P54727 (RD23B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UV excision repair protein RAD23 homolog B
Short name=HR23B
Short name=hHR23B

Alternative name(s):
XP-C repair-complementing complex 58 kDa protein
Short name=p58

Gene names

Name:

RAD23B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.9 Ref.12 Ref.14 Ref.16 Ref.17 Ref.26 Ref.27 Ref.29 Ref.30 Ref.36 Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation. Ref.8 Ref.9 Ref.12 Ref.14 Ref.16 Ref.17 Ref.26 Ref.27 Ref.29 Ref.30 Ref.36 The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1. Ref.8 Ref.9 Ref.12 Ref.14 Ref.16 Ref.17 Ref.26 Ref.27 Ref.29 Ref.30 Ref.36
Subunit structure	Component of the XPC complex composed of XPC, RAD23B and CETN2. Interacts with NGLY1 and PSMC1. Interacts with ATXN3. Interacts with PSMD4 and PSMC5. Interacts with AMFR. Interacts with VCP; the interaction is indirect and mediated by NGLY1 By similarity. Ref.10 Ref.11 Ref.13 Ref.15 Ref.18 Ref.20 Ref.22
Subcellular location	Nucleus. Cytoplasm. Note: The intracellular distribution is cell cycle dependent. Localized to the nucleus and the cytoplasm during G1 phase. Nuclear levels decrease during S-phase; upon entering mitosis, relocalizes in the cytoplasm without association with chromatin. Ref.13 Ref.19
Domain	The ubiquitin-like domain mediates interaction with ATXN3.
Sequence similarities	Belongs to the RAD23 family. Contains 1 STI1 domain. Contains 2 UBA domains. Contains 1 ubiquitin-like domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	nucleotide-excision repair, DNA damage recognition Inferred from direct assay Ref.27. Source: UniProtKB nucleotide-excision repair, DNA damage removal Traceable author statement. Source: Reactome proteasomal ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.26. Source: UniProtKB spermatogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	XPC complex Inferred from direct assay Ref.13. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome proteasome complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	damaged DNA binding Inferred from electronic annotation. Source: InterPro polyubiquitin binding Inferred from direct assay Ref.26. Source: UniProtKB single-stranded DNA binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERCC3	P19447	2	EBI-954531,EBI-1183307
Pax3	P24610	4	EBI-954531,EBI-1208116	From a different organism.
PSMD4	P55036	5	EBI-954531,EBI-359318
XPC	Q01831	5	EBI-954531,EBI-372610

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P54727-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P54727-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Note: Highly expressed in the testis and in ejaculated spermatozoa.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 409

409

UV excision repair protein RAD23 homolog B

PRO_0000114906

Regions

Domain

1 – 79

79

Ubiquitin-like

Domain

188 – 228

41

UBA 1

Domain

274 – 317

44

STI1

Domain

364 – 404

41

UBA 2

Compositional bias

103 – 106

4

Poly-Thr

Compositional bias

254 – 260

7

Poly-Ala

Compositional bias

261 – 269

9

Poly-Thr

Compositional bias

336 – 348

13

Poly-Gly

Amino acid modifications

Modified residue

155

1

Phosphothreonine Ref.23

Modified residue

160

1

Phosphoserine Ref.25 Ref.28 Ref.31 Ref.33

Natural variations

Alternative sequence

1 – 72

72

Missing in isoform 2.

VSP_045606

Natural variant

249

1

A → V. Ref.2 Ref.3 Ref.7
Corresponds to variant rs1805329 [ dbSNP | Ensembl ].

VAR_014350

Experimental info

Mutagenesis

6

1

K → A: Impairs interaction with EEF1A1. Ref.22

Secondary structure

1

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409

Helix Strand Turn

Details...

