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NUP93_RAT
ID   NUP93_RAT               Reviewed;         819 AA.
AC   Q66HC5;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Nuclear pore complex protein Nup93;
DE   AltName: Full=93 kDa nucleoporin;
DE   AltName: Full=Nucleoporin Nup93;
GN   Name=Nup93;
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=Testis;
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; NUP35;
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).
CC   -!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly
CC       and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to
CC       the NPC. During renal development, regulates podocyte migration and
CC       proliferation through SMAD4 signaling. {ECO:0000250|UniProtKB:Q8N1F7}.
CC   -!- SUBUNIT: Part of the nuclear pore complex (NPC). Component of the p62
CC       complex, a complex composed of NUP62 and NUP54. Forms a complex with
CC       NUP35, NUP155, NUP205 and lamin B; the interaction with NUP35 is
CC       direct. Does not interact with TPR. Interacts with SMAD4 and IPO7;
CC       translocates SMAD4 to the nucleus through the NPC upon BMP7 stimulation
CC       resulting in activation of SMAD4 signaling.
CC       {ECO:0000250|UniProtKB:Q8N1F7}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:15703211};
CC       Peripheral membrane protein {ECO:0000269|PubMed:15703211}. Nucleus,
CC       nuclear pore complex {ECO:0000250|UniProtKB:Q8N1F7}. Nucleus envelope
CC       {ECO:0000250|UniProtKB:Q8N1F7}. Note=Localizes at the nuclear basket
CC       and at or near the nuclear entry to the gated channel of the pore.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the nucleoporin interacting component (NIC)
CC       family. {ECO:0000305}.
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DR   EMBL; BC081925; AAH81925.1; -; mRNA.
DR   RefSeq; NP_001011925.1; NM_001011925.1.
DR   AlphaFoldDB; Q66HC5; -.
DR   SMR; Q66HC5; -.
DR   BioGRID; 253671; 3.
DR   CORUM; Q66HC5; -.
DR   STRING; 10116.ENSRNOP00000025086; -.
DR   iPTMnet; Q66HC5; -.
DR   PhosphoSitePlus; Q66HC5; -.
DR   jPOST; Q66HC5; -.
DR   PaxDb; Q66HC5; -.
DR   PRIDE; Q66HC5; -.
DR   Ensembl; ENSRNOT00000025086; ENSRNOP00000025086; ENSRNOG00000018564.
DR   GeneID; 291874; -.
DR   KEGG; rno:291874; -.
DR   UCSC; RGD:1311525; rat.
DR   CTD; 9688; -.
DR   RGD; 1311525; Nup93.
DR   eggNOG; KOG2168; Eukaryota.
DR   GeneTree; ENSGT00390000016353; -.
DR   HOGENOM; CLU_011846_1_0_1; -.
DR   InParanoid; Q66HC5; -.
DR   OMA; LLMCGQF; -.
DR   OrthoDB; 187731at2759; -.
DR   PhylomeDB; Q66HC5; -.
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:Q66HC5; -.
DR   Proteomes; UP000002494; Chromosome 19.
DR   Bgee; ENSRNOG00000018564; Expressed in thymus and 20 other tissues.
DR   Genevisible; Q66HC5; RN.
DR   GO; GO:0005813; C:centrosome; ISO:RGD.
DR   GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR   GO; GO:0034399; C:nuclear periphery; ISS:UniProtKB.
DR   GO; GO:0005643; C:nuclear pore; ISS:UniProtKB.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; ISS:UniProtKB.
DR   GO; GO:0006998; P:nuclear envelope organization; ISS:UniProtKB.
DR   GO; GO:0051292; P:nuclear pore complex assembly; ISS:UniProtKB.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR   GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
DR   InterPro; IPR007231; Nucleoporin_int_Nup93/Nic96.
DR   PANTHER; PTHR11225; PTHR11225; 1.
DR   Pfam; PF04097; Nic96; 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..819
FT                   /note="Nuclear pore complex protein Nup93"
FT                   /id="PRO_0000356296"
FT   MOD_RES         49
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT   MOD_RES         430
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT   MOD_RES         767
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1F7"
SQ   SEQUENCE   819 AA;  93302 MW;  F49DE268CA25B863 CRC64;
     MDTEGFGELL QQAEQLAAET EGISELPHVE RNLQEIQQAG ERLRSRTLTR TSQETADVKA
     SVLLGSRGLD ISHISQRLES LSAATTFEPL EPVKDTDIQG FLKNEKDNAL LSAIEESRKR
     TFGMAEEYHR ESMLVEWEQV KQRILHTLLA SGEDALDFTQ ESEPSYVSDV SPPGRSSLDS
     IEMAYARQIY IYNEKIVSGH LQPNLVDLCA SVAELDDKSI SDMWAMVKQM TDVVLTPATD
     ALKSRSSVEV RMDFVKQALG YLEQSYKNYT LVTVFGNLHQ AQLGGVPGTY QLVRSFLNIK
     LPAPSPGLQD GEVEGHPVWA LIYYCMRCGD LLAASQVVSR AQHQLGEFKT WFQEYMNSKD
     RRLSPATENK LRLHYRRALR NNTDPYKRAV YCIIGRCDIT DNQSEVADKT EDYLWLKLNQ
     VCFDDDGTSS PQDRLTLSQF QKQLLEDYGE SHFTVNQQPF LYFQVLFLTA QFEAAIAFLF
     RMERLRCHAV HVALVLFELK LLLKSSGQSA QLLSHEPGDP PCMRRLNFVR LLMLYTRKFE
     STDPREALQY FYFLRDEKDS QGENMFLRCV SELVIESREF DMILGKLEND GSRKPGVIDK
     FTSDTKPIIN KVASVAENKG LFEEAAKLYD LAKNADKVLE LMNKLLSPVV PQISAPQSNK
     ERLKNMALSI AERYRAQGIS ANKFVDSTFY LLLDLITFFD EYHSGHIDRA FDIIDRLKLV
     PLNQESMEER VAAFRNFSDE IRHNLSEVLL ATMNILFTQF KRLKGTSPSS ATRPQRVIED
     RDSQLRSQAR ALITFAGMIP YRTSGDTNAR LVQMEVLMN
 
 
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