Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q14978

- NOLC1_HUMAN

UniProt

Q14978 - NOLC1_HUMAN

Protein

Nucleolar and coiled-body phosphoprotein 1

Gene

NOLC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Related to nucleologenesis, may play a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus. It has intrinsic GTPase and ATPase activities. May play an important role in transcription catalyzed by RNA polymerase I.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. GTP binding Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. cell cycle Source: ProtInc
    2. mitotic nuclear division Source: ProtInc
    3. nucleolus organization Source: Ensembl
    4. rRNA processing Source: ProtInc

    Keywords - Ligandi

    ATP-binding, GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleolar and coiled-body phosphoprotein 1
    Alternative name(s):
    140 kDa nucleolar phosphoprotein
    Short name:
    Nopp140
    Hepatitis C virus NS5A-transactivated protein 13
    Short name:
    HCV NS5A-transactivated protein 13
    Nucleolar 130 kDa protein
    Nucleolar phosphoprotein p130
    Gene namesi
    Name:NOLC1
    Synonyms:KIAA0035, NS5ATP13
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:15608. NOLC1.

    Subcellular locationi

    Nucleusnucleolus. Cytoplasm
    Note: Shuttles between the nucleolus and the cytoplasm. At telophase it begins to assemble into granular-like pre-nucleolar bodies which are subsequently relocated to nucleoli at the early G1-phase.

    GO - Cellular componenti

    1. Cajal body Source: Ensembl
    2. cytoplasm Source: ProtInc
    3. nucleolus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31679.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 699699Nucleolar and coiled-body phosphoprotein 1PRO_0000096942Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei33 – 331N6-acetyllysine1 Publication
    Modified residuei87 – 871Phosphoserine1 Publication
    Modified residuei90 – 901Phosphoserine1 Publication
    Modified residuei91 – 911Phosphoserine1 Publication
    Modified residuei366 – 3661Phosphoserine1 Publication
    Modified residuei397 – 3971Phosphoserine2 Publications
    Modified residuei415 – 4151N6-acetyllysine1 Publication
    Modified residuei508 – 5081Phosphoserine3 Publications
    Modified residuei538 – 5381Phosphoserine4 Publications
    Modified residuei563 – 5631Phosphoserine3 Publications
    Modified residuei580 – 5801Phosphoserine2 Publications
    Modified residuei582 – 5821Phosphoserine2 Publications
    Modified residuei607 – 6071Phosphothreonine3 Publications
    Modified residuei610 – 6101Phosphothreonine3 Publications
    Modified residuei622 – 6221Phosphoserine1 Publication
    Modified residuei643 – 6431Phosphoserine4 Publications
    Modified residuei663 – 6631N6-acetyllysine1 Publication
    Modified residuei686 – 6861Phosphoserine1 Publication
    Modified residuei698 – 6981Phosphoserine6 Publications

    Post-translational modificationi

    Undergoes rapid and massive phosphorylation/dephosphorylation cycles on CK2 and PKC sites. There is evidence suggesting that CDK1 kinase phosphorylates p130 at the M-phase.9 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14978.
    PaxDbiQ14978.
    PRIDEiQ14978.

    PTM databases

    PhosphoSiteiQ14978.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14978.
    BgeeiQ14978.
    CleanExiHS_NOLC1.
    GenevestigatoriQ14978.

    Organism-specific databases

    HPAiHPA037366.
    HPA050388.

    Interactioni

    Subunit structurei

    Interacts with RNA polymerase I 194 kDa subunit (RPA194) and with casein kinase-II.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARRB1P494073EBI-396155,EBI-743313
    ARRB2P321213EBI-396155,EBI-714559
    gagP045912EBI-396155,EBI-6179719From a different organism.

