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NUP88_RAT
ID   NUP88_RAT               Reviewed;         742 AA.
AC   O08658;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Nuclear pore complex protein Nup88;
DE   AltName: Full=88 kDa nucleoporin;
DE   AltName: Full=Nucleoporin Nup84;
DE   AltName: Full=Nucleoporin Nup88;
GN   Name=Nup88; Synonyms=Nup84;
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 [MRNA], AND INTERACTION WITH NUP214/CAN.
RC   TISSUE=Thyroid carcinoma;
RX   PubMed=9166401; DOI=10.1083/jcb.137.5.989;
RA   Bastos R., Ribas de Pouplana L., Enarson M., Bodoor K., Burke B.;
RT   "Nup84, a novel nucleoporin that is associated with CAN/Nup214 on the
RT   cytoplasmic face of the nuclear pore complex.";
RL   J. Cell Biol. 137:989-1000(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518 AND SER-699, 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: Component of nuclear pore complex.
CC       {ECO:0000250|UniProtKB:Q99567}.
CC   -!- SUBUNIT: Interacts with NUP214/CAN. Interacts with NUP62 and NUP98 (By
CC       similarity). {ECO:0000250|UniProtKB:Q99567,
CC       ECO:0000269|PubMed:9166401}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC       {ECO:0000250|UniProtKB:Q99567}.
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DR   EMBL; U93692; AAB52419.1; -; mRNA.
DR   EMBL; BC072524; AAH72524.1; -; mRNA.
DR   RefSeq; NP_446068.1; NM_053616.1.
DR   AlphaFoldDB; O08658; -.
DR   SMR; O08658; -.
DR   CORUM; O08658; -.
DR   STRING; 10116.ENSRNOP00000009015; -.
DR   iPTMnet; O08658; -.
DR   PhosphoSitePlus; O08658; -.
DR   jPOST; O08658; -.
DR   PaxDb; O08658; -.
DR   PRIDE; O08658; -.
DR   GeneID; 113929; -.
DR   KEGG; rno:113929; -.
DR   UCSC; RGD:620182; rat.
DR   CTD; 4927; -.
DR   RGD; 620182; Nup88.
DR   VEuPathDB; HostDB:ENSRNOG00000006126; -.
DR   eggNOG; KOG4460; Eukaryota.
DR   HOGENOM; CLU_017144_0_0_1; -.
DR   InParanoid; O08658; -.
DR   OMA; HINQIQL; -.
DR   OrthoDB; 1149034at2759; -.
DR   PhylomeDB; O08658; -.
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   PRO; PR:O08658; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000006126; Expressed in testis and 20 other tissues.
DR   Genevisible; O08658; RN.
DR   GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR   GO; GO:0005643; C:nuclear pore; IDA:RGD.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; IEA:InterPro.
DR   GO; GO:0000278; P:mitotic cell cycle; IDA:RGD.
DR   GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central.
DR   GO; GO:0000056; P:ribosomal small subunit export from nucleus; IBA:GO_Central.
DR   InterPro; IPR019321; Nucleoporin_Nup88.
DR   InterPro; IPR037700; NUP88/NUP82.
DR   PANTHER; PTHR13257; PTHR13257; 2.
DR   Pfam; PF10168; Nup88; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; mRNA transport; Nuclear pore complex; Nucleus;
KW   Phosphoprotein; Protein transport; Reference proteome; Translocation;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q99567"
FT   CHAIN           2..742
FT                   /note="Nuclear pore complex protein Nup88"
FT                   /id="PRO_0000204889"
FT   REGION          34..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          597..652
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99567"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99567"
FT   MOD_RES         380
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99567"
FT   MOD_RES         438
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99567"
FT   MOD_RES         518
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         541
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99567"
FT   MOD_RES         699
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   742 AA;  83585 MW;  E2C38D0DCEFFB3D8 CRC64;
     MAAAAGPVGD GELWQSWLPN HVVFLRLREG LKNQSPAEAD KPATSTSPSC PPLPPHLPTR
     NLVFGLGGEL FLWDAEGSAF LVVRLRGPSG GSVEPPLSQY QRLLCINPPL FEIHQVLLSP
     TQHHVALIGT KGLMALELPQ RWGKDSEFEG GKATVNCSTI PIAERFFTSS TSLTLKHAAW
     YPSEMLDPHI VLLTSDNVIR IYSLREPQTP TKVIVLSEAE EESLILNKGR AYTASLGETA
     VAFDFGPLVT VSKNMFEQKD REAVAYPLYI LYENGETFLT YVSLLHSPGN IGKLLGPLPM
     HPAAEDNYGY DACAILCLPC VPNILVIATE SGMLYHCVVL EGEEDDDQTL EKSWDPRADL
     IPSLYVFECV ELELALKLAS AEDDPFASDF SCPIKLHRDP KCPSRYHCSH EAGVHSVGLT
     WIHKLHKFLG SDEEDKDSLQ ELTAEQKCFV EHILCTKPLP CRQPAPIRGF WIVPDILGPT
     MICITSTYEC LIRPLLSTVH PASPPLLCTR EDAGVAESPL RILAEAPDSF EKHIKRILQR
     SAANPALLKS SEKDLAPPPE ECLQLISRAT QVFREQYILK QDLAKEEIQR RVKLLCDQKR
     KQLEDLNYCR EERKSLREMA ERLADKYEEA KEKQEDIMNR MKKVLHSFHT QLPVLSDSER
     DMKKELQLIP DQLRHLGNAI KQVTMKKDYQ QRKMEKVLSP QKPTITLSAY QRKCIQSILK
     EEGEHIREMV KQINDIRNHV NF
 
 
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