NUP62_MOUSE
ID NUP62_MOUSE Reviewed; 526 AA.
AC Q63850; Q99JN7;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Nuclear pore glycoprotein p62;
DE AltName: Full=62 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup62;
GN Name=Nup62;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1915419;
RA Cordes V., Waizenegger I., Krohne G.;
RT "Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse: cDNA
RT cloning and identification of its glycosylated region.";
RL Eur. J. Cell Biol. 55:31-47(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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-412, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP DISULFIDE BONDS, AND MUTAGENESIS OF CYS-479 AND CYS-510.
RX PubMed=23641069; DOI=10.1242/jcs.124172;
RA Yoshimura S.H., Otsuka S., Kumeta M., Taga M., Takeyasu K.;
RT "Intermolecular disulfide bonds between nucleoporins regulate karyopherin-
RT dependent nuclear transport.";
RL J. Cell Sci. 126:3141-3150(2013).
CC -!- FUNCTION: Essential component of the nuclear pore complex. The N-
CC terminal is probably involved in nucleocytoplasmic transport. The C-
CC terminal is involved in protein-protein interaction probably via
CC coiled-coil formation, promotes its association with centrosomes and
CC may function in anchorage of p62 to the pore complex. Plays a role in
CC mitotic cell cycle progression by regulating centrosome segregation,
CC centriole maturation and spindle orientation. It might be involved in
CC protein recruitment to the centrosome after nuclear breakdown.
CC {ECO:0000250|UniProtKB:P37198}.
CC -!- SUBUNIT: Component of the p62 complex, a complex at least composed of
CC NUP62, NUP54, and NUP58. Interacts with NUP88. Interacts with NUTF2.
CC Interacts with HIKESHI. Interacts with OSBPL8. Interacts with CAPG.
CC Interacts with SAS6 and TUBG1 at the centrosome. Interacts with MCM3AP
CC (By similarity). {ECO:0000250|UniProtKB:P17955,
CC ECO:0000250|UniProtKB:P37198}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:P37198}. Nucleus envelope
CC {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P37198}.
CC Note=Central region of the nuclear pore, within the transporter. During
CC mitotic cell division, it associates with the poles of the mitotic
CC spindle. {ECO:0000250|UniProtKB:P37198}.
CC -!- DOMAIN: Contains FG repeats.
CC -!- PTM: O-glycosylated. {ECO:0000303|PubMed:1915419}.
CC -!- PTM: The inner channel of the NPC has a different redox environment
CC from the cytoplasm and allows the formation of interchain disulfide
CC bonds between some nucleoporins, the significant increase of these
CC linkages upon oxidative stress reduces the permeability of the NPC.
CC -!- SIMILARITY: Belongs to the nucleoporin NSP1/NUP62 family.
CC {ECO:0000305}.
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DR EMBL; S59342; AAB19953.1; -; mRNA.
DR EMBL; BC005784; AAH05784.1; -; mRNA.
DR CCDS; CCDS21216.1; -.
DR PIR; A56573; A56573.
DR RefSeq; NP_444304.1; NM_053074.2.
DR AlphaFoldDB; Q63850; -.
DR SMR; Q63850; -.
DR BioGRID; 201879; 13.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q63850; 1.
DR MINT; Q63850; -.
DR STRING; 10090.ENSMUSP00000056785; -.
DR GlyGen; Q63850; 2 sites.
DR iPTMnet; Q63850; -.
DR PhosphoSitePlus; Q63850; -.
DR SwissPalm; Q63850; -.
DR EPD; Q63850; -.
DR MaxQB; Q63850; -.
DR PaxDb; Q63850; -.
DR PRIDE; Q63850; -.
DR ProteomicsDB; 293814; -.
DR Antibodypedia; 1686; 378 antibodies from 38 providers.
DR DNASU; 18226; -.
DR Ensembl; ENSMUST00000057195; ENSMUSP00000056785; ENSMUSG00000109511.
DR Ensembl; ENSMUST00000207103; ENSMUSP00000147181; ENSMUSG00000109511.
DR Ensembl; ENSMUST00000208626; ENSMUSP00000146695; ENSMUSG00000109511.
DR GeneID; 18226; -.
DR KEGG; mmu:18226; -.
DR UCSC; uc009gqw.2; mouse.
DR CTD; 23636; -.
DR MGI; MGI:1351500; Nup62.
DR VEuPathDB; HostDB:ENSMUSG00000109511; -.
DR eggNOG; KOG2196; Eukaryota.
DR GeneTree; ENSGT00940000161737; -.
DR HOGENOM; CLU_025936_0_0_1; -.
DR InParanoid; Q63850; -.
DR OMA; EMMSKQV; -.
