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Protein

Nuclear pore glycoprotein p62

Gene

NUP62

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of the nuclear pore complex (PubMed:1915414). The N-terminal is probably involved in nucleocytoplasmic transport (PubMed:1915414). The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex (PubMed:1915414, PubMed:24107630). Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation (PubMed:24107630). It might be involved in protein recruitment to the centrosome after nuclear breakdown (PubMed:24107630).2 Publications

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • Hsp70 protein binding Source: Ensembl
  • Hsp90 protein binding Source: Ensembl
  • kinesin binding Source: Ensembl
  • nucleocytoplasmic transporter activity Source: GO_Central
  • phospholipid binding Source: GO_Central
  • PTB domain binding Source: Ensembl
  • receptor signaling complex scaffold activity Source: UniProtKB
  • SH2 domain binding Source: UniProtKB
  • structural constituent of nuclear pore Source: GO_Central
  • thyroid hormone receptor binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

GO - Biological processi

  • cell aging Source: Ensembl
  • cell death Source: UniProtKB
  • cell surface receptor signaling pathway Source: UniProtKB
  • centriole assembly Source: UniProtKB
  • centrosome cycle Source: UniProtKB
  • hormone-mediated signaling pathway Source: UniProtKB
  • intracellular transport of virus Source: Reactome
  • mitotic centrosome separation Source: UniProtKB
  • mitotic metaphase plate congression Source: UniProtKB
  • mitotic nuclear envelope disassembly Source: Reactome
  • mRNA export from nucleus Source: Reactome
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of epidermal growth factor receptor signaling pathway Source: Ensembl
  • negative regulation of MAP kinase activity Source: Ensembl
  • negative regulation of programmed cell death Source: UniProtKB
  • negative regulation of Ras protein signal transduction Source: Ensembl
  • positive regulation of centriole replication Source: UniProtKB
  • positive regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of mitotic cytokinetic process Source: UniProtKB
  • positive regulation of mitotic nuclear division Source: UniProtKB
  • positive regulation of protein localization to centrosome Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • protein heterotrimerization Source: Ensembl
  • protein import into nucleus Source: GO_Central
  • protein sumoylation Source: Reactome
  • regulation of cellular response to heat Source: Reactome
  • regulation of gene silencing by miRNA Source: Reactome
  • regulation of glycolytic process Source: Reactome
  • regulation of mitotic spindle organization Source: UniProtKB
  • regulation of protein import into nucleus Source: Ensembl
  • regulation of Ras protein signal transduction Source: UniProtKB
  • regulation of signal transduction Source: UniProtKB
  • ribonucleoprotein complex export from nucleus Source: GO_Central
  • spermatogenesis Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB
  • tRNA export from nucleus Source: Reactome
  • viral process Source: Reactome
  • viral transcription Source: Reactome

Keywordsi

Biological processHost-virus interaction, mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-191859. snRNP Assembly.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4551638. SUMOylation of chromatin organization proteins.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-6784531. tRNA processing in the nucleus.

Protein family/group databases

TCDBi1.I.1.1.3. the eukaryotic nuclear pore complex (e-npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear pore glycoprotein p62
Alternative name(s):
62 kDa nucleoporin
Nucleoporin Nup62
Gene namesi
Name:NUP62
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000213024.11.
HGNCiHGNC:8066. NUP62.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nuclear pore complex, Nucleus

Pathology & Biotechi

Involvement in diseasei

Infantile striatonigral degeneration (SNDI)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionNeurological disorder characterized by symmetrical degeneration of the caudate nucleus, putamen, and occasionally the globus pallidus, with little involvement of the rest of the brain. The clinical features include developmental regression, choreoathetosis, dystonia, spasticity, dysphagia, failure to thrive, nystagmus, optic atrophy, and mental retardation.
See also OMIM:271930
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_034904391Q → P in SNDI. 1 PublicationCorresponds to variant dbSNP:rs121917865Ensembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi23636.
MalaCardsiNUP62.
MIMi271930. phenotype.
OpenTargetsiENSG00000213024.
Orphaneti225154. Familial infantile bilateral striatal necrosis.
PharmGKBiPA31854.

Polymorphism and mutation databases

BioMutaiNUP62.
DMDMi134047855.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002048802 – 522Nuclear pore glycoprotein p62Add BLAST521

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Glycosylationi373O-linked (GlcNAc) threonineBy similarity1
Modified residuei408PhosphoserineCombined sources1
Modified residuei418PhosphoserineCombined sources1
Glycosylationi468O-linked (GlcNAc) serineBy similarity1
Disulfide bondi475Interchain (with NUP155)By similarity
Disulfide bondi506Interchain (with NUP155)By similarity

Post-translational modificationi

O-glycosylated. Contains about 10 N-acetylglucosamine side chain sites predicted for the entire protein, among which only one in the C-terminal.Curated
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

EPDiP37198.
MaxQBiP37198.
PaxDbiP37198.
PeptideAtlasiP37198.
PRIDEiP37198.

PTM databases

iPTMnetiP37198.
PhosphoSitePlusiP37198.
UniCarbKBiP37198.

Expressioni

Gene expression databases

BgeeiENSG00000213024.
CleanExiHS_NUP62.
ExpressionAtlasiP37198. baseline and differential.
GenevisibleiP37198. HS.

Organism-specific databases

HPAiCAB020724.
HPA005435.

Interactioni

Subunit structurei

Component of the p62 complex, a complex at least composed of NUP62, NUP54, and NUP58 (By similarity). Interacts with NUTF2 (By similarity). Interacts with HIKESHI (PubMed:22541429). Interacts with OSBPL8 (PubMed:21698267). Interacts with CAPG (PubMed:18266911). Interacts with SAS6 and TUBG1 at the centrosome (PubMed:24107630).By similarity4 Publications
(Microbial infection) Interacts with Epstein-barr virus BGLF4; this interaction allows BGLF4 nuclear entry.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9H6143EBI-347978,EBI-10249899
ABI2Q9NYB93EBI-347978,EBI-743598
ADAM15Q134443EBI-347978,EBI-77818
AGR3Q8TD065EBI-347978,EBI-3925742
ATXN7O152652EBI-347978,EBI-708350
BFSP1Q129343EBI-347978,EBI-10227494
BLOC1S6Q9UL455EBI-347978,EBI-465781
C1orf216Q8TAB55EBI-347978,EBI-747505
CAF40P538293EBI-347978,EBI-28306From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).
CCDC121Q6ZUS54EBI-347978,EBI-2836982
CCDC146Q8IYE04EBI-347978,EBI-10749669
CCDC146Q8IYE0-23EBI-347978,EBI-10247802
CCDC150Q8NCX03EBI-347978,EBI-10269342
CCDC153Q494R43EBI-347978,EBI-10241443
CCHCR1Q8TD31-35EBI-347978,EBI-10175300
CCR4P313843EBI-347978,EBI-4396From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).
CENPUQ71F233EBI-347978,EBI-2515234
CEP57L1Q8IYX8-23EBI-347978,EBI-10181988
CRCT1Q9UGL95EBI-347978,EBI-713677
DTNBO609414EBI-347978,EBI-740402
FABP3P054136EBI-347978,EBI-704216
HAUS1Q96CS23EBI-347978,EBI-2514791
hCG_1987119A0A024R8L24EBI-347978,EBI-14103818
HSF2Q039333EBI-347978,EBI-2556750
HSF2Q03933-23EBI-347978,EBI-10223348
IFT20Q8IY313EBI-347978,EBI-744203
IKBIPQ70UQ03EBI-347978,EBI-2557212
ISCUQ9H1K15EBI-347978,EBI-1047335
KANSL1Q7Z3B34EBI-347978,EBI-740244
KIFC3Q9BVG83EBI-347978,EBI-2125614
KLHL32Q5THT13EBI-347978,EBI-10247181
KPNA2P522923EBI-347978,EBI-349938
KRT1P042646EBI-347978,EBI-298429
KRT20P359005EBI-347978,EBI-742094
LMO2P257913EBI-347978,EBI-739696
NUP54Q7Z3B48EBI-347978,EBI-741048
NUP57P488373EBI-347978,EBI-12324From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).
NUP58Q9BVL25EBI-347978,EBI-2811583
NUP82P403683EBI-347978,EBI-12331From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).
NUTF2P619705EBI-347978,EBI-591778
NXF1Q9UBU99EBI-347978,EBI-398874
OIP5O434825EBI-347978,EBI-536879
ORF10E5LBS62EBI-347978,EBI-14033439From Human herpesvirus 8.
PHF21AQ96BD55EBI-347978,EBI-745085
PIN1Q135265EBI-347978,EBI-714158
SMARCE1Q969G33EBI-347978,EBI-455078
SNAPC5O759713EBI-347978,EBI-749483
SNN1P482323EBI-347978,EBI-28775From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).
SPC25P400143EBI-347978,EBI-22458From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).
SSC5DA1L4H15EBI-347978,EBI-10172867
SUOXP516875EBI-347978,EBI-3921347
SWC7Q067073EBI-347978,EBI-32671From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).
THAP1Q9NVV911EBI-347978,EBI-741515
TXLNAP402225EBI-347978,EBI-359793
UL54P102383EBI-347978,EBI-6883946From Human herpesvirus 1 (strain 17).
WASHC3Q9Y3C07EBI-347978,EBI-712969
XPO6Q96QU8-23EBI-347978,EBI-10293124
YPL077CQ028313EBI-347978,EBI-31828From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).

