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Q8WUM0

- NU133_HUMAN

UniProt

Q8WUM0 - NU133_HUMAN

Protein

Nuclear pore complex protein Nup133

Gene

NUP133

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    Involved in poly(A)+ RNA transport.1 Publication

    GO - Molecular functioni

    1. nucleocytoplasmic transporter activity Source: UniProtKB
    2. protein binding Source: UniProtKB

    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 export from nucleus Source: UniProtKB
    8. nuclear pore organization Source: UniProtKB
    9. paraxial mesoderm development Source: Ensembl
    10. protein transport Source: UniProtKB-KW
    11. regulation of glucose transport Source: Reactome
    12. small molecule metabolic process Source: Reactome
    13. transmembrane transport Source: Reactome
    14. viral process Source: Reactome

    Keywords - Biological processi

    mRNA transport, Protein transport, Translocation, Transport

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    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_682. Mitotic Prometaphase.
    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 Nup133
    Alternative name(s):
    133 kDa nucleoporin
    Nucleoporin Nup133
    Gene namesi
    Name:NUP133
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:18016. NUP133.

    Subcellular locationi

    Nucleusnuclear pore complex. Chromosomecentromerekinetochore
    Note: Located on both the cytoplasmic and nuclear sides of the nuclear pore. During mitosis, localizes to the kinetochores.

    GO - Cellular componenti

    1. condensed chromosome kinetochore Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB
    4. nuclear envelope Source: Reactome
    5. nuclear pore Source: UniProtKB
    6. nuclear pore outer ring Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Kinetochore, Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31847.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11561156Nuclear pore complex protein Nup133PRO_0000204838Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei7 – 71Phosphoserine1 Publication
    Modified residuei27 – 271Phosphoserine2 Publications
    Modified residuei28 – 281Phosphothreonine2 Publications
    Modified residuei41 – 411Phosphoserine1 Publication
    Modified residuei45 – 451Phosphoserine4 Publications
    Modified residuei50 – 501Phosphoserine7 Publications
    Modified residuei480 – 4801Phosphoserine1 Publication
    Modified residuei787 – 7871N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8WUM0.
    PaxDbiQ8WUM0.
    PRIDEiQ8WUM0.

    PTM databases

    PhosphoSiteiQ8WUM0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8WUM0.
    BgeeiQ8WUM0.
    CleanExiHS_NUP133.
    GenevestigatoriQ8WUM0.

    Organism-specific databases

    HPAiHPA059767.

    Interactioni

    Subunit structurei

    Forms part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, NUP133, NUP107 and Nup96. This complex plays a role in RNA export and in tethering Nup98 and NUP153 to the nucleus.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CENPFP494542EBI-295695,EBI-968343
    LRRK2Q5S0072EBI-295695,EBI-5323863
    NUP107P577406EBI-295695,EBI-295687

    Protein-protein interaction databases

    BioGridi120864. 29 interactions.
    IntActiQ8WUM0. 15 interactions.
    MINTiMINT-3046670.
    STRINGi9606.ENSP00000261396.

    Structurei

    Secondary structure

    1
    1156
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi77 – 837
    Helixi90 – 989
    Beta strandi105 – 1095
    Beta strandi113 – 1197
    Beta strandi122 – 1276
    Helixi134 – 1363
    Beta strandi139 – 1435
    Helixi153 – 1553
    Beta strandi156 – 1605
    Beta strandi172 – 1787
    Beta strandi183 – 1886
    Beta strandi197 – 2004
    Beta strandi209 – 2157
    Turni216 – 2183
    Beta strandi219 – 2246
    Beta strandi229 – 2346
    Beta strandi240 – 2445
    Beta strandi274 – 2807
    Turni281 – 2844
    Beta strandi285 – 29915
    Beta strandi304 – 3118
    Helixi312 – 32514
    Helixi331 – 3355
    Beta strandi339 – 34810
    Beta strandi351 – 3599
    Beta strandi363 – 3653
    Beta strandi367 – 3759
    Beta strandi386 – 3905
    Helixi400 – 4023
    Beta strandi406 – 4083
    Beta strandi412 – 4209
    Beta strandi422 – 4298
    Beta strandi440 – 4434
    Helixi446 – 4483
    Beta strandi451 – 4577
    Beta strandi460 – 4656
    Turni466 – 4683
    Beta strandi469 – 4757
    Helixi936 – 9427
    Helixi946 – 95914
    Helixi964 – 98017
    Helixi985 – 100622
    Helixi1012 – 10154
    Beta strandi1020 – 10234
    Helixi1028 – 10347
    Helixi1045 – 10517
    Turni1052 – 10576
    Helixi1067 – 107913
    Helixi1096 – 11027
    Helixi1125 – 11284
    Helixi1142 – 115514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XKSX-ray2.35A67-514[»]
    3CQCX-ray2.53B935-1156[»]
    3CQGX-ray3.00B934-1156[»]
    3I4RX-ray3.53B517-1156[»]
    DisProtiDP00318.
    ProteinModelPortaliQ8WUM0.
    SMRiQ8WUM0. Positions 75-477, 518-1156.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8WUM0.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the nucleoporin Nup133 family.Curated

    Phylogenomic databases

    eggNOGiNOG312399.
    HOGENOMiHOG000293246.
    HOVERGENiHBG052678.
    InParanoidiQ8WUM0.
    KOiK14300.
    OMAiMCRLMVP.
    OrthoDBiEOG7P8P70.
    PhylomeDBiQ8WUM0.
    TreeFamiTF106141.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR007187. Nucleoporin_Nup133/Nup155_C.
    IPR014908. Nucleoporin_Nup133/Nup155_N.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view]
    PfamiPF03177. Nucleoporin_C. 1 hit.
    PF08801. Nucleoporin_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8WUM0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFPAAPSPRT PGTGSRRGPL AGLGPGSTPR TASRKGLPLG SAVSSPVLFS     50
    PVGRRSSLSS RGTPTRMFPH HSITESVNYD VKTFGSSLPV KVMEALTLAE 100
    VDDQLTINID EGGWACLVCK EKLIIWKIAL SPITKLSVCK ELQLPPSDFH 150
    WSADLVALSY SSPSGEAHST QAVAVMVATR EGSIRYWPSL AGEDTYTEAF 200
    VDSGGDKTYS FLTAVQGGSF ILSSSGSQLI RLIPESSGKI HQHILPQGQG 250
    MLSGIGRKVS SLFGILSPSS DLTLSSVLWD RERSSFYSLT SSNISKWELD 300
    DSSEKHAYSW DINRALKENI TDAIWGSESN YEAIKEGVNI RYLDLKQNCD 350
    GLVILAAAWH SADNPCLIYY SLITIEDNGC QMSDAVTVEV TQYNPPFQSE 400
    DLILCQLTVP NFSNQTAYLY NESAVYVCST GTGKFSLPQE KIVFNAQGDS 450
    VLGAGACGGV PIIFSRNSGL VSITSRENVS ILAEDLEGSL ASSVAGPNSE 500
    SMIFETTTKN ETIAQEDKIK LLKAAFLQYC RKDLGHAQMV VDELFSSHSD 550
    LDSDSELDRA VTQISVDLMD DYPASDPRWA ESVPEEAPGF SNTSLIILHQ 600
    LEDKMKAHSF LMDFIHQVGL FGRLGSFPVR GTPMATRLLL CEHAEKLSAA 650
    IVLKNHHSRL SDLVNTAILI ALNKREYEIP SNLTPADVFF REVSQVDTIC 700
    ECLLEHEEQV LRDAPMDSIE WAEVVINVNN ILKDMLQAAS HYRQNRNSLY 750
    RREESLEKEP EYVPWTATSG PGGIRTVIIR QHEIVLKVAY PQADSNLRNI 800
    VTEQLVALID CFLDGYVSQL KSVDKSSNRE RYDNLEMEYL QKRSDLLSPL 850
    LSLGQYLWAA SLAEKYCDFD ILVQMCEQTD NQSRLQRYMT QFADQNFSDF 900
    LFRWYLEKGK RGKLLSQPIS QHGQLANFLQ AHEHLSWLHE INSQELEKAH 950
    ATLLGLANME TRYFAKKKTL LGLSKLAALA SDFSEDMLQE KIEEMAEQER 1000
    FLLHQETLPE QLLAEKQLNL SAMPVLTAPQ LIGLYICEEN RRANEYDFKK 1050
    ALDLLEYIDE EEDININDLK LEILCKALQR DNWSSSDGKD DPIEVSKDSI 1100
    FVKILQKLLK DGIQLSEYLP EVKDLLQADQ LGSLKSNPYF EFVLKANYEY 1150
    YVQGQI 1156
    Length:1,156
    Mass (Da):128,979
    Last modified:April 3, 2007 - v2
    Checksum:i78B733E353824577
    GO

