P49427 (UB2R1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CDC34
Synonyms:	UBCH3, UBE2R1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	236 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.8 Ref.10 Ref.14 Ref.15 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine. Ref.15
Enzyme regulation	CDC34-catalyzed polyubiquitin chain assembly activity is stimulated by the conjugation of NEDD8 to the CUL1 SCF E3 ligase complex subunit. Ref.14
Pathway	Protein modification; protein ubiquitination.
Subunit structure	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. Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.21 Ref.22 Ref.23
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. Ref.9 Ref.12
Tissue specificity	Expressed in testes during spermatogenesis to regulate repression of cAMP-induced transcription. Ref.8
Induction	Negatively regulated by the let-7 microRNA. Ref.14 Ref.24
Domain	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. Ref.9 Ref.22
Post-translational modification	Autoubiquitinated. Autoubiquitination is promoted by the human herpes virus 1 protein ICP0 and leads to degradation by the Ubiquitin-proteasomal pathway. Phosphorylated by CK2. Phosphorylation of the C-terminal tail by CK2 controles the nuclear localization. Ref.12 Ref.15 Ref.19
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.
Biophysicochemical properties	Kinetic parameters: KM=0.11 µM for beta-catenin-monoubiquin Ref.22
Sequence caution	The sequence AAC37534.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication initiation Non-traceable author statement Ref.1. Source: UniProtKB G1/S transition of mitotic cell cycle Non-traceable author statement Ref.1. Source: UniProtKB negative regulation of cAMP-mediated signaling Inferred from direct assay Ref.8. Source: UniProtKB proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.8Ref.26. Source: UniProtKB protein K48-linked ubiquitination Inferred from direct assay Ref.25. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay Ref.8Ref.25Ref.26. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CUL1	Q13616	3	EBI-975634,EBI-359390

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 236

236

Ubiquitin-conjugating enzyme E2 R1

PRO_0000082451

Regions

Region

190 – 236

47

SCF-binding

Compositional bias

200 – 236

37

Asp/Glu-rich (acidic)

Sites

Active site

93

1

Glycyl thioester intermediate

Amino acid modifications

Modified residue

203

1

Phosphoserine; by CK2 Ref.12 Ref.19

Modified residue

222

1

Phosphoserine; by CK2 Ref.12 Ref.19

Modified residue

231

1

Phosphoserine; by CK2 Ref.12 Ref.15 Ref.19

Modified residue

233

1

Phosphothreonine; by CK2 Ref.12

Modified residue

236

1

Phosphoserine; by CK2 Ref.12

Natural variations

Natural variant

227

1

D → H. Ref.3
Corresponds to variant rs16990650 [ dbSNP | Ensembl ].

VAR_021277

Experimental info

Mutagenesis

85

1

N → Q: Inhibits both mono and polyubiquitination of NFKBIA. Ref.20

Mutagenesis

87

1

Y → A: Decreases polyubiquitination of NFKBIA. Ref.20

Mutagenesis

93

1

C → S or A: Loss of function. Ref.7 Ref.15

Mutagenesis

95

1

S → D: Inhibits both mono and polyubiquitination of NFKBIA. Ref.20

Mutagenesis

97

1

L → S: Loss of function. Ref.15

Mutagenesis

102

1

D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-103. Ref.20

Mutagenesis

103

1

D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-102. Ref.20

Mutagenesis

108

1

E → A: Inhibits both mono and polyubiquitination of NFKBIA; when associated with A-112. Ref.20

Mutagenesis

112

1

E → A: Inhibits both mono andpolyubiquitination of NFKBIA; when associated with A-108. Ref.20

Mutagenesis

138

1

S → A: Decreases monoubiquitination of NFKBIA and inhibits polyubiquitination of NFKBIA. Ref.20

Mutagenesis

143

1

D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-149; A-150 and A-153. Ref.20

Mutagenesis

147

1

M → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-149; A-150 and A-153. Ref.20

Mutagenesis

149

1

R → A: Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-147; A-150 and A-153. Ref.20

Mutagenesis

150

1

K → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-153. Ref.20

Mutagenesis

153

1

E → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-150. Ref.20

Mutagenesis

203

1

S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-222; A-231; A-233 and A-236. Ref.12

Mutagenesis

222

1

S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-231; A-233 and A-236. Ref.12

Mutagenesis

231

1

S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-233 and A-236. Ref.12 Ref.15

Mutagenesis

233

1

T → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-236. Ref.12

Mutagenesis

236

1

S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-233. Ref.12

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

236

Helix Strand Turn

Details...

Helix

8 – 22

15

Beta strand

28 – 32

5

Beta strand

40 – 46

7

Turn

52 – 55

4

Beta strand

57 – 63

7

Turn

66 – 69

4

Beta strand

74 – 79

6

Beta strand

90 – 92

3

Helix

94 – 97

4

Helix

120 – 132

13

Helix

142 – 153

12

Turn

154 – 156

3

Helix

160 – 178

19

Sequences

	Sequence		Length	Mass (Da)
	P49427 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 258960666B589DB3	FASTA	236	26,737
	10 20 30 40 50 60 MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN TYYEGGYFKA 70 80 90 100 110 120 RLKFPIDYPY SPPAFRFLTK MWHPNIYETG DVCISILHPP VDDPQSGELP SERWNPTQNV 130 140 150 160 170 180 RTILLSVISL LNEPNTFSPA NVDASVMYRK WKESKGKDRE YTDIIRKQVL GTKVDAERDG 190 200 210 220 230 VKVPTTLAEY CVKTKAPAPD EGSDLFYDDY YEDGEVEEEA DSCFGDDEDD SGTEES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00027120.

PIR

A49630.

RefSeq

NP_004350.1. NM_004359.1.

UniGene

Hs.514997.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P49427.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37783N.

IntAct

P49427. 10 interactions.

MINT

MINT-238910.

STRING

9606.ENSP00000215574.

PTM databases

PhosphoSite

P49427.

Polymorphism databases

DMDM

2507505.

Proteomic databases

PaxDb

P49427.

PeptideAtlas

P49427.

PRIDE

P49427.

Protocols and materials databases

DNASU

997.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000215574; ENSP00000215574; ENSG00000099804.

GeneID

997.

KEGG

hsa:997.

UCSC

uc002lov.3. human.

Organism-specific databases

CTD

997.

GeneCards

GC19P000532.

HGNC

HGNC:1734. CDC34.

HPA

CAB005109.
CAB047311.
HPA002382.

MIM

116948. gene.

neXtProt

NX_P49427.

PharmGKB

PA26265.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5078.

HOGENOM

HOG000233454.

HOVERGEN

HBG063308.

InParanoid

P49427.

KO

K02207.

OMA

EYCIKSK.

OrthoDB

EOG4DBTFM.

PhylomeDB

P49427.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

Bgee

P49427.

CleanEx

HS_CDC34.

Genevestigator

P49427.

GermOnline

ENSG00000099804. Homo sapiens.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

P49427.

GenomeRNAi

997.

NextBio

4188.

SOURCE

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Entry information

Entry name

UB2R1_HUMAN

Accession

Primary (citable) accession number: P49427
Secondary accession number(s): A8K689

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.