    Protein-protein interaction databases

    BioGridi114654. 59 interactions.
    IntActiQ14978. 13 interactions.
    MINTiMINT-111465.
    STRINGi9606.ENSP00000359024.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14978.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 4233LisHPROSITE-ProRule annotationAdd
    BLAST
    Repeati84 – 9512Acidic serine cluster 1Add
    BLAST
    Repeati125 – 13612Acidic serine cluster 2Add
    BLAST
    Repeati167 – 17812Acidic serine cluster 3Add
    BLAST
    Repeati221 – 23212Acidic serine cluster 4Add
    BLAST
    Repeati264 – 27512Acidic serine cluster 5Add
    BLAST
    Repeati325 – 33612Acidic serine cluster 6Add
    BLAST
    Repeati363 – 37513Acidic serine cluster 7Add
    BLAST
    Repeati425 – 43612Acidic serine cluster 8Add
    BLAST
    Repeati470 – 48112Acidic serine cluster 9Add
    BLAST
    Repeati519 – 52911Acidic serine cluster 10Add
    BLAST
    Repeati555 – 56612Acidic serine cluster 11Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni84 – 56648311 X 12 AA approximate repeats of an acidic serine clusterAdd
    BLAST
    Regioni204 – 382179Interacts with RPA194Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi68 – 8215Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi384 – 587204Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi601 – 61717Nuclear localization signalSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 LisH domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG318801.
    HOGENOMiHOG000113823.
    HOVERGENiHBG075370.
    OMAiMSIIQDL.
    OrthoDBiEOG7GTT6H.
    PhylomeDBiQ14978.
    TreeFamiTF341730.

    Family and domain databases

    InterProiIPR006594. LisH_dimerisation.
    IPR007718. SRP40_C.
    [Graphical view]
    PfamiPF05022. SRP40_C. 1 hit.
    [Graphical view]
    SMARTiSM00667. LisH. 1 hit.
    [Graphical view]
    PROSITEiPS50896. LISH. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Alpha (identifier: Q14978-1) [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

    MADAGIRRVV PSDLYPLVLG FLRDNQLSEV ANKFAKATGA TQQDANASSL    50
    LDIYSFWLKS AKVPERKLQA NGPVAKKAKK KASSSDSEDS SEEEEEVQGP 100
    PAKKAAVPAK RVGLPPGKAA AKASESSSSE ESSDDDDEED QKKQPVQKGV 150
    KPQAKAAKAP PKKAKSSDSD SDSSSEDEPP KNQKPKITPV TVKAQTKAPP 200
    KPARAAPKIA NGKAASSSSS SSSSSSSDDS EEEKAAATPK KTVPKKQVVA 250
    KAPVKAATTP TRKSSSSEDS SSDEEEEQKK PMKNKPGPYS SVPPPSAPPP 300
    KKSLGTQPPK KAVEKQQPVE SSEDSSDESD SSSEEEKKPP TKAVVSKATT 350
    KPPPAKKAAE SSSDSSDSDS SEDDEAPSKP AGTTKNSSNK PAVTTKSPAV 400
    KPAAAPKQPV GGGQKLLTRK ADSSSSEEES SSSEEEKTKK MVATTKPKAT 450
    AKAALSLPAK QAPQGSRDSS SDSDSSSSEE EEEKTSKSAV KKKPQKVAGG 500
    AAPSKPASAK KGKAESSNSS SSDDSSEEEE EKLKGKGSPR PQAPKANGTS 550
    ALTAQNGKAA KNSEEEEEEK KKAAVVVSKS GSLKKRKQNE AAKEAETPQA 600
    KKIKLQTPNT FPKRKKGEKR ASSPFRRVRE EEIEVDSRVA DNSFDAKRGA 650
    AGDWGERANQ VLKFTKGKSF RHEKTKKKRG SYRGGSISVQ VNSIKFDSE 699
    Length:699
    Mass (Da):73,603
    Last modified:April 17, 2007 - v2
    Checksum:i7C5C4F25677E2E61
    GO
    Isoform Beta (identifier: Q14978-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         241-241: K → KVWTITSVRAE

