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Q99567

- NUP88_HUMAN

UniProt

Q99567 - NUP88_HUMAN

Protein

Nuclear pore complex protein Nup88

Gene

NUP88

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (08 Nov 2002)
      Previous versions | rss
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    Functioni

    Essential component of nuclear pore complex.

    GO - Molecular functioni

    1. transporter activity Source: ProtInc

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cytokine-mediated signaling pathway Source: Reactome
    3. glucose transport Source: Reactome
    4. hexose transport Source: Reactome
    5. mitotic cell cycle Source: Reactome
    6. mitotic nuclear envelope disassembly Source: Reactome
    7. mRNA transport Source: UniProtKB-KW
    8. protein transport Source: UniProtKB-KW
    9. regulation of glucose transport Source: Reactome
    10. small molecule metabolic process Source: Reactome
    11. transmembrane transport Source: Reactome
    12. 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 complex protein Nup88
    Alternative name(s):
    88 kDa nucleoporin
    Nucleoporin Nup88
    Gene namesi
    Name:NUP88
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:8067. NUP88.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nuclear pore Source: ProtInc
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31855.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 741740Nuclear pore complex protein Nup88PRO_0000204887Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei35 – 351Phosphoserine1 Publication
    Modified residuei50 – 501Phosphoserine1 Publication
    Modified residuei517 – 5171Phosphoserine7 Publications
    Modified residuei525 – 5251Phosphothreonine4 Publications
    Modified residuei540 – 5401Phosphoserine1 Publication
    Modified residuei698 – 6981PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ99567.
    PaxDbiQ99567.
    PeptideAtlasiQ99567.
    PRIDEiQ99567.

    PTM databases

    PhosphoSiteiQ99567.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ99567.
    BgeeiQ99567.
    CleanExiHS_NUP88.
    GenevestigatoriQ99567.

    Organism-specific databases

    HPAiCAB002209.
    HPA021816.

    Interactioni

    Subunit structurei

    Interacts with NUP214/CAN.1 Publication

    Protein-protein interaction databases

    BioGridi110981. 24 interactions.
    IntActiQ99567. 13 interactions.
    MINTiMINT-191368.
    STRINGi9606.ENSP00000225696.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99567.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili585 – 65167Sequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG274278.
    HOGENOMiHOG000234330.
    HOVERGENiHBG052700.
    InParanoidiQ99567.
    KOiK14318.
    OMAiLYENGET.
    OrthoDBiEOG72C500.
    PhylomeDBiQ99567.
    TreeFamiTF105307.

    Family and domain databases

    InterProiIPR019321. Nucleoporin_Nup88.
    [Graphical view]
    PfamiPF10168. Nup88. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q99567-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAEGPVGD GELWQTWLPN HVVFLRLREG LKNQSPTEAE KPASSSLPSS    50
    PPPQLLTRNV VFGLGGELFL WDGEDSSFLV VRLRGPSGGG EEPALSQYQR 100
    LLCINPPLFE IYQVLLSPTQ HHVALIGIKG LMVLELPKRW GKNSEFEGGK 150
    STVNCSTTPV AERFFTSSTS LTLKHAAWYP SEILDPHVVL LTSDNVIRIY 200
    SLREPQTPTN VIILSEAEEE SLVLNKGRAY TASLGETAVA FDFGPLAAVP 250
    KTLFGQNGKD EVVAYPLYIL YENGETFLTY ISLLHSPGNI GKLLGPLPMH 300
    PAAEDNYGYD ACAVLCLPCV PNILVIATES GMLYHCVVLE GEEEDDHTSE 350
    KSWDSRIDLI PSLYVFECVE LELALKLASG EDDPFDSDFS CPVKLHRDPK 400
    CPSRYHCTHE AGVHSVGLTW IHKLHKFLGS DEEDKDSLQE LSTEQKCFVE 450
    HILCTKPLPC RQPAPIRGFW IVPDILGPTM ICITSTYECL IWPLLSTVHP 500
    ASPPLLCTRE DVEVAESPLR VLAETPDSFE KHIRSILQRS VANPAFLKAS 550
    EKDIAPPPEE CLQLLSRATQ VFREQYILKQ DLAKEEIQRR VKLLCDQKKK 600
    QLEDLSYCRE ERKSLREMAE RLADKYEEAK EKQEDIMNRM KKLLHSFHSE 650
    LPVLSDSERD MKKELQLIPD QLRHLGNAIK QVTMKKDYQQ QKMEKVLSLP 700
    KPTIILSAYQ RKCIQSILKE EGEHIREMVK QINDIRNHVN F 741
    Length:741
    Mass (Da):83,542
    Last modified:November 8, 2002 - v2
    Checksum:i954A8E2E203BC20B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti247 – 2471A → D in CAA69904. (PubMed:9049309)Curated
    Sequence conflicti291 – 30111GKLLGPLPMHP → WKAVGSIAHAS in CAA69904. (PubMed:9049309)CuratedAdd
    BLAST
    Sequence conflicti456 – 4561K → R in CAA69904. (PubMed:9049309)Curated
    Sequence conflicti518 – 5181P → S in CAA69904. (PubMed:9049309)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti289 – 2891N → S.
    Corresponds to variant rs1806245 [ dbSNP | Ensembl ].
    VAR_029340