Beta strand

1 – 7

7

Beta strand

12 – 17

6

Helix

23 – 34

12

Turn

36 – 38

3

Helix

41 – 43

3

Beta strand

44 – 48

5

Helix

59 – 62

4

Beta strand

68 – 74

7

Helix

277 – 279

3

Turn

283 – 287

5

Helix

288 – 292

5

Helix

296 – 298

3

Helix

299 – 307

9

Helix

311 – 318

8

Helix

321 – 329

9

Helix

335 – 338

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: C026C78273BCB289	FASTA	409	43,171
	10 20 30 40 50 60 MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG KILNDDTALK 70 80 90 100 110 120 EYKIDEKNFV VVMVTKPKAV STPAPATTQQ SAPASTTAVT SSTTTTVAQA PTPVPALAPT 130 140 150 160 170 180 STPASITPAS ATASSEPAPA SAAKQEKPAE KPAETPVATS PTATDSTSGD SSRSNLFEDA 190 200 210 220 230 240 TSALVTGQSY ENMVTEIMSM GYEREQVIAA LRASFNNPDR AVEYLLMGIP GDRESQAVVD 250 260 270 280 290 300 PPQAASTGAP QSSAVAAAAA TTTATTTTTS SGGHPLEFLR NQPQFQQMRQ IIQQNPSLLP 310 320 330 340 350 360 ALLQQIGREN PQLLQQISQH QEHFIQMLNE PVQEAGGQGG GGGGGSGGIA EAGSGHMNYI 370 380 390 400 QVTPQEKEAI ERLKALGFPE GLVIQAYFAC EKNENLAANF LLQQNFDED
	Isoform 2 [UniParc]. Checksum: 6E4AF08BD3920158	FASTA	337	35,005
	10 20 30 40 50 60 MVTKPKAVST PAPATTQQSA PASTTAVTSS TTTTVAQAPT PVPALAPTST PASITPASAT 70 80 90 100 110 120 ASSEPAPASA AKQEKPAEKP AETPVATSPT ATDSTSGDSS RSNLFEDATS ALVTGQSYEN 130 140 150 160 170 180 MVTEIMSMGY EREQVIAALR ASFNNPDRAV EYLLMGIPGD RESQAVVDPP QAASTGAPQS 190 200 210 220 230 240 SAVAAAAATT TATTTTTSSG GHPLEFLRNQ PQFQQMRQII QQNPSLLPAL LQQIGRENPQ 250 260 270 280 290 300 LLQQISQHQE HFIQMLNEPV QEAGGQGGGG GGGSGGIAEA GSGHMNYIQV TPQEKEAIER 310 320 330 LKALGFPEGL VIQAYFACEK NENLAANFLL QQNFDED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification and cloning of a nucleotide excision repair complex involving the Xeroderma pigmentosum group C protein and a human homologue of yeast RAD23." Masutani C., Sugasawa K., Yanagisawa J., Sonoyama T., Ui M., Enomoto T., Takio K., Tanaka K., van der Spek P.J., Bootsma D., Hoeijmakers J.H.J., Hanaoka F. EMBO J. 13:1831-1843(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[2]	"Expression of a novel RAD23B mRNA splice variant in the human testis." Huang X., Wang H., Xu M., Lu L., Xu Z., Li J., Zhou Z., Sha J. J. Androl. 25:363-368(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-249, ALTERNATIVE SPLICING, TISSUE SPECIFICITY (ISOFORM 2). Tissue: Testis.
[3]	NIEHS SNPs program Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-249.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-249. Tissue: Uterus.
[8]	"Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity." Sugasawa K., Ng J.M., Masutani C., Maekawa T., Uchida A., van der Spek P.J., Eker A.P., Rademakers S., Visser C., Aboussekhra A., Wood R.D., Hanaoka F., Bootsma D., Hoeijmakers J.H. Mol. Cell. Biol. 17:6924-6931(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair." Sugasawa K., Ng J.M., Masutani C., Iwai S., van der Spek P.J., Eker A.P., Hanaoka F., Bootsma D., Hoeijmakers J.H. Mol. Cell 2:223-232(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE XPC COMPLEX.
[10]	"Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome." Hiyama H., Yokoi M., Masutani C., Sugasawa K., Maekawa T., Tanaka K., Hoeijmakers J.H., Hanaoka F. J. Biol. Chem. 274:28019-28025(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PSMD4 AND PSMC5.
[11]	"Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B." Wang G., Sawai N., Kotliarova S., Kanazawa I., Nukina N. Hum. Mol. Genet. 9:1795-1803(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATXN3.
[12]	"Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites." Batty D., Rapic'-Otrin V., Levine A.S., Wood R.D. J. Mol. Biol. 300:275-290(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, FUNCTION OF THE XPC COMPLEX.
[13]	"Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair." Araki M., Masutani C., Takemura M., Uchida A., Sugasawa K., Kondoh J., Ohkuma Y., Hanaoka F. J. Biol. Chem. 276:18665-18672(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CETN2, SUBCELLULAR LOCATION, CHARACTERIZATION OF THE XPC COMPLEX.
[14]	"A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex." Sugasawa K., Shimizu Y., Iwai S., Hanaoka F. DNA Repair 1:95-107(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE XPC COMPLEX.
[15]	"The carboxy-terminal domain of the XPC protein plays a crucial role in nucleotide excision repair through interactions with transcription factor IIH." Uchida A., Sugasawa K., Masutani C., Dohmae N., Araki M., Yokoi M., Ohkuma Y., Hanaoka F. DNA Repair 1:449-461(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH XPC.