    Show »
    Length:709
    Mass (Da):74,747
    Checksum:i5A02742A231255AB
    GO
    Isoform 3 (identifier: Q14978-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         58-59: LK → LNR

    Show »
    Length:700
    Mass (Da):73,745
    Checksum:i5F8699563FBA24A9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31D → A in BAA04803. (PubMed:7584026)Curated
    Sequence conflicti133 – 1331S → R in CAA84063. (PubMed:7657714)Curated
    Sequence conflicti291 – 2922SV → YA in CAA84063. (PubMed:7657714)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti412 – 4121G → V.
    Corresponds to variant rs11191224 [ dbSNP | Ensembl ].
    VAR_031677
    Natural varianti456 – 4561S → P.1 Publication
    Corresponds to variant rs1049455 [ dbSNP | Ensembl ].
    VAR_031678

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei58 – 592LK → LNR in isoform 3. 2 PublicationsVSP_035415
    Alternative sequencei241 – 2411K → KVWTITSVRAE in isoform Beta. 1 PublicationVSP_004338

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z34289 mRNA. Translation: CAA84063.1.
    AY820769 mRNA. Translation: AAV67777.1.
    AL500527 Genomic DNA. Translation: CAH72220.1.
    CH471066 Genomic DNA. Translation: EAW49714.1.
    CH471066 Genomic DNA. Translation: EAW49715.1.
    BC001883 mRNA. Translation: AAH01883.1.
    D21262 mRNA. Translation: BAA04803.1.
    CCDSiCCDS65925.1. [Q14978-3]
    CCDS65926.1. [Q14978-2]
    CCDS7530.1. [Q14978-1]
    PIRiI38073.
    RefSeqiNP_001271317.1. NM_001284388.1. [Q14978-2]
    NP_001271318.1. NM_001284389.1. [Q14978-3]
    NP_004732.2. NM_004741.4. [Q14978-1]
    UniGeneiHs.523238.

    Genome annotation databases

    EnsembliENST00000405356; ENSP00000385410; ENSG00000166197. [Q14978-2]
    ENST00000488254; ENSP00000475080; ENSG00000166197. [Q14978-3]
    ENST00000605788; ENSP00000474710; ENSG00000166197. [Q14978-1]
    GeneIDi9221.
    KEGGihsa:9221.
    UCSCiuc001kuo.2. human. [Q14978-1]
    uc001kup.2. human. [Q14978-2]
    uc001kuq.2. human. [Q14978-3]

    Polymorphism databases

    DMDMi145559503.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z34289 mRNA. Translation: CAA84063.1 .
    AY820769 mRNA. Translation: AAV67777.1 .
    AL500527 Genomic DNA. Translation: CAH72220.1 .
    CH471066 Genomic DNA. Translation: EAW49714.1 .
    CH471066 Genomic DNA. Translation: EAW49715.1 .
    BC001883 mRNA. Translation: AAH01883.1 .
    D21262 mRNA. Translation: BAA04803.1 .
    CCDSi CCDS65925.1. [Q14978-3 ]
    CCDS65926.1. [Q14978-2 ]
    CCDS7530.1. [Q14978-1 ]
    PIRi I38073.
    RefSeqi NP_001271317.1. NM_001284388.1. [Q14978-2 ]
    NP_001271318.1. NM_001284389.1. [Q14978-3 ]
    NP_004732.2. NM_004741.4. [Q14978-1 ]
    UniGenei Hs.523238.

    3D structure databases

    ProteinModelPortali Q14978.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114654. 59 interactions.
    IntActi Q14978. 13 interactions.
    MINTi MINT-111465.
    STRINGi 9606.ENSP00000359024.

    PTM databases

    PhosphoSitei Q14978.

    Polymorphism databases

    DMDMi 145559503.

