chen X., Hou F., Adhikari A., Xu M., Chen Z.J.
    Cell 141:315-330(2010) [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. "The N terminus of Cbl-c regulates ubiquitin ligase activity by modulating affinity for the ubiquitin-conjugating enzyme."
    Ryan P.E., Sivadasan-Nair N., Nau M.M., Nicholas S., Lipkowitz S.
    J. Biol. Chem. 285:23687-23698(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CBLC, MUTAGENESIS OF CYS-85.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Solution structure of the ubiquitin-conjugating enzyme UbcH5B."
    Houben K., Dominguez C., van Schaik F.M., Timmers H.T., Bonvin A.M., Boelens R.
    J. Mol. Biol. 344:513-526(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  24. "Crystal structure of UbcH5b~ubiquitin intermediate: insight into the formation of the self-assembled E2~Ub conjugates."
    Sakata E., Satoh T., Yamamoto S., Yamaguchi Y., Yagi-Utsumi M., Kurimoto E., Tanaka K., Wakatsuki S., Kato K.
    Structure 18:138-147(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).

Entry informationi

Entry nameiUB2D2_HUMAN
AccessioniPrimary (citable) accession number: P62837
Secondary accession number(s): D3DQC9
, P51669, Q3MN78, Q96RP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: October 29, 2014
This is version 125 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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