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P37198 (NUP62_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear pore glycoprotein p62
Alternative name(s):
62 kDa nucleoporin
Nucleoporin Nup62
Gene names
Name:NUP62
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length522 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Component of the p62 complex, a complex at least composed of NUP62, NUP54, and NUPL1 By similarity. Interacts with C11orf73/Hikeshi. Ref.12

Subcellular location

Nucleusnuclear pore complex. Cytoplasmcytoskeletonspindle pole. Note: Central region of the nuclear pore, within the transporter. During mitotic cell division, it associates with the poles of the mitotic spindle.

Domain

Contains F-X-F-G repeats.

Post-translational modification

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

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.

Involvement in disease

Infantile striatonigral degeneration (SNDI) [MIM:271930]: Neurological 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Sequence similarities

Belongs to the nucleoporin NSP1/NUP62 family.

Ontologies

Keywords
   Biological processmRNA transport
Protein transport
Translocation
Transport
   Cellular componentCytoplasm
Cytoskeleton
Nuclear pore complex
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainCoiled coil
Repeat
   PTMAcetylation
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cell aging

Inferred from electronic annotation. Source: Ensembl

cell death

Inferred from mutant phenotype PubMed 11244088. Source: UniProtKB

cell surface receptor signaling pathway

Inferred from direct assay PubMed 10799545. Source: UniProtKB

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

glucose transport

Traceable author statement. Source: Reactome

hexose transport

Traceable author statement. Source: Reactome

hormone-mediated signaling pathway

Non-traceable author statement PubMed 15625236. Source: UniProtKB

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear envelope disassembly

Traceable author statement. Source: Reactome

negative regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of Ras protein signal transduction

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from direct assay PubMed 11755531. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay PubMed 11013214. Source: UniProtKB

negative regulation of epidermal growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of programmed cell death

Inferred from direct assay PubMed 11244088. Source: UniProtKB

nucleocytoplasmic transport

Non-traceable author statement PubMed 8589458. Source: GOC

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay PubMed 10356400. Source: UniProtKB

positive regulation of epidermal growth factor receptor signaling pathway

Non-traceable author statement PubMed 11244088. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15625236. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of Ras protein signal transduction

Non-traceable author statement PubMed 11553620. Source: UniProtKB

regulation of glucose transport

Traceable author statement. Source: Reactome

regulation of signal transduction

Non-traceable author statement PubMed 8702753. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from direct assay PubMed 10373430. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Non-traceable author statement PubMed 10373430. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nuclear envelope

Inferred from direct assay PubMed 17098863. Source: UniProtKB

nuclear membrane

Inferred from direct assay. Source: HPA

nuclear pore

Inferred from direct assay Ref.1. Source: UniProtKB

nucleocytoplasmic shuttling complex

Non-traceable author statement PubMed 8589458. Source: UniProtKB

pore complex

Non-traceable author statement PubMed 15175862. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay PubMed 18809582. Source: MGI

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionSH2 domain binding

Inferred from direct assay PubMed 8650207. Source: UniProtKB

chromatin binding

Non-traceable author statement PubMed 11852044. Source: UniProtKB

receptor signaling complex scaffold activity

Inferred from direct assay PubMed 11244088. Source: UniProtKB

structural constituent of nuclear pore

Inferred from electronic annotation. Source: InterPro

thyroid hormone receptor binding

Inferred from physical interaction PubMed 15625236. Source: UniProtKB

ubiquitin binding

Inferred from direct assay PubMed 8702753. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATXN7O152652EBI-347978,EBI-708350
NXF1Q9UBU93EBI-347978,EBI-398874
UL54P102383EBI-347978,EBI-6883946From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 522521Nuclear pore glycoprotein p62
PRO_0000204880

Regions

Repeat2 – 981
Repeat13 – 2192
Repeat29 – 3793
Repeat39 – 4794
Repeat57 – 6595
Repeat71 – 7996
Repeat85 – 9397
Repeat111 – 11998
Repeat137 – 14599
Repeat155 – 163910
Repeat168 – 176911
Repeat185 – 193912
Repeat234 – 242913
Repeat253 – 261914
Repeat287 – 295915
Region2 – 29529415 X 9 AA approximate repeats
Coiled coil328 – 458131 Potential
Compositional bias9 – 288280Thr-rich
Compositional bias176 – 331156Ala-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.8 Ref.13
Modified residue4081Phosphoserine Ref.9 Ref.10
Glycosylation3731O-linked (GlcNAc) By similarity
Glycosylation4681O-linked (GlcNAc) By similarity
Disulfide bond475Interchain (with NUP155) By similarity
Disulfide bond506Interchain (with NUP155) By similarity

Natural variations

Natural variant1391G → S.
Corresponds to variant rs3745489 [ dbSNP | Ensembl ].
VAR_028064
Natural variant2331A → S.
Corresponds to variant rs2290772 [ dbSNP | Ensembl ].
VAR_013467
Natural variant2831S → T. Ref.1 Ref.2 Ref.7
Corresponds to variant rs1062798 [ dbSNP | Ensembl ].
VAR_028065
Natural variant3911Q → P in SNDI. Ref.14
VAR_034904

Experimental info

Sequence conflict418 – 4192SG → RA in CAA41411. Ref.1
Sequence conflict4311E → Q in CAA41411. Ref.1
Sequence conflict5071E → V in CAA41411. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P37198 [UniParc].

