CDC34
entrez
997
canonical
uniprot
P49427
canonical
ensembl
ENSG00000099804
resolver
ensp
ENSP00000215574
resolver
ensp
ENSP00000475282
resolver
ensp
ENSP00000791488
resolver
enst
ENST00000215574
resolver
genesymbol
CDC34
resolver
genesymbol_syn
UBCH3
resolver
genesymbol_syn
UBE2R1
resolver
hgnc
HGNC:1734
resolver
uniprot
A8K689
resolver
uniprot_entry
UB2R1_HUMAN
resolver
uniprot_sec
A8K689
resolver
activity_regulation
ACTIVITY REGULATION: CDC34-catalyzed polyubiquitin chain assembly activity is stimulated by the conjugation of NEDD8 to the CUL1 SCF E3 ligase complex subunit. {ECO:0000269|PubMed:11675391}.
uniprot
proteins
amino_acid_sequence
MARPLVPSSQKALLLELKGLQEEPVEGFRVTLVDEGDLYNWEVAIFGPPNTYYEGGYFKARLKFPIDYPYSPPAFRFLTKMWHPNIYETGDVCISILHPPVDDPQSGELPSERWNPTQNVRTILLSVISLLNEPNTFSPANVDASVMYRKWKESKGKDREYTDIIRKQVLGTKVDAERDGVKVPTTLAEYCVKTKAPAPDEGSDLFYDDYYEDGEVEEEADSCFGDDEDDSGTEES
uniprot
proteins
ec_number
2.3.2.23
uniprot
proteins
ec_number
2.3.2.24
uniprot
proteins
function
FUNCTION: E2 ubiquitin-conjugating enzyme that accepts ubiquitin from an E1 ubiquitin-activating protein, and catalyzes its covalent attachment to other proteins by an E3 ubiquitin-protein ligase complex (PubMed:10329681, PubMed:17588522, PubMed:20061386, PubMed:38326650). In vitro catalyzes 'Lys-48'-linked polyubiquitination (PubMed:22496338). Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation (PubMed:10329681, PubMed:10918611, PubMed:17698585). 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 (PubMed:10871850, PubMed:15652359, PubMed:19112177). 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 (PubMed:19126550). Also involved in the degradation of beta-catenin (PubMed:12037680). Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes (PubMed:11805320, PubMed:12060736). {ECO:0000269|PubMed:10329681, ECO:0000269|PubMed:10871850, ECO:0000269|PubMed:10918611, ECO:0000269|PubMed:11805320, ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:12060736, ECO:0000269|PubMed:15652359, ECO:0000269|PubMed:17588522, ECO:0000269|PubMed:17698585, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19126550, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:22496338, ECO:0000269|PubMed:38326650}.
uniprot
proteins
mass_dalton
26737
uniprot
proteins
mutagenesis
MUTAGEN 70; /note="Y->R: Loss of RBX1-binding."; /evidence="ECO:0000269|PubMed:24316736"; MUTAGEN 85; /note="N->Q: Inhibits both mono and polyubiquitination of NFKBIA."; /evidence="ECO:0000269|PubMed:17698585"; MUTAGEN 87; /note="Y->A: Decreases polyubiquitination of NFKBIA."; /evidence="ECO:0000269|PubMed:17698585"; MUTAGEN 93; /note="C->S,A: Loss of function."; /evidence="ECO:0000269|PubMed:10329681, ECO:0000269|PubMed:12037680"; MUTAGEN 95; /note="S->D: Inhibits both mono and polyubiquitination of NFKBIA."; /evidence="ECO:0000269|PubMed:17698585"; MUTAGEN 97; /note="L->S: Loss of function."; /evidence="ECO:0000269|PubMed:12037680"; MUTAGEN 102; /note="D->A: Inhibits polyubiquitination of NFKBIA; when associated with A-103."; /evidence="ECO:0000269|PubMed:17698585"; MUTAGEN 103; /note="D->A: Inhibits polyubiquitination of NFKBIA; when associated with A-102."; /evidence="ECO:0000269|PubMed:17698585"; MUTAGEN 108; /note="E->A: Decrease in substrate affinity and ubiquitin transfer rate for neddylated CRL2(FEM1C)-UBE2R1 complex. Inhibits both mono and polyubiquitination of NFKBIA; when associated with A-112."; /evidence="ECO:0000269|PubMed:17698585, ECO:0000269|PubMed:38326650"; MUTAGEN 112; /note="E->A: Inhibits both mono and polyubiquitination of NFKBIA; when associated with A-108."; /evidence="ECO:0000269|PubMed:17698585"; MUTAGEN 113; /note="R->A: Decrease in substrate affinity and ubiquitin transfer rate for neddylated CRL2(FEM1C)-UBE2R1 complex."; /evidence="ECO:0000269|PubMed:38326650"; MUTAGEN 117; /note="T->E: Loss of