GO - Molecular functioni

  • Hsp70 protein binding Source: Ensembl
  • Hsp90 protein binding Source: Ensembl
  • kinesin binding Source: Ensembl
  • PTB domain binding Source: Ensembl
  • receptor signaling complex scaffold activity Source: UniProtKB
  • SH2 domain binding Source: UniProtKB
  • thyroid hormone receptor binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117165. 168 interactors.
DIPiDIP-29749N.
IntActiP37198. 106 interactors.
MINTiMINT-121394.
STRINGi9606.ENSP00000305503.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H4Dmodel-A1-522[»]
5IJNelectron microscopy21.40H/N/T/Z1-522[»]
5IJOelectron microscopy21.40H/N/T/Z1-522[»]
ProteinModelPortaliP37198.
SMRiP37198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati6 – 712
Repeati44 – 4522
Repeati76 – 7732
Repeati114 – 11542
Repeati142 – 14352

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni6 – 1435 X 2 AA repeats of F-GAdd BLAST138
Regioni328 – 458Required for centrosome localization1 PublicationAdd BLAST131

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili328 – 458Sequence analysisAdd BLAST131

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi9 – 288Thr-richAdd BLAST280
Compositional biasi176 – 331Ala-richAdd BLAST156

Domaini

Contains FG repeats.

Sequence similaritiesi

Belongs to the nucleoporin NSP1/NUP62 family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG2196. Eukaryota.
ENOG410XT5X. LUCA.
GeneTreeiENSGT00730000111010.
HOGENOMiHOG000007693.
HOVERGENiHBG052699.
InParanoidiP37198.
KOiK14306.
OMAiDEMMSKQ.
OrthoDBiEOG091G0KV9.
PhylomeDBiP37198.
TreeFamiTF324795.