Last modified March 20, 2007. Version 3.
Checksum: 1FF65018452719A3

FASTA52253,255
        10         20         30         40         50         60 
MSGFNFGGTG APTGGFTFGT AKTATTTPAT GFSFSTSGTG GFNFGAPFQP ATSTPSTGLF 

        70         80         90        100        110        120 
SLATQTPATQ TTGFTFGTAT LASGGTGFSL GIGASKLNLS NTAATPAMAN PSGFGLGSSN 

       130        140        150        160        170        180 
LTNAISSTVT SSQGTAPTGF VFGPSTTSVA PATTSGGFSF TGGSTAQPSG FNIGSAGNSA 

       190        200        210        220        230        240 
QPTAPATLPF TPATPAATTA GATQPAAPTP TATITSTGPS LFASIATAPT SSATTGLSLC 

       250        260        270        280        290        300 
TPVTTAGAPT AGTQGFSLKA PGAASGTSTT TSTAATATAT TTSSSSTTGF ALNLKPLAPA 

       310        320        330        340        350        360 
GIPSNTAAAV TAPPGPGAAA GAAASSAMTY AQLESLINKW SLELEDQERH FLQQATQVNA 

       370        380        390        400        410        420 
WDRTLIENGE KITSLHREVE KVKLDQKRLD QELDFILSQQ KELEDLLSPL EELVKEQSGT 

       430        440        450        460        470        480 
IYLQHADEER EKTYKLAENI DAQLKRMAQD LKDIIEHLNT SGAPADTSDP LQQICKILNA 

       490        500        510        520 
HMDSLQWIDQ NSALLQRKVE EVTKVCEGRR KEQERSFRIT FD 

« Hide

References

« Hide 'large scale' references
[1]"Human nucleoporin p62 and the essential yeast nuclear pore protein NSP1 show sequence homology and a similar domain organization."
Carmo-Fonseca M., Kern H., Hurt E.C.
Eur. J. Cell Biol. 55:17-30(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-283.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-283.
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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], VARIANT THR-283.
Tissue: Pancreas, Skin and Urinary bladder.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Hikeshi, a nuclear import carrier for hsp70s, protects cells from heat shock-induced nuclear damage."
Kose S., Furuta M., Imamoto N.
Cell 149:578-589(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C11ORF73.
[13]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Mutated nup62 causes autosomal recessive infantile bilateral striatal necrosis."
Basel-Vanagaite L., Muncher L., Straussberg R., Pasmanik-Chor M., Yahav M., Rainshtein L., Walsh C.A., Magal N., Taub E., Drasinover V., Shalev H., Attia R., Rechavi G., Simon A.J., Shohat M.
Ann. Neurol. 60:214-222(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SNDI PRO-391.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS41819.
RefSeqNP_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.
UniGeneHs.574492.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H4Dmodel-A1-522[»]
ProteinModelPortalP37198.
SMRP37198. Positions 361-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117165. 46 interactions.
DIPDIP-29749N.
IntActP37198. 29 interactions.
MINTMINT-121394.
STRING9606.ENSP00000305503.

PTM databases

PhosphoSiteP37198.
UniCarbKBP37198.

Polymorphism databases

DMDM134047855.

Proteomic databases

PaxDbP37198.
PRIDEP37198.

Protocols and materials databases

DNASU23636.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000352066; ENSP00000305503; ENSG00000213024.
ENST00000413454; ENSP00000387991; ENSG00000213024.
ENST00000422090; ENSP00000407331; ENSG00000213024.
ENST00000596217; ENSP00000471191; ENSG00000213024.
ENST00000597029; ENSP00000473192; ENSG00000213024.
GeneID23636.
KEGGhsa:23636.
UCSCuc002pqx.3. human.

Organism-specific databases

CTD23636.
GeneCardsGC19M050410.
H-InvDBHIX0016974.
HGNCHGNC:8066. NUP62.
HPACAB020724.
HPA005435.
MIM271930. phenotype.
605815. gene.
neXtProtNX_P37198.
Orphanet225154. Familial infantile bilateral striatal necrosis.
PharmGKBPA31854.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000007693.
HOVERGENHBG052699.
InParanoidP37198.
KOK14306.
OMATSPVMTY.
OrthoDBEOG7PZRZB.
PhylomeDBP37198.
TreeFamTF324795.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP37198.
BgeeP37198.
CleanExHS_NUP62.
GenevestigatorP37198.

Family and domain databases

InterProIPR026010. NSP1/NUP62.
IPR007758. Nucleoporin_NSP1_C.
[Graphical view]
PANTHERPTHR12084. PTHR12084. 1 hit.
PfamPF05064. Nsp1_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNucleoporin_62.
GenomeRNAi23636.
NextBio46419.
PROP37198.
SOURCESearch...

Entry information

Entry nameNUP62_HUMAN
AccessionPrimary (citable) accession number: P37198
Secondary accession number(s): B3KWU5 expand/collapse secondary AC list , Q503A4, Q6GTM2, Q96C43, Q9NSL1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: March 20, 2007
Last modified: April 16, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM