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Q9Y266

- NUDC_HUMAN

UniProt

Q9Y266 - NUDC_HUMAN

Protein

Nuclear migration protein nudC

Gene

NUDC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Plays a role in neurogenesis and neuronal migration By similarity. Necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Necessary for cytokinesis and cell proliferation.By similarity2 Publications

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. mitotic cell cycle Source: Reactome
    3. mitotic nuclear division Source: UniProtKB-KW
    4. multicellular organismal development Source: ProtInc

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_1932. Mitotic Telophase/Cytokinesis.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear migration protein nudC
    Alternative name(s):
    Nuclear distribution protein C homolog
    Gene namesi
    Name:NUDC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:8045. NUDC.

    Subcellular locationi

    Cytoplasmcytoskeleton. Nucleus
    Note: In a filamentous pattern adjacent to the nucleus of migrating cerebellar granule cells. Colocalizes with tubulin and dynein and with the microtubule organizing center. Distributed throughout the cytoplasm of non-migrating cells. A small proportion is nuclear, in a punctate pattern.

    GO - Cellular componenti

    1. cytoplasm Source: LIFEdb
    2. cytosol Source: Reactome
    3. microtubule Source: UniProtKB-KW
    4. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi274 – 2741S → A: Abolishes phosphorylation by PLK1; when associated with A-326. 1 Publication
    Mutagenesisi326 – 3261S → A: Abolishes phosphorylation by PLK1; when associated with A-274. 1 Publication

    Organism-specific databases

    PharmGKBiPA31827.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 331331Nuclear migration protein nudCPRO_0000057990Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei108 – 1081Phosphothreonine1 Publication
    Modified residuei139 – 1391Phosphoserine4 Publications
    Modified residuei145 – 1451Phosphothreonine4 Publications
    Modified residuei239 – 2391N6-acetyllysine1 Publication
    Modified residuei274 – 2741Phosphoserine; by PLK11 Publication
    Modified residuei326 – 3261Phosphoserine; by PLK11 Publication

    Post-translational modificationi

    Reversibly phosphorylated on serine residues during the M phase of the cell cycle. Phosphorylation on Ser-274 and Ser-326 is necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Phosphorylated by PLK and other kinases.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y266.
    PaxDbiQ9Y266.
    PeptideAtlasiQ9Y266.
    PRIDEiQ9Y266.

    PTM databases

    PhosphoSiteiQ9Y266.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed in fetal liver, kidney, lung and brain. Highly expressed in adult pancreas, kidney, skeletal muscle, liver, lung, placenta, prostate, brain and heart.2 Publications

    Inductioni

    Up-regulated in actively dividing hematopoietic precursor cells. Up-regulated in cultured erythroleukemia TF-1 cells by granulocyte-macrophage colony-stimulating factor. Strongly down-regulated during maturation of erythroid precursor cells.1 Publication

    Gene expression databases

    BgeeiQ9Y266.
    CleanExiHS_NUDC.
    GenevestigatoriQ9Y266.

    Organism-specific databases

    HPAiHPA027183.
    HPA028105.

    Interactioni

    Subunit structurei

    Binds PLK1. Binds PAFAH1B1 By similarity. Part of a complex containing PLK1, NUDC, dynein and dynactin.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DNAJA2O608842EBI-357298,EBI-352957
    FBXW2Q9UKT82EBI-357298,EBI-914727

    Protein-protein interaction databases

    BioGridi115950. 40 interactions.
    IntActiQ9Y266. 90 interactions.
    MINTiMINT-1132616.
    STRINGi9606.ENSP00000319664.

    Structurei

    Secondary structure

    1
    331
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi173 – 1764
    Beta strandi178 – 1869
    Helixi195 – 1973
    Beta strandi198 – 2036
    Beta strandi206 – 2116
    Beta strandi217 – 2248
    Helixi228 – 2303
    Beta strandi232 – 2365
    Turni237 – 2393
    Beta strandi240 – 25112
    Helixi266 – 2683

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3QORX-ray1.75A/B/C/D/E158-274[»]
    ProteinModelPortaliQ9Y266.
    SMRiQ9Y266. Positions 158-273.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini167 – 25892CSPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili60 – 13475Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi68 – 747Nuclear localization signalSequence Analysis

    Sequence similaritiesi

    Belongs to the nudC family.Curated
    Contains 1 CS domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG292552.
    HOGENOMiHOG000182245.
    HOVERGENiHBG052690.
    InParanoidiQ9Y266.
    OMAiLKGHPPV.
    OrthoDBiEOG7HQN8G.
    PhylomeDBiQ9Y266.
    TreeFamiTF300147.

