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NUP45_SCHPO
ID   NUP45_SCHPO             Reviewed;         425 AA.
AC   Q09793;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Nucleoporin nup45;
DE   AltName: Full=Nuclear pore protein nup45;
GN   Name=nup45; ORFNames=SPAC22G7.09c;
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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15116432; DOI=10.1002/yea.1115;
RA   Chen X.Q., Du X., Liu J., Balasubramanian M.K., Balasundaram D.;
RT   "Identification of genes encoding putative nucleoporins and transport
RT   factors in the fission yeast Schizosaccharomyces pombe: a deletion
RT   analysis.";
RL   Yeast 21:495-509(2004).
RN   [3]
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-290, 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: Functions as a component of the nuclear pore complex (NPC).
CC       NPC components, collectively referred to as nucleoporins (NUPs), can
CC       play the role of both NPC structural components and of docking or
CC       interaction partners for transiently associated nuclear transport
CC       factors. Active directional transport is assured by both, a Phe-Gly
CC       (FG) repeat affinity gradient for these transport factors across the
CC       NPC and a transport cofactor concentration gradient across the nuclear
CC       envelope. {ECO:0000269|PubMed:15116432}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nuclear pore complex.
CC   -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC       karyopherins (importins, exportins) and form probably an affinity
CC       gradient, guiding the transport proteins unidirectionally with their
CC       cargo through the NPC. FG repeat regions are highly flexible and lack
CC       ordered secondary structure. The overall conservation of FG repeats
CC       regarding exact sequence, spacing, and repeat unit length is limited.
CC       FG repeat types and their physico-chemical environment change across
CC       the NPC from the nucleoplasmic to the cytoplasmic side.
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DR   EMBL; CU329670; CAA91133.2; -; Genomic_DNA.
DR   PIR; S62453; S62453.
DR   PIR; T11619; T11619.
DR   RefSeq; NP_593058.1; NM_001018456.2.
DR   AlphaFoldDB; Q09793; -.
DR   SMR; Q09793; -.
DR   BioGRID; 278380; 3.
DR   STRING; 4896.SPAC22G7.09c.1; -.
DR   iPTMnet; Q09793; -.
DR   MaxQB; Q09793; -.
DR   PaxDb; Q09793; -.
DR   PRIDE; Q09793; -.
DR   EnsemblFungi; SPAC22G7.09c.1; SPAC22G7.09c.1:pep; SPAC22G7.09c.
DR   GeneID; 2541890; -.
DR   KEGG; spo:SPAC22G7.09c; -.
DR   PomBase; SPAC22G7.09c; nup45.
DR   VEuPathDB; FungiDB:SPAC22G7.09c; -.
DR   eggNOG; KOG0845; Eukaryota.
DR   HOGENOM; CLU_645843_0_0_1; -.
DR   InParanoid; Q09793; -.
DR   OMA; RWYKATI; -.
DR   PhylomeDB; Q09793; -.
DR   Reactome; R-SPO-159227; Transport of the SLBP independent Mature mRNA.
DR   Reactome; R-SPO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR   Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-SPO-3232142; SUMOylation of ubiquitinylation proteins.
DR   Reactome; R-SPO-4085377; SUMOylation of SUMOylation proteins.
DR   Reactome; R-SPO-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-SPO-4570464; SUMOylation of RNA binding proteins.
DR   Reactome; R-SPO-5578749; Transcriptional regulation by small RNAs.
DR   PRO; PR:Q09793; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR   GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; IC:PomBase.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR025574; Nucleoporin_FG_rpt.
DR   InterPro; IPR024882; Nucleoporin_p58/p45.
DR   PANTHER; PTHR13437; PTHR13437; 1.
DR   Pfam; PF13634; Nucleoporin_FG; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Translocation; Transport.
FT   CHAIN           1..425
FT                   /note="Nucleoporin nup45"
FT                   /id="PRO_0000204863"
FT   REGION          1..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         290
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   425 AA;  44983 MW;  FA46FC04BEBE9B71 CRC64;
     MFGLNKTPSF GSTGTQNQNT GTSAGTGLFS SNTFGNNTQA NTPASTGFGG VTGGAFGQTK
     PQTGGSLFGN KPNATSTTPG LNLFGQNPQA APGGSLFGAS TTKPQAPGGL FNQNQTQAQP
     AQAAPTGGLF GLSGQNQTQS QTQPAQANTS LFGQSNIGTT GGLFDQNRPN TSTFGQFSTQ
     PASAGLFGQS TQPSGSTGFG LSNNTQTTPF FSAAQQQPST TQLPSNPAIN ATTRYSSLNA
     NTQKFLDDLD KEIFSQIQLA EELQTKLGTV SELVESVPND VAEVQRRLSS VSTALLIDSD
     EIETTKRVVD EDTSNARISS RILDVFKTPG ATYPFASNDP LMNYFEQFTE NAKKRTDLYA
     ATIGELEQHL EQVETTPQNN SPEALLKTIK EEHKLFMALS NRFAQVHDEV KRLQVNTSTS
     LPFIS
 
 
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