    Proteomic databases

    MaxQBi Q14978.
    PaxDbi Q14978.
    PRIDEi Q14978.

    Protocols and materials databases

    DNASUi 9221.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000405356 ; ENSP00000385410 ; ENSG00000166197 . [Q14978-2 ]
    ENST00000488254 ; ENSP00000475080 ; ENSG00000166197 . [Q14978-3 ]
    ENST00000605788 ; ENSP00000474710 ; ENSG00000166197 . [Q14978-1 ]
    GeneIDi 9221.
    KEGGi hsa:9221.
    UCSCi uc001kuo.2. human. [Q14978-1 ]
    uc001kup.2. human. [Q14978-2 ]
    uc001kuq.2. human. [Q14978-3 ]

    Organism-specific databases

    CTDi 9221.
    GeneCardsi GC10P103902.
    H-InvDB HIX0009150.
    HGNCi HGNC:15608. NOLC1.
    HPAi HPA037366.
    HPA050388.
    MIMi 602394. gene.
    neXtProti NX_Q14978.
    PharmGKBi PA31679.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG318801.
    HOGENOMi HOG000113823.
    HOVERGENi HBG075370.
    OMAi MSIIQDL.
    OrthoDBi EOG7GTT6H.
    PhylomeDBi Q14978.
    TreeFami TF341730.

    Miscellaneous databases

    ChiTaRSi NOLC1. human.
    GeneWikii Nucleolar_phosphoprotein_p130.
    GenomeRNAii 9221.
    NextBioi 34571.
    PROi Q14978.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14978.
    Bgeei Q14978.
    CleanExi HS_NOLC1.
    Genevestigatori Q14978.

    Family and domain databases

    InterProi IPR006594. LisH_dimerisation.
    IPR007718. SRP40_C.
    [Graphical view ]
    Pfami PF05022. SRP40_C. 1 hit.
    [Graphical view ]
    SMARTi SM00667. LisH. 1 hit.
    [Graphical view ]
    PROSITEi PS50896. LISH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cell-cycle-dependent alterations of a highly phosphorylated nucleolar protein p130 are associated with nucleologenesis."
      Pai C.-Y., Chen H.-K., Sheu H.-L., Yeh N.-H.
      J. Cell Sci. 108:1911-1920(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
      Tissue: Leukemia.
    2. Ying Z.L., Hong D., Jun C.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 3).
      Tissue: Lung.
    6. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
      Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
      DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-699 (ISOFORM BETA), VARIANT PRO-456.
      Tissue: Bone marrow.
    7. "Cell proliferation-dependent expression of two isoforms of the nucleolar phosphoprotein p130."
      Pai C.-Y., Yeh N.-H.
      Biochem. Biophys. Res. Commun. 221:581-587(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
    8. "The nucleolar phosphoprotein P130 is a GTPase/ATPase with intrinsic property to form large complexes triggered by F- and Mg2+."
      Chen H.-K., Yeh N.-H.
      Biochem. Biophys. Res. Commun. 230:370-375(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "Human Nopp140, which interacts with RNA polymerase I: implications for rRNA gene transcription and nucleolar structural organization."
      Chen H.-K., Pai C.-Y., Huang J.-Y., Yeh N.-H.
      Mol. Cell. Biol. 19:8536-8546(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607 AND THR-610, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-538; SER-563 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-607; THR-610; SER-643 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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 SER-508; SER-538; THR-607; THR-610 AND SER-643, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-90; SER-91; SER-366; SER-508; SER-580; SER-582; SER-686 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    16. "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].
    17. "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-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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-33; LYS-415 AND LYS-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-397; SER-508; SER-538; SER-563; SER-580; SER-582; SER-643 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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-397; SER-538; SER-622; SER-643 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNOLC1_HUMAN
    AccessioniPrimary (citable) accession number: Q14978
    Secondary accession number(s): Q15030, Q5VV70, Q9BUV3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 141 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 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3