RBX1

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RBX1
Dostupne strukture
PDBPretraga Human UniProta: PDBe RCSB
Spisak PDB ID kodova

1LDJ, 1LDK, 1U6G, 2HYE, 2LGV, 3DPL, 3DQV, 3RTR, 4F52, 4P5O

Identifikatori
AliasiRBX1
Vanjski ID-jeviOMIM: 603814 MGI: 3710517 HomoloGene: 6872 GeneCards: RBX1
Lokacija gena (čovjek)
Hromosom 22 (čovjek)
Hrom.Hromosom 22 (čovjek)[1]
Hromosom 22 (čovjek)
Genomska lokacija za RBX1
Genomska lokacija za RBX1
Bend22q13.2Početak40,951,347 bp[1]
Kraj40,973,309 bp[1]
Obrazac RNK ekspresije
Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija cullin family protein binding
GO:1904264, GO:1904822, GO:0090622, GO:0090302 ubiquitin protein ligase activity
zinc ion binding
metal ion binding
ubiquitin-ubiquitin ligase activity
GO:0001948, GO:0016582 protein binding
ubiquitin protein ligase binding
GO:0050372 ubiquitin-protein transferase activity
NEDD8 transferase activity
transcription factor binding
transferase activity
GO:0032403 protein-containing complex binding
Ćelijska komponenta citoplazma
cullin-RING ubiquitin ligase complex
citosol
SCF ubiquitin ligase complex
VCB complex
Cul2-RING ubiquitin ligase complex
Cul3-RING ubiquitin ligase complex
Cul5-RING ubiquitin ligase complex
Cul7-RING ubiquitin ligase complex
Cul4A-RING E3 ubiquitin ligase complex
Cul4B-RING E3 ubiquitin ligase complex
Jedro
Nukleoplazma
nuclear SCF ubiquitin ligase complex
Cul4-RING E3 ubiquitin ligase complex
Biološki proces nucleotide-excision repair, DNA damage recognition
protein monoubiquitination
MAPK cascade
cellular response to DNA damage stimulus
protein neddylation
global genome nucleotide-excision repair
GO:0044257 protein catabolic process
regulation of transcription from RNA polymerase II promoter in response to hypoxia
transcription-coupled nucleotide-excision repair
nucleotide-excision repair, DNA incision
negative regulation of canonical Wnt signaling pathway
nucleotide-excision repair, preincision complex stabilization
GO:0100026 Popravka DNK
GO:0022415 viral process
protein polyubiquitination
nucleotide-excision repair, preincision complex assembly
nucleotide-excision repair, DNA incision, 5'-to lesion
Wnt-signalni put
SCF complex assembly
negative regulation of G2/M transition of mitotic cell cycle
Posttranslacione modifikacije
positive regulation of proteasomal ubiquitin-dependent protein catabolic process
interleukin-1-mediated signaling pathway
protein ubiquitination
SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
proteasome-mediated ubiquitin-dependent protein catabolic process
ubiquitin-dependent protein catabolic process
nucleotide-excision repair, DNA duplex unwinding
nucleotide-excision repair, DNA incision, 3'-to lesion
Izvori:Amigo / QuickGO
Ortolozi
VrsteČovjekMiš
Entrez
Ensembl
UniProt
RefSeq (mRNK)

NM_014248

XM_006525232
XM_006536722
XM_006537452

RefSeq (bjelančevina)

NP_055063

n/a

Lokacija (UCSC)Chr 22: 40.95 – 40.97 Mbn/a
PubMed pretraga[2][3]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/uredi – miš

RING-kutijski protein 1 jest protein koji je kod ljudi kodiran genom RBX1 sa hromosoma 22.[4][5]

Aminokiselinska sekvenca[uredi | uredi izvor]

Dužina polipeptidnog lanca je aminokiselina, a molekulska težina 108 12.274 Da.[6]

1020304050
MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIM
DLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNRE
WEFQKYGH

