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Protein

Nuclear pore glycoprotein p62

Gene

Nup62

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is probably involved in protein-protein interaction via coiled-coil formation and may function in anchorage of p62 to the pore complex.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

ReactomeiR-RNO-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-RNO-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-RNO-3108214. SUMOylation of DNA damage response and repair proteins.
R-RNO-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-RNO-3371453. Regulation of HSF1-mediated heat shock response.
R-RNO-4570464. SUMOylation of RNA binding proteins.
R-RNO-4615885. SUMOylation of DNA replication proteins.
R-RNO-5578749. Transcriptional regulation by small RNAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear pore glycoprotein p62
Alternative name(s):
62 kDa nucleoporin
Nucleoporin Nup62
Gene namesi
Name:Nup62
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi619938. Nup62.

Subcellular locationi

GO - Cellular componenti

  • annulate lamellae Source: RGD
  • cytoplasm Source: UniProtKB-KW
  • Flemming body Source: Ensembl
  • intracellular ribonucleoprotein complex Source: Ensembl
  • nuclear membrane Source: RGD
  • nuclear pore Source: UniProtKB
  • protein complex Source: RGD
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 525524Nuclear pore glycoprotein p62PRO_0000204882Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei411 – 4111PhosphoserineCombined sources
Glycosylationi471 – 4711O-linked (GlcNAc)1 Publication
Disulfide bondi478 – 478Interchain (with NUP155)By similarity
Disulfide bondi509 – 509Interchain (with NUP155)By similarity

Post-translational modificationi

The the inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP17955.
PRIDEiP17955.

PTM databases

iPTMnetiP17955.
PhosphoSiteiP17955.
UniCarbKBiP17955.

Expressioni

Gene expression databases

GenevisibleiP17955. RN.

Interactioni

Subunit structurei

Component of the p62 complex, a complex at least composed of NUP62, NUP54, and NUP58 (PubMed:8707840). Interacts with C11orf73/Hikeshi. Interacts with OSBPL8 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi249332. 4 interactions.
DIPiDIP-44925N.
MINTiMINT-1522948.
STRINGi10116.ENSRNOP00000067556.

Structurei

Secondary structure

1
525
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi367 – 40438Combined sources
Helixi406 – 4105Combined sources
Turni411 – 4166Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3T97X-ray2.80A/C362-425[»]
ProteinModelPortaliP17955.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili331 – 461131Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi17 – 294278Thr-richAdd
BLAST
Compositional biasi105 – 269165Ala-richAdd
BLAST
Compositional biasi271 – 28414Poly-ThrAdd
BLAST
Compositional biasi291 – 2944Poly-Thr

Domaini

Contains F-X-F-G repeats.

Sequence similaritiesi

Belongs to the nucleoporin NSP1/NUP62 family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG2196. Eukaryota.
ENOG410XT5X. LUCA.
GeneTreeiENSGT00730000111010.
HOVERGENiHBG052699.
InParanoidiP17955.
KOiK14306.
OMAiTSPVMTY.
OrthoDBiEOG7PZRZB.
PhylomeDBiP17955.

Family and domain databases

InterProiIPR026010. NSP1/NUP62.
IPR007758. Nucleoporin_NSP1_C.
IPR033072. NUP62_met.
[Graphical view]
PANTHERiPTHR12084. PTHR12084. 1 hit.
PTHR12084:SF2. PTHR12084:SF2. 1 hit.
PfamiPF05064. Nsp1_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17955-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGFNFGGTG APAGGFTFGT AKTATTTPAT GFSFSASGTG TGGFNFGTPS
60 70 80 90 100
QPAATTPSTS LFSLATQTST TQTPGFNFGT TPASGGTGFS LGISTPKLSL
110 120 130 140 150
SSTAATPATA NTGSFGLGSS TLTNAISGAS TSSQGTAPTG FVFGSSTTSA
160 170 180 190 200
PSTGTTGFSF TSGSASQPGA SGFNIGSVGS LAQPTALSGS PFTPATLATT
210 220 230 240 250
TAGATQPAAA TPTAATTSAG STLFASIAAA PASSSTTVLS LSAPATTAAT
260 270 280 290 300
PTAGTLGFSL KAPGAAPGAS TTSTTTTTTT TTTTASTSSS TTTTGFALSL
310 320 330 340 350
KPLVPAGPSS VAATALPASS TAVGTTTGPA MTYAQLESLI NKWSLELEDQ
360 370 380 390 400
ERHFLQQATQ VNAWDRTLIE NGEKITSLHR EVEKVKLDQK RLDQELDFIL
410 420 430 440 450
SQQKELEDLL SPLEESVKEQ SGTIYLQHAD EEREKTYKLA ENIDAQLKRM
460 470 480 490 500
AQDLKDIIEH LNMAGGPADT SDPLQQICKI LNAHMDSLQW VDQSSALLQR
510 520
RVEEASRVCE SRRKEQERSL RIAFD
Length:525
Mass (Da):53,397
Last modified:November 1, 1990 - v1
Checksum:iB0F02F6BF6C0816E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti371 – 3722NG → FR in AAA60741 (PubMed:3200844).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52583 mRNA. Translation: CAA36813.1.
M62992 Genomic DNA. Translation: AAA41789.1.
BC128709 mRNA. Translation: AAI28710.1.
J04143 mRNA. Translation: AAA60741.1.
PIRiA35596.
RefSeqiNP_075586.1. NM_023098.2.
XP_006229212.1. XM_006229150.2.
XP_006229213.1. XM_006229151.2.
UniGeneiRn.54450.

