NUP35_RAT
ID NUP35_RAT Reviewed; 325 AA.
AC Q68FY1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nucleoporin NUP35 {ECO:0000312|RGD:1303069};
DE AltName: Full=35 kDa nucleoporin;
DE AltName: Full=Nuclear pore complex protein Nup53;
DE AltName: Full=Nucleoporin NUP53 {ECO:0000250|UniProtKB:Q8NFH5};
GN Name=Nup35; Synonyms=Nup53;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH LAMIN B; NUP93;
RP NUP155 AND NUP205.
RX PubMed=15703211; DOI=10.1091/mbc.e04-10-0857;
RA Hawryluk-Gara L.A., Shibuya E.K., Wozniak R.W.;
RT "Vertebrate Nup53 interacts with the nuclear lamina and is required for the
RT assembly of a Nup93-containing complex.";
RL Mol. Biol. Cell 16:2382-2394(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 AND THR-264, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. May play a role in the association of MAD1 with the NPC (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TMEM48/NDC1 (By similarity). Forms a complex
CC with NUP93, NUP155, NUP205 and lamin B. The interaction with NUP93 is
CC direct (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:Q8NFH5}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q8NFH5, ECO:0000269|PubMed:15703211}; Peripheral
CC membrane protein {ECO:0000269|PubMed:15703211}. Note=Tightly associated
CC with the nuclear membrane and lamina. {ECO:0000250|UniProtKB:Q8NFH5}.
CC -!- SIMILARITY: Belongs to the Nup35 family. {ECO:0000305}.
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DR EMBL; BC078914; AAH78914.1; -; mRNA.
DR RefSeq; NP_001004229.1; NM_001004229.1.
DR AlphaFoldDB; Q68FY1; -.
DR SMR; Q68FY1; -.
DR CORUM; Q68FY1; -.
DR STRING; 10116.ENSRNOP00000012628; -.
DR iPTMnet; Q68FY1; -.
DR PhosphoSitePlus; Q68FY1; -.
DR jPOST; Q68FY1; -.
DR PaxDb; Q68FY1; -.
DR PRIDE; Q68FY1; -.
DR Ensembl; ENSRNOT00000113802; ENSRNOP00000095061; ENSRNOG00000009290.
DR GeneID; 295692; -.
DR KEGG; rno:295692; -.
DR UCSC; RGD:1303069; rat.
DR CTD; 129401; -.
DR RGD; 1303069; Nup35.
DR eggNOG; KOG4285; Eukaryota.
DR GeneTree; ENSGT00390000005923; -.
DR HOGENOM; CLU_056189_0_0_1; -.
DR InParanoid; Q68FY1; -.
DR OMA; FWVTIFG; -.
DR OrthoDB; 1163548at2759; -.
DR PhylomeDB; Q68FY1; -.
DR TreeFam; TF325369; -.
DR Reactome; R-RNO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-RNO-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-RNO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-RNO-191859; snRNP Assembly.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-RNO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-RNO-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-RNO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-RNO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:Q68FY1; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000009290; Expressed in testis and 19 other tissues.
DR Genevisible; Q68FY1; RN.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0005652; C:nuclear lamina; IDA:RGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
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:0042802; F:identical protein binding; ISO:RGD.
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:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
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: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 PIRSF; PIRSF038119; Nucleoporin_NUP53; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51472; RRM_NUP35; 1.
PE 1: Evidence at protein level;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..325
FT /note="Nucleoporin NUP35"
FT /id="PRO_0000234296"
FT DOMAIN 169..249
FT /note="RRM Nup35-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00804"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 128
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R4R6"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R4R6"
FT MOD_RES 264
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 272
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 307
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
SQ SEQUENCE 325 AA; 34802 MW; 5EC3D9E5FE80B9FB CRC64;
MAAFAVDPQA PTLGSEPMML GSPTSPKPGA NAQFLPGFLM GDLPAPVTPQ PRSISGPSVG
VMEMRSPLLA GGSPPQPVVP AHKDKSGAPP VRSIYDDISS PGLGSTPLPS RRQANISVLQ
SPLVGVTTPV TGQSMFSPAN IGQPRKTTLS PAQLDPFYTQ GDSLTSEDHL DDTWVTVFGF
PQASASYILL QFAQYGNILK HVMSNTGNWM HIRYQSKLQA RKALSKDGRI FGESIMIGVK
PCIDKNVMEN SDRGVLSSPS LAFTPPIRTL GTPTQPGSTP RVSTMRPLAT AYKASTSDYQ
VISDRQTPKK DESLVSRAME YMFGW
