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P49427

- UB2R1_HUMAN

UniProt

P49427 - UB2R1_HUMAN

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Protein

Ubiquitin-conjugating enzyme E2 R1

Gene

CDC34

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. Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin. Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes.13 Publications

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.1 PublicationPROSITE-ProRule annotation

Enzyme regulationi

CDC34-catalyzed polyubiquitin chain assembly activity is stimulated by the conjugation of NEDD8 to the CUL1 SCF E3 ligase complex subunit.1 Publication

Kineticsi

  1. KM=0.11 µM for beta-catenin-monoubiquin1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei93 – 931Glycyl thioester intermediate

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: UniProtKB
  2. DNA replication initiation Source: UniProtKB
  3. G1/S transition of mitotic cell cycle Source: UniProtKB
  4. negative regulation of cAMP-mediated signaling Source: UniProtKB
  5. positive regulation of inclusion body assembly Source: Ensembl
  6. positive regulation of neuron apoptotic process Source: Ensembl
  7. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  8. protein K48-linked ubiquitination Source: UniProtKB
  9. protein polyubiquitination Source: UniProtKB
  10. protein ubiquitination Source: UniProtKB
  11. response to growth factor Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP49427.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 R1 (EC:6.3.2.19)
Alternative name(s):
Ubiquitin-conjugating enzyme E2-32 kDa complementing
Ubiquitin-conjugating enzyme E2-CDC34
Ubiquitin-protein ligase R1
Gene namesi
Name:CDC34
Synonyms:UBCH3, UBE2R1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:1734. CDC34.

Subcellular locationi

Cytoplasm. Nucleus
Note: The phosphorylation of the C-terminal tail plays an important role in mediating nuclear localization. Colocalizes with beta-tubulin on mitotic spindles in anaphase.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi85 – 851N → Q: Inhibits both mono and polyubiquitination of NFKBIA. 1 Publication
Mutagenesisi87 – 871Y → A: Decreases polyubiquitination of NFKBIA. 1 Publication
Mutagenesisi93 – 931C → S or A: Loss of function. 2 Publications
Mutagenesisi95 – 951S → D: Inhibits both mono and polyubiquitination of NFKBIA. 1 Publication
Mutagenesisi97 – 971L → S: Loss of function. 1 Publication
Mutagenesisi102 – 1021D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-103. 1 Publication
Mutagenesisi103 – 1031D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-102. 1 Publication
Mutagenesisi108 – 1081E → A: Inhibits both mono and polyubiquitination of NFKBIA; when associated with A-112. 1 Publication
Mutagenesisi112 – 1121E → A: Inhibits both mono andpolyubiquitination of NFKBIA; when associated with A-108. 1 Publication
Mutagenesisi138 – 1381S → A: Decreases monoubiquitination of NFKBIA and inhibits polyubiquitination of NFKBIA. 1 Publication
Mutagenesisi143 – 1431D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-149; A-150 and A-153. 1 Publication
Mutagenesisi147 – 1471M → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-149; A-150 and A-153. 1 Publication
Mutagenesisi149 – 1491R → A: Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-147; A-150 and A-153. 1 Publication
Mutagenesisi150 – 1501K → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-153. 1 Publication
Mutagenesisi153 – 1531E → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-150. 1 Publication
Mutagenesisi203 – 2031S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-222; A-231; A-233 and A-236. 1 Publication
Mutagenesisi222 – 2221S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-231; A-233 and A-236. 1 Publication
Mutagenesisi231 – 2311S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-233 and A-236. 2 Publications
Mutagenesisi233 – 2331T → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-236. 1 Publication
Mutagenesisi236 – 2361S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-233. 1 Publication

Organism-specific databases

PharmGKBiPA26265.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 236236Ubiquitin-conjugating enzyme E2 R1PRO_0000082451Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031Phosphoserine; by CK22 Publications
Modified residuei222 – 2221Phosphoserine; by CK22 Publications
Modified residuei231 – 2311Phosphoserine; by CK23 Publications
Modified residuei233 – 2331Phosphothreonine; by CK21 Publication
Modified residuei236 – 2361Phosphoserine; by CK21 Publication

Post-translational modificationi

Autoubiquitinated. Autoubiquitination is promoted by the human herpes virus 1 protein ICP0 and leads to degradation by the Ubiquitin-proteasomal pathway.2 Publications
Phosphorylated by CK2. Phosphorylation of the C-terminal tail by CK2 controles the nuclear localization.3 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP49427.
PaxDbiP49427.
PeptideAtlasiP49427.
PRIDEiP49427.

