CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008886
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 UV excision repair protein RAD23 homolog B 
Protein Synonyms/Alias
 HR23B; mHR23B; XP-C repair-complementing complex 58 kDa protein; p58 
Gene Name
 Rad23b 
Gene Synonyms/Alias
 Mhr23b 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
6**MQVTLKTLQQQTFubiquitination[1]
14TLQQQTFKIDIDPEEubiquitination[1]
24IDPEETVKALKEKIEubiquitination[1]
36KIESEKGKDAFPVAGubiquitination[1]
45AFPVAGQKLIYAGKIubiquitination[1]
51QKLIYAGKILSDDTAacetylation[2, 3, 4]
51QKLIYAGKILSDDTAubiquitination[1, 5]
60LSDDTALKEYKIDEKacetylation[2]
60LSDDTALKEYKIDEKubiquitination[1]
67KEYKIDEKNFVVVMVacetylation[2]
67KEYKIDEKNFVVVMVubiquitination[1]
76FVVVMVTKPKAVTTAacetylation[2]
76FVVVMVTKPKAVTTAubiquitination[1, 5]
78VVMVTKPKAVTTAVPubiquitination[5]
151QPEKPAEKPAQTPVLubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
 Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
 Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144] 
Functional Description
 Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum- associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. 
Sequence Annotation
 DOMAIN 1 79 Ubiquitin-like.
 DOMAIN 188 228 UBA 1.
 DOMAIN 274 317 STI1.
 DOMAIN 371 411 UBA 2.
 MOD_RES 155 155 Phosphothreonine (By similarity).
 MOD_RES 160 160 Phosphoserine (By similarity).
 MOD_RES 174 174 Phosphoserine (By similarity).
 MOD_RES 186 186 Phosphothreonine (By similarity).
 MOD_RES 199 199 Phosphoserine (By similarity).
 MOD_RES 202 202 Phosphotyrosine (By similarity).  
Keyword
 3D-structure; Complete proteome; Cytoplasm; DNA damage; DNA repair; Nucleus; Phosphoprotein; Proteasome; Reference proteome; Repeat; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 416 AA 
Protein Sequence
MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG KILSDDTALK 60
EYKIDEKNFV VVMVTKPKAV TTAVPATTQP SSTPSPTAVS SSPAVAAAQA PAPTPALPPT 120
STPASTAPAS TTASSEPAPA GATQPEKPAE KPAQTPVLTS PAPADSTPGD SSRSNLFEDA 180
TSALVTGQSY ENMVTEIMSM GYEREQVIAA LRASFNNPDR AVEYLLMGIP GDRESQAVVD 240
PPPQAVSTGT PQSPAVAAAA ATTTATTTTT SGGHPLEFLR NQPQFQQMRQ IIQQNPSLLP 300
ALLQQIGREN PQLLQQISQH QEHFIQMLNE PVQEAGSQGG GGGGGGGGGG GGGGGIAEAG 360
SGHMNYIQVT PQEKEAIERL KALGFPEGLV IQAYFACEKN ENLAANFLLQ QNFDED 416 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
 GO:0071942; C:XPC complex; ISS:UniProtKB.
 GO:0003684; F:damaged DNA binding; IEA:InterPro.
 GO:0000715; P:nucleotide-excision repair, DNA damage recognition; IEA:Compara.
 GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IEA:InterPro.
 GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Compara.
 GO:0006974; P:response to DNA damage stimulus; IDA:MGI.
 GO:0007283; P:spermatogenesis; IMP:MGI. 
Interpro
 IPR004806; Rad23.
 IPR006636; STI1_HS-bd.
 IPR009060; UBA-like.
 IPR000449; UBA/transl_elong_EF1B_N.
 IPR015940; UBA/transl_elong_EF1B_N_euk.
 IPR000626; Ubiquitin.
 IPR019955; Ubiquitin_supergroup.
 IPR015360; XPC-bd. 
Pfam
 PF00627; UBA
 PF00240; ubiquitin
 PF09280; XPC-binding 
SMART
 SM00727; STI1
 SM00165; UBA
 SM00213; UBQ 
PROSITE
 PS50030; UBA
 PS00299; UBIQUITIN_1
 PS50053; UBIQUITIN_2 
PRINTS
 PR01839; RAD23PROTEIN.