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)

O00567

- NOP56_HUMAN

UniProt

O00567 - NOP56_HUMAN

Protein

Nucleolar protein 56

Gene

NOP56

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 142 (01 Oct 2014)
      Sequence version 4 (31 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs.2 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: BHF-UCL
    3. RNA binding Source: ProtInc
    4. snoRNA binding Source: BHF-UCL

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. rRNA processing Source: ProtInc

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    Ribosome biogenesis

    Enzyme and pathway databases

    ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleolar protein 56
    Alternative name(s):
    Nucleolar protein 5A
    Gene namesi
    Name:NOP56
    Synonyms:NOL5A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15911. NOP56.

    Subcellular locationi

    Nucleusnucleolus. Cytoplasm By similarity. Nucleusnucleoplasm Curated

    GO - Cellular componenti

    1. box C/D snoRNP complex Source: BHF-UCL
    2. cytoplasm Source: UniProtKB-SubCell
    3. membrane Source: UniProtKB
    4. nucleolus Source: HPA
    5. nucleoplasm Source: UniProtKB-SubCell
    6. pre-snoRNP complex Source: BHF-UCL
    7. small nucleolar ribonucleoprotein complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Spinocerebellar ataxia 36 (SCA36) [MIM:614153]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA36 is characterized by complicated clinical features, with ataxia as the first symptom, followed by characteristic late-onset involvement of the motor neuron system. Ataxic symptoms, such as gait and truncal instability, ataxic dysarthria, and uncoordinated limbs, start in late forties to fifties. Characteristically, affected individuals exhibit tongue atrophy with fasciculation. Progression of motor neuron involvement is typically limited to the tongue and main proximal skeletal muscles in both upper and lower extremities.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry. Caused by large hexanucleotide CGCCTG repeat expansions within intron 1. These expansions induce RNA foci and sequester the RNA-binding protein SRSF2. In addition, the transcription of MIR1292, a microRNA gene located just 19 bp 3' of the GGCCTG repeat, is significantly decreased.

    Keywords - Diseasei

    Neurodegeneration, Spinocerebellar ataxia

    Organism-specific databases

    MIMi614153. phenotype.
    Orphaneti276198. Spinocerebellar ataxia type 36.
    PharmGKBiPA164724063.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 594594Nucleolar protein 56PRO_0000219025Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei314 – 3141Phosphoserine1 Publication
    Modified residuei467 – 4671PhosphoserineBy similarity
    Modified residuei468 – 4681PhosphothreonineBy similarity
    Modified residuei511 – 5111Phosphoserine1 Publication
    Modified residuei519 – 5191Phosphoserine2 Publications
    Modified residuei520 – 5201Phosphoserine3 Publications
    Modified residuei561 – 5611N6-acetyllysineBy similarity
    Modified residuei563 – 5631PhosphoserineBy similarity
    Modified residuei569 – 5691Phosphoserine1 Publication
    Modified residuei570 – 5701Phosphoserine3 Publications
    Modified residuei579 – 5791Phosphoserine1 Publication
    Modified residuei581 – 5811Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00567.
    PaxDbiO00567.
    PRIDEiO00567.

    2D gel databases

    SWISS-2DPAGEO00567.

    PTM databases

    PhosphoSiteiO00567.

    Expressioni

    Gene expression databases

    ArrayExpressiO00567.
    BgeeiO00567.
    GenevestigatoriO00567.

    Organism-specific databases

    HPAiHPA049918.

    Interactioni

    Subunit structurei

    Part of a large pre-ribosomal ribonucleoprotein (RNP) complex, that consists of at least 62 ribosomal proteins, 45 nonribosomal proteins and both pre-rRNA and mature rRNA species. Within this complex directly interacts with TCOF1 in an RNA-independent manner. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles; the core proteins NHP2L1, NOP56, NOP58 and FBL assemble stepwise onto the snoRNA. Interacts NOP1 and NOP58. Interacts with NUFIP1, RUVBL1 and RUVBL2; RUVBL1:RUVBL2 seem to bridge the association of NOP56 with NUFIP1.3 Publications

    Protein-protein interaction databases

    BioGridi115783. 122 interactions.
    IntActiO00567. 18 interactions.
    MINTiMINT-2997885.
    STRINGi9606.ENSP00000370589.

    Structurei

    3D structure databases

    ProteinModelPortaliO00567.
    SMRiO00567. Positions 148-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini292 – 410119NopPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi438 – 589152Lys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the NOP5/NOP56 family.Curated
    Contains 1 Nop domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1498.
    HOGENOMiHOG000196309.
    InParanoidiO00567.
    KOiK14564.
    OMAiRIDCFMD.
    OrthoDBiEOG7T7GT0.
    PhylomeDBiO00567.
    TreeFamiTF105713.

    Family and domain databases

    InterProiIPR012974. NOP5_N.
    IPR002687. Nop_dom.
    IPR012976. NOSIC.
    [Graphical view]
    PfamiPF01798. Nop. 1 hit.
    PF08156. NOP5NT. 1 hit.
    PF08060. NOSIC. 1 hit.
    [Graphical view]
    SMARTiSM00931. NOSIC. 1 hit.
    [Graphical view]
    PROSITEiPS51358. NOP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O00567-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLLHVLFEH AVGYALLALK EVEEISLLQP QVEESVLNLG KFHSIVRLVA    50
    FCPFASSQVA LENANAVSEG VVHEDLRLLL ETHLPSKKKK VLLGVGDPKI 100
    GAAIQEELGY NCQTGGVIAE ILRGVRLHFH NLVKGLTDLS ACKAQLGLGH 150
    SYSRAKVKFN VNRVDNMIIQ SISLLDQLDK DINTFSMRVR EWYGYHFPEL 200
    VKIINDNATY CRLAQFIGNR RELNEDKLEK LEELTMDGAK AKAILDASRS 250
    SMGMDISAID LINIESFSSR VVSLSEYRQS LHTYLRSKMS QVAPSLSALI 300
    GEAVGARLIA HAGSLTNLAK YPASTVQILG AEKALFRALK TRGNTPKYGL 350
    IFHSTFIGRA AAKNKGRISR YLANKCSIAS RIDCFSEVPT SVFGEKLREQ 400
    VEERLSFYET GEIPRKNLDV MKEAMVQAEE AAAEITRKLE KQEKKRLKKE 450
    KKRLAALALA SSENSSSTPE ECEEMSEKPK KKKKQKPQEV PQENGMEDPS 500
    ISFSKPKKKK SFSKEELMSS DLEETAGSTS IPKRKKSTPK EETVNDPEEA 550
    GHRSGSKKKR KFSKEEPVSS GPEEAVGKSS SKKKKKFHKA SQED 594
    Length:594
    Mass (Da):66,050
    Last modified:October 31, 2006 - v4
    Checksum:i17D81E25DEBD052F
    GO

    Sequence cautioni

    The sequence CAA72789.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171L → V in CAA72789. (PubMed:9372940)Curated
    Sequence conflicti427 – 4271Q → QAE in CAA72789. (PubMed:9372940)Curated
    Sequence conflicti555 – 5551G → R in CAA72789. (PubMed:9372940)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti121 – 1211I → V.
    Corresponds to variant rs2273137 [ dbSNP | Ensembl ].
    VAR_028793
    Natural varianti475 – 4751M → T.1 Publication
    Corresponds to variant rs6753 [ dbSNP | Ensembl ].
    VAR_028794
    Natural varianti576 – 5761V → A.
    Corresponds to variant rs5856 [ dbSNP | Ensembl ].
    VAR_014471

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12065 mRNA. Translation: CAA72789.1. Different initiation.
    AL049712 Genomic DNA. Translation: CAC01444.2.
    BC104791 mRNA. Translation: AAI04792.1.
    BC104793 mRNA. Translation: AAI04794.1.
    CCDSiCCDS13030.1.
    RefSeqiNP_006383.2. NM_006392.3.
    UniGeneiHs.376064.

    Genome annotation databases

    EnsembliENST00000329276; ENSP00000370589; ENSG00000101361.
    GeneIDi10528.
    KEGGihsa:10528.
    UCSCiuc002wgh.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12065 mRNA. Translation: CAA72789.1 . Different initiation.
    AL049712 Genomic DNA. Translation: CAC01444.2 .
    BC104791 mRNA. Translation: AAI04792.1 .
    BC104793 mRNA. Translation: AAI04794.1 .
    CCDSi CCDS13030.1.
    RefSeqi NP_006383.2. NM_006392.3.
    UniGenei Hs.376064.

    3D structure databases

    ProteinModelPortali O00567.
    SMRi O00567. Positions 148-405.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115783. 122 interactions.
    IntActi O00567. 18 interactions.
    MINTi MINT-2997885.
    STRINGi 9606.ENSP00000370589.

    PTM databases

    PhosphoSitei O00567.

    2D gel databases

    SWISS-2DPAGE O00567.

