UBE4B

Protein-coding gene in the species Homo sapiens
UBE4B
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2KRE, 3L1X, 3L1Z

Identifiers
AliasesUBE4B, E4, HDNB1, UBOX3, UFD2, UFD2A, ubiquitination factor E4B
External IDsOMIM: 613565; MGI: 1927086; HomoloGene: 107623; GeneCards: UBE4B; OMA:UBE4B - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for UBE4B
Genomic location for UBE4B
Band1p36.22Start10,032,832 bp[1]
End10,181,239 bp[1]
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)[2]
Chromosome 4 (mouse)
Genomic location for UBE4B
Genomic location for UBE4B
Band4 E2|4 79.08 cMStart149,328,416 bp[2]
End149,426,749 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • buccal mucosa cell

  • skin of thigh

  • hair follicle

  • cerebellar hemisphere

  • right hemisphere of cerebellum

  • gastric mucosa

  • gastrocnemius muscle

  • inferior olivary nucleus

  • Skeletal muscle tissue of rectus abdominis

  • right adrenal cortex
Top expressed in
  • tail of embryo

  • genital tubercle

  • secondary oocyte

  • zygote

  • internal carotid artery

  • external carotid artery

  • yolk sac

  • facial motor nucleus

  • renal corpuscle

  • ureter
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • ubiquitin protein ligase activity
  • ATPase binding
  • ubiquitin-protein transferase activity
  • enzyme binding
  • ATP binding
  • transferase activity
  • ubiquitin-ubiquitin ligase activity
  • protein binding
Cellular component
  • ubiquitin ligase complex
  • nucleus
  • cytoplasm
Biological process
  • protein monoubiquitination
  • response to endoplasmic reticulum stress
  • ventricular trabecula myocardium morphogenesis
  • protein ubiquitination
  • neuron projection development
  • granzyme-mediated apoptotic signaling pathway
  • response to UV
  • proteasome-mediated ubiquitin-dependent protein catabolic process
  • protein autoubiquitination
  • protein polyubiquitination
  • ubiquitin-dependent ERAD pathway
  • ubiquitin-dependent protein catabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10277

63958

Ensembl

ENSG00000130939

ENSMUSG00000028960

UniProt

O95155

Q9ES00

RefSeq (mRNA)

NM_001105562
NM_006048

NM_022022

RefSeq (protein)

NP_001099032
NP_006039

NP_071305
NP_001391797
NP_001391798

Location (UCSC)Chr 1: 10.03 – 10.18 MbChr 4: 149.33 – 149.43 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ubiquitin conjugation factor E4 B is a protein that in humans is encoded by the UBE4B gene.[5][6][7]

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 an additional conjugation factor, E4, which is involved in multiubiquitin chain assembly. This gene is also the strongest candidate in the neuroblastoma tumor suppressor genes.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000130939 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028960 – 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. ^ Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Dec 1998). "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 5 (3): 169–76. doi:10.1093/dnares/5.3.169. PMID 9734811.
  6. ^ Koegl M, Hoppe T, Schlenker S, Ulrich HD, Mayer TU, Jentsch S (Apr 1999). "A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly". Cell. 96 (5): 635–44. doi:10.1016/S0092-8674(00)80574-7. PMID 10089879.
  7. ^ a b "Entrez Gene: UBE4B ubiquitination factor E4B (UFD2 homolog, yeast)".

Further reading

  • Onyango P, Lubyova B, Gardellin P, et al. (1998). "Molecular cloning and expression analysis of five novel genes in chromosome 1p36". Genomics. 50 (2): 187–98. doi:10.1006/geno.1997.5186. PMID 9653645.
  • Ohira M, Kageyama H, Mihara M, et al. (2000). "Identification and characterization of a 500-kb homozygously deleted region at 1p36.2-p36.3 in a neuroblastoma cell line". Oncogene. 19 (37): 4302–7. doi:10.1038/sj.onc.1203786. PMID 10980605. S2CID 24163907.
  • Mahoney JA, Odin JA, White SM, et al. (2002). "The human homologue of the yeast polyubiquitination factor Ufd2p is cleaved by caspase 6 and granzyme B during apoptosis". Biochem. J. 361 (Pt 3): 587–95. doi:10.1042/0264-6021:3610587. PMC 1222341. PMID 11802788.
  • 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.
  • Kaneko C, Hatakeyama S, Matsumoto M, et al. (2003). "Characterization of the mouse gene for the U-box-type ubiquitin ligase UFD2a". Biochem. Biophys. Res. Commun. 300 (2): 297–304. doi:10.1016/S0006-291X(02)02834-6. PMID 12504083.
  • Krona C, Ejeskär K, Abel F, et al. (2003). "Screening for gene mutations in a 500 kb neuroblastoma tumor suppressor candidate region in chromosome 1p; mutation and stage-specific expression in UBE4B/UFD2". Oncogene. 22 (15): 2343–51. doi:10.1038/sj.onc.1206324. PMID 12700669. S2CID 7749013.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Okumura F, Hatakeyama S, Matsumoto M, et al. (2005). "Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesis". J. Biol. Chem. 279 (51): 53533–43. doi:10.1074/jbc.M402916200. PMID 15466860.
  • 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.
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
  • Spinette S, Mahoney JA, Rosen A (2006). "The MPAC domain is a novel mitotically regulated domain, removed by apoptotic protease cleavage during cell death". Biochem. Biophys. Res. Commun. 347 (4): 1103–12. doi:10.1016/j.bbrc.2006.06.194. PMID 16870146.
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.


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