    Family and domain databases

    Gene3Di2.60.40.790. 1 hit.
    InterProiIPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    IPR025934. NudC_N_dom.
    [Graphical view]
    PfamiPF04969. CS. 1 hit.
    PF14050. Nudc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF49764. SSF49764. 1 hit.
    PROSITEiPS51203. CS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y266-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGGEQEEERF DGMLLAMAQQ HEGGVQELVN TFFSFLRRKT DFFIGGEEGM    50
    AEKLITQTFS HHNQLAQKTR REKRARQEAE RREKAERAAR LAKEAKSETS 100
    GPQIKELTDE EAERLQLEID QKKDAENHEA QLKNGSLDSP GKQDTEEDEE 150
    EDEKDKGKLK PNLGNGADLP NYRWTQTLSE LDLAVPFCVN FRLKGKDMVV 200
    DIQRRHLRVG LKGQPAIIDG ELYNEVKVEE SSWLIEDGKV VTVHLEKINK 250
    MEWWSRLVSS DPEINTKKIN PENSKLSDLD SETRSMVEKM MYDQRQKSMG 300
    LPTSDEQKKQ EILKKFMDQH PEMDFSKAKF N 331
    Length:331
    Mass (Da):38,243
    Last modified:November 1, 1999 - v1
    Checksum:i34F591170F7594AF
    GO

    Sequence cautioni

    The sequence BAA76628.1 differs from that shown. Reason: Frameshift at positions 140, 231 and 273.
    The sequence CAI13560.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI13563.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191Q → H in BAA76628. 1 PublicationCurated
    Sequence conflicti69 – 691T → N in CAB66659. (PubMed:11230166)Curated
    Sequence conflicti74 – 741R → I in BAA76628. 1 PublicationCurated
    Sequence conflicti111 – 1111E → K in BAA76628. 1 PublicationCurated
    Sequence conflicti114 – 1141R → K in BAA76628. 1 PublicationCurated
    Sequence conflicti128 – 1281H → P in BAA76628. 1 PublicationCurated
    Sequence conflicti149 – 1491E → V in CAB66659. (PubMed:11230166)Curated
    Sequence conflicti169 – 1691L → P in CAB66659. (PubMed:11230166)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF130736 mRNA. Translation: AAD30517.1.
    AF125465 mRNA. Translation: AAD39921.1.
    AF100760 mRNA. Translation: AAD43024.1.
    AB019408 mRNA. Translation: BAA76628.1. Frameshift.
    AF086922 mRNA. Translation: AAP97152.1.
    AL136725 mRNA. Translation: CAB66659.1.
    AL356390 Genomic DNA. Translation: CAI13560.1. Sequence problems.
    AL356390 Genomic DNA. Translation: CAI13561.1.
    AL356390 Genomic DNA. Translation: CAI13563.1. Sequence problems.
    BC002399 mRNA. Translation: AAH02399.1.
    BC003132 mRNA. Translation: AAH03132.1.
    BC006147 mRNA. Translation: AAH06147.1.
    BC007280 mRNA. Translation: AAH07280.1.
    BC015153 mRNA. Translation: AAH15153.1.
    BC021139 mRNA. Translation: AAH21139.1.
    CCDSiCCDS292.1.
    RefSeqiNP_006591.1. NM_006600.3.
    UniGeneiHs.263812.

    Genome annotation databases

    EnsembliENST00000321265; ENSP00000319664; ENSG00000090273.
    GeneIDi10726.
    KEGGihsa:10726.
    UCSCiuc001bng.2. human.

    Polymorphism databases

    DMDMi62287138.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF130736 mRNA. Translation: AAD30517.1 .
    AF125465 mRNA. Translation: AAD39921.1 .
    AF100760 mRNA. Translation: AAD43024.1 .
    AB019408 mRNA. Translation: BAA76628.1 . Frameshift.
    AF086922 mRNA. Translation: AAP97152.1 .
    AL136725 mRNA. Translation: CAB66659.1 .
    AL356390 Genomic DNA. Translation: CAI13560.1 . Sequence problems.
    AL356390 Genomic DNA. Translation: CAI13561.1 .
    AL356390 Genomic DNA. Translation: CAI13563.1 . Sequence problems.
    BC002399 mRNA. Translation: AAH02399.1 .
    BC003132 mRNA. Translation: AAH03132.1 .
    BC006147 mRNA. Translation: AAH06147.1 .
    BC007280 mRNA. Translation: AAH07280.1 .
    BC015153 mRNA. Translation: AAH15153.1 .
    BC021139 mRNA. Translation: AAH21139.1 .
    CCDSi CCDS292.1.
    RefSeqi NP_006591.1. NM_006600.3.
    UniGenei Hs.263812.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QOR X-ray 1.75 A/B/C/D/E 158-274 [» ]
    ProteinModelPortali Q9Y266.
    SMRi Q9Y266. Positions 158-273.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115950. 40 interactions.
    IntActi Q9Y266. 90 interactions.
    MINTi MINT-1132616.
    STRINGi 9606.ENSP00000319664.