Funkcija[uredi | uredi izvor]

Ovaj gen kodira evolucijski konzervirani protein koji je u interakciji sa kulinima. Protein ima jedinstvenu ulogu u reakciji [[ubikvitin]acije heterodimerizacijom sa kulinom-1, da bi katalizirao polimerizaciju ubikvitina. Također može biti uključen i u regulaciju prometa proteina.[6]

Interakcije[uredi | uredi izvor]

Pokazalo se da je RBX1 u interakciji sa:

Reference[uredi | uredi izvor]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100387 - Ensembl, maj 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Kamura T, Koepp DM, Conrad MN, Skowyra D, Moreland RJ, Iliopoulos O, Lane WS, Kaelin WG, Elledge SJ, Conaway RC, Harper JW, Conaway JW (Apr 1999). "Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase". Science. 284 (5414): 657–61. doi:10.1126/science.284.5414.657. PMID 10213691.
  5. ^ a b c d e Ohta T, Michel JJ, Schottelius AJ, Xiong Y (Apr 1999). "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity". Molecular Cell. 3 (4): 535–41. doi:10.1016/S1097-2765(00)80482-7. PMID 10230407.
  6. ^ a b "Entrez Gene: RBX1 ring-box 1".
  7. ^ a b Min KW, Hwang JW, Lee JS, Park Y, Tamura TA, Yoon JB (May 2003). "TIP120A associates with cullins and modulates ubiquitin ligase activity". The Journal of Biological Chemistry. 278 (18): 15905–10. doi:10.1074/jbc.M213070200. PMID 12609982.
  8. ^ a b c Kim AY, Bommeljé CC, Lee BE, Yonekawa Y, Choi L, Morris LG, Huang G, Kaufman A, Ryan RJ, Hao B, Ramanathan Y, Singh B (Nov 2008). "SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation". The Journal of Biological Chemistry. 283 (48): 33211–20. doi:10.1074/jbc.M804440200. PMC 2586271. PMID 18826954.
  9. ^ a b c d Dias DC, Dolios G, Wang R, Pan ZQ (Dec 2002). "CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16601–6. doi:10.1073/pnas.252646399. PMC 139190. PMID 12481031.
  10. ^ Kim J, Kim JH, Lee SH, Kim DH, Kang HY, Bae SH, Pan ZQ, Seo YS (Jul 2002). "The novel human DNA helicase hFBH1 is an F-box protein". The Journal of Biological Chemistry. 277 (27): 24530–7. doi:10.1074/jbc.M201612200. PMID 11956208.
  11. ^ Zheng N, Schulman BA, Song L, Miller JJ, Jeffrey PD, Wang P, Chu C, Koepp DM, Elledge SJ, Pagano M, Conaway RC, Conaway JW, Harper JW, Pavletich NP (Apr 2002). "Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex". Nature. 416 (6882): 703–9. doi:10.1038/416703a. PMID 11961546. S2CID 4423882.
  12. ^ Guerrero-Santoro J, Kapetanaki MG, Hsieh CL, Gorbachinsky I, Levine AS, Rapić-Otrin V (Jul 2008). "The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A". Cancer Research. 68 (13): 5014–22. doi:10.1158/0008-5472.CAN-07-6162. PMID 18593899.
  13. ^ Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA (Sep 2008). "Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation". Cell. 134 (6): 995–1006. doi:10.1016/j.cell.2008.07.022. PMC 2628631. PMID 18805092.
  14. ^ Panasyuk G, Nemazanyy I, Filonenko V, Gout I (May 2008). "Ribosomal protein S6 kinase 1 interacts with and is ubiquitinated by ubiquitin ligase ROC1". Biochemical and Biophysical Research Communications. 369 (2): 339–43. doi:10.1016/j.bbrc.2008.02.016. PMID 18279656.

Dopunska literatura[uredi | uredi izvor]

Vanjski linkovi[uredi | uredi izvor]