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P37198

- NUP62_HUMAN

UniProt

P37198 - NUP62_HUMAN

Protein

Nuclear pore glycoprotein p62

Gene

NUP62

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (20 Mar 2007)
      Previous versions | rss
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    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

    1. chromatin binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. receptor signaling complex scaffold activity Source: UniProtKB
    4. SH2 domain binding Source: UniProtKB
    5. structural constituent of nuclear pore Source: InterPro
    6. thyroid hormone receptor binding Source: UniProtKB
    7. ubiquitin binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cell aging Source: Ensembl
    3. cell death Source: UniProtKB
    4. cell surface receptor signaling pathway Source: UniProtKB
    5. cytokine-mediated signaling pathway Source: Reactome
    6. glucose transport Source: Reactome
    7. hexose transport Source: Reactome
    8. hormone-mediated signaling pathway Source: UniProtKB
    9. mitotic cell cycle Source: Reactome
    10. mitotic nuclear envelope disassembly Source: Reactome
    11. mRNA transport Source: UniProtKB-KW
    12. negative regulation of apoptotic process Source: UniProtKB
    13. negative regulation of cell proliferation Source: UniProtKB
    14. negative regulation of epidermal growth factor receptor signaling pathway Source: Ensembl
    15. negative regulation of MAP kinase activity Source: Ensembl
    16. negative regulation of programmed cell death Source: UniProtKB
    17. negative regulation of Ras protein signal transduction Source: Ensembl
    18. nucleocytoplasmic transport Source: GOC
    19. positive regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
    20. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    21. positive regulation of transcription, DNA-templated Source: UniProtKB
    22. protein transport Source: UniProtKB-KW
    23. regulation of glucose transport Source: Reactome
    24. regulation of Ras protein signal transduction Source: UniProtKB
    25. regulation of signal transduction Source: UniProtKB
    26. small molecule metabolic process Source: Reactome
    27. transcription, DNA-templated Source: UniProtKB
    28. transmembrane transport Source: Reactome
    29. viral process Source: Reactome

    Keywords - Biological processi

    mRNA transport, Protein transport, Translocation, Transport

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
    REACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
    REACT_7991. Vpr-mediated nuclear import of PICs.
    REACT_9395. Nuclear import of Rev protein.

    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
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:8066. NUP62.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. intracellular membrane-bounded organelle Source: HPA
    3. nuclear envelope Source: UniProtKB
    4. nuclear membrane Source: HPA
    5. nuclear pore Source: UniProtKB
    6. nucleocytoplasmic shuttling complex Source: UniProtKB
    7. pore complex Source: UniProtKB
    8. ribonucleoprotein complex Source: MGI
    9. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti391 – 3911Q → P in SNDI. 1 Publication
    VAR_034904

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi271930. phenotype.
    Orphaneti225154. Familial infantile bilateral striatal necrosis.
    PharmGKBiPA31854.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 522521Nuclear pore glycoprotein p62PRO_0000204880Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Glycosylationi373 – 3731O-linked (GlcNAc)By similarity
    Modified residuei408 – 4081Phosphoserine2 Publications
    Glycosylationi468 – 4681O-linked (GlcNAc)By similarity
    Disulfide bondi475 – 475Interchain (with NUP155)By similarity
    Disulfide bondi506 – 506Interchain (with NUP155)By similarity

    Post-translational modificationi

    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

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP37198.
    PaxDbiP37198.
    PRIDEiP37198.

    PTM databases

    PhosphoSiteiP37198.
    UniCarbKBiP37198.

    Expressioni

    Gene expression databases

    ArrayExpressiP37198.
    BgeeiP37198.
    CleanExiHS_NUP62.
    GenevestigatoriP37198.

    Organism-specific databases

    HPAiCAB020724.
    HPA005435.

    Interactioni

    Subunit structurei

    Component of the p62 complex, a complex at least composed of NUP62, NUP54, and NUPL1 By similarity. Interacts with C11orf73/Hikeshi.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN7O152652EBI-347978,EBI-708350
    NXF1Q9UBU93EBI-347978,EBI-398874
    UL54P102383EBI-347978,EBI-6883946From a different organism.

    Protein-protein interaction databases

    BioGridi117165. 46 interactions.
    DIPiDIP-29749N.
    IntActiP37198. 29 interactions.
    MINTiMINT-121394.
    STRINGi9606.ENSP00000305503.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H4Dmodel-A1-522[»]
    ProteinModelPortaliP37198.
    SMRiP37198. Positions 361-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati2 – 981
    Repeati13 – 2192
    Repeati29 – 3793
    Repeati39 – 4794
    Repeati57 – 6595
    Repeati71 – 7996
    Repeati85 – 9397
    Repeati111 – 11998
    Repeati137 – 14599
    Repeati155 – 163910
    Repeati168 – 176911
    Repeati185 – 193912
    Repeati234 – 242913
    Repeati253 – 261914
    Repeati287 – 295915

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 29529415 X 9 AA approximate repeatsAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili328 – 458131Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 288280Thr-richAdd
    BLAST
    Compositional biasi176 – 331156Ala-richAdd
    BLAST

    Domaini

    Contains F-X-F-G repeats.

    Sequence similaritiesi

    Belongs to the nucleoporin NSP1/NUP62 family.Curated

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000007693.
    HOVERGENiHBG052699.
    InParanoidiP37198.
    KOiK14306.
    OMAiPAMTYAQ.
    OrthoDBiEOG7PZRZB.
    PhylomeDBiP37198.
    TreeFamiTF324795.

    Family and domain databases

    InterProiIPR026010. NSP1/NUP62.
    IPR007758. Nucleoporin_NSP1_C.
    [Graphical view]
    PANTHERiPTHR12084. PTHR12084. 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.

