UniProt Accession

 RD23B_HUMAN; P54727; B3KWK8; G5E9P0; Q7Z5K8; Q8WUB0 

Genbank Protein ID

 D21090; AY313777; AY165178; AK125226; AL137852; CH471105; CH471105; BC020973 

Genbank Nucleotide ID

 BAA04652.1; AAP81008.1; AAN47194.1; BAG54170.1; CAD13275.1; EAW59016.1; EAW59017.1; AAH20973.1 

Protein Name

 UV excision repair protein RAD23 homolog B 

Protein Synonyms/Alias

 HR23B; hHR23B; XP-C repair-complementing complex 58 kDa protein; p58 

Gene Name

 RAD23B 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MQVTLKTLQQQTF	ubiquitination	[1, 2, 3]
14	TLQQQTFKIDIDPEE	ubiquitination	[1, 2, 3, 4, 5, 6]
24	IDPEETVKALKEKIE	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9]
36	KIESEKGKDAFPVAG	ubiquitination	[2, 4, 5, 6, 8, 9]
45	AFPVAGQKLIYAGKI	ubiquitination	[2, 4, 5, 6, 9, 10]
51	QKLIYAGKILNDDTA	acetylation	[11]
51	QKLIYAGKILNDDTA	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14]
60	LNDDTALKEYKIDEK	ubiquitination	[1, 2, 3, 4, 5, 6, 9]
63	DTALKEYKIDEKNFV	ubiquitination	[4, 5, 6, 8, 9]
67	KEYKIDEKNFVVVMV	ubiquitination	[1, 2, 3, 4, 5, 8, 9, 10]
76	FVVVMVTKPKAVSTP	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 14]
78	VVMVTKPKAVSTPAP	ubiquitination	[6, 9]
147	ASAAKQEKPAEKPAE	ubiquitination	[4, 5, 9, 10, 14]
151	KQEKPAEKPAETPVA	ubiquitination	[4, 5, 9, 10, 14]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [9] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [10] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [11] 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]
 [12] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [13] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [14] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 

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 364 404 UBA 2.
 MOD_RES 155 155 Phosphothreonine.
 MOD_RES 160 160 Phosphoserine.
 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; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair; Nucleus; Phosphoprotein; Polymorphism; Proteasome; Reference proteome; Repeat; Ubl conjugation pathway. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 409 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
 GO:0071942; C:XPC complex; IDA:UniProtKB.
 GO:0003684; F:damaged DNA binding; IEA:InterPro.
 GO:0031593; F:polyubiquitin binding; IDA:UniProtKB.
 GO:0003697; F:single-stranded DNA binding; TAS:ProtInc.
 GO:0000715; P:nucleotide-excision repair, DNA damage recognition; IDA:UniProtKB.
 GO:0000718; P:nucleotide-excision repair, DNA damage removal; TAS:Reactome.
 GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IEA:InterPro.
 GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
 GO:0007283; P:spermatogenesis; IEA:Compara. 

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.