NUP62_RAT
ID NUP62_RAT Reviewed; 525 AA.
AC P17955; A2VCW0;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Nuclear pore glycoprotein p62;
DE AltName: Full=62 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup62;
GN Name=Nup62;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Fischer; TISSUE=Thyroid;
RX PubMed=2190987; DOI=10.1083/jcb.110.6.1861;
RA Starr C.M., D'Onofrio M., Park M.K., Hanover J.A.;
RT "Primary sequence and heterologous expression of nuclear pore glycoprotein
RT p62.";
RL J. Cell Biol. 110:1861-1871(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2050692; DOI=10.1016/s0021-9258(18)99053-8;
RA D'Onofrio M., Lee M.D., Starr C.M., Miller M., Hanover J.A.;
RT "The gene encoding rat nuclear pore glycoprotein p62 is intronless.";
RL J. Biol. Chem. 266:11980-11985(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 370-525, PARTIAL PROTEIN SEQUENCE, AND
RP GLYCOSYLATION AT SER-471.
RC TISSUE=Thyroid;
RX PubMed=3200844; DOI=10.1073/pnas.85.24.9595;
RA D'Onofrio M., Starr C.M., Park M.K., Holt G.D., Haltiwanger R.S.,
RA Hart G.W., Hanover J.A.;
RT "Partial cDNA sequence encoding a nuclear pore protein modified by O-linked
RT N-acetylglucosamine.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:9595-9599(1988).
RN [5]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH NUP58 AND NUP54, INTERACTION
RP WITH NUTF2, AND SUBCELLULAR LOCATION.
RX PubMed=8707840; DOI=10.1083/jcb.134.3.589;
RA Hu T., Guan T., Gerace L.;
RT "Molecular and functional characterization of the p62 complex, an assembly
RT of nuclear pore complex glycoproteins.";
RL J. Cell Biol. 134:589-601(1996).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND IDENTIFICATION BY
RP 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: Essential component of the nuclear pore complex
CC (PubMed:2190987, PubMed:8707840). The N-terminal is probably involved
CC in nucleocytoplasmic transport (By similarity). The C-terminal is
CC involved in protein-protein interaction probably via coiled-coil
CC formation, promotes its association with centrosomes and may function
CC in anchorage of p62 to the pore complex (By similarity). Plays a role
CC in mitotic cell cycle progression by regulating centrosome segregation,
CC centriole maturation and spindle orientation (By similarity). It might
CC be involved in protein recruitment to the centrosome after nuclear
CC breakdown (By similarity). {ECO:0000250|UniProtKB:P37198,
CC ECO:0000269|PubMed:2190987, ECO:0000269|PubMed:8707840}.
CC -!- SUBUNIT: Component of the p62 complex, a complex at least composed of
CC NUP62, NUP54, and NUP58 (PubMed:8707840). Interacts with NUP88 (By
CC similarity). Interacts with NUTF2 (PubMed:8707840). Interacts with
CC HIKESHI (By similarity). Interacts with OSBPL8 (By similarity).
CC Interacts with CAPG (By similarity). Interacts with SAS6 and TUBG1 at
CC the centrosome (By similarity). Interacts with MCM3AP (By similarity).
CC {ECO:0000250|UniProtKB:P37198, ECO:0000269|PubMed:8707840}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:8707840}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:P37198}. Nucleus envelope
CC {ECO:0000269|PubMed:2190987}. 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: 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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nucleoporin NSP1/NUP62 family.
CC {ECO:0000305}.
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DR EMBL; X52583; CAA36813.1; -; mRNA.
DR EMBL; M62992; AAA41789.1; -; Genomic_DNA.
DR EMBL; BC128709; AAI28710.1; -; mRNA.
DR EMBL; J04143; AAA60741.1; -; mRNA.
DR PIR; A35596; A35596.
DR RefSeq; NP_075586.1; NM_023098.2.
DR RefSeq; XP_006229212.1; XM_006229150.3.
DR RefSeq; XP_006229213.1; XM_006229151.3.
DR PDB; 3T97; X-ray; 2.80 A; A/C=362-425.
DR PDB; 5H1X; X-ray; 2.41 A; A/B/C=361-412.
DR PDBsum; 3T97; -.
DR PDBsum; 5H1X; -.
DR AlphaFoldDB; P17955; -.
DR SMR; P17955; -.
DR BioGRID; 249332; 4.
DR CORUM; P17955; -.
DR DIP; DIP-44925N; -.
DR IntAct; P17955; 1.
DR STRING; 10116.ENSRNOP00000067556; -.
DR GlyConnect; 470; 1 O-Linked glycan.