    P37198-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGFNFGGTG APTGGFTFGT AKTATTTPAT GFSFSTSGTG GFNFGAPFQP    50
    ATSTPSTGLF SLATQTPATQ TTGFTFGTAT LASGGTGFSL GIGASKLNLS 100
    NTAATPAMAN PSGFGLGSSN LTNAISSTVT SSQGTAPTGF VFGPSTTSVA 150
    PATTSGGFSF TGGSTAQPSG FNIGSAGNSA QPTAPATLPF TPATPAATTA 200
    GATQPAAPTP TATITSTGPS LFASIATAPT SSATTGLSLC TPVTTAGAPT 250
    AGTQGFSLKA PGAASGTSTT TSTAATATAT TTSSSSTTGF ALNLKPLAPA 300
    GIPSNTAAAV TAPPGPGAAA GAAASSAMTY AQLESLINKW SLELEDQERH 350
    FLQQATQVNA WDRTLIENGE KITSLHREVE KVKLDQKRLD QELDFILSQQ 400
    KELEDLLSPL EELVKEQSGT IYLQHADEER EKTYKLAENI DAQLKRMAQD 450
    LKDIIEHLNT SGAPADTSDP LQQICKILNA HMDSLQWIDQ NSALLQRKVE 500
    EVTKVCEGRR KEQERSFRIT FD 522
    Length:522
    Mass (Da):53,255
    Last modified:March 20, 2007 - v3
    Checksum:i1FF65018452719A3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti418 – 4192SG → RA in CAA41411. (PubMed:1915414)Curated
    Sequence conflicti431 – 4311E → Q in CAA41411. (PubMed:1915414)Curated
    Sequence conflicti507 – 5071E → V in CAA41411. (PubMed:1915414)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti139 – 1391G → S.
    Corresponds to variant rs3745489 [ dbSNP | Ensembl ].
    VAR_028064
    Natural varianti233 – 2331A → S.
    Corresponds to variant rs2290772 [ dbSNP | Ensembl ].
    VAR_013467
    Natural varianti283 – 2831S → T.3 Publications
    Corresponds to variant rs1062798 [ dbSNP | Ensembl ].
    VAR_028065
    Natural varianti391 – 3911Q → P in SNDI. 1 Publication
    VAR_034904

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    ENST00000413454; ENSP00000387991; ENSG00000213024.
    ENST00000422090; ENSP00000407331; ENSG00000213024.
    ENST00000596217; ENSP00000471191; ENSG00000213024.
    ENST00000597029; ENSP00000473192; ENSG00000213024.
    GeneIDi23636.
    KEGGihsa:23636.
    UCSCiuc002pqx.3. human.

    Polymorphism databases

    DMDMi134047855.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS12788.1.
    PIRi S41819.
    RefSeqi NP_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.
    UniGenei Hs.574492.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H4D model - A 1-522 [» ]
    ProteinModelPortali P37198.
    SMRi P37198. Positions 361-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117165. 46 interactions.
    DIPi DIP-29749N.
    IntActi P37198. 29 interactions.
    MINTi MINT-121394.
    STRINGi 9606.ENSP00000305503.

    PTM databases

    PhosphoSitei P37198.
    UniCarbKBi P37198.

    Polymorphism databases

    DMDMi 134047855.

    Proteomic databases

    MaxQBi P37198.
    PaxDbi P37198.
    PRIDEi P37198.

    Protocols and materials databases

    DNASUi 23636.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000352066 ; ENSP00000305503 ; ENSG00000213024 .
    ENST00000413454 ; ENSP00000387991 ; ENSG00000213024 .
    ENST00000422090 ; ENSP00000407331 ; ENSG00000213024 .
    ENST00000596217 ; ENSP00000471191 ; ENSG00000213024 .
    ENST00000597029 ; ENSP00000473192 ; ENSG00000213024 .
    GeneIDi 23636.
    KEGGi hsa:23636.
    UCSCi uc002pqx.3. human.

    Organism-specific databases

    CTDi 23636.
    GeneCardsi GC19M050410.
    H-InvDB HIX0016974.
    HGNCi HGNC:8066. NUP62.
    HPAi CAB020724.
    HPA005435.
    MIMi 271930. phenotype.
    605815. gene.
    neXtProti NX_P37198.
    Orphaneti 225154. Familial infantile bilateral striatal necrosis.
    PharmGKBi PA31854.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000007693.
    HOVERGENi HBG052699.
    InParanoidi P37198.
    KOi K14306.
    OMAi PAMTYAQ.
    OrthoDBi EOG7PZRZB.
    PhylomeDBi P37198.
    TreeFami TF324795.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
    REACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
    REACT_7991. Vpr-mediated nuclear import of PICs.
    REACT_9395. Nuclear import of Rev protein.

    Miscellaneous databases

    GeneWikii Nucleoporin_62.
    GenomeRNAii 23636.
    NextBioi 46419.
    PROi P37198.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P37198.
    Bgeei P37198.
    CleanExi HS_NUP62.
    Genevestigatori P37198.

    Family and domain databases

    InterProi IPR026010. NSP1/NUP62.
    IPR007758. Nucleoporin_NSP1_C.
    [Graphical view ]
    PANTHERi PTHR12084. PTHR12084. 1 hit.
    Pfami PF05064. Nsp1_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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.
      , 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. 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. 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. Cited for: VARIANT SNDI PRO-391.

    Entry informationi

    Entry nameiNUP62_HUMAN
    AccessioniPrimary (citable) accession number: P37198
    Secondary accession number(s): B3KWU5
    , Q503A4, Q6GTM2, Q96C43, Q9NSL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 155 of the entry and version 3 of the sequence. [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

    External Data

    Dasty 3