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P57740

- NU107_HUMAN

UniProt

P57740 - NU107_HUMAN

Protein

Nuclear pore complex protein Nup107

Gene

NUP107

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (11 Jan 2001)
      Previous versions | rss
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    Functioni

    Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC.2 Publications

    GO - Molecular functioni

    1. nucleocytoplasmic transporter activity Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. structural constituent of nuclear pore 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 complex assembly Source: UniProtKB
    9. protein transport Source: UniProtKB-KW
    10. regulation of glucose transport Source: Reactome
    11. small molecule metabolic process Source: Reactome
    12. transmembrane transport Source: Reactome
    13. 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 Nup107
    Alternative name(s):
    107 kDa nucleoporin
    Nucleoporin Nup107
    Gene namesi
    Name:NUP107
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:29914. NUP107.

    Subcellular locationi

    Nucleus membrane. Nucleusnuclear pore complex. Chromosomecentromerekinetochore
    Note: Located on both the cytoplasmic and nuclear sides of the NPC core structure. During mitosis, localizes to the kinetochores. Dissociates from the dissasembled NPC structure late during prophase of mitosis.

    GO - Cellular componenti

    1. centrosome Source: HPA
    2. condensed chromosome kinetochore Source: UniProtKB-SubCell
    3. cytosol Source: Reactome
    4. membrane Source: UniProtKB
    5. nuclear envelope Source: Reactome
    6. nuclear membrane Source: UniProtKB
    7. nuclear periphery Source: UniProtKB
    8. nuclear pore Source: UniProtKB
    9. nuclear pore outer ring Source: UniProtKB
    10. nucleus Source: HPA

    Keywords - Cellular componenti

    Centromere, Chromosome, Kinetochore, Membrane, Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134890486.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 925925Nuclear pore complex protein Nup107PRO_0000204831Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei4 – 41Phosphoserine2 Publications
    Modified residuei11 – 111Phosphoserine2 Publications
    Modified residuei37 – 371Phosphoserine3 Publications
    Modified residuei46 – 461Phosphothreonine4 Publications
    Modified residuei55 – 551Phosphothreonine1 Publication
    Modified residuei58 – 581Phosphoserine1 Publication
    Modified residuei64 – 641Phosphothreonine1 Publication
    Modified residuei69 – 691Phosphoserine1 Publication
    Modified residuei86 – 861Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP57740.
    PaxDbiP57740.
    PeptideAtlasiP57740.
    PRIDEiP57740.

    PTM databases

    PhosphoSiteiP57740.

    Expressioni

    Gene expression databases

    ArrayExpressiP57740.
    BgeeiP57740.
    CleanExiHS_NUP107.
    GenevestigatoriP57740.

    Organism-specific databases

    HPAiHPA024141.
    HPA031679.

    Interactioni

    Subunit structurei

    Part of the nuclear pore complex (NPC). 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. Does not interact with TPR.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NUP133Q8WUM06EBI-295687,EBI-295695

    Protein-protein interaction databases

    BioGridi121386. 34 interactions.
    IntActiP57740. 10 interactions.
    MINTiMINT-3021765.
    STRINGi9606.ENSP00000229179.

    Structurei

    Secondary structure

    1
    925
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi668 – 68013
    Helixi682 – 6843
    Helixi685 – 70117
    Helixi705 – 71410
    Helixi719 – 7235
    Helixi738 – 76730
    Helixi782 – 82140
    Turni824 – 8263
    Helixi840 – 86728
    Helixi871 – 8755
    Helixi877 – 8826
    Turni884 – 8863
    Helixi888 – 8914
    Helixi894 – 91219
    Turni913 – 9153

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CQCX-ray2.53A658-925[»]
    3CQGX-ray3.00A658-771[»]
    A802-925[»]
    3I4RX-ray3.53A658-925[»]
    ProteinModelPortaliP57740.
    SMRiP57740. Positions 324-580, 667-924.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP57740.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the nucleoporin Nup84/Nup107 family.Curated

    Phylogenomic databases

    eggNOGiNOG258212.
    HOGENOMiHOG000006750.
    HOVERGENiHBG052677.
    InParanoidiP57740.
    KOiK14301.
    OMAiYLETNWT.
    OrthoDBiEOG773XFG.
    PhylomeDBiP57740.
    TreeFamiTF324259.

