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YBI8_SCHPO
ID   YBI8_SCHPO              Reviewed;         284 AA.
AC   O42914; P78760; Q1L854;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Uncharacterized protein C16A3.08c;
GN   ORFNames=SPBC16A3.08c;
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 MRNA].
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
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   INTERACTION WITH SAD1, AND SUBCELLULAR LOCATION.
RX   PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA   Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT   "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT   membrane-bound components of the spindle pole body in fission yeast.";
RL   Mol. Genet. Genomics 270:449-461(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-51; THR-160; SER-162
RP   AND THR-166, 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   -!- SUBUNIT: Interacts with sad1. {ECO:0000269|PubMed:14655046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14655046}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA13771.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D89108; BAA13771.1; ALT_INIT; mRNA.
DR   EMBL; CU329671; CAA16859.1; -; Genomic_DNA.
DR   PIR; T39544; T39544.
DR   PIR; T42085; T42085.
DR   RefSeq; NP_596781.1; NM_001023802.2.
DR   AlphaFoldDB; O42914; -.
DR   BioGRID; 276295; 41.
DR   IntAct; O42914; 1.
DR   STRING; 4896.SPBC16A3.08c.1; -.
DR   iPTMnet; O42914; -.
DR   MaxQB; O42914; -.
DR   PaxDb; O42914; -.
DR   PRIDE; O42914; -.
DR   EnsemblFungi; SPBC16A3.08c.1; SPBC16A3.08c.1:pep; SPBC16A3.08c.
DR   GeneID; 2539743; -.
DR   KEGG; spo:SPBC16A3.08c; -.
DR   PomBase; SPBC16A3.08c; -.
DR   VEuPathDB; FungiDB:SPBC16A3.08c; -.
DR   eggNOG; ENOG502S4DF; Eukaryota.
DR   HOGENOM; CLU_980580_0_0_1; -.
DR   InParanoid; O42914; -.
DR   OMA; KADKKWA; -.
DR   PhylomeDB; O42914; -.
DR   Reactome; R-SPO-114608; Platelet degranulation.
DR   PRO; PR:O42914; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0051880; F:G-quadruplex DNA binding; IDA:PomBase.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0043555; P:regulation of translation in response to stress; ISO:PomBase.
DR   GO; GO:0031929; P:TOR signaling; ISO:PomBase.
DR   InterPro; IPR039764; HABP4/SERBP1.
DR   InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR   InterPro; IPR019084; Stm1-like_N.
DR   PANTHER; PTHR12299; PTHR12299; 1.
DR   Pfam; PF09598; Stm1_N; 1.
DR   SMART; SM01233; HABP4_PAI-RBP1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..284
FT                   /note="Uncharacterized protein C16A3.08c"
FT                   /id="PRO_0000116512"
FT   REGION          1..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         160
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         166
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        115..116
FT                   /note="RA -> LL (in Ref. 1; BAA13771)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   284 AA;  30949 MW;  F87C9651EF2B304E CRC64;
     MSVASKNLFD LLGEETPAAT TTEKKTAASR DKKRSDSPPV PRELVAQSTT SRKRDPNQPT
     PRERTVNKKA DQPRRRRQAP QGNEAFAREG KEARANNAAH PVDATGAPSN RRNARARRGR
     EFDRHSQTGR VDTKKATERG WGDLVNSAAN PDVAENEGNT PSGAQTPAAE EENVKTLDEY
     LSERKSAAKP VGRTVEKLEN ATKVEKSAPE ELFASLKKSA SQKKSAAKES KPKKVLLDIE
     QTFTARPARG GRPNRAPRRG PSETASKTQQ APPTLSETDF PALA
 
 
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