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P54727

- RD23B_HUMAN

UniProt

P54727 - RD23B_HUMAN

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Protein
UV excision repair protein RAD23 homolog B
Gene
RAD23B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.11 Publications
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.11 Publications
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 SMUG1.11 Publications

GO - Molecular functioni

  1. damaged DNA binding Source: InterPro
  2. polyubiquitin binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. single-stranded DNA binding Source: ProtInc

GO - Biological processi

  1. DNA repair Source: Reactome
  2. nucleotide-excision repair Source: UniProtKB
  3. nucleotide-excision repair, DNA damage recognition Source: UniProtKB
  4. nucleotide-excision repair, DNA damage removal Source: Reactome
  5. proteasome-mediated ubiquitin-dependent protein catabolic process Source: InterPro
  6. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  7. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_257. Formation of incision complex in GG-NER.
REACT_311. Dual incision reaction in GG-NER.
REACT_476. DNA Damage Recognition in GG-NER.

Names & Taxonomyi

Protein namesi
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 namesi
Name:RAD23B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:9813. RAD23B.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. XPC complex Source: UniProtKB
  2. cytoplasm Source: HPA
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
  5. proteasome complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi6 – 61K → A: Impairs interaction with EEF1A1. 1 Publication

Organism-specific databases

PharmGKBiPA34173.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409UV excision repair protein RAD23 homolog B
PRO_0000114906Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei155 – 1551Phosphothreonine1 Publication
Modified residuei160 – 1601Phosphoserine4 Publications
Modified residuei174 – 1741Phosphoserine By similarity
Modified residuei186 – 1861Phosphothreonine By similarity
Modified residuei199 – 1991Phosphoserine By similarity
Modified residuei202 – 2021Phosphotyrosine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP54727.
PaxDbiP54727.
PeptideAtlasiP54727.
PRIDEiP54727.

2D gel databases

OGPiP54727.

PTM databases

PhosphoSiteiP54727.

Miscellaneous databases

PMAP-CutDBP54727.

Expressioni

Gene expression databases

ArrayExpressiP54727.
BgeeiP54727.
CleanExiHS_RAD23B.
GenevestigatoriP54727.

Organism-specific databases

HPAiCAB033868.
HPA029718.
HPA029719.
HPA029720.

Interactioni

Subunit structurei

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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADRM1Q161862EBI-954531,EBI-954387
ATXN3P542522EBI-954531,EBI-946046
ERCC3P194472EBI-954531,EBI-1183307
Pax3P246104EBI-954531,EBI-1208116From a different organism.
PSMD4P5503612EBI-954531,EBI-359318
RPN10P550343EBI-954531,EBI-2620423From a different organism.
UBA3Q8TBC42EBI-954531,EBI-717567
UBCP0CG484EBI-954531,EBI-3390054
USP5P459742EBI-954531,EBI-741277
VIMP086702EBI-954531,EBI-353844
XPCQ018315EBI-954531,EBI-372610

Protein-protein interaction databases

BioGridi111824. 232 interactions.
DIPiDIP-39944N.
IntActiP54727. 39 interactions.
MINTiMINT-5006025.
STRINGi9606.ENSP00000350708.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 77
Beta strandi12 – 176
Helixi23 – 3412
Turni36 – 383
Helixi41 – 433
Beta strandi44 – 485
Helixi59 – 624
Beta strandi68 – 747
Helixi277 – 2793
Turni283 – 2875
Helixi288 – 2925
Helixi296 – 2983
Helixi299 – 3079
Helixi311 – 3188
Helixi321 – 3299
Helixi335 – 3384

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P1ANMR-A1-82[»]
1PVENMR-A275-342[»]
1UELNMR-A1-87[»]
ProteinModelPortaliP54727.
SMRiP54727. Positions 1-409.

Miscellaneous databases

EvolutionaryTraceiP54727.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7979Ubiquitin-like
Add
BLAST
Domaini188 – 22841UBA 1
Add
BLAST
Domaini274 – 31744STI1
Add
BLAST
Domaini364 – 40441UBA 2
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi103 – 1064Poly-Thr
Compositional biasi254 – 2607Poly-Ala
Compositional biasi261 – 2699Poly-Thr
Compositional biasi336 – 34813Poly-Gly
Add
BLAST

Domaini

The ubiquitin-like domain mediates interaction with ATXN3.

Sequence similaritiesi

Belongs to the RAD23 family.
Contains 1 STI1 domain.
Contains 2 UBA domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5272.
HOGENOMiHOG000172162.
HOVERGENiHBG055042.
InParanoidiP54727.
KOiK10839.
OMAiEDEMPHA.
OrthoDBiEOG72C51D.
PhylomeDBiP54727.
TreeFamiTF101216.

Family and domain databases

Gene3Di1.10.10.540. 1 hit.
InterProiIPR004806. Rad23.
IPR006636. STI1_HS-bd.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR015360. XPC-bd.
[Graphical view]
PfamiPF00627. UBA. 2 hits.
PF00240. ubiquitin. 1 hit.
PF09280. XPC-binding. 1 hit.
[Graphical view]
PRINTSiPR01839. RAD23PROTEIN.
SMARTiSM00727. STI1. 1 hit.
SM00165. UBA. 2 hits.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF101238. SSF101238. 1 hit.
SSF46934. SSF46934. 2 hits.
SSF54236. SSF54236. 1 hit.
TIGRFAMsiTIGR00601. rad23. 1 hit.
PROSITEiPS50030. UBA. 2 hits.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P54727-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG    50
KILNDDTALK EYKIDEKNFV VVMVTKPKAV STPAPATTQQ SAPASTTAVT 100
SSTTTTVAQA PTPVPALAPT STPASITPAS ATASSEPAPA SAAKQEKPAE 150
KPAETPVATS PTATDSTSGD SSRSNLFEDA TSALVTGQSY ENMVTEIMSM 200
GYEREQVIAA LRASFNNPDR AVEYLLMGIP GDRESQAVVD PPQAASTGAP 250
QSSAVAAAAA TTTATTTTTS SGGHPLEFLR NQPQFQQMRQ IIQQNPSLLP 300
ALLQQIGREN PQLLQQISQH QEHFIQMLNE PVQEAGGQGG GGGGGSGGIA 350
EAGSGHMNYI QVTPQEKEAI ERLKALGFPE GLVIQAYFAC EKNENLAANF 400
LLQQNFDED 409
Length:409
Mass (Da):43,171
Last modified:October 1, 1996 - v1
Checksum:iC026C78273BCB289
GO
Isoform 2 (identifier: P54727-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:337
Mass (Da):35,005
Checksum:i6E4AF08BD3920158
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti249 – 2491A → V.3 Publications
Corresponds to variant rs1805329 [ dbSNP | Ensembl ].
VAR_014350

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7272Missing in isoform 2.
VSP_045606Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS59138.1. [P54727-2]
CCDS6769.1. [P54727-1]
PIRiS44346.
RefSeqiNP_001231653.1. NM_001244724.1. [P54727-2]
NP_002865.1. NM_002874.4. [P54727-1]
UniGeneiHs.521640.

Genome annotation databases

EnsembliENST00000358015; ENSP00000350708; ENSG00000119318. [P54727-1]
ENST00000416373; ENSP00000405623; ENSG00000119318. [P54727-2]
GeneIDi5887.
KEGGihsa:5887.
UCSCiuc004bde.3. human. [P54727-1]

Polymorphism databases

DMDMi1709985.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS59138.1. [P54727-2 ]
CCDS6769.1. [P54727-1 ]
PIRi S44346.
RefSeqi NP_001231653.1. NM_001244724.1. [P54727-2 ]
NP_002865.1. NM_002874.4. [P54727-1 ]
UniGenei Hs.521640.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P1A NMR - A 1-82 [» ]
1PVE NMR - A 275-342 [» ]
1UEL NMR - A 1-87 [» ]
ProteinModelPortali P54727.
SMRi P54727. Positions 1-409.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111824. 232 interactions.
DIPi DIP-39944N.
IntActi P54727. 39 interactions.
MINTi MINT-5006025.
STRINGi 9606.ENSP00000350708.

PTM databases

PhosphoSitei P54727.

Polymorphism databases

DMDMi 1709985.

2D gel databases

OGPi P54727.

Proteomic databases

MaxQBi P54727.
PaxDbi P54727.
PeptideAtlasi P54727.
PRIDEi P54727.

Protocols and materials databases

DNASUi 5887.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358015 ; ENSP00000350708 ; ENSG00000119318 . [P54727-1 ]
ENST00000416373 ; ENSP00000405623 ; ENSG00000119318 . [P54727-2 ]
GeneIDi 5887.
KEGGi hsa:5887.
UCSCi uc004bde.3. human. [P54727-1 ]

Organism-specific databases

CTDi 5887.
GeneCardsi GC09P110045.
HGNCi HGNC:9813. RAD23B.
HPAi CAB033868.
HPA029718.
HPA029719.
HPA029720.
MIMi 600062. gene.
neXtProti NX_P54727.
PharmGKBi PA34173.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5272.
HOGENOMi HOG000172162.
HOVERGENi HBG055042.
InParanoidi P54727.
KOi K10839.
OMAi EDEMPHA.
OrthoDBi EOG72C51D.
PhylomeDBi P54727.
TreeFami TF101216.

Enzyme and pathway databases

Reactomei REACT_257. Formation of incision complex in GG-NER.
REACT_311. Dual incision reaction in GG-NER.
REACT_476. DNA Damage Recognition in GG-NER.

Miscellaneous databases

ChiTaRSi RAD23B. human.
EvolutionaryTracei P54727.
GeneWikii RAD23B.
GenomeRNAii 5887.
NextBioi 22892.
PMAP-CutDB P54727.
PROi P54727.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54727.
Bgeei P54727.
CleanExi HS_RAD23B.
Genevestigatori P54727.

Family and domain databases

Gene3Di 1.10.10.540. 1 hit.
InterProi IPR004806. Rad23.
IPR006636. STI1_HS-bd.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR015360. XPC-bd.
[Graphical view ]
Pfami PF00627. UBA. 2 hits.
PF00240. ubiquitin. 1 hit.
PF09280. XPC-binding. 1 hit.
[Graphical view ]
PRINTSi PR01839. RAD23PROTEIN.
SMARTi SM00727. STI1. 1 hit.
SM00165. UBA. 2 hits.
SM00213. UBQ. 1 hit.
[Graphical view ]
SUPFAMi SSF101238. SSF101238. 1 hit.
SSF46934. SSF46934. 2 hits.
SSF54236. SSF54236. 1 hit.
TIGRFAMsi TIGR00601. rad23. 1 hit.
PROSITEi PS50030. UBA. 2 hits.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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.
  28. "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.
  29. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  30. "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.
  31. "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 2010:455-459(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE XPC COMPLEX.
  32. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "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.
  36. "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.
  37. "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.

Entry informationi

Entry nameiRD23B_HUMAN
AccessioniPrimary (citable) accession number: P54727
Secondary accession number(s): B3KWK8
, G5E9P0, Q7Z5K8, Q8WUB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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