RHP23_SCHPO
ID RHP23_SCHPO Reviewed; 368 AA.
AC O74803;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=UV excision repair protein rhp23;
DE AltName: Full=RAD23 homolog;
GN Name=rhp23; ORFNames=SPBC2D10.12;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=SP223;
RX PubMed=11788722; DOI=10.1093/nar/30.2.581;
RA Elder R.T., Song X.-Q., Chen M., Hopkins K.M., Lieberman H.B., Zhao Y.;
RT "Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human
RT HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes,
RT in cell cycle control and protein ubiquitination.";
RL Nucleic Acids Res. 30:581-591(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10652237; DOI=10.1006/bbrc.2000.2100;
RA Lombaerts M., Goeloe J.I., den Dulk H., Brandsma J.A., Brouwer J.;
RT "Identification and characterization of the rhp23(+) DNA repair gene in
RT Schizosaccharomyces pombe.";
RL Biochem. Biophys. Res. Commun. 268:210-215(2000).
RN [4]
RP FUNCTION.
RX PubMed=12560082; DOI=10.1016/s0014-5793(02)03874-7;
RA Hartmann-Petersen R., Hendil K.B., Gordon C.;
RT "Ubiquitin binding proteins protect ubiquitin conjugates from
RT disassembly.";
RL FEBS Lett. 535:77-81(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-87 AND SER-364, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in postreplication repair of UV-damaged DNA.
CC Postreplication repair functions in gap-filling of a daughter strand on
CC replication of damaged DNA. {ECO:0000269|PubMed:12560082}.
CC -!- FUNCTION: Protects ubiquitin chains against dissambly by
CC deubiquitinating enzymes thereby promoting protein degradation.
CC {ECO:0000269|PubMed:12560082}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11788722}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF174293; AAD51975.1; -; mRNA.
DR EMBL; CU329671; CAA21170.1; -; Genomic_DNA.
DR PIR; T40115; T40115.
DR RefSeq; NP_596231.1; NM_001022151.2.
DR AlphaFoldDB; O74803; -.
DR SMR; O74803; -.
DR BioGRID; 277009; 38.
DR MINT; O74803; -.
DR STRING; 4896.SPBC2D10.12.1; -.
DR iPTMnet; O74803; -.
DR MaxQB; O74803; -.
DR PaxDb; O74803; -.
DR PRIDE; O74803; -.
DR EnsemblFungi; SPBC2D10.12.1; SPBC2D10.12.1:pep; SPBC2D10.12.
DR GeneID; 2540481; -.
DR KEGG; spo:SPBC2D10.12; -.
DR PomBase; SPBC2D10.12; rhp23.
DR VEuPathDB; FungiDB:SPBC2D10.12; -.
DR eggNOG; KOG0011; Eukaryota.
DR HOGENOM; CLU_040364_0_0_1; -.
DR InParanoid; O74803; -.
DR OMA; ANTVESY; -.
DR PhylomeDB; O74803; -.
DR Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
DR PRO; PR:O74803; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003684; F:damaged DNA binding; ISO:PomBase.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IDA:PomBase.
DR GO; GO:0006289; P:nucleotide-excision repair; IMP:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:PomBase.
DR Gene3D; 1.10.10.540; -; 1.
DR InterPro; IPR004806; Rad23.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR015360; XPC-bd.
DR InterPro; IPR036353; XPC-bd_sf.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF09280; XPC-binding; 1.
DR PRINTS; PR01839; RAD23PROTEIN.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF101238; SSF101238; 1.
DR SUPFAM; SSF46934; SSF46934; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR TIGRFAMs; TIGR00601; rad23; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation pathway.
FT CHAIN 1..368
FT /note="UV excision repair protein rhp23"
FT /id="PRO_0000114903"
FT DOMAIN 1..77
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 135..185
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 320..360
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 76..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 368 AA; 40135 MW; 5CE75EB7E190EFD4 CRC64;
MNLTFKNLQQ QKFVISDVSA DTKISELKEK IQTQQNYEVE RQKLIYSGRI LADDKTVGEY
NIKEQDFIVC MVSRPKTSTS TPKSAASPAP NPPASVPEKK VEAPSSTVAE STSTTQTVAA
AAPSNPDTTA TSEAPIDANT LAVGAQRNVA VENMVEMGYE RSEVERAMRA AFNNPDRAVE
YLLTGIPEDI LNRQREESAA ALAAQQQQSE ALAPTSTGQP ANLFEQAALS ENENQEQPSN
TVGDDPLGFL RSIPQFQQLR QIVQQNPQML ETILQQIGQG DPALAQAITQ NPEAFLQLLA
EGAEGESALP SGGIQIQITQ EESESIDRLC QLGFDRNIVI QAYLACDKNE ELAANYLFEH
GHESEDEP
