Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P49427 (UB2R1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Protein existenceEvidence 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 ICERIIgammaand 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 processCell cycle
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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

cellular protein modification process

Non-traceable author statement Ref.1. Source: UniProtKB

negative regulation of cAMP-mediated signaling

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of inclusion body assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

proteasome-mediated 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

protein polyubiquitination

Inferred from direct assay Ref.26. Source: UniProtKB

protein ubiquitination

Inferred from direct assay Ref.8. Source: UniProtKB

response to growth factor

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleus

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay Ref.8Ref.25Ref.26. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CUL1Q136163EBI-975634,EBI-359390

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 236236Ubiquitin-conjugating enzyme E2 R1
PRO_0000082451

Regions

Region190 – 23647SCF-binding
Compositional bias200 – 23637Asp/Glu-rich (acidic)

Sites

Active site931Glycyl thioester intermediate

Amino acid modifications

Modified residue2031Phosphoserine; by CK2 Ref.12 Ref.19
Modified residue2221Phosphoserine; by CK2 Ref.12 Ref.19
Modified residue2311Phosphoserine; by CK2 Ref.12 Ref.15 Ref.19
Modified residue2331Phosphothreonine; by CK2 Ref.12
Modified residue2361Phosphoserine; by CK2 Ref.12

Natural variations

Natural variant2271D → H. Ref.3
Corresponds to variant rs16990650 [ dbSNP | Ensembl ].
VAR_021277

Experimental info

Mutagenesis851N → Q: Inhibits both mono and polyubiquitination of NFKBIA. Ref.20
Mutagenesis871Y → A: Decreases polyubiquitination of NFKBIA. Ref.20
Mutagenesis931C → S or A: Loss of function. Ref.7 Ref.15
Mutagenesis951S → D: Inhibits both mono and polyubiquitination of NFKBIA. Ref.20
Mutagenesis971L → S: Loss of function. Ref.15
Mutagenesis1021D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-103. Ref.20
Mutagenesis1031D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-102. Ref.20
Mutagenesis1081E → A: Inhibits both mono and polyubiquitination of NFKBIA; when associated with A-112. Ref.20
Mutagenesis1121E → A: Inhibits both mono andpolyubiquitination of NFKBIA; when associated with A-108. Ref.20
Mutagenesis1381S → A: Decreases monoubiquitination of NFKBIA and inhibits polyubiquitination of NFKBIA. Ref.20
Mutagenesis1431D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-149; A-150 and A-153. Ref.20
Mutagenesis1471M → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-149; A-150 and A-153. Ref.20
Mutagenesis1491R → A: Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-147; A-150 and A-153. Ref.20
Mutagenesis1501K → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-153. Ref.20
Mutagenesis1531E → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-150. Ref.20
Mutagenesis2031S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-222; A-231; A-233 and A-236. Ref.12
Mutagenesis2221S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-231; A-233 and A-236. Ref.12
Mutagenesis2311S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-233 and A-236. Ref.12 Ref.15
Mutagenesis2331T → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-236. Ref.12
Mutagenesis2361S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-233. Ref.12

Secondary structure

.......................... 236
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49427 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 258960666B589DB3

FASTA23626,737
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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

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.
CCDSCCDS12030.1.
PIRA49630.
RefSeqNP_004350.1. NM_004359.1.
UniGeneHs.514997.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OB4X-ray2.40A7-184[»]
3RZ3X-ray2.30A/B/C/D7-184[»]
4MDKX-ray2.61A/B/C/D7-184[»]
ProteinModelPortalP49427.
SMRP49427. Positions 7-184.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107432. 52 interactions.
DIPDIP-37783N.
IntActP49427. 11 interactions.
MINTMINT-238910.
STRING9606.ENSP00000215574.

PTM databases

PhosphoSiteP49427.

Polymorphism databases

DMDM2507505.

Proteomic databases

MaxQBP49427.
PaxDbP49427.
PeptideAtlasP49427.
PRIDEP49427.

Protocols and materials databases

DNASU997.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215574; ENSP00000215574; ENSG00000099804.
GeneID997.
KEGGhsa:997.
UCSCuc002lov.3. human.

Organism-specific databases

CTD997.
GeneCardsGC19P000532.
HGNCHGNC:1734. CDC34.
HPACAB005109.
CAB047311.
HPA002382.
MIM116948. gene.
neXtProtNX_P49427.
PharmGKBPA26265.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233454.
HOVERGENHBG063308.
InParanoidP49427.
KOK02207.
OMARVNLVDE.
OrthoDBEOG7VB2HT.
PhylomeDBP49427.
TreeFamTF101107.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP49427.
UniPathwayUPA00143.

Gene expression databases

BgeeP49427.
CleanExHS_CDC34.
GenevestigatorP49427.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP49427.
GeneWikiCDC34.
GenomeRNAi997.
NextBio4188.
PROP49427.
SOURCESearch...

Entry information

Entry nameUB2R1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM