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P19338

- NUCL_HUMAN

UniProt

P19338 - NUCL_HUMAN

Protein

Nucleolin

Gene

NCL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats.1 Publication

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. nucleotide binding Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein C-terminus binding Source: UniProtKB
    6. RNA binding Source: UniProtKB
    7. telomeric DNA binding Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. positive regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: UniProt

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleolin
    Alternative name(s):
    Protein C23
    Gene namesi
    Name:NCL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:7667. NCL.

    Subcellular locationi

    Nucleusnucleolus. Cytoplasm
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB
    2. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB
    5. nucleolus Source: UniProtKB
    6. nucleoplasm Source: Ensembl
    7. nucleus Source: ParkinsonsUK-UCL
    8. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31469.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 710709NucleolinPRO_0000081691Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91N6-acetyllysine1 Publication
    Modified residuei15 – 151N6-acetyllysine1 Publication
    Modified residuei16 – 161N6-acetyllysineBy similarity
    Modified residuei28 – 281Phosphoserine2 Publications
    Modified residuei34 – 341Phosphoserine2 Publications
    Modified residuei41 – 411Phosphoserine1 Publication
    Modified residuei42 – 421Phosphoserine1 Publication
    Modified residuei67 – 671Phosphoserine3 Publications
    Modified residuei69 – 691Phosphothreonine3 Publications
    Modified residuei76 – 761Phosphothreonine2 Publications
    Modified residuei84 – 841Phosphothreonine1 Publication
    Modified residuei92 – 921Phosphothreonine1 Publication
    Modified residuei96 – 961N6-acetyllysineBy similarity
    Modified residuei99 – 991Phosphothreonine1 Publication
    Modified residuei102 – 1021N6-acetyllysine1 Publication
    Modified residuei106 – 1061Phosphothreonine1 Publication
    Modified residuei109 – 1091N6-acetyllysineBy similarity
    Modified residuei113 – 1131Phosphothreonine1 Publication
    Modified residuei116 – 1161N6-acetyllysine1 Publication
    Modified residuei121 – 1211Phosphothreonine2 Publications
    Modified residuei124 – 1241N6-acetyllysine1 Publication
    Modified residuei145 – 1451Phosphoserine3 Publications
    Modified residuei153 – 1531Phosphoserine2 Publications
    Modified residuei184 – 1841Phosphoserine2 Publications
    Modified residuei206 – 2061Phosphoserine2 Publications
    Modified residuei214 – 2141Phosphothreonine1 Publication
    Modified residuei301 – 3011Phosphothreonine1 Publication
    Modified residuei304 – 3041Phosphothreonine1 Publication
    Modified residuei305 – 3051Phosphothreonine1 Publication
    Modified residuei318 – 3181N6-acetyllysine1 Publication
    Modified residuei348 – 3481N6-acetyllysineBy similarity
    Modified residuei377 – 3771N6-acetyllysine1 Publication
    Modified residuei398 – 3981N6-acetyllysine1 Publication
    Modified residuei403 – 4031N6-acetyllysine1 Publication
    Modified residuei427 – 4271N6-acetyllysineBy similarity
    Modified residuei444 – 4441N6-acetyllysineBy similarity
    Modified residuei467 – 4671N6-acetyllysineBy similarity
    Modified residuei477 – 4771N6-acetyllysineBy similarity
    Modified residuei513 – 5131N6-acetyllysine1 Publication
    Modified residuei521 – 5211N6-acetyllysineBy similarity
    Modified residuei563 – 5631Phosphoserine3 Publications
    Modified residuei572 – 5721N6-acetyllysine1 Publication
    Modified residuei577 – 5771N6-acetyllysine1 Publication
    Modified residuei580 – 5801Phosphoserine2 Publications
    Modified residuei619 – 6191Phosphoserine2 Publications
    Modified residuei646 – 6461N6-acetyllysine1 Publication
    Modified residuei656 – 6561Asymmetric dimethylarginineBy similarity
    Modified residuei660 – 6601Asymmetric dimethylarginineBy similarity
    Modified residuei666 – 6661Asymmetric dimethylarginineBy similarity
    Modified residuei670 – 6701Asymmetric dimethylarginineBy similarity
    Modified residuei673 – 6731Asymmetric dimethylarginineBy similarity

    Post-translational modificationi

    Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group By similarity.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP19338.
    PaxDbiP19338.
    PRIDEiP19338.

    2D gel databases

    DOSAC-COBS-2DPAGEP19338.
    SWISS-2DPAGEP19338.

    PTM databases

    PhosphoSiteiP19338.

    Miscellaneous databases

    PMAP-CutDBP19338.

    Expressioni

    Gene expression databases

    ArrayExpressiP19338.
    BgeeiP19338.
    CleanExiHS_NCL.
    GenevestigatoriP19338.

    Organism-specific databases

    HPAiCAB004210.
    HPA023981.

    Interactioni

    Subunit structurei

    Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with APTX and NSUN2. Component of the SWAP complex that consists of NPM1, NCL/nucleolin, PARP1 and SWAP70. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. Interacts (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains) with TERT; the interaction is important for nucleolar localization of TERT. Interacts with ERBB4. Interacts with GZF1; this interaction is important for nucleolar localization of GZF1. Interacts with NVL and C1QBP. Interacts with AICDA By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-346967,EBI-346967
    P279584EBI-346967,EBI-6904388From a different organism.
    ARRB1P494073EBI-346967,EBI-743313
    ARRB2P321213EBI-346967,EBI-714559
    COL18A1P3906012EBI-346967,EBI-2566375
    EBNA-LPQ8AZK72EBI-346967,EBI-1185167From a different organism.
    MDM2Q009878EBI-346967,EBI-389668
    MYH9P355793EBI-346967,EBI-350338
    PA2G4Q9UQ802EBI-346967,EBI-924893
    PAX8Q067102EBI-346967,EBI-2683132
    RHOAP615863EBI-346967,EBI-446668
    TP53P046372EBI-346967,EBI-366083
    YWHAZP631042EBI-346967,EBI-347088

    Protein-protein interaction databases

    BioGridi110771. 182 interactions.
    DIPiDIP-89N.
    IntActiP19338. 73 interactions.
    MINTiMINT-4999081.
    STRINGi9606.ENSP00000318195.

    Structurei

    Secondary structure

    1
    710
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi304 – 3063
    Beta strandi308 – 3125
    Beta strandi316 – 3183
    Helixi321 – 33313
    Beta strandi338 – 3436
    Beta strandi345 – 35612
    Helixi357 – 3659
    Beta strandi377 – 3793
    Helixi388 – 3914
    Beta strandi394 – 3996
    Helixi406 – 4138
    Beta strandi416 – 4249
    Beta strandi427 – 4359
    Helixi439 – 4424
    Turni443 – 4453
    Helixi446 – 4494
    Beta strandi460 – 4634
    Beta strandi486 – 4927
    Helixi499 – 5057
    Beta strandi510 – 5134
    Beta strandi518 – 5203
    Beta strandi524 – 5296
    Helixi533 – 54210
    Beta strandi544 – 5485
    Beta strandi551 – 5577
    Beta strandi565 – 5684
    Beta strandi572 – 5776
    Helixi585 – 5906
    Beta strandi596 – 6027
    Beta strandi604 – 6063
    Beta strandi608 – 6169
    Helixi620 – 63011
    Beta strandi641 – 6444
    Beta strandi650 – 6523

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FC8NMR-A564-652[»]
    2FC9NMR-A478-565[»]
    2KRRNMR-A300-466[»]
    ProteinModelPortaliP19338.
    SMRiP19338. Positions 300-649.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19338.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati58 – 6581
    Repeati75 – 8282
    Repeati83 – 9083
    Repeati91 – 9884
    Repeati99 – 10465; truncated
    Repeati105 – 11286
    Repeati120 – 12787
    Repeati128 – 13588
    Domaini307 – 38377RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini393 – 46674RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini486 – 56075RRM 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini572 – 64776RRM 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 135788 X 8 AA tandem repeats of X-T-P-X-K-K-X-XAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi143 – 17129Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi185 – 20925Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi234 – 27138Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi649 – 69850Arg/Gly/Phe-richAdd
    BLAST

    Sequence similaritiesi

    Contains 4 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000113885.
    HOVERGENiHBG002295.
    InParanoidiP19338.
    KOiK11294.
    OMAiEIEPAAM.
    OrthoDBiEOG73V6KP.
    PhylomeDBiP19338.
    TreeFamiTF328499.

    Family and domain databases

    Gene3Di3.30.70.330. 4 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 4 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 4 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P19338-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKLAKAGKN QGDPKKMAPP PKEVEEDSED EEMSEDEEDD SSGEEVVIPQ    50
    KKGKKAAATS AKKVVVSPTK KVAVATPAKK AAVTPGKKAA ATPAKKTVTP 100
    AKAVTTPGKK GATPGKALVA TPGKKGAAIP AKGAKNGKNA KKEDSDEEED 150
    DDSEEDEEDD EDEDEDEDEI EPAAMKAAAA APASEDEDDE DDEDDEDDDD 200
    DEEDDSEEEA METTPAKGKK AAKVVPVKAK NVAEDEDEEE DDEDEDDDDD 250
    EDDEDDDDED DEEEEEEEEE EPVKEAPGKR KKEMAKQKAA PEAKKQKVEG 300
    TEPTTAFNLF VGNLNFNKSA PELKTGISDV FAKNDLAVVD VRIGMTRKFG 350
    YVDFESAEDL EKALELTGLK VFGNEIKLEK PKGKDSKKER DARTLLAKNL 400
    PYKVTQDELK EVFEDAAEIR LVSKDGKSKG IAYIEFKTEA DAEKTFEEKQ 450
    GTEIDGRSIS LYYTGEKGQN QDYRGGKNST WSGESKTLVL SNLSYSATEE 500
    TLQEVFEKAT FIKVPQNQNG KSKGYAFIEF ASFEDAKEAL NSCNKREIEG 550
    RAIRLELQGP RGSPNARSQP SKTLFVKGLS EDTTEETLKE SFDGSVRARI 600
    VTDRETGSSK GFGFVDFNSE EDAKAAKEAM EDGEIDGNKV TLDWAKPKGE 650
    GGFGGRGGGR GGFGGRGGGR GGRGGFGGRG RGGFGGRGGF RGGRGGGGDH 700
    KPQGKKTKFE 710
    Length:710
    Mass (Da):76,614
    Last modified:January 23, 2007 - v3
    Checksum:iC97F6E34E5CA6727
    GO

    Sequence cautioni

    The sequence BAC03738.1 differs from that shown. Reason: Unlikely isoform. Aberrant splice sites.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti549 – 5491E → G in BAC03738. (PubMed:14702039)Curated
    Sequence conflicti623 – 6264Missing in AAA59954. (PubMed:2394707)Curated
    Sequence conflicti625 – 6273Missing(PubMed:2737305)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti68 – 681P → L.
    Corresponds to variant rs11542691 [ dbSNP | Ensembl ].
    VAR_046353
    Natural varianti122 – 1221P → L.
    Corresponds to variant rs11542687 [ dbSNP | Ensembl ].
    VAR_046354
    Natural varianti174 – 1741A → V.
    Corresponds to variant rs11542689 [ dbSNP | Ensembl ].
    VAR_046355

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60858 Genomic DNA. Translation: AAA59954.1.
    AK091742 mRNA. Translation: BAC03738.1. Sequence problems.
    AC017104 Genomic DNA. Translation: AAY24247.1.
    CCDSiCCDS33397.1.
    PIRiA35804.
    S53728.
    RefSeqiNP_005372.2. NM_005381.2.
    UniGeneiHs.79110.

    Genome annotation databases

    EnsembliENST00000322723; ENSP00000318195; ENSG00000115053.
    GeneIDi4691.
    KEGGihsa:4691.
    UCSCiuc002vru.3. human.

    Polymorphism databases

    DMDMi90110781.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60858 Genomic DNA. Translation: AAA59954.1 .
    AK091742 mRNA. Translation: BAC03738.1 . Sequence problems.
    AC017104 Genomic DNA. Translation: AAY24247.1 .
    CCDSi CCDS33397.1.
    PIRi A35804.
    S53728.
    RefSeqi NP_005372.2. NM_005381.2.
    UniGenei Hs.79110.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FC8 NMR - A 564-652 [» ]
    2FC9 NMR - A 478-565 [» ]
    2KRR NMR - A 300-466 [» ]
    ProteinModelPortali P19338.
    SMRi P19338. Positions 300-649.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110771. 182 interactions.
    DIPi DIP-89N.
    IntActi P19338. 73 interactions.
    MINTi MINT-4999081.
    STRINGi 9606.ENSP00000318195.

    PTM databases

    PhosphoSitei P19338.

    Polymorphism databases

    DMDMi 90110781.

    2D gel databases

    DOSAC-COBS-2DPAGE P19338.
    SWISS-2DPAGE P19338.

    Proteomic databases

    MaxQBi P19338.
    PaxDbi P19338.
    PRIDEi P19338.

    Protocols and materials databases

    DNASUi 4691.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322723 ; ENSP00000318195 ; ENSG00000115053 .
    GeneIDi 4691.
    KEGGi hsa:4691.
    UCSCi uc002vru.3. human.

    Organism-specific databases

    CTDi 4691.
    GeneCardsi GC02M232318.
    HGNCi HGNC:7667. NCL.
    HPAi CAB004210.
    HPA023981.
    MIMi 164035. gene.
    neXtProti NX_P19338.
    PharmGKBi PA31469.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000113885.
    HOVERGENi HBG002295.
    InParanoidi P19338.
    KOi K11294.
    OMAi EIEPAAM.
    OrthoDBi EOG73V6KP.
    PhylomeDBi P19338.
    TreeFami TF328499.