DR PhylomeDB; Q63850; -.
DR TreeFam; TF324795; -.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR BioGRID-ORCS; 18226; 18 hits in 72 CRISPR screens.
DR ChiTaRS; Nup62; mouse.
DR PRO; PR:Q63850; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q63850; protein.
DR Bgee; ENSMUSG00000109511; Expressed in floor plate of midbrain and 252 other tissues.
DR ExpressionAtlas; Q63850; baseline and differential.
DR Genevisible; Q63850; MM.
DR GO; GO:0005642; C:annulate lamellae; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0090543; C:Flemming body; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IDA:MGI.
DR GO; GO:0005643; C:nuclear pore; IDA:MGI.
DR GO; GO:0044613; C:nuclear pore central transport channel; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:MGI.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0051425; F:PTB domain binding; IPI:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; ISS:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; NAS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; IDA:MGI.
DR GO; GO:0098534; P:centriole assembly; ISO:MGI.
DR GO; GO:0007098; P:centrosome cycle; ISO:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:MGI.
DR GO; GO:0007100; P:mitotic centrosome separation; ISO:MGI.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:MGI.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:UniProtKB.
DR GO; GO:0043069; P:negative regulation of programmed cell death; ISS:UniProtKB.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0046601; P:positive regulation of centriole replication; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:1903438; P:positive regulation of mitotic cytokinetic process; ISO:MGI.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:MGI.
DR GO; GO:1904781; P:positive regulation of protein localization to centrosome; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISO:MGI.
DR GO; GO:0042306; P:regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR InterPro; IPR026010; NSP1/NUP62.
DR InterPro; IPR007758; Nucleoporin_NSP1_C.
DR InterPro; IPR033072; NUP62_met.
DR PANTHER; PTHR12084; PTHR12084; 1.
DR PANTHER; PTHR12084:SF12; PTHR12084:SF12; 1.
DR Pfam; PF05064; Nsp1_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Disulfide bond;
KW Glycoprotein; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT CHAIN 2..526
FT /note="Nuclear pore glycoprotein p62"
FT /id="PRO_0000204881"
FT REPEAT 6..7
FT /note="1"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT REPEAT 46..47
FT /note="2"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT REPEAT 78..79
FT /note="3"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT REPEAT 115..116
FT /note="4"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT REPEAT 143..144
FT /note="5"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT REGION 6..144
FT /note="5 X 2 AA repeats of F-G"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT REGION 43..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..462
FT /note="Required for centrosome localization"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT COILED 332..462
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT CARBOHYD 377
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 472
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT DISULFID 479
FT /note="Interchain (with NUP155)"
FT /evidence="ECO:0000305|PubMed:23641069"
FT DISULFID 510
FT /note="Interchain (with NUP155)"
FT /evidence="ECO:0000305|PubMed:23641069"
FT MUTAGEN 479
FT /note="C->S: Loss of reduction of influx rate of NLS cargo
FT upon oxidative stress; when associated with S-509."
FT /evidence="ECO:0000269|PubMed:23641069"
FT MUTAGEN 510
FT /note="C->S: Loss of reduction of influx rate of NLS cargo
FT upon oxidative stress; when associated with S-478."
FT /evidence="ECO:0000269|PubMed:23641069"
FT CONFLICT 113
FT /note="G -> V (in Ref. 1; AAB19953)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="A -> V (in Ref. 1; AAB19953)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 53255 MW; 54AE74B211018FE4 CRC64;
MSGFNFGGTG APAGGFTFGT AKTATTTPAT GFSFSASGTG TGGFNFGTPS QPAATTPSTS
LFSLTTQTPT TQTPGFNFGT TPASGGTGFS LGISTPKLSL SNAAATPATA NTGSFGLGSS
TLTNAISSGS TSNQGTAPTG FVFGSSTTSA PSTGSTGFSF TSGSASQPGA SGFSLGSVGS
SAQPTALSGS PFTPATLVTT TAGATQPAAA APTAATTSAG STLFASIAAA PASSSATGLS
LPAPVTTAAT PSAGTLGFSL KAPGAAPGAS TTSTTTTTTT TTTTAAAAAA STTTTGFALS
LKPLVSAGPS SVAATALPAS STAAGTATGP AMTYAQLESL INKWSLELED QERHFLQQAT
QVNAWDRTLI ENGEKITSLH REVEKVKLDQ KRLDQELDFI LSQQKELEDL LSPLEESVKE
QSGTIYLQHA DEEREKTYKL AENIDAQLKR MAQDLKDIIE HLNMAGGPAD TSDPLQQICK
ILNAHMDSLQ WVDQSSALLQ RRVEEASRVC EGRRKEQERS LRIAFD
