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Identification
HMDB Protein ID HMDBP09289
Secondary Accession Numbers
  • 15119
Name Ubiquitin-conjugating enzyme E2 R2
Synonyms
  1. Ubiquitin carrier protein R2
  2. Ubiquitin-conjugating enzyme E2-CDC34B
  3. Ubiquitin-protein ligase R2
Gene Name UBE2R2
Protein Type Enzyme
Biological Properties
General Function Involved in acid-amino acid ligase activity
Specific Function Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. May be involved in degradation of katenin.
Pathways
  • Herpes simplex virus 1 infection
  • protein ubiquitination
  • Ubiquitin mediated proteolysis
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysine details
GO Classification
Biological Process
protein K48-linked ubiquitination
protein monoubiquitination
Function
catalytic activity
small conjugating protein ligase activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
acid-amino acid ligase activity
Molecular Function
ubiquitin-protein ligase activity
ATP binding
Process
metabolic process
regulation of protein metabolic process
macromolecule metabolic process
biological regulation
regulation of biological process
regulation of metabolic process
regulation of macromolecule metabolic process
post-translational protein modification
macromolecule modification
protein modification process
Cellular Location Not Available
Gene Properties
Chromosome Location 9
Locus 9p13.3
SNPs UBE2R2
Gene Sequence
>717 bp
ATGGCCCAGCAGCAGATGACCAGCTCGCAGAAGGCCCTGATGCTCGAGCTGAAATCCCTG
CAGGAGGAACCGGTGGAGGGCTTCCGGATCACCCTGGTGGACGAGTCCGACCTCTACAAC
TGGGAGGTGGCCATCTTCGGACCCCCCAACACCCTCTACGAAGGCGGCTACTTCAAGGCG
CATATTAAATTTCCTATTGACTACCCCTATTCACCACCTACCTTCAGATTCTTGACCAAA
ATGTGGCACCCCAACATTTATGAGAATGGAGATGTATGCATTTCGATTCTTCATCCGCCT
GTAGATGACCCACAGAGTGGAGAACTGCCTTCTGAAAGGTGGAATCCTACTCAGAATGTG
AGGACTATCCTATTAAGTGTAATCTCACTGCTTAATGAGCCCAACACCTTCTCCCCAGCC
AATGTCGATGCTTCAGTTATGTTCAGGAAATGGAGAGACAGTAAAGGAAAAGACAAAGAA
TATGCTGAAATTATTAGGAAACAAGTTTCAGCCACTAAGGCCGAAGCAGAAAAGGATGGA
GTGAAGGTCCCCACAACCCTGGCGGAATACTGCATCAAAACTAAAGTGCCTTCCAATGAC
AACAGCTCAGATTTGCTTTACGACGACTTGTATGATGACGACATTGATGATGAAGATGAG
GAGGAGGAAGATGCCGACTGTTATGATGATGATGATTCTGGGAATGAGGAGTCGTGA
Protein Properties
Number of Residues 238
Molecular Weight 27165.725
Theoretical pI 4.418
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Ubiquitin-conjugating enzyme E2 R2
MAQQQMTSSQKALMLELKSLQEEPVEGFRITLVDESDLYNWEVAIFGPPNTLYEGGYFKA
HIKFPIDYPYSPPTFRFLTKMWHPNIYENGDVCISILHPPVDDPQSGELPSERWNPTQNV
RTILLSVISLLNEPNTFSPANVDASVMFRKWRDSKGKDKEYAEIIRKQVSATKAEAEKDG
VKVPTTLAEYCIKTKVPSNDNSSDLLYDDLYDDDIDDEDEEEEDADCYDDDDSGNEES
GenBank ID Protein 17645997
UniProtKB/Swiss-Prot ID Q712K3
UniProtKB/Swiss-Prot Entry Name UB2R2_HUMAN
PDB IDs Not Available
GenBank Gene ID AJ240087
GeneCard ID UBE2R2
GenAtlas ID UBE2R2
HGNC ID HGNC:19907
References
General References
  1. 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 TO, 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: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
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  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed:15164053 ]
  5. David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. doi: 10.1074/jbc.M109.089003. Epub 2010 Jan 8. [PubMed:20061386 ]
  6. Semplici F, Meggio F, Pinna LA, Oliviero S: CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TrCP and enhances beta-catenin degradation. Oncogene. 2002 Jun 6;21(25):3978-87. [PubMed:12037680 ]