[16]	"DNA bending by the human damage recognition complex XPC-HR23B." Janicijevic A., Sugasawa K., Shimizu Y., Hanaoka F., Wijgers N., Djurica M., Hoeijmakers J.H., Wyman C. DNA Repair 2:325-336(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE XPC COMPLEX.
[17]	"A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein." Ng J.M., Vermeulen W., van der Horst G.T., Bergink S., Sugasawa K., Vrieling H., Hoeijmakers J.H. Genes Dev. 17:1630-1645(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"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 W.J. Proc. Natl. Acad. Sci. U.S.A. 101:13774-13779(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NGLY1 AND PSMC1.
[19]	"Studies on the intracellular localization of hHR23B." Katiyar S., Lennarz W.J. Biochem. Biophys. Res. Commun. 337:1296-1300(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[20]	"Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein." Nishi R., Okuda Y., Watanabe E., Mori T., Iwai S., Masutani C., Sugasawa K., Hanaoka F. Mol. Cell. Biol. 25:5664-5674(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH XPC.
[21]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[22]	"Evidence for distinct functions for human DNA repair factors hHR23A and hHR23B." Chen L., Madura K. FEBS Lett. 580:3401-3408(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EEF1A1, MUTAGENESIS OF LYS-6.
[23]	"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex." Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L. Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-155, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[24]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[25]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"Variably modulated gating of the 26S proteasome by ATP and polyubiquitin." Li X., Demartino G.N. Biochem. J. 421:397-404(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PROTEASOMAL DEGRADATION, POLYUBIQUITIN-BINDING.
[27]	"Two-step recognition of DNA damage for mammalian nucleotide excision repair: Directional binding of the XPC complex and DNA strand scanning." Sugasawa K., Akagi J., Nishi R., Iwai S., Hanaoka F. Mol. Cell 36:642-653(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE XPC COMPLEX.
[28]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[29]	"Photo-cross-linking of XPC-Rad23B to cisplatin-damaged DNA reveals contacts with both strands of the DNA duplex and spans the DNA adduct." Neher T.M., Rechkunova N.I., Lavrik O.I., Turchi J.J. Biochemistry 49:669-678(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE XPC COMPLEX.
[30]	"Stimulation of DNA glycosylase activities by XPC Protein Complex: Roles of protein-protein interactions." Shimizu Y., Uchimura Y., Dohmae N., Saitoh H., Hanaoka F., Sugasawa K. J. Nucleic Acids 2010:0-0(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE XPC COMPLEX.
[31]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[32]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, MASS SPECTROMETRY.
[34]	"Binding surface mapping of intra- and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5a." Ryu K.-S., Lee K.-J., Bae S.-H., Kim B.-K., Kim K.-A., Choi B.-S. J. Biol. Chem. 278:36621-36627(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-82.
[35]	"Structure of the ubiquitin-interacting motif of S5a bound to the ubiquitin-like domain of HR23B." Fujiwara K., Tenno T., Sugasawa K., Jee J.-G., Ohki I., Kojima C., Tochio H., Hiroaki H., Hanaoka F., Shirakawa M. J. Biol. Chem. 279:4760-4767(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-87 IN COMPLEX WITH PSMD4.
[36]	"Solution structure and backbone dynamics of the XPC-binding domain of the human DNA repair protein hHR23B." Kim B., Ryu K.-S., Kim H.-J., Cho S.-J., Choi B.-S. FEBS J. 272:2467-2476(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 275-342, FUNCTION.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D21090 mRNA. Translation: BAA04652.1.
AY313777 mRNA. Translation: AAP81008.1.
AY165178 Genomic DNA. Translation: AAN47194.1.
AK125226 mRNA. Translation: BAG54170.1.
AL137852 Genomic DNA. Translation: CAD13275.1.
CH471105 Genomic DNA. Translation: EAW59016.1.
CH471105 Genomic DNA. Translation: EAW59017.1.
BC020973 mRNA. Translation: AAH20973.1.