RBX1-binding."; /evidence="ECO:0000269|PubMed:24316736"; MUTAGEN 129; /note="S->L: No effect on activity, when assayed in a Sic1-SCF-cdc4 ubiquitination assay."; /evidence="ECO:0000269|PubMed:24316736"; MUTAGEN 129; /note="S->R: Complete loss of activity, when assayed in a Sic1-SCF-cdc4 ubiquitination assay."; /evidence="ECO:0000269|PubMed:24316736"; MUTAGEN 133; /note="E->R: No effect on activity, when assayed in a Sic1-SCF-cdc4 ubiquitination assay."; /evidence="ECO:0000269|PubMed:24316736"; MUTAGEN 138; /note="S->A: Decreases monoubiquitination of NFKBIA and inhibits polyubiquitination of NFKBIA."; /evidence="ECO:0000269|PubMed:17698585"; MUTAGEN 143; /note="D->A: Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-149; A-150 and A-153."; /evidence="ECO:0000269|PubMed:17698585"; MUTAGEN 147; /note="M->A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-149; A-150 and A-153."; /evidence="ECO:0000269|PubMed:17698585"; MUTAGEN 149; /note="R->A: Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-147; A-150 and A-153."; /evidence="ECO:0000269|PubMed:17698585"; MUTAGEN 150; /note="K->A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-153."; /evidence="ECO:0000269|PubMed:17698585"; MUTAGEN 153; /note="E->A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-150."; /evidence="ECO:0000269|PubMed:17698585"; MUTAGEN 203; /note="S->A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-222; A-231; A-233 and A-236."; /evidence="ECO:0000269|PubMed:11546811"; MUTAGEN 222; /note="S->A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-231; A-233 and A-236."; /evidence="ECO:0000269|PubMed:11546811"; MUTAGEN 231; /note="S->A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-233 and A-236."; /evidence="ECO:0000269|PubMed:11546811, ECO:0000269|PubMed:12037680"; MUTAGEN 233; /note="T->A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-236."; /evidence="ECO:0000269|PubMed:11546811"; MUTAGEN 236; /note="S->A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-233."; /evidence="ECO:0000269|PubMed:11546811
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:38326650}.
uniprot
proteins
post_translational_modification
PTM: Autoubiquitinated (PubMed:11805320, PubMed:12060736, PubMed:22496338). Autoubiquitination is promoted by the human herpes virus 1 protein ICP0 and leads to degradation by the Ubiquitin-proteasomal pathway (PubMed:11805320, PubMed:12060736). {ECO:0000269|PubMed:11805320, ECO:0000269|PubMed:12060736, ECO:0000269|PubMed:22496338}.; PTM: Phosphorylated by CK2. Phosphorylation of the C-terminal tail by CK2 controls the nuclear localization. {ECO:0000269|PubMed:11546811, ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:17461777}.
uniprot
proteins
protein_family
Ubiquitin-conjugating enzyme family
uniprot
proteins
pubmed
10329681
uniprot
proteins
pubmed
10373550
uniprot
proteins
pubmed
10769200
uniprot
proteins
pubmed
10871850
uniprot
proteins
pubmed
10918611
uniprot
proteins
pubmed
11447293
uniprot
proteins
pubmed
11546811
uniprot
proteins
pubmed
11675391
uniprot
proteins
pubmed
11805320
uniprot
proteins
pubmed
12037680
uniprot
proteins
pubmed
12060736
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15652359
uniprot
proteins
pubmed
17461777
uniprot
proteins
pubmed
17588522
uniprot
proteins
pubmed
17698585
uniprot
proteins
pubmed
18851830
uniprot
proteins
pubmed
19112177
uniprot
proteins
pubmed
19126550
uniprot
proteins
pubmed
19945379
uniprot
proteins
pubmed
20061386
uniprot
proteins
pubmed
20347421
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21683433
uniprot
proteins
pubmed
22496338
uniprot
proteins
pubmed
24316736
uniprot
proteins
pubmed
38326650
uniprot
proteins
pubmed
8248134
uniprot
proteins
sequence_length
236
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: 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.
uniprot
proteins