    Family and domain databases

    InterProiIPR007252. Nup84_Nup100.
    [Graphical view]
    PANTHERiPTHR13003. PTHR13003. 1 hit.
    PfamiPF04121. Nup84_Nup100. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P57740-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDRSGFGEIS SPVIREAEVT RTARKQSAQK RVLLQASQDE NFGNTTPRNQ    50
    VIPRTPSSFR QPFTPTSRSL LRQPDISCIL GTGGKSPRLT QSSGFFGNLS 100
    MVTNLDDSNW AAAFSSQRSG LFTNTEPHSI TEDVTISAVM LREDDPGEAA 150
    SMSMFSDFLQ SFLKHSSSTV FDLVEEYENI CGSQVNILSK IVSRATPGLQ 200
    KFSKTASMLW LLQQEMVTWR LLASLYRDRI QSALEEESVF AVTAVNASEK 250
    TVVEALFQRD SLVRQSQLVV DWLESIAKDE IGEFSDNIEF YAKSVYWENT 300
    LHTLKQRQLT SYVGSVRPLV TELDPDAPIR QKMPLDDLDR EDEVRLLKYL 350
    FTLIRAGMTE EAQRLCKRCG QAWRAATLEG WKLYHDPNVN GGTELEPVEG 400
    NPYRRIWKIS CWRMAEDELF NRYERAIYAA LSGNLKQLLP VCDTWEDTVW 450
    AYFRVMVDSL VEQEIQTSVA TLDETEELPR EYLGANWTLE KVFEELQATD 500
    KKRVLEENQE HYHIVQKFLI LGDIDGLMDE FSKWLSKSRN NLPGHLLRFM 550
    THLILFFRTL GLQTKEEVSI EVLKTYIQLL IREKHTNLIA FYTCHLPQDL 600
    AVAQYALFLE SVTEFEQRHH CLELAKEADL DVATITKTVV ENIRKKDNGE 650
    FSHHDLAPAL DTGTTEEDRL KIDVIDWLVF DPAQRAEALK QGNAIMRKFL 700
    ASKKHEAAKE VFVKIPQDSI AEIYNQCEEQ GMESPLPAED DNAIREHLCI 750
    RAYLEAHETF NEWFKHMNSV PQKPALIPQP TFTEKVAHEH KEKKYEMDFG 800
    IWKGHLDALT ADVKEKMYNV LLFVDGGWMV DVREDAKEDH ERTHQMVLLR 850
    KLCLPMLCFL LHTILHSTGQ YQECLQLADM VSSERHKLYL VFSKEELRKL 900
    LQKLRESSLM LLDQGLDPLG YEIQL 925
    Length:925
    Mass (Da):106,374
    Last modified:January 11, 2001 - v1
    Checksum:iCE1E4DA6C832A5A5
    GO
    Isoform 2 (identifier: P57740-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-63: MDRSGFGEIS...RTPSSFRQPF → MKILVILHQETRLSLELLAHFDSLVLSTNLLFIV

    Note: No experimental confirmation available.

    Show »
    Length:896
    Mass (Da):103,175
    Checksum:i5F39C26B982CE197
    GO
    Isoform 3 (identifier: P57740-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-151: Missing.
         579-666: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:686
    Mass (Da):79,971
    Checksum:iBC61E0588F57AA4B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti845 – 8451Q → R in AAH43343. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 151151Missing in isoform 3. 1 PublicationVSP_054262Add
    BLAST
    Alternative sequencei1 – 6363MDRSG…FRQPF → MKILVILHQETRLSLELLAH FDSLVLSTNLLFIV in isoform 2. 1 PublicationVSP_054263Add
    BLAST
    Alternative sequencei579 – 66688Missing in isoform 3. 1 PublicationVSP_054264Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ295745 mRNA. Translation: CAC03716.1.
    AK302773 mRNA. Translation: BAG63979.1.
    AC090061 Genomic DNA. No translation available.
    AC124890 Genomic DNA. No translation available.
    BC017167 mRNA. Translation: AAH17167.1.
    BC043343 mRNA. Translation: AAH43343.1.
    CCDSiCCDS8985.1. [P57740-1]
    RefSeqiNP_065134.1. NM_020401.2. [P57740-1]
    UniGeneiHs.524574.

    Genome annotation databases

    EnsembliENST00000229179; ENSP00000229179; ENSG00000111581. [P57740-1]
    ENST00000378905; ENSP00000368185; ENSG00000111581. [P57740-3]
    ENST00000539906; ENSP00000441448; ENSG00000111581. [P57740-2]
    GeneIDi57122.
    KEGGihsa:57122.
    UCSCiuc001suf.3. human. [P57740-1]

    Polymorphism databases

    DMDMi12230339.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ295745 mRNA. Translation: CAC03716.1 .
    AK302773 mRNA. Translation: BAG63979.1 .
    AC090061 Genomic DNA. No translation available.
    AC124890 Genomic DNA. No translation available.
    BC017167 mRNA. Translation: AAH17167.1 .
    BC043343 mRNA. Translation: AAH43343.1 .
    CCDSi CCDS8985.1. [P57740-1 ]
    RefSeqi NP_065134.1. NM_020401.2. [P57740-1 ]
    UniGenei Hs.524574.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CQC X-ray 2.53 A 658-925 [» ]
    3CQG X-ray 3.00 A 658-771 [» ]
    A 802-925 [» ]
    3I4R X-ray 3.53 A 658-925 [» ]
    ProteinModelPortali P57740.
    SMRi P57740. Positions 324-580, 667-924.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121386. 34 interactions.
    IntActi P57740. 10 interactions.
    MINTi MINT-3021765.
    STRINGi 9606.ENSP00000229179.

    PTM databases

    PhosphoSitei P57740.

    Polymorphism databases

    DMDMi 12230339.

    Proteomic databases

    MaxQBi P57740.
    PaxDbi P57740.
    PeptideAtlasi P57740.
    PRIDEi P57740.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229179 ; ENSP00000229179 ; ENSG00000111581 . [P57740-1 ]
    ENST00000378905 ; ENSP00000368185 ; ENSG00000111581 . [P57740-3 ]
    ENST00000539906 ; ENSP00000441448 ; ENSG00000111581 . [P57740-2 ]
    GeneIDi 57122.
    KEGGi hsa:57122.
    UCSCi uc001suf.3. human. [P57740-1 ]

    Organism-specific databases

    CTDi 57122.
    GeneCardsi GC12P069080.
    HGNCi HGNC:29914. NUP107.
    HPAi HPA024141.
    HPA031679.
    MIMi 607617. gene.
    neXtProti NX_P57740.
    PharmGKBi PA134890486.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258212.
    HOGENOMi HOG000006750.
    HOVERGENi HBG052677.
    InParanoidi P57740.
    KOi K14301.
    OMAi YLETNWT.
    OrthoDBi EOG773XFG.
    PhylomeDBi P57740.
    TreeFami TF324259.

    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

    EvolutionaryTracei P57740.
    GeneWikii NUP107.
    GenomeRNAii 57122.
    NextBioi 35476405.
    PROi P57740.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P57740.
    Bgeei P57740.
    CleanExi HS_NUP107.
    Genevestigatori P57740.

    Family and domain databases

    InterProi IPR007252. Nup84_Nup100.
    [Graphical view ]
    PANTHERi PTHR13003. PTHR13003. 1 hit.
    Pfami PF04121. Nup84_Nup100. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequential assembly of structural modules forming the vertebrate nuclear pore complex."
      Cordes V.C., Hunziker A., Mueller-Pillasch F.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Pancreatic cancer.
    2. "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] (ISOFORM 2).
      Tissue: Testis.
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 3).
      Tissue: Uterus.
    5. "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: SUBUNIT, SUBCELLULAR LOCATION.
    6. "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: SUBUNIT, SUBCELLULAR LOCATION.
    7. "Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex."
      Hase M.E., Cordes V.C.
      Mol. Biol. Cell 14:1923-1940(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABSENCE OF INTERACTION WITH TPR, SUBCELLULAR LOCATION.
    8. "Depletion of a single nucleoporin, Nup107, prevents the assembly of a subset of nucleoporins into the nuclear pore complex."
      Boehmer T., Enninga J., Dales S., Blobel G., Zhong H.
      Proc. Natl. Acad. Sci. U.S.A. 100:981-985(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket."
      Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.
      Mol. Biol. Cell 15:4261-4277(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION.
    10. "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-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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 THR-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-11; SER-37; THR-46; THR-55; SER-58; THR-64; SER-69 AND SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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-37 AND THR-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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-4; SER-11 AND THR-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNU107_HUMAN
    AccessioniPrimary (citable) accession number: P57740
    Secondary accession number(s): B4DZ67, Q6PJE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 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 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3