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Q9Y2X3

- NOP58_HUMAN

UniProt

Q9Y2X3 - NOP58_HUMAN

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Protein

Nucleolar protein 58

Gene

NOP58

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9Y2X3.
ExpressionAtlasiQ9Y2X3. baseline and differential.
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. 67 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.
GeneTreeiENSGT00550000074998.
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

        10         20         30         40         50
MLVLFETSVG YAIFKVLNEK KLQEVDSLWK EFETPEKANK IVKLKHFEKF
60 70 80 90 100
QDTAEALAAF TALMEGKINK QLKKVLKKIV KEAHEPLAVA DAKLGGVIKE
110 120 130 140 150
KLNLSCIHSP VVNELMRGIR SQMDGLIPGV EPREMAAMCL GLAHSLSRYR
160 170 180 190 200
LKFSADKVDT MIVQAISLLD DLDKELNNYI MRCREWYGWH FPELGKIISD
210 220 230 240 250
NLTYCKCLQK VGDRKNYASA KLSELLPEEV EAEVKAAAEI SMGTEVSEED
260 270 280 290 300
ICNILHLCTQ VIEISEYRTQ LYEYLQNRMM AIAPNVTVMV GELVGARLIA
310 320 330 340 350
HAGSLLNLAK HAASTVQILG AEKALFRALK SRRDTPKYGL IYHASLVGQT
360 370 380 390 400
SPKHKGKISR MLAAKTVLAI RYDAFGEDSS SAMGVENRAK LEARLRTLED
410 420 430 440 450
RGIRKISGTG KALAKTEKYE HKSEVKTYDP SGDSTLPTCS KKRKIEQVDK
460 470 480 490 500
EDEITEKKAK KAKIKVKVEE EEEEKVAEEE ETSVKKKKKR GKKKHIKEEP
510 520
LSEEEPCTST AIASPEKKKK KKKKRENED
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 67 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.
GeneTreei ENSGT00550000074998.
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

Bgeei Q9Y2X3.
ExpressionAtlasi Q9Y2X3. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 135 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