    Proteomic databases

    MaxQBi O00567.
    PaxDbi O00567.
    PRIDEi O00567.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000329276 ; ENSP00000370589 ; ENSG00000101361 .
    GeneIDi 10528.
    KEGGi hsa:10528.
    UCSCi uc002wgh.3. human.

    Organism-specific databases

    CTDi 10528.
    GeneCardsi GC20P002723.
    HGNCi HGNC:15911. NOP56.
    HPAi HPA049918.
    MIMi 614153. phenotype.
    614154. gene.
    neXtProti NX_O00567.
    Orphaneti 276198. Spinocerebellar ataxia type 36.
    PharmGKBi PA164724063.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1498.
    HOGENOMi HOG000196309.
    InParanoidi O00567.
    KOi K14564.
    OMAi RIDCFMD.
    OrthoDBi EOG7T7GT0.
    PhylomeDBi O00567.
    TreeFami TF105713.

    Enzyme and pathway databases

    Reactomei REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

    Miscellaneous databases

    ChiTaRSi NOP56. human.
    GeneWikii NOL5A.
    GenomeRNAii 10528.
    NextBioi 39942.
    PROi O00567.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00567.
    Bgeei O00567.
    Genevestigatori O00567.

    Family and domain databases

    InterProi IPR012974. NOP5_N.
    IPR002687. Nop_dom.
    IPR012976. NOSIC.
    [Graphical view ]
    Pfami PF01798. Nop. 1 hit.
    PF08156. NOP5NT. 1 hit.
    PF08060. NOSIC. 1 hit.
    [Graphical view ]
    SMARTi SM00931. NOSIC. 1 hit.
    [Graphical view ]
    PROSITEi PS51358. NOP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p and are required for ribosome biogenesis."
      Gautier T., Berges T., Tollervey D., Hurt E.
      Mol. Cell. Biol. 17:7088-7098(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-475.
      Tissue: Cervix carcinoma.
    2. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. Bienvenut W.V.
      Submitted (AUG-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 21-41; 78-87; 91-99; 127-134; 191-202; 213-220; 231-240; 271-278; 289-333; 348-359; 405-415; 423-437 AND 541-553, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP."
      Watkins N.J., Dickmanns A., Luhrmann R.
      Mol. Cell. Biol. 22:8342-8352(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH U14 BOX C/D SNORNA.
    7. "Proteomic analysis of human Nop56p-associated pre-ribosomal ribonucleoprotein complexes. Possible link between Nop56p and the nucleolar protein treacle responsible for Treacher Collins syndrome."
      Hayano T., Yanagida M., Yamauchi Y., Shinkawa T., Isobe T., Takahashi N.
      J. Biol. Chem. 278:34309-34319(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A PRE-RIBOSOMAL RNP COMPLEX, INTERACTION WITH TCOF1, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large dynamic multiprotein complex."
      Watkins N.J., Lemm I., Ingelfinger D., Schneider C., Hossbach M., Urlaub H., Luehrmann R.
      Mol. Cell 16:789-798(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN BOX C/D SNORNA BIOGENESIS, ASSOCIATION WITH U3 BOX C/D SNORNA.
    9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    11. "A dynamic scaffold of pre-snoRNP factors facilitates human box C/D snoRNP assembly."
      McKeegan K.S., Debieux C.M., Boulon S., Bertrand E., Watkins N.J.
      Mol. Cell. Biol. 27:6782-6793(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH U8 BOX C/D SNORNA, INTERACTION WITH NUFIP1.
    12. "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.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511; SER-519; SER-520; SER-570; SER-579 AND SER-581, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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].
    15. "Evidence that the AAA+ proteins TIP48 and TIP49 bridge interactions between 15.5K and the related NOP56 and NOP58 proteins during box C/D snoRNP biogenesis."
      McKeegan K.S., Debieux C.M., Watkins N.J.
      Mol. Cell. Biol. 29:4971-4981(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RUVBL1 AND RUVBL2.
    16. "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-519; SER-520; SER-569 AND SER-570, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "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-520, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Expansion of intronic GGCCTG hexanucleotide repeat in NOP56 causes SCA36, a type of spinocerebellar ataxia accompanied by motor neuron involvement."
      Kobayashi H., Abe K., Matsuura T., Ikeda Y., Hitomi T., Akechi Y., Habu T., Liu W., Okuda H., Koizumi A.
      Am. J. Hum. Genet. 89:121-130(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SCA36.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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-314 AND SER-570, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNOP56_HUMAN
    AccessioniPrimary (citable) accession number: O00567
    Secondary accession number(s): Q2M3T6, Q9NQ05
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 31, 2006
    Last modified: October 1, 2014
    This is version 142 of the entry and version 4 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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