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Rad23b |
Protein FULL name:
UV excision repair protein RAD23 homolog B [Mus musculus].
Rad23b (Mus musculus) is product of expression of Rad23b gene.
FUNCTION: Plays a central role both in proteosomal degradation of misfolded proteins and DNA repair. Central component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulun that are retrotranslocated in the cytosol. Involved in DNA excision repair by stabilizing XPC protein. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage-processing enzymes.
SUBUNIT: Interacts with the 26S proteasome (By similarity). Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Interacts directly with NGLY1. Heterodimer of a 125 kDa subunit (p125) and of a 58 kDa subunit (p58). Interacts with MJD and XPC.
SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
SIMILARITY: Belongs to the RAD23 family.
SIMILARITY: Contains 1 STI1 domain.
SIMILARITY: Contains 2 UBA domains.
SIMILARITY: Contains 1 ubiquitin-like domain.
| NCBI GenPept GI number(s): |
171906578 |
| Species: | Mus musculus |
Links to other databases:
| Database | ID | Link |
| Uniprot | P54728 |
P54728 |
| PFAM: | - |
P54728 (Link - using uniprot id) |
| InterPro: | - |
P54728 (Link - using uniprot id) |
| CATH: | - | - |
| SCOP: | - | - |
| PDB: | - | - |
Protein sequence:
|
MQVTLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAG KILSDDTALKEYKIDEKNFVVVMVTKPKAVTTAVPATTQPSSTPSPTAVS SSPAVAAAQAPAPTPALPPTSTPASTAPASTTASSEPAPAGATQPEKPAE KPAQTPVLTSPAPADSTPGDSSRSNLFEDATSALVTGQSYENMVTEIMSM GYEREQVIAALRASFNNPDRAVEYLLMGIPGDRESQAVVDPPPQAVSTGT PQSPAVAAAAATTTATTTTTSGGHPLEFLRNQPQFQQMRQIIQQNPSLLP ALLQQIGRENPQLLQQISQHQEHFIQMLNEPVQEAGSQGGGGGGGGGGGG GGGGGIAEAGSGHMNYIQVTPQEKEAIERLKALGFPEGLVIQAYFACEKN ENLAANFLLQQNFDED |
Rad23b (Mus musculus) belongs to following protein families:
References:
| Title | Authors | Journal |
| Cloning, comparative mapping, and RNA expression of the mouse homologues of the Saccharomyces cerevisiae nucleotide excision repair gene RAD23. | van der Spek PJ, Visser CE, Hanaoka F, Smit B, Hagemeijer A, Bootsma D, Hoeijmakers JH | Genomics Feb. 1, 1996 |
| Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation. | Park H, Suzuki T, Lennarz WJ | Proc Natl Acad Sci U S A Sept. 25, 2001 |
| A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins. | Katiyar S, Li G, Lennarz WJ | Proc Natl Acad Sci U S A Sept. 21, 2004 |
| The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). | Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J | Genome Res Oct. 1, 2004 |
| Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome. | Li G, Zhou X, Zhao G, Schindelin H, Lennarz WJ | Proc Natl Acad Sci U S A Nov. 1, 2005 |
| The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor. | Li G, Zhao G, Zhou X, Schindelin H, Lennarz WJ | Proc Natl Acad Sci U S A May 1, 2006 |
| Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways. | Zhao G, Zhou X, Wang L, Li G, Kisker C, Lennarz WJ, Schindelin H | J Biol Chem May 12, 2006 |
Last modification of this entry: Oct. 6, 2010.
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