    Sequence cautioni

    The sequence BAA91885.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB14106.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611R → G in BAA91829. (PubMed:14702039)Curated
    Sequence conflicti146 – 1461P → S in BAA91829. (PubMed:14702039)Curated
    Sequence conflicti345 – 3451L → F in AAH20107. (PubMed:15489334)Curated
    Sequence conflicti626 – 6261S → N in BAA91829. (PubMed:14702039)Curated
    Sequence conflicti928 – 9281F → L in BAA91885. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061T → P.
    Corresponds to variant rs428231 [ dbSNP | Ensembl ].
    VAR_030829
    Natural varianti294 – 2941I → V.
    Corresponds to variant rs11805194 [ dbSNP | Ensembl ].
    VAR_030830
    Natural varianti326 – 3261G → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035854
    Natural varianti406 – 4061Q → R.
    Corresponds to variant rs1065674 [ dbSNP | Ensembl ].
    VAR_030831
    Natural varianti448 – 4481G → R in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035855

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK001676 mRNA. Translation: BAA91829.1.
    AK001754 mRNA. Translation: BAA91885.1. Different initiation.
    AK022572 mRNA. Translation: BAB14106.1. Different initiation.
    AK314431 mRNA. Translation: BAG37045.1.
    AL121990, AL139252, AL160004 Genomic DNA. Translation: CAI22011.1.
    AL139252, AL121990, AL160004 Genomic DNA. Translation: CAI22354.1.
    AL160004, AL121990, AL139252 Genomic DNA. Translation: CAI19048.1.
    BC020107 mRNA. Translation: AAH20107.1.
    CCDSiCCDS1579.1.
    RefSeqiNP_060700.2. NM_018230.2.
    UniGeneiHs.12457.

    Genome annotation databases

    EnsembliENST00000261396; ENSP00000261396; ENSG00000069248.
    GeneIDi55746.
    KEGGihsa:55746.
    UCSCiuc001htn.3. human.

    Polymorphism databases

    DMDMi143811430.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK001676 mRNA. Translation: BAA91829.1 .
    AK001754 mRNA. Translation: BAA91885.1 . Different initiation.
    AK022572 mRNA. Translation: BAB14106.1 . Different initiation.
    AK314431 mRNA. Translation: BAG37045.1 .
    AL121990 , AL139252 , AL160004 Genomic DNA. Translation: CAI22011.1 .
    AL139252 , AL121990 , AL160004 Genomic DNA. Translation: CAI22354.1 .
    AL160004 , AL121990 , AL139252 Genomic DNA. Translation: CAI19048.1 .
    BC020107 mRNA. Translation: AAH20107.1 .
    CCDSi CCDS1579.1.
    RefSeqi NP_060700.2. NM_018230.2.
    UniGenei Hs.12457.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XKS X-ray 2.35 A 67-514 [» ]
    3CQC X-ray 2.53 B 935-1156 [» ]
    3CQG X-ray 3.00 B 934-1156 [» ]
    3I4R X-ray 3.53 B 517-1156 [» ]
    DisProti DP00318.
    ProteinModelPortali Q8WUM0.
    SMRi Q8WUM0. Positions 75-477, 518-1156.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120864. 29 interactions.
    IntActi Q8WUM0. 15 interactions.
    MINTi MINT-3046670.
    STRINGi 9606.ENSP00000261396.

