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Q9Y2X3

- NOP58_HUMAN

UniProt

Q9Y2X3 - NOP58_HUMAN

Protein

Nucleolar protein 58

Gene

NOP58

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Required for 60S ribosomal subunit biogenesis By similarity. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 snoRNAs.By similarity3 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell growth Source: UniProtKB
    2. rRNA processing Source: UniProtKB
    3. snRNP protein import into nucleus Source: UniProtKB

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    Ribosome biogenesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleolar protein 58
    Alternative name(s):
    Nucleolar protein 5
    Gene namesi
    Name:NOP58
    Synonyms:NOL5, NOP5
    ORF Names:HSPC120
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:29926. NOP58.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164724092.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 529529Nucleolar protein 58PRO_0000219023Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei109 – 1091Phosphoserine1 Publication
    Modified residuei351 – 3511Phosphoserine2 Publications
    Cross-linki467 – 467Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei483 – 4831Phosphoserine1 Publication
    Cross-linki497 – 497Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei502 – 5021Phosphoserine6 Publications
    Modified residuei514 – 5141Phosphoserine6 Publications

    Post-translational modificationi

    Sumoylation is essential for high-affinity binding to snoRNAs.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y2X3.
    PaxDbiQ9Y2X3.
    PeptideAtlasiQ9Y2X3.
    PRIDEiQ9Y2X3.

    2D gel databases

    SWISS-2DPAGEQ9Y2X3.

    PTM databases

    PhosphoSiteiQ9Y2X3.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ9Y2X3.
    BgeeiQ9Y2X3.
    GenevestigatoriQ9Y2X3.

    Organism-specific databases

    HPAiHPA018472.
    HPA021062.

    Interactioni

    Subunit structurei

    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 with NOLC1/Nopp140. Interacts with NUFIP1, RUVBL1 AND RUVBL2; RUVBL1:RUVBL2 seem to bridge the association of NOP58 with NUFIP1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TGS1Q96RS02EBI-395469,EBI-949244

    Protein-protein interaction databases

    BioGridi119631. 66 interactions.
    IntActiQ9Y2X3. 22 interactions.
    MINTiMINT-3085086.
    STRINGi9606.ENSP00000264279.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y2X3.
    SMRiQ9Y2X3. Positions 142-401.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini282 – 400119NopPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi441 – 52484Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1498.
    HOGENOMiHOG000196310.
    InParanoidiQ9Y2X3.
    KOiK14565.
    OMAiKNRMTAI.
    OrthoDBiEOG7T7GT0.
    PhylomeDBiQ9Y2X3.
    TreeFamiTF105688.

    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.

    Q9Y2X3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLVLFETSVG YAIFKVLNEK KLQEVDSLWK EFETPEKANK IVKLKHFEKF    50
    QDTAEALAAF TALMEGKINK QLKKVLKKIV KEAHEPLAVA DAKLGGVIKE 100
    KLNLSCIHSP VVNELMRGIR SQMDGLIPGV EPREMAAMCL GLAHSLSRYR 150
    LKFSADKVDT MIVQAISLLD DLDKELNNYI MRCREWYGWH FPELGKIISD 200
    NLTYCKCLQK VGDRKNYASA KLSELLPEEV EAEVKAAAEI SMGTEVSEED 250
    ICNILHLCTQ VIEISEYRTQ LYEYLQNRMM AIAPNVTVMV GELVGARLIA 300
    HAGSLLNLAK HAASTVQILG AEKALFRALK SRRDTPKYGL IYHASLVGQT 350
    SPKHKGKISR MLAAKTVLAI RYDAFGEDSS SAMGVENRAK LEARLRTLED 400
    RGIRKISGTG KALAKTEKYE HKSEVKTYDP SGDSTLPTCS KKRKIEQVDK 450
    EDEITEKKAK KAKIKVKVEE EEEEKVAEEE ETSVKKKKKR GKKKHIKEEP 500
    LSEEEPCTST AIASPEKKKK KKKKRENED 529
    Length:529
    Mass (Da):59,578
    Last modified:November 1, 1999 - v1
    Checksum:i27CD73CFF5B9A556
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21L → M in CAB55989. (PubMed:17974005)Curated
    Sequence conflicti129 – 1291G → V in CAB55989. (PubMed:17974005)Curated
    Sequence conflicti202 – 22120LTYCK…YASAK → YHTASVYRKLAIGRLCLCQ in AAF29084. (PubMed:11042152)CuratedAdd
    BLAST
    Sequence conflicti235 – 26026KAAAE…HLCTQ → EGSCRDIHGNRGFRRRYLQY SASLHP in AAF29084. (PubMed:11042152)CuratedAdd
    BLAST
    Sequence conflicti280 – 2801M → V in CAB55989. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti387 – 3871N → T.
    Corresponds to variant rs34748654 [ dbSNP | Ensembl ].
    VAR_059461
    Natural varianti389 – 3891A → P.
    Corresponds to variant rs34458926 [ dbSNP | Ensembl ].
    VAR_059462
    Natural varianti400 – 4001D → A.
    Corresponds to variant rs35900977 [ dbSNP | Ensembl ].
    VAR_059463
    Natural varianti508 – 5081T → P.
    Corresponds to variant rs34523815 [ dbSNP | Ensembl ].
    VAR_059464