PTM databases

PhosphoSiteiP49427.

Expressioni

Tissue specificityi

Expressed in testes during spermatogenesis to regulate repression of cAMP-induced transcription.1 Publication

Inductioni

Negatively regulated by the let-7 microRNA.1 Publication

Gene expression databases

BgeeiP49427.
CleanExiHS_CDC34.
ExpressionAtlasiP49427. baseline and differential.
GenevestigatoriP49427.

Organism-specific databases

HPAiCAB005109.
CAB047311.
HPA002382.

Interactioni

Subunit structurei

Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex. Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex together with HINT1 and RBX1. When cullin is neddylated, the interaction between the E2 and the SCF complex is strengthened. When phosphorylated, interacts with beta-TrCP (BTRC). Interacts with human herpes virus 1 protein ICP0 and associates with the proteasome for degradation. Interacts with casein kinase subunit CSNK2B.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CUL1Q136163EBI-975634,EBI-359390

Protein-protein interaction databases

BioGridi107432. 55 interactions.
DIPiDIP-37783N.
IntActiP49427. 11 interactions.
MINTiMINT-238910.
STRINGi9606.ENSP00000215574.

Structurei

Secondary structure

1
236
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2215Combined sources
Beta strandi28 – 325Combined sources
Beta strandi40 – 467Combined sources
Turni52 – 554Combined sources
Beta strandi57 – 637Combined sources
Turni66 – 694Combined sources
Beta strandi74 – 796Combined sources
Beta strandi90 – 923Combined sources
Helixi94 – 974Combined sources
Helixi120 – 13213Combined sources
Helixi142 – 15312Combined sources
Turni154 – 1563Combined sources
Helixi160 – 17819Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OB4X-ray2.40A7-184[»]
3RZ3X-ray2.30A/B/C/D7-184[»]
4MDKX-ray2.61A/B/C/D7-184[»]
ProteinModelPortaliP49427.
SMRiP49427. Positions 7-184.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49427.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 23647SCF-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi200 – 23637Asp/Glu-rich (acidic)Add
BLAST

Domaini

The C-terminal acidic tail is required for nuclear localization and is involved in the binding to SCF E3 ligase complexes, and more specifically with the CUL1 subunit.2 Publications

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110436.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP49427.
KOiK02207.
OMAiRVNLVDE.
OrthoDBiEOG7VB2HT.
PhylomeDBiP49427.
TreeFamiTF101107.

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.

P49427-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN
60 70 80 90 100
TYYEGGYFKA RLKFPIDYPY SPPAFRFLTK MWHPNIYETG DVCISILHPP
110 120 130 140 150
VDDPQSGELP SERWNPTQNV RTILLSVISL LNEPNTFSPA NVDASVMYRK
160 170 180 190 200
WKESKGKDRE YTDIIRKQVL GTKVDAERDG VKVPTTLAEY CVKTKAPAPD
210 220 230
EGSDLFYDDY YEDGEVEEEA DSCFGDDEDD SGTEES
Length:236
Mass (Da):26,737
Last modified:November 1, 1997 - v2
Checksum:i258960666B589DB3
GO

Sequence cautioni

The sequence AAC37534.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti227 – 2271D → H.1 Publication
Corresponds to variant rs16990650 [ dbSNP | Ensembl ].
VAR_021277

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L22005 mRNA. Translation: AAC37534.1. Different initiation.
BT006659 mRNA. Translation: AAP35305.1.
AY650399 Genomic DNA. Translation: AAT46688.1.
AK291554 mRNA. Translation: BAF84243.1.
CH471242 Genomic DNA. Translation: EAW61190.1.
BC009850 mRNA. Translation: AAH09850.1.
BC018143 mRNA. Translation: AAH18143.1.
BC023979 mRNA. Translation: AAH23979.1.
CCDSiCCDS12030.1.
PIRiA49630.
RefSeqiNP_004350.1. NM_004359.1.
UniGeneiHs.514997.