Family and domain databases

InterProiView protein in InterPro
IPR026010. NSP1/NUP62.
IPR007758. Nucleoporin_NSP1_C.
IPR033072. NUP62_met.
PANTHERiPTHR12084. PTHR12084. 1 hit.
PTHR12084:SF6. PTHR12084:SF6. 1 hit.
PfamiView protein in Pfam
PF05064. Nsp1_C. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P37198-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGFNFGGTG APTGGFTFGT AKTATTTPAT GFSFSTSGTG GFNFGAPFQP
60 70 80 90 100
ATSTPSTGLF SLATQTPATQ TTGFTFGTAT LASGGTGFSL GIGASKLNLS
110 120 130 140 150
NTAATPAMAN PSGFGLGSSN LTNAISSTVT SSQGTAPTGF VFGPSTTSVA
160 170 180 190 200
PATTSGGFSF TGGSTAQPSG FNIGSAGNSA QPTAPATLPF TPATPAATTA
210 220 230 240 250
GATQPAAPTP TATITSTGPS LFASIATAPT SSATTGLSLC TPVTTAGAPT
260 270 280 290 300
AGTQGFSLKA PGAASGTSTT TSTAATATAT TTSSSSTTGF ALNLKPLAPA
310 320 330 340 350
GIPSNTAAAV TAPPGPGAAA GAAASSAMTY AQLESLINKW SLELEDQERH
360 370 380 390 400
FLQQATQVNA WDRTLIENGE KITSLHREVE KVKLDQKRLD QELDFILSQQ
410 420 430 440 450
KELEDLLSPL EELVKEQSGT IYLQHADEER EKTYKLAENI DAQLKRMAQD
460 470 480 490 500
LKDIIEHLNT SGAPADTSDP LQQICKILNA HMDSLQWIDQ NSALLQRKVE
510 520
EVTKVCEGRR KEQERSFRIT FD
Length:522
Mass (Da):53,255
Last modified:March 20, 2007 - v3
Checksum:i1FF65018452719A3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti418 – 419SG → RA in CAA41411 (PubMed:1915414).Curated2
Sequence conflicti431E → Q in CAA41411 (PubMed:1915414).Curated1
Sequence conflicti507E → V in CAA41411 (PubMed:1915414).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_028064139G → S. Corresponds to variant dbSNP:rs3745489Ensembl.1
Natural variantiVAR_013467233A → S. Corresponds to variant dbSNP:rs2290772Ensembl.1
Natural variantiVAR_028065283S → T3 PublicationsCorresponds to variant dbSNP:rs1062798Ensembl.1
Natural variantiVAR_034904391Q → P in SNDI. 1 PublicationCorresponds to variant dbSNP:rs121917865Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58521 mRNA. Translation: CAA41411.1.
AL162061 mRNA. Translation: CAB82399.1.
AK125857 mRNA. Translation: BAG54257.1.
CR541721 mRNA. Translation: CAG46522.1.
AC011452 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52576.1.
BC003663 mRNA. Translation: AAH03663.1.
BC014842 mRNA. Translation: AAH14842.1.
BC050717 mRNA. Translation: AAH50717.1.
BC095410 mRNA. Translation: AAH95410.1.
BC101104 mRNA. Translation: AAI01105.1.
BC101105 mRNA. Translation: AAI01106.1.
BC101106 mRNA. Translation: AAI01107.1.
BC101107 mRNA. Translation: AAI01108.1.
CCDSiCCDS12788.1.
PIRiS41819.
RefSeqiNP_001180286.1. NM_001193357.1.
NP_036478.2. NM_012346.4.
NP_057637.2. NM_016553.4.
NP_714940.1. NM_153718.3.
NP_714941.1. NM_153719.3.
UniGeneiHs.574492.

Genome annotation databases

EnsembliENST00000352066; ENSP00000305503; ENSG00000213024.
ENST00000422090; ENSP00000407331; ENSG00000213024.
ENST00000596217; ENSP00000471191; ENSG00000213024.
ENST00000597029; ENSP00000473192; ENSG00000213024.
GeneIDi23636.
KEGGihsa:23636.
UCSCiuc002pqy.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiNUP62_HUMAN
AccessioniPrimary (citable) accession number: P37198
Secondary accession number(s): B3KWU5
, Q503A4, Q6GTM2, Q96C43, Q9NSL1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: March 20, 2007
Last modified: September 27, 2017
This is version 187 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families