DR GlyGen; P17955; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P17955; -.
DR PhosphoSitePlus; P17955; -.
DR jPOST; P17955; -.
DR PaxDb; P17955; -.
DR PRIDE; P17955; -.
DR Ensembl; ENSRNOT00000074847; ENSRNOP00000067556; ENSRNOG00000048733.
DR Ensembl; ENSRNOT00000117253; ENSRNOP00000081212; ENSRNOG00000048733.
DR GeneID; 65274; -.
DR KEGG; rno:65274; -.
DR UCSC; RGD:619938; rat.
DR CTD; 23636; -.
DR RGD; 619938; Nup62.
DR eggNOG; KOG2196; Eukaryota.
DR GeneTree; ENSGT00940000161737; -.
DR HOGENOM; CLU_025936_0_0_1; -.
DR InParanoid; P17955; -.
DR OMA; EMMSKQV; -.
DR PhylomeDB; P17955; -.
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:P17955; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000048733; Expressed in testis and 20 other tissues.
DR Genevisible; P17955; RN.
DR GO; GO:0005642; C:annulate lamellae; IDA:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0090543; C:Flemming body; ISO:RGD.
DR GO; GO:0072686; C:mitotic spindle; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; IDA:RGD.
DR GO; GO:0005643; C:nuclear pore; IDA:GO_Central.
DR GO; GO:0044613; C:nuclear pore central transport channel; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0000922; C:spindle pole; ISO:RGD.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:RGD.
DR GO; GO:0019894; F:kinesin binding; IPI:RGD.
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; IPI:RGD.
DR GO; GO:0051425; F:PTB domain binding; ISO:RGD.
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; IDA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; ISO:RGD.
DR GO; GO:0098534; P:centriole assembly; ISO:RGD.
DR GO; GO:0007098; P:centrosome cycle; ISO:RGD.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:RGD.
DR GO; GO:0007100; P:mitotic centrosome separation; ISO:RGD.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0046601; P:positive regulation of centriole replication; ISO:RGD.
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:RGD.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:RGD.
DR GO; GO:1904781; P:positive regulation of protein localization to centrosome; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:RGD.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISO:RGD.
DR GO; GO:0042306; P:regulation of protein import into nucleus; IDA:RGD.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
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 3D-structure; Acetylation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT CHAIN 2..525
FT /note="Nuclear pore glycoprotein p62"
FT /id="PRO_0000204882"
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 260..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..461
FT /note="Required for centrosome localization"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT COILED 331..461
FT /evidence="ECO:0000255"
FT COMPBIAS 266..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37198"
FT CARBOHYD 471
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:3200844"
FT DISULFID 478
FT /note="Interchain (with NUP155)"
FT /evidence="ECO:0000250"
FT DISULFID 509
FT /note="Interchain (with NUP155)"
FT /evidence="ECO:0000250"
FT CONFLICT 371..372
FT /note="NG -> FR (in Ref. 4; AAA60741)"
FT /evidence="ECO:0000305"
FT HELIX 363..403
FT /evidence="ECO:0007829|PDB:5H1X"
FT HELIX 406..410
FT /evidence="ECO:0007829|PDB:3T97"
FT TURN 411..416
FT /evidence="ECO:0007829|PDB:3T97"
SQ SEQUENCE 525 AA; 53397 MW; B0F02F6BF6C0816E CRC64;
MSGFNFGGTG APAGGFTFGT AKTATTTPAT GFSFSASGTG TGGFNFGTPS QPAATTPSTS
LFSLATQTST TQTPGFNFGT TPASGGTGFS LGISTPKLSL SSTAATPATA NTGSFGLGSS
TLTNAISGAS TSSQGTAPTG FVFGSSTTSA PSTGTTGFSF TSGSASQPGA SGFNIGSVGS
LAQPTALSGS PFTPATLATT TAGATQPAAA TPTAATTSAG STLFASIAAA PASSSTTVLS
LSAPATTAAT PTAGTLGFSL KAPGAAPGAS TTSTTTTTTT TTTTASTSSS TTTTGFALSL
KPLVPAGPSS VAATALPASS TAVGTTTGPA MTYAQLESLI NKWSLELEDQ ERHFLQQATQ
VNAWDRTLIE NGEKITSLHR EVEKVKLDQK RLDQELDFIL SQQKELEDLL SPLEESVKEQ
SGTIYLQHAD EEREKTYKLA ENIDAQLKRM AQDLKDIIEH LNMAGGPADT SDPLQQICKI
LNAHMDSLQW VDQSSALLQR RVEEASRVCE SRRKEQERSL RIAFD