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF123534 mRNA. Translation: AAD27610.1.
    AF263608 mRNA. Translation: AAF91394.1.
    AC064836 Genomic DNA. Translation: AAY24145.1.
    BC032592 mRNA. Translation: AAH32592.1.
    BC009306 mRNA. Translation: AAH09306.1.
    AL117554 mRNA. Translation: CAB55989.2.
    AF161469 mRNA. Translation: AAF29084.1.
    CCDSiCCDS2353.1.
    PIRiT17299.
    RefSeqiNP_057018.1. NM_015934.3.
    UniGeneiHs.471104.

    Genome annotation databases

    EnsembliENST00000264279; ENSP00000264279; ENSG00000055044.
    GeneIDi51602.
    KEGGihsa:51602.
    UCSCiuc002uzb.3. human.

    Polymorphism databases

    DMDMi17380155.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF123534 mRNA. Translation: AAD27610.1 .
    AF263608 mRNA. Translation: AAF91394.1 .
    AC064836 Genomic DNA. Translation: AAY24145.1 .
    BC032592 mRNA. Translation: AAH32592.1 .
    BC009306 mRNA. Translation: AAH09306.1 .
    AL117554 mRNA. Translation: CAB55989.2 .
    AF161469 mRNA. Translation: AAF29084.1 .
    CCDSi CCDS2353.1.
    PIRi T17299.
    RefSeqi NP_057018.1. NM_015934.3.
    UniGenei Hs.471104.

    3D structure databases

    ProteinModelPortali Q9Y2X3.
    SMRi Q9Y2X3. Positions 142-401.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119631. 66 interactions.
    IntActi Q9Y2X3. 22 interactions.
    MINTi MINT-3085086.
    STRINGi 9606.ENSP00000264279.

    PTM databases

    PhosphoSitei Q9Y2X3.

    Polymorphism databases

    DMDMi 17380155.

    2D gel databases

    SWISS-2DPAGE Q9Y2X3.

    Proteomic databases

    MaxQBi Q9Y2X3.
    PaxDbi Q9Y2X3.
    PeptideAtlasi Q9Y2X3.
    PRIDEi Q9Y2X3.

    Protocols and materials databases

    DNASUi 51602.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264279 ; ENSP00000264279 ; ENSG00000055044 .
    GeneIDi 51602.
    KEGGi hsa:51602.
    UCSCi uc002uzb.3. human.

    Organism-specific databases

    CTDi 51602.
    GeneCardsi GC02P203130.
    HGNCi HGNC:29926. NOP58.
    HPAi HPA018472.
    HPA021062.
    neXtProti NX_Q9Y2X3.
    PharmGKBi PA164724092.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1498.
    HOGENOMi HOG000196310.
    InParanoidi Q9Y2X3.
    KOi K14565.
    OMAi KNRMTAI.
    OrthoDBi EOG7T7GT0.
    PhylomeDBi Q9Y2X3.
    TreeFami TF105688.

    Miscellaneous databases

    ChiTaRSi NOP58. human.
    GeneWikii NOP5/NOP58.
    GenomeRNAii 51602.
    NextBioi 55479.
    PROi Q9Y2X3.

    Gene expression databases

    ArrayExpressi Q9Y2X3.
    Bgeei Q9Y2X3.
    Genevestigatori Q9Y2X3.

    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. "Human Nop5/Nop58 is a component common to the box C/D small nucleolar ribonucleoproteins."
      Lyman S.K., Gerace L., Baserga S.J.
      RNA 5:1597-1604(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION.
    2. "Isolation and characterization of a novel PDGF-induced human gene."
      Nelson S.A., Santora K.E., LaRochelle W.J.
      Gene 253:87-93(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skin and Uterus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-442.
      Tissue: Brain.
    6. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-529.
      Tissue: Umbilical cord blood.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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.
    9. "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.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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: FUNCTION IN U3 BOX C/D SNORNA BIOGENESIS, ASSOCIATION WITH U8 BOX C/D SNORNA, INTERACTION WITH NUFIP1.
    12. "Involvement of nuclear import and export factors in U8 box C/D snoRNP biogenesis."
      Watkins N.J., Lemm I., Luhrmann R.
      Mol. Cell. Biol. 27:7018-7027(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH U8 BOX C/D SNORNP COMPLEX.
    13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; SER-502 AND SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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. "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: FUNCTION IN U3 AND U8 BOX C/D SNORNA BIOGENESIS, INTERACTION WITH RUVBL1 AND RUVBL2.
    18. "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-502 AND SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58."
      Westman B.J., Verheggen C., Hutten S., Lam Y.W., Bertrand E., Lamond A.I.
      Mol. Cell 39:618-631(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-467 AND LYS-497.
    20. "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-351; SER-483; SER-502 AND SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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-502 AND SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNOP58_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2X3
    Secondary accession number(s): Q53SA4
    , Q6PK08, Q9P036, Q9UFN3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 134 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

    Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3