Genome annotation databases

EnsembliENST00000215574; ENSP00000215574; ENSG00000099804.
GeneIDi997.
KEGGihsa:997.
UCSCiuc002lov.3. human.

Polymorphism databases

DMDMi2507505.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L22005 mRNA. Translation: AAC37534.1 . Different initiation.
BT006659 mRNA. Translation: AAP35305.1 .
AY650399 Genomic DNA. Translation: AAT46688.1 .
AK291554 mRNA. Translation: BAF84243.1 .
CH471242 Genomic DNA. Translation: EAW61190.1 .
BC009850 mRNA. Translation: AAH09850.1 .
BC018143 mRNA. Translation: AAH18143.1 .
BC023979 mRNA. Translation: AAH23979.1 .
CCDSi CCDS12030.1.
PIRi A49630.
RefSeqi NP_004350.1. NM_004359.1.
UniGenei Hs.514997.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OB4 X-ray 2.40 A 7-184 [» ]
3RZ3 X-ray 2.30 A/B/C/D 7-184 [» ]
4MDK X-ray 2.61 A/B/C/D 7-184 [» ]
ProteinModelPortali P49427.
SMRi P49427. Positions 7-184.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107432. 55 interactions.
DIPi DIP-37783N.
IntActi P49427. 11 interactions.
MINTi MINT-238910.
STRINGi 9606.ENSP00000215574.

PTM databases

PhosphoSitei P49427.

Polymorphism databases

DMDMi 2507505.

Proteomic databases

MaxQBi P49427.
PaxDbi P49427.
PeptideAtlasi P49427.
PRIDEi P49427.

Protocols and materials databases

DNASUi 997.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000215574 ; ENSP00000215574 ; ENSG00000099804 .
GeneIDi 997.
KEGGi hsa:997.
UCSCi uc002lov.3. human.

Organism-specific databases

CTDi 997.
GeneCardsi GC19P000532.
HGNCi HGNC:1734. CDC34.
HPAi CAB005109.
CAB047311.
HPA002382.
MIMi 116948. gene.
neXtProti NX_P49427.
PharmGKBi PA26265.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00730000110436.
HOGENOMi HOG000233454.
HOVERGENi HBG063308.
InParanoidi P49427.
KOi K02207.
OMAi RVNLVDE.
OrthoDBi EOG7VB2HT.
PhylomeDBi P49427.
TreeFami TF101107.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki P49427.

Miscellaneous databases

EvolutionaryTracei P49427.
GeneWikii CDC34.
GenomeRNAii 997.
NextBioi 4188.
PROi P49427.
SOURCEi Search...

Gene expression databases

Bgeei P49427.
CleanExi HS_CDC34.
ExpressionAtlasi P49427. baseline and differential.
Genevestigatori P49427.

