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RCQ1_SCHPO
ID   RCQ1_SCHPO              Reviewed;         656 AA.
AC   O13796; Q9P7G1;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Ribosome quality control complex subunit 1 {ECO:0000250|UniProtKB:Q05468};
GN   Name=rqc1 {ECO:0000250|UniProtKB:Q05468};
GN   ORFNames=SPAC1142.01 {ECO:0000312|PomBase:SPAC1142.01}, SPAC17G6.18;
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 SER-56; SER-61; SER-63; SER-110
RP   AND SER-111, AND 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: Component of the ribosome quality control complex (RQC), a
CC       ribosome-associated complex that mediates ubiquitination and extraction
CC       of incompletely synthesized nascent chains for proteasomal degradation.
CC       Rqc1 is essential for the recruitment of cdc48 to ribosomal subunits.
CC       {ECO:0000250|UniProtKB:Q05468}.
CC   -!- SUBUNIT: Component of the ribosome quality control complex (RQC),
CC       composed of the E3 ubiquitin ligase rkr1/ltn1, rqc1 and mtr1/rqc2, as
CC       well as cdc48 and its ubiquitin-binding cofactors. RQC forms a stable
CC       complex with 60S ribosomal subunits. {ECO:0000250|UniProtKB:Q05468}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the TCF25 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16229.2; -; Genomic_DNA.
DR   PIR; T37850; T37850.
DR   RefSeq; NP_594265.2; NM_001019688.3.
DR   AlphaFoldDB; O13796; -.
DR   BioGRID; 278672; 16.
DR   STRING; 4896.SPAC1142.01.1; -.
DR   iPTMnet; O13796; -.
DR   MaxQB; O13796; -.
DR   PaxDb; O13796; -.
DR   PRIDE; O13796; -.
DR   EnsemblFungi; SPAC1142.01.1; SPAC1142.01.1:pep; SPAC1142.01.
DR   PomBase; SPAC1142.01; rqc1.
DR   VEuPathDB; FungiDB:SPAC1142.01; -.
DR   eggNOG; KOG2422; Eukaryota.
DR   HOGENOM; CLU_008321_1_1_1; -.
DR   InParanoid; O13796; -.
DR   OMA; WPPLTKN; -.
DR   PhylomeDB; O13796; -.
DR   PRO; PR:O13796; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:1990112; C:RQC complex; ISO:PomBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:PomBase.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
DR   GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISO:PomBase.
DR   InterPro; IPR006994; TCF25/Rqc1.
DR   PANTHER; PTHR22684; PTHR22684; 1.
DR   Pfam; PF04910; Tcf25; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..656
FT                   /note="Ribosome quality control complex subunit 1"
FT                   /id="PRO_0000116835"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          634..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..99
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         61
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         63
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         110
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         111
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   656 AA;  75015 MW;  9C0FF49C0B6351BA CRC64;
     MSSRALRKLQ RQRQTELLEE ALDSESDEDD EFSSTSGKKV VNVFEILEKE NNAINSEAEK
     SVSEEEQDEP LVEGESPIVS TNKKAKNKKK KKKQQKKKKV TGKRDLDNQS SDNEKLEGLE
     SSKNIDDDID EIEKAAAELK LKYREQDQVE HVAGVEESAT IPLDKELDEK LNKLLGVNIS
     MLNPDLEIRK IFGRIVEKRS VNARHDNLRR KRHVLVQPQE GWPPLVRSGL GMKLTGQSQD
     LECFFEITQS RAYQEVQETF EYYVQTYDPN NLLMLLRSHP FHIDTLLQVS EIIDQQGDHE
     LSAELVARGL YAFDSILHPR FNLATGATRL PFAIPSNRRL FLCIWRYLQS LQSRGCWRTV
     FEFCKALLQF DMSDPYAIGT CIDIYALRRR EFAWIIDFAN YLENSNKISD TPNMLYSSAL
     AMFYVHGDTT DTRASMLAAF ERAPYMLSEL LDTLNISFTK SSIPSPQDPV QELHSAMYAL
     YAKDSWSDPT VLAFINSILE KETVTLHDVE GQFAELTENL SRRVILLNEQ SLRKFLPQRI
     LQGTILSFDP LPPDTYLSES QVFGRDISRR IASFLSDYLS RAREVNENEE EPPAHEFDLP
     PAEQLLQQIE SEVGEESEDG TPVMTRLRSF FGSLFTSTNS ETEPAEESTE EMGQGD
 
 
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