IPI

IPI00008223.

PIR

S44346.

RefSeq

NP_001231653.1. NM_001244724.1.
NP_002865.1. NM_002874.4.

UniGene

Hs.521640.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P1A	NMR	-	A	1-82	[»]
1PVE	NMR	-	A	275-342	[»]
1UEL	NMR	-	A	1-87	[»]

ProteinModelPortal

P54727.

ModBase

Search...

Protein-protein interaction databases

IntAct

P54727. 17 interactions.

MINT

MINT-5006025.

STRING

9606.ENSP00000350708.

PTM databases

PhosphoSite

P54727.

Polymorphism databases

DMDM

1709985.

2D gel databases

OGP

P54727.

Proteomic databases

PaxDb

P54727.

PeptideAtlas

P54727.

PRIDE

P54727.

Protocols and materials databases

DNASU

5887.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000358015; ENSP00000350708; ENSG00000119318.
ENST00000416373; ENSP00000405623; ENSG00000119318.

GeneID

5887.

KEGG

hsa:5887.

UCSC

uc004bde.3. human.

Organism-specific databases

CTD

5887.

GeneCards

GC09P110045.

HGNC

HGNC:9813. RAD23B.

HPA

CAB033868.
HPA029718.
HPA029720.

MIM

600062. gene.

neXtProt

NX_P54727.

PharmGKB

PA34173.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5272.

HOGENOM

HOG000172162.

HOVERGEN

HBG055042.

InParanoid

P54727.

KO

K10839.

OMA

NDTIMAV.

OrthoDB

EOG4M399F.

PhylomeDB

P54727.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

P54727.

Bgee

P54727.

CleanEx

HS_RAD23B.

Genevestigator

P54727.

GermOnline

ENSG00000119318. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.540. 1 hit.

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.
[Graphical view]

Pfam

PF00627. UBA. 2 hits.
PF00240. ubiquitin. 1 hit.
PF09280. XPC-binding. 1 hit.
[Graphical view]

PRINTS

PR01839. RAD23PROTEIN.

SMART

SM00727. STI1. 1 hit.
SM00165. UBA. 2 hits.
SM00213. UBQ. 1 hit.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 2 hits.
SSF101238. XPC-bd. 1 hit.

TIGRFAMs

TIGR00601. rad23. 1 hit.

PROSITE

PS50030. UBA. 2 hits.
PS00299. UBIQUITIN_1. False negative.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RAD23B. human.

EvolutionaryTrace

P54727.

GenomeRNAi

5887.

NextBio

22892.

PMAP-CutDB

P54727.

SOURCE

Search...

Entry information

Entry name

RD23B_HUMAN

Accession

Primary (citable) accession number: P54727
Secondary accession number(s): B3KWK8 , G5E9P0, Q7Z5K8, Q8WUB0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.