    Miscellaneous databases

    ChiTaRSi NCL. human.
    EvolutionaryTracei P19338.
    GenomeRNAii 4691.
    NextBioi 18090.
    PMAP-CutDB P19338.
    PROi P19338.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19338.
    Bgeei P19338.
    CleanExi HS_NCL.
    Genevestigatori P19338.

    Family and domain databases

    Gene3Di 3.30.70.330. 4 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 4 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 4 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of the human nucleolin cDNA."
      Srivastava M., Fleming P.J., Pollard H.B., Burns A.L.
      FEBS Lett. 250:99-105(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Retina.
    2. "Genomic organization and chromosomal localization of the human nucleolin gene."
      Srivastava M., McBride O.W., Fleming P.J., Pollard H.B., Burns A.L.
      J. Biol. Chem. 265:14922-14931(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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: Hair follicle dermal papilla.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Purification and partial amino acid sequencing of a fructosyllysine-specific binding protein from cell membranes of the monocyte-like cell line U937."
      Krantz S., Salazar R., Brandt R., Kellermann J., Lottspeich F.
      Biochim. Biophys. Acta 1266:109-112(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-7; 349-362 AND 610-624.
      Tissue: Lymphoma.
    6. "Major cell surface-located protein substrates of an ecto-protein kinase are homologs of known nuclear proteins."
      Jordan P., Heid H., Kinzel V., Kubler D.
      Biochemistry 33:14696-14706(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 231-236; 349-362; 399-403; 458-461 AND 649-653.
    7. "Nuclear proteins that bind the pre-mRNA 3' splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n."
      Ishikawa F., Matunis M.J., Dreyfuss G., Cech T.R.
      Mol. Cell. Biol. 13:4301-4310(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 458-474, NUCLEOTIDE-BINDING.
      Tissue: Cervix carcinoma.
    8. "A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription."
      Parada C.A., Roeder R.G.
      EMBO J. 18:3688-3701(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH HTATSF1; CCNT1; RNA POLYMERASE II; SUPT5H AND CDK9.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: INTERACTION WITH APTX.
    11. Cited for: INTERACTION WITH TERT.
    12. "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-145; SER-153 AND SER-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
      Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
      Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-153; SER-184 AND SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    15. "Nucleolin modulates the subcellular localization of GDNF-inducible zinc finger protein 1 and its roles in transcription and cell proliferation."
      Dambara A., Morinaga T., Fukuda N., Yamakawa Y., Kato T., Enomoto A., Asai N., Murakumo Y., Matsuo S., Takahashi M.
      Exp. Cell Res. 313:3755-3766(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GZF1, SUBCELLULAR LOCATION.
    16. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-76 AND THR-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: INTERACTION WITH NSUN2.
    18. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-69; SER-184; SER-206 AND THR-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "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].
    21. "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-28; SER-34; SER-41; SER-42; THR-301; THR-304 AND THR-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-15; LYS-102; LYS-116; LYS-124; LYS-318; LYS-377; LYS-398; LYS-403; LYS-513; LYS-572; LYS-577 AND LYS-646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways."
      Gilmore-Hebert M., Ramabhadran R., Stern D.F.
      Mol. Cancer Res. 8:1388-1398(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
    24. "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-28; SER-34; SER-67; THR-69; THR-76; THR-84; THR-92; THR-99; THR-106; THR-113; THR-121; SER-145; SER-563 AND SER-619, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Structure and function of the N-terminal nucleolin binding domain of nuclear valosin-containing protein-like 2 (NVL2) harboring a nucleolar localization signal."
      Fujiwara Y., Fujiwara K., Goda N., Iwaya N., Tenno T., Shirakawa M., Hiroaki H.
      J. Biol. Chem. 286:21732-21741(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NVL.
    27. "Splicing factor 2-associated protein p32 participates in ribosome biogenesis by regulating the binding of Nop52 and fibrillarin to preribosome particles."
      Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K., Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T., Takahashi N.
      Mol. Cell. Proteomics 10:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH C1QBP.
    28. "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-67; THR-69; SER-563; SER-580 AND SER-619, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Solution structure of the RRM_1 domain of NCL protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 478-566.

    Entry informationi

    Entry nameiNUCL_HUMAN
    AccessioniPrimary (citable) accession number: P19338
    Secondary accession number(s): Q53SK1
    , Q8NB06, Q9UCF0, Q9UDG1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 168 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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