UBE2B

Protein-coding gene in the species Homo sapiens
UBE2B
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1JAS, 2Y4W, 2YB6, 2YBF

Identifiers
AliasesUBE2B, E2-17kDa, HHR6B, HR6B, RAD6B, UBC2, ubiquitin conjugating enzyme E2 B
External IDsOMIM: 179095; MGI: 102944; HomoloGene: 101298; GeneCards: UBE2B; OMA:UBE2B - orthologs
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for UBE2B
Genomic location for UBE2B
Band5q31.1Start134,371,184 bp[1]
End134,392,108 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for UBE2B
Genomic location for UBE2B
Band11|11 B1.3Start51,876,324 bp[2]
End51,891,589 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • muscle of thigh

  • gastrocnemius muscle

  • Skeletal muscle tissue of rectus abdominis

  • right lung

  • right auricle

  • biceps brachii

  • body of pancreas

  • Descending thoracic aorta

  • anterior pituitary

  • ganglionic eminence
Top expressed in
  • intercostal muscle

  • medial head of gastrocnemius muscle

  • muscle of thigh

  • quadriceps femoris muscle

  • triceps brachii muscle

  • vastus lateralis muscle

  • sternocleidomastoid muscle

  • temporal muscle

  • atrioventricular valve

  • arcuate nucleus
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • nucleotide binding
  • ubiquitin protein ligase activity
  • ubiquitin-protein transferase activity
  • protein binding
  • ATP binding
  • ubiquitin conjugating enzyme activity
  • ubiquitin protein ligase binding
Cellular component
  • cytoplasm
  • membrane
  • plasma membrane
  • replication fork
  • HULC complex
  • nucleoplasm
  • XY body
  • chromatin
  • nucleus
Biological process
  • chiasma assembly
  • histone H2A ubiquitination
  • negative regulation of cAMP-mediated signaling
  • postreplication repair
  • ubiquitin-dependent protein catabolic process
  • protein K63-linked ubiquitination
  • meiotic telomere clustering
  • positive regulation of reciprocal meiotic recombination
  • protein stabilization
  • protein polyubiquitination
  • negative regulation of apoptotic process
  • in utero embryonic development
  • protein monoubiquitination
  • sperm axoneme assembly
  • cellular response to DNA damage stimulus
  • protein K11-linked ubiquitination
  • histone lysine demethylation
  • protein K48-linked ubiquitination
  • regulation of histone modification
  • spermatogenesis
  • canonical Wnt signaling pathway
  • synaptonemal complex organization
  • response to UV
  • proteasome-mediated ubiquitin-dependent protein catabolic process
  • protein autoubiquitination
  • DNA repair
  • protein ubiquitination
  • positive regulation of canonical Wnt signaling pathway
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7320

22210

Ensembl

ENSG00000119048

ENSMUSG00000020390

UniProt

P63146

P63147

RefSeq (mRNA)

NM_003337

NM_009458
NM_001362685
NM_001362686

RefSeq (protein)

NP_003328

NP_033484
NP_001349614
NP_001349615

Location (UCSC)Chr 5: 134.37 – 134.39 MbChr 11: 51.88 – 51.89 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ubiquitin-conjugating enzyme E2 B is a protein that in humans is encoded by the UBE2B gene.[5][6]

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is required for post-replicative DNA damage repair. Its protein sequence is 100% identical to the mouse, rat, and rabbit homologs, which indicates that this enzyme is highly conserved in eukaryotic evolution.[6]

Interactions

UBE2B has been shown to interact with RAD18.[7][8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000119048 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020390 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Koken MH, Smit EM, Jaspers-Dekker I, Oostra BA, Hagemeijer A, Bootsma D, Hoeijmakers JH (May 1992). "Localization of two human homologs, HHR6A and HHR6B, of the yeast DNA repair gene RAD6 to chromosomes Xq24-q25 and 5q23-q31". Genomics. 12 (3): 447–53. doi:10.1016/0888-7543(92)90433-S. hdl:1765/3036. PMID 1559696.
  6. ^ a b "Entrez Gene: UBE2B ubiquitin-conjugating enzyme E2B (RAD6 homolog)".
  7. ^ Xin H, Lin W, Sumanasekera W, Zhang Y, Wu X, Wang Z (July 2000). "The human RAD18 gene product interacts with HHR6A and HHR6B". Nucleic Acids Res. 28 (14). ENGLAND: 2847–54. doi:10.1093/nar/28.14.2847. PMC 102657. PMID 10908344.
  8. ^ Tateishi S, Sakuraba Y, Masuyama S, Inoue H, Yamaizumi M (July 2000). "Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens". Proc. Natl. Acad. Sci. U.S.A. 97 (14). UNITED STATES: 7927–32. Bibcode:2000PNAS...97.7927T. doi:10.1073/pnas.97.14.7927. ISSN 0027-8424. PMC 16647. PMID 10884424.

