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NUP35_CAEEL
ID   NUP35_CAEEL             Reviewed;         381 AA.
AC   Q09601; O62340;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Nucleoporin NUP35 {ECO:0000250|UniProtKB:Q8NFH5};
DE   AltName: Full=35 kDa nucleoporin;
DE   AltName: Full=Nuclear pore complex protein Nup53;
DE   AltName: Full=Nucleoporin NUP53 {ECO:0000250|UniProtKB:Q8NFH5};
DE   AltName: Full=Nucleoporin npp-19;
GN   Name=npp-19; ORFNames=R06F6.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=12937276; DOI=10.1091/mbc.e03-04-0237;
RA   Galy V., Mattaj I.W., Askjaer P.;
RT   "Caenorhabditis elegans nucleoporins Nup93 and Nup205 determine the limit
RT   of nuclear pore complex size exclusion in vivo.";
RL   Mol. Biol. Cell 14:5104-5115(2003).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28122936; DOI=10.1242/jcs.196709;
RA   Ferreira J., Stear J.H., Saumweber H.;
RT   "Nucleoporins NPP-10, NPP-13 and NPP-20 are required for HCP-4 nuclear
RT   import to establish correct centromere assembly.";
RL   J. Cell Sci. 130:963-974(2017).
CC   -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC)
CC       (By similarity). NPC components, collectively referred to as
CC       nucleoporins (NUPs), can play the role of both NPC structural
CC       components and of docking or interaction partners for transiently
CC       associated nuclear transport factors (By similarity). Required for the
CC       proper organization of chromosomes on the mitotic spindle during
CC       anaphase (PubMed:28122936). {ECO:0000250|UniProtKB:Q8NFH5,
CC       ECO:0000269|PubMed:28122936}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC       {ECO:0000250|UniProtKB:Q8NFH5}. Nucleus membrane
CC       {ECO:0000269|PubMed:12937276}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=b;
CC         IsoId=Q09601-1; Sequence=Displayed;
CC       Name=a;
CC         IsoId=Q09601-2; Sequence=VSP_020780;
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos (at protein level).
CC       {ECO:0000269|PubMed:12937276}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in embryonic
CC       lethality (PubMed:12937276, PubMed:28122936). Also causes severe
CC       defects in mitosis due to abnormal chromosome organization on the
CC       mitotic spindle during anaphase (PubMed:28122936). Two-cell embryos
CC       appear to lack nuclei and pronuclei. {ECO:0000269|PubMed:12937276,
CC       ECO:0000269|PubMed:28122936}.
CC   -!- SIMILARITY: Belongs to the Nup35 family. {ECO:0000305}.
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DR   EMBL; Z46794; CAA86775.1; -; Genomic_DNA.
DR   EMBL; Z46794; CAA86784.1; -; Genomic_DNA.
DR   PIR; T23976; T23976.
DR   PIR; T23985; T23985.
DR   RefSeq; NP_496324.1; NM_063923.5. [Q09601-1]
DR   RefSeq; NP_496325.1; NM_063924.5. [Q09601-2]
DR   AlphaFoldDB; Q09601; -.
DR   SMR; Q09601; -.
DR   BioGRID; 39976; 29.
DR   IntAct; Q09601; 19.
DR   STRING; 6239.R06F6.5b; -.
DR   iPTMnet; Q09601; -.
DR   EPD; Q09601; -.
DR   PaxDb; Q09601; -.
DR   PeptideAtlas; Q09601; -.
DR   EnsemblMetazoa; R06F6.5a.1; R06F6.5a.1; WBGene00003805. [Q09601-2]
DR   EnsemblMetazoa; R06F6.5b.1; R06F6.5b.1; WBGene00003805. [Q09601-1]
DR   GeneID; 174663; -.
DR   KEGG; cel:CELE_R06F6.5; -.
DR   UCSC; R06F6.5b; c. elegans. [Q09601-1]
DR   CTD; 174663; -.
DR   WormBase; R06F6.5a; CE01621; WBGene00003805; npp-19. [Q09601-2]
DR   WormBase; R06F6.5b; CE18121; WBGene00003805; npp-19. [Q09601-1]
DR   eggNOG; KOG4285; Eukaryota.
DR   GeneTree; ENSGT00390000005923; -.
DR   InParanoid; Q09601; -.
DR   OMA; HGEVVSH; -.
DR   OrthoDB; 1022149at2759; -.
DR   PhylomeDB; Q09601; -.
DR   Reactome; R-CEL-159227; Transport of the SLBP independent Mature mRNA.
DR   Reactome; R-CEL-159230; Transport of the SLBP Dependant Mature mRNA.
DR   Reactome; R-CEL-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR   Reactome; R-CEL-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-CEL-191859; snRNP Assembly.
DR   Reactome; R-CEL-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-CEL-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR   Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-CEL-4085377; SUMOylation of SUMOylation proteins.
DR   Reactome; R-CEL-4551638; SUMOylation of chromatin organization proteins.
DR   PRO; PR:Q09601; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00003805; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR   GO; GO:0044613; C:nuclear pore central transport channel; IBA:GO_Central.
DR   GO; GO:0044615; C:nuclear pore nuclear basket; IBA:GO_Central.
DR   GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR   GO; GO:0006999; P:nuclear pore organization; IBA:GO_Central.
DR   GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR   GO; GO:0007096; P:regulation of exit from mitosis; IMP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR017389; Nucleoporin_NUP53.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR007846; RRM_NUP35_dom.
DR   PANTHER; PTHR21527; PTHR21527; 1.
DR   Pfam; PF05172; Nup35_RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS51472; RRM_NUP35; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Membrane; Mitosis;
KW   mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW   Reference proteome; Translocation; Transport.
FT   CHAIN           1..381
FT                   /note="Nucleoporin NUP35"
FT                   /id="PRO_0000065418"
FT   DOMAIN          195..275
FT                   /note="RRM Nup35-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00804"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         356..358
FT                   /note="Missing (in isoform a)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_020780"
SQ   SEQUENCE   381 AA;  40786 MW;  209A625812D6A823 CRC64;
     MFSHLNQNTS GRHNSMDLNN SSISNFGTPV EQSTPALLFG KRKATVPSSY TASPLNTASA
     PCSDIFAVSA PAVPQHLKDT PGSKSVHWSP SLVQSGEKSA AQTQNTPANL SFGGNSSFSA
     PTKPAPQSIQ TSSFGGQAMH APPLRSLRDK VEPAKKISRR NTFTARSTPL STPITQRVTS
     RLAEAEEQPM EEEADAADTW VTVFGFQPSQ VSILLNLFSR HGEVVSHQTP SKGNFIHMRY
     SCVTHAQQAI SRNGTLLDQD TFIGVVQCTN KDVINGSASG IVARSSNIAA AANRSASMYN
     SFVENDMADQ SVNHNENSVL NSSNVFDANN SLNSSRISVR SGVGMRPLAA DQRTNILQGT
     PSVRKAPDGL LNKFWNTIGL N
 
 
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