Genome annotation databases

EnsembliENSRNOT00000074847; ENSRNOP00000067556; ENSRNOG00000048733.
GeneIDi65274.
KEGGirno:65274.
UCSCiRGD:619938. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52583 mRNA. Translation: CAA36813.1.
M62992 Genomic DNA. Translation: AAA41789.1.
BC128709 mRNA. Translation: AAI28710.1.
J04143 mRNA. Translation: AAA60741.1.
PIRiA35596.
RefSeqiNP_075586.1. NM_023098.2.
XP_006229212.1. XM_006229150.2.
XP_006229213.1. XM_006229151.2.
UniGeneiRn.54450.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3T97X-ray2.80A/C362-425[»]
ProteinModelPortaliP17955.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249332. 4 interactions.
DIPiDIP-44925N.
MINTiMINT-1522948.
STRINGi10116.ENSRNOP00000067556.

PTM databases

iPTMnetiP17955.
PhosphoSiteiP17955.
UniCarbKBiP17955.

Proteomic databases

PaxDbiP17955.
PRIDEiP17955.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000074847; ENSRNOP00000067556; ENSRNOG00000048733.
GeneIDi65274.
KEGGirno:65274.
UCSCiRGD:619938. rat.

Organism-specific databases

CTDi23636.
RGDi619938. Nup62.

Phylogenomic databases

eggNOGiKOG2196. Eukaryota.
ENOG410XT5X. LUCA.
GeneTreeiENSGT00730000111010.
HOVERGENiHBG052699.
InParanoidiP17955.
KOiK14306.
OMAiTSPVMTY.
OrthoDBiEOG7PZRZB.
PhylomeDBiP17955.

Enzyme and pathway databases

ReactomeiR-RNO-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-RNO-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-RNO-3108214. SUMOylation of DNA damage response and repair proteins.
R-RNO-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-RNO-3371453. Regulation of HSF1-mediated heat shock response.
R-RNO-4570464. SUMOylation of RNA binding proteins.
R-RNO-4615885. SUMOylation of DNA replication proteins.
R-RNO-5578749. Transcriptional regulation by small RNAs.

Miscellaneous databases

PROiP17955.

Gene expression databases

GenevisibleiP17955. RN.

Family and domain databases

InterProiIPR026010. NSP1/NUP62.
IPR007758. Nucleoporin_NSP1_C.
IPR033072. NUP62_met.
[Graphical view]
PANTHERiPTHR12084. PTHR12084. 1 hit.
PTHR12084:SF2. PTHR12084:SF2. 1 hit.
PfamiPF05064. Nsp1_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary sequence and heterologous expression of nuclear pore glycoprotein p62."
    Starr C.M., D'Onofrio M., Park M.K., Hanover J.A.
    J. Cell Biol. 110:1861-1871(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer.
    Tissue: Thyroid.
  2. "The gene encoding rat nuclear pore glycoprotein p62 is intronless."
    D'Onofrio M., Lee M.D., Starr C.M., Miller M., Hanover J.A.
    J. Biol. Chem. 266:11980-11985(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Partial cDNA sequence encoding a nuclear pore protein modified by O-linked N-acetylglucosamine."
    D'Onofrio M., Starr C.M., Park M.K., Holt G.D., Haltiwanger R.S., Hart G.W., Hanover J.A.
    Proc. Natl. Acad. Sci. U.S.A. 85:9595-9599(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 370-525, PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT SER-471.
    Tissue: Thyroid.
  5. "Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins."
    Hu T., Guan T., Gerace L.
    J. Cell Biol. 134:589-601(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH NUP58 AND NUP54.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNUP62_RAT
AccessioniPrimary (citable) accession number: P17955
Secondary accession number(s): A2VCW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 8, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.