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08612 mRNA. Translation: CAA69904.1.
    CH471108 Genomic DNA. Translation: EAW90340.1.
    CH471108 Genomic DNA. Translation: EAW90342.1.
    BC000335 mRNA. Translation: AAH00335.1.
    CCDSiCCDS11070.1.
    RefSeqiNP_002523.2. NM_002532.4.
    UniGeneiHs.584784.

    Genome annotation databases

    EnsembliENST00000573584; ENSP00000458954; ENSG00000108559.
    GeneIDi4927.
    KEGGihsa:4927.
    UCSCiuc002gbo.2. human.

    Polymorphism databases

    DMDMi25008854.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08612 mRNA. Translation: CAA69904.1 .
    CH471108 Genomic DNA. Translation: EAW90340.1 .
    CH471108 Genomic DNA. Translation: EAW90342.1 .
    BC000335 mRNA. Translation: AAH00335.1 .
    CCDSi CCDS11070.1.
    RefSeqi NP_002523.2. NM_002532.4.
    UniGenei Hs.584784.

    3D structure databases

    ProteinModelPortali Q99567.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110981. 24 interactions.
    IntActi Q99567. 13 interactions.
    MINTi MINT-191368.
    STRINGi 9606.ENSP00000225696.

    PTM databases

    PhosphoSitei Q99567.

    Polymorphism databases

    DMDMi 25008854.

    Proteomic databases

    MaxQBi Q99567.
    PaxDbi Q99567.
    PeptideAtlasi Q99567.
    PRIDEi Q99567.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000573584 ; ENSP00000458954 ; ENSG00000108559 .
    GeneIDi 4927.
    KEGGi hsa:4927.
    UCSCi uc002gbo.2. human.

    Organism-specific databases

    CTDi 4927.
    GeneCardsi GC17M005180.
    HGNCi HGNC:8067. NUP88.
    HPAi CAB002209.
    HPA021816.
    MIMi 602552. gene.
    neXtProti NX_Q99567.
    PharmGKBi PA31855.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG274278.
    HOGENOMi HOG000234330.
    HOVERGENi HBG052700.
    InParanoidi Q99567.
    KOi K14318.
    OMAi LYENGET.
    OrthoDBi EOG72C500.
    PhylomeDBi Q99567.
    TreeFami TF105307.

    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

    ChiTaRSi NUP88. human.
    GeneWikii NUP88.
    GenomeRNAii 4927.
    NextBioi 18975.
    PROi Q99567.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99567.
    Bgeei Q99567.
    CleanExi HS_NUP88.
    Genevestigatori Q99567.

    Family and domain databases

    InterProi IPR019321. Nucleoporin_Nup88.
    [Graphical view ]
    Pfami PF10168. Nup88. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and the novel nuclear pore component Nup88."
      Fornerod M., van Deursen J.M., van Baal S., Reynolds A., Davis D., Murti K.G., Fransen J., Grosveld G.
      EMBO J. 16:807-816(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NUP214/CAN.
      Tissue: Placenta.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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: Lung.
    4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517 AND THR-525, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517 AND THR-525, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-50; SER-517 AND THR-525, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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: IDENTIFICATION BY MASS SPECTROMETRY [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-517, 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-517; THR-525 AND SER-540, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNUP88_HUMAN
    AccessioniPrimary (citable) accession number: Q99567
    Secondary accession number(s): D3DTM2, Q9BWE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2002
    Last sequence update: November 8, 2002
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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

    External Data

    Dasty 3