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. "Cloning of the human homolog of the CDC34 cell cycle gene by complementation in yeast."
    Plon S.E., Leppig K.A., Do H.N., Groudine M.
    Proc. Natl. Acad. Sci. U.S.A. 90:10484-10488(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
  3. NIEHS SNPs program
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-227.
  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: Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Brain and Lung.
  7. "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-93.
  8. "Human Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors of cyclic AMP-induced transcription for proteolysis."
    Pati D., Meistrich M.L., Plon S.E.
    Mol. Cell. Biol. 19:5001-5013(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATF5 AND CREM, FUNCTION, TISSUE SPECIFICITY.
  9. "Association of human ubiquitin-conjugating enzyme CDC34 with the mitotic spindle in anaphase."
    Reymond F., Wirbelauer C., Krek W.
    J. Cell Sci. 113:1687-1694(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DOMAIN.
  10. "Degradation of B-Myb by ubiquitin-mediated proteolysis: involvement of the Cdc34-SCF(p45Skp2) pathway."
    Charrasse S., Carena I., Brondani V., Klempnauer K.H., Ferrari S.
    Oncogene 19:2986-2995(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  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. "Phosphorylation of the human ubiquitin-conjugating enzyme, CDC34, by casein kinase 2."
    Block K., Boyer T.G., Yew P.R.
    J. Biol. Chem. 276:41049-41058(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSNK2B, PHOSPHORYLATION AT SER-203; SER-222; SER-231; THR-233 AND SER-236, MUTAGENESIS OF SER-203; SER-222; SER-231; THR-233 AND SER-236, SUBCELLULAR LOCATION.
  13. "The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin-conjugating enzyme, and possesses in vitro E3 ubiquitin ligase activity."
    Van Sant C., Hagglund R., Lopez P., Roizman B.
    Proc. Natl. Acad. Sci. U.S.A. 98:8815-8820(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN HERPESVIRUS 1 PROTEIN ICP0, ASSOCIATION WITH THE PROTEASOME.
  14. "The Nedd8-conjugated ROC1-CUL1 core ubiquitin ligase utilizes Nedd8 charged surface residues for efficient polyubiquitin chain assembly catalyzed by Cdc34."
    Wu K., Chen A., Tan P., Pan Z.Q.
    J. Biol. Chem. 277:516-527(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCF COMPLEX, FUNCTION, ENZYME REGULATION.
  15. "CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TrCP and enhances beta-catenin degradation."
    Semplici F., Meggio F., Pinna L.A., Oliviero S.
    Oncogene 21:3978-3987(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, FUNCTION, INTERACTION WITH BTRC, PHOSPHORYLATION AT SER-231, MUTAGENESIS OF CYS-93; LEU-97 AND SER-231.
  16. "Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymes."
    Hagglund R., Van Sant C., Lopez P., Roizman B.
    Proc. Natl. Acad. Sci. U.S.A. 99:631-636(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN HERPES VIRUS 1 PROTEIN ICP0, AUTOUBIQUITINATION.
  17. "Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0."
    Hagglund R., Roizman B.
    Proc. Natl. Acad. Sci. U.S.A. 99:7889-7894(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN HERPES VIRUS 1 PROTEIN ICP0, AUTOUBIQUITINATION.
  18. "The human ubiquitin-conjugating enzyme Cdc34 controls cellular proliferation through regulation of p27Kip1 protein levels."
    Butz N., Ruetz S., Natt F., Hall J., Weiler J., Mestan J., Ducarre M., Grossenbacher R., Hauser P., Kempf D., Hofmann F.
    Exp. Cell Res. 303:482-493(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Cdc34 C-terminal tail phosphorylation regulates Skp1/cullin/F-box (SCF)-mediated ubiquitination and cell cycle progression."
    Sadowski M., Mawson A., Baker R., Sarcevic B.
    Biochem. J. 405:569-581(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-203; SER-222 AND SER-231, FUNCTION.
  20. "Human Cdc34 employs distinct sites to coordinate attachment of ubiquitin to a substrate and assembly of polyubiquitin chains."
    Gazdoiu S., Yamoah K., Wu K., Pan Z.Q.
    Mol. Cell. Biol. 27:7041-7052(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASN-85; TYR-87; SER-95; ASP-102; ASP-103; GLU-108; GLU-112; SER-138; ASP-143; MET-147; ARG-149; LYS-150 AND GLU-153.
  21. "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.
  22. "Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates."
    Kleiger G., Saha A., Lewis S., Kuhlman B., Deshaies R.J.
    Cell 139:957-968(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SCF COMPLEX, DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES.
  23. "Histidine triad nucleotide-binding protein 1 up-regulates cellular levels of p27KIP1 by targeting ScfSKP2 ubiquitin ligase and Src."
    Cen B., Li H., Weinstein I.B.
    J. Biol. Chem. 284:5265-5276(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A UBIQUITIN LIGASE COMPLEX WITH HINT1 AND RBX1, FUNCTION.
  24. "let-7 Overexpression leads to an increased fraction of cells in G2/M, direct down-regulation of Cdc34, and stabilization of Wee1 kinase in primary fibroblasts."
    Legesse-Miller A., Elemento O., Pfau S.J., Forman J.J., Tavazoie S., Coller H.A.
    J. Biol. Chem. 284:6605-6609(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, FUNCTION.
  25. "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.
  26. "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.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Human ubiquitin-conjugating enzyme cdc34."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 7-184.

Entry informationi

Entry nameiUB2R1_HUMAN
AccessioniPrimary (citable) accession number: P49427
Secondary accession number(s): A8K689
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 142 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

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