CUE3_SCHPO
ID CUE3_SCHPO Reviewed; 581 AA.
AC O74485;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=CUE domain-containing protein 3;
GN Name=slh1 {ECO:0000312|PomBase:SPCC1906.02c};
GN ORFNames=SPCC1906.02c {ECO:0000312|PomBase:SPCC1906.02c};
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 [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 [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-386, AND IDENTIFICATION BY
RP 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 activation of the ribosome quality control (RQC)
CC pathway, a pathway that degrades nascent peptide chains during
CC problematic translation (By similarity). As part of the ribosome
CC quality control trigger (RQT) complex, recognizes specifically
CC ubiquitinated stalled ribosomes (By similarity).
CC {ECO:0000250|UniProtKB:P53137}.
CC -!- SUBUNIT: Component of the RQT (ribosome quality control trigger)
CC complex. {ECO:0000250|UniProtKB:P53137}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329672; CAA20771.1; -; Genomic_DNA.
DR PIR; T41210; T41210.
DR RefSeq; NP_588406.1; NM_001023397.2.
DR AlphaFoldDB; O74485; -.
DR BioGRID; 275347; 1.
DR IntAct; O74485; 1.
DR STRING; 4896.SPCC1906.02c.1; -.
DR iPTMnet; O74485; -.
DR MaxQB; O74485; -.
DR PaxDb; O74485; -.
DR PRIDE; O74485; -.
DR EnsemblFungi; SPCC1906.02c.1; SPCC1906.02c.1:pep; SPCC1906.02c.
DR GeneID; 2538764; -.
DR KEGG; spo:SPCC1906.02c; -.
DR PomBase; SPCC1906.02c; -.
DR VEuPathDB; FungiDB:SPCC1906.02c; -.
DR eggNOG; KOG4501; Eukaryota.
DR HOGENOM; CLU_483252_0_0_1; -.
DR InParanoid; O74485; -.
DR OMA; IEGWRRM; -.
DR PRO; PR:O74485; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0099053; C:activating signal cointegrator 1 complex; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0043130; F:ubiquitin binding; ISM:PomBase.
DR InterPro; IPR003892; CUE.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 1.
DR PROSITE; PS51140; CUE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..581
FT /note="CUE domain-containing protein 3"
FT /id="PRO_0000310343"
FT DOMAIN 271..314
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 422..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..574
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 386
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 581 AA; 65858 MW; F69156858FC6C632 CRC64;
MSENVISSSK NVVSKLLYVK DEYWPSVAPA ATELISKLIN AFWCQTLNGQ LVEEDEGERN
CIFLFDRCLK TEGCLKKIGP VTVMQFLACF LLSSQNHAYA WSVCRQIPSD DMAFKFTKCF
QNSQQFRDAN FCKLVLVWTV CQCVSSTVYY PAILDLLPVL SDLVKEMEKD PASLQAKENE
FWLKKLIQTS LHHSSDNSLV FYLEMLLDSL DLRNCIYVVF EDEALFRRLK DIGNPEIRMM
LDSGLRDWRK QRSGRSSSHV ASKGINKVVN INPGDVKSLI ELFPQLSVEE AVEHLSASLG
NIDAACESVI TSSLPEELDS STHSPIYTKP NVDSMHKQPK KAIAPLSLSS SVTAVISNRT
SDKKTRSTVA EEDDITHLNI SPDRLYLNKK PEDLNFWKKS VPETDKSRVL NLLAMAEDDE
YDDTYDDLDT TGPVDSGVGD DDPEASSKDA HDFQKFINQT LYDFYQQNPE VFDQKARKSK
ERADLLAKLD NSLTHEQIEG WRRMFTTDSK FAEAVKKEVT FGSGNTNIGS LRQTKFKQSN
YTPPELNDGS RQHRPSRPSK NPSLKKKKYV RTKPKKASNE K