    PTM databases

    PhosphoSitei Q8WUM0.

    Polymorphism databases

    DMDMi 143811430.

    Proteomic databases

    MaxQBi Q8WUM0.
    PaxDbi Q8WUM0.
    PRIDEi Q8WUM0.

    Protocols and materials databases

    DNASUi 55746.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261396 ; ENSP00000261396 ; ENSG00000069248 .
    GeneIDi 55746.
    KEGGi hsa:55746.
    UCSCi uc001htn.3. human.

    Organism-specific databases

    CTDi 55746.
    GeneCardsi GC01M229580.
    H-InvDB HIX0001680.
    HGNCi HGNC:18016. NUP133.
    HPAi HPA059767.
    MIMi 607613. gene.
    neXtProti NX_Q8WUM0.
    PharmGKBi PA31847.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG312399.
    HOGENOMi HOG000293246.
    HOVERGENi HBG052678.
    InParanoidi Q8WUM0.
    KOi K14300.
    OMAi MCRLMVP.
    OrthoDBi EOG7P8P70.
    PhylomeDBi Q8WUM0.
    TreeFami TF106141.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    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_682. Mitotic Prometaphase.
    REACT_7991. Vpr-mediated nuclear import of PICs.
    REACT_9395. Nuclear import of Rev protein.

    Miscellaneous databases

    ChiTaRSi NUP133. human.
    EvolutionaryTracei Q8WUM0.
    GeneWikii NUP133.
    GenomeRNAii 55746.
    NextBioi 60719.
    PROi Q8WUM0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WUM0.
    Bgeei Q8WUM0.
    CleanExi HS_NUP133.
    Genevestigatori Q8WUM0.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR007187. Nucleoporin_Nup133/Nup155_C.
    IPR014908. Nucleoporin_Nup133/Nup155_N.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view ]
    Pfami PF03177. Nucleoporin_C. 1 hit.
    PF08801. Nucleoporin_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Placenta.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      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: Skin.
    4. "An evolutionarily conserved NPC subcomplex, which redistributes in part to kinetochores in mammalian cells."
      Belgareh N., Rabut G., Bai S.W., van Overbeek M., Beaudouin J., Daigle N., Zatsepina O.V., Pasteau F., Labas V., Fromont-Racine M., Ellenberg J., Doye V.
      J. Cell Biol. 154:1147-1160(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, SUBUNIT, SUBCELLULAR LOCATION.
    5. "Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export."
      Vasu S., Shah S., Orjalo A., Park M., Fischer W.H., Forbes D.J.
      J. Cell Biol. 155:339-354(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    6. "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-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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-45 AND SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; THR-28; SER-41; SER-45 AND SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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].
    12. "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-45; SER-50 AND SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-27; THR-28; SER-45 AND SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex."
      Berke I.C., Boehmer T., Blobel G., Schwartz T.U.
      J. Cell Biol. 167:591-597(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 67-514.
    18. Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-326 AND ARG-448.

    Entry informationi

    Entry nameiNU133_HUMAN
    AccessioniPrimary (citable) accession number: Q8WUM0
    Secondary accession number(s): B2RAZ8
    , Q5T8N0, Q9H9W2, Q9NV71, Q9NVC4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 28, 2003
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 126 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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