    PTM databases

    PhosphoSitei Q9Y266.

    Polymorphism databases

    DMDMi 62287138.

    Proteomic databases

    MaxQBi Q9Y266.
    PaxDbi Q9Y266.
    PeptideAtlasi Q9Y266.
    PRIDEi Q9Y266.

    Protocols and materials databases

    DNASUi 10726.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321265 ; ENSP00000319664 ; ENSG00000090273 .
    GeneIDi 10726.
    KEGGi hsa:10726.
    UCSCi uc001bng.2. human.

    Organism-specific databases

    CTDi 10726.
    GeneCardsi GC01P027226.
    HGNCi HGNC:8045. NUDC.
    HPAi HPA027183.
    HPA028105.
    MIMi 610325. gene.
    neXtProti NX_Q9Y266.
    PharmGKBi PA31827.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292552.
    HOGENOMi HOG000182245.
    HOVERGENi HBG052690.
    InParanoidi Q9Y266.
    OMAi LKGHPPV.
    OrthoDBi EOG7HQN8G.
    PhylomeDBi Q9Y266.
    TreeFami TF300147.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_1932. Mitotic Telophase/Cytokinesis.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    GeneWikii NUDC.
    GenomeRNAii 10726.
    NextBioi 40723.
    PROi Q9Y266.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y266.
    CleanExi HS_NUDC.
    Genevestigatori Q9Y266.

    Family and domain databases

    Gene3Di 2.60.40.790. 1 hit.
    InterProi IPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    IPR025934. NudC_N_dom.
    [Graphical view ]
    Pfami PF04969. CS. 1 hit.
    PF14050. Nudc_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49764. SSF49764. 1 hit.
    PROSITEi PS51203. CS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A homolog of the fungal nuclear migration gene nudC is involved in normal and malignant human hematopoiesis."
      Miller B.A., Zhang M.-Y., Gocke C.D., De Souza C., Osmani A.H., Lynch C., Davies J., Bell L., Osmani S.A.
      Exp. Hematol. 27:742-750(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Heart.
    2. "Molecular cloning and characterization of the human NUDC gene."
      Matsumoto N., Ledbetter D.H.
      Hum. Genet. 104:498-504(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    3. "Human MNUDC protein gene."
      Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pituitary.
    4. "Unique genes expressed in fibroblasts of periodontal ligament."
      Yamamoto T., Takashiba S., Myokai F., Washio N., Nishimura F., Arai H., Murayama Y.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Periodontal ligament.
    5. "Cloning and characterization of a novel human cDNA homology to murine SIG-92 mRNA."
      Li N.G., Yu L., Tu Q., Fu Q., Wang X.K., Zhao S.Y.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.
    7. "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].
    8. "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: Eye, Kidney, Lung and Skin.
    9. "A role for Plk1 phosphorylation of NudC in cytokinesis."
      Zhou T., Aumais J.P., Liu X., Yu-Lee L.-Y., Erikson R.L.
      Dev. Cell 5:127-138(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PLK1, IDENTIFICATION IN A COMPLEX WITH DYNACTIN AND DYNEIN, MUTAGENESIS OF SER-274 AND SER-326, PHOSPHORYLATION AT SER-274 AND SER-326.
    10. "Role for NudC, a dynein-associated nuclear movement protein, in mitosis and cytokinesis."
      Aumais J.P., Williams S.N., Luo W., Nishino M., Caldwell K.A., Caldwell G.A., Lin S.-H., Yu-Lee L.-Y.
      J. Cell Sci. 116:1991-2003(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    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-139 AND THR-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND THR-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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].
    14. "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-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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 THR-108; SER-139 AND THR-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-139 AND THR-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNUDC_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y266
    Secondary accession number(s): Q5QP31
    , Q5QP35, Q9H0N2, Q9Y2B6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 127 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 1
      Human chromosome 1: 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