Further reading

  • Koken MH, Reynolds P, Jaspers-Dekker I, et al. (1991). "Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6". Proc. Natl. Acad. Sci. U.S.A. 88 (20): 8865–9. Bibcode:1991PNAS...88.8865K. doi:10.1073/pnas.88.20.8865. PMC 52611. PMID 1717990.
  • Woffendin C, Chen ZY, Staskus K, et al. (1991). "Mammalian mRNAs encoding protein closely related to ubiquitin-conjugating enzyme encoded by yeast DNA repair gene RAD6". Biochim. Biophys. Acta. 1090 (1): 81–5. doi:10.1016/0167-4781(91)90039-o. PMID 1883845.
  • Schneider R, Eckerskorn C, Lottspeich F, Schweiger M (1990). "The human ubiquitin carrier protein E2(Mr = 17,000) is homologous to the yeast DNA repair gene RAD6". EMBO J. 9 (5): 1431–5. doi:10.1002/j.1460-2075.1990.tb08259.x. PMC 551831. PMID 2158443.
  • Koken MH, Hoogerbrugge JW, Jasper-Dekker I, et al. (1996). "Expression of the ubiquitin-conjugating DNA repair enzymes HHR6A and B suggests a role in spermatogenesis and chromatin modification". Dev. Biol. 173 (1): 119–32. doi:10.1006/dbio.1996.0011. hdl:1765/3093. PMID 8575614.
  • Tateishi S, Sakuraba Y, Masuyama S, et al. (2000). "Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens". Proc. Natl. Acad. Sci. U.S.A. 97 (14): 7927–32. Bibcode:2000PNAS...97.7927T. doi:10.1073/pnas.97.14.7927. PMC 16647. PMID 10884424.
  • Xin H, Lin W, Sumanasekera W, et al. (2000). "The human RAD18 gene product interacts with HHR6A and HHR6B". Nucleic Acids Res. 28 (14): 2847–54. doi:10.1093/nar/28.14.2847. PMC 102657. PMID 10908344.
  • Miura T, Klaus W, Ross A, et al. (2003). "The NMR structure of the class I human ubiquitin-conjugating enzyme 2b". J. Biomol. NMR. 22 (1): 89–92. doi:10.1023/A:1013807519703. PMID 11885984. S2CID 27799378.
  • Shekhar MP, Lyakhovich A, Visscher DW, et al. (2002). "Rad6 overexpression induces multinucleation, centrosome amplification, abnormal mitosis, aneuploidy, and transformation". Cancer Res. 62 (7): 2115–24. PMID 11929833.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Kwon YT, Xia Z, An JY, et al. (2003). "Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway". Mol. Cell. Biol. 23 (22): 8255–71. doi:10.1128/MCB.23.22.8255-8271.2003. PMC 262401. PMID 14585983.
  • Lyakhovich A, Shekhar MP (2004). "RAD6B overexpression confers chemoresistance: RAD6 expression during cell cycle and its redistribution to chromatin during DNA damage-induced response". Oncogene. 23 (17): 3097–106. doi:10.1038/sj.onc.1207449. PMID 14981545. S2CID 6180818.
  • Watanabe K, Tateishi S, Kawasuji M, et al. (2005). "Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination". EMBO J. 23 (19): 3886–96. doi:10.1038/sj.emboj.7600383. PMC 522788. PMID 15359278.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
  • Shekhar MP, Tait L, Gerard B (2007). "Essential role of T-cell factor/beta-catenin in regulation of Rad6B: a potential mechanism for Rad6B overexpression in breast cancer cells". Mol. Cancer Res. 4 (10): 729–45. doi:10.1158/1541-7786.MCR-06-0136. PMID 17050667.
  • v
  • t
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  • 1jas: HsUbc2b
    1jas: HsUbc2b
  • v
  • t
  • e
Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targeting
Ubiquitin
(ubiquitylation)
Ubiquitin-like proteins
(UBL)
SUMO protein
(SUMOylation)
  • E1 SUMO-activating enzyme
  • E2 SUMO-conjugating enzyme
Other


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