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Q9Y2X3 (NOP58_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleolar protein 58
Alternative name(s):
Nucleolar protein 5
Gene names
Name:NOP58
Synonyms:NOL5, NOP5
ORF Names:HSPC120
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.11 Ref.17

Subunit structure

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. Ref.1 Ref.11 Ref.17

Subcellular location

Nucleusnucleolus. Nucleusnucleoplasm Probable Ref.1 Ref.7.

Tissue specificity

Ubiquitous.

Post-translational modification

Sumoylation is essential for high-affinity binding to snoRNAs. Ref.19

Sequence similarities

Belongs to the NOP5/NOP56 family.

Contains 1 Nop domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TGS1Q96RS02EBI-395469,EBI-949244

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 529529Nucleolar protein 58
PRO_0000219023

Regions

Domain282 – 400119Nop
Compositional bias441 – 52484Lys-rich

Amino acid modifications

Modified residue1091Phosphoserine Ref.13
Modified residue3511Phosphoserine Ref.15 Ref.20
Modified residue4831Phosphoserine Ref.20
Modified residue5021Phosphoserine Ref.10 Ref.14 Ref.15 Ref.18 Ref.20 Ref.22
Modified residue5141Phosphoserine Ref.10 Ref.14 Ref.15 Ref.18 Ref.20 Ref.22
Cross-link467Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.19
Cross-link497Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.19

Natural variations

Natural variant3871N → T.
Corresponds to variant rs34748654 [ dbSNP | Ensembl ].
VAR_059461
Natural variant3891A → P.
Corresponds to variant rs34458926 [ dbSNP | Ensembl ].
VAR_059462
Natural variant4001D → A.
Corresponds to variant rs35900977 [ dbSNP | Ensembl ].
VAR_059463
Natural variant5081T → P.
Corresponds to variant rs34523815 [ dbSNP | Ensembl ].
VAR_059464

Experimental info

Sequence conflict21L → M in CAB55989. Ref.5
Sequence conflict1291G → V in CAB55989. Ref.5
Sequence conflict202 – 22120LTYCK…YASAK → YHTASVYRKLAIGRLCLCQ in AAF29084. Ref.6
Sequence conflict235 – 26026KAAAE…HLCTQ → EGSCRDIHGNRGFRRRYLQY SASLHP in AAF29084. Ref.6
Sequence conflict2801M → V in CAB55989. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9Y2X3 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 27CD73CFF5B9A556

FASTA52959,578
        10         20         30         40         50         60 
MLVLFETSVG YAIFKVLNEK KLQEVDSLWK EFETPEKANK IVKLKHFEKF QDTAEALAAF 

        70         80         90        100        110        120 
TALMEGKINK QLKKVLKKIV KEAHEPLAVA DAKLGGVIKE KLNLSCIHSP VVNELMRGIR 

       130        140        150        160        170        180 
SQMDGLIPGV EPREMAAMCL GLAHSLSRYR LKFSADKVDT MIVQAISLLD DLDKELNNYI 

       190        200        210        220        230        240 
MRCREWYGWH FPELGKIISD NLTYCKCLQK VGDRKNYASA KLSELLPEEV EAEVKAAAEI 

       250        260        270        280        290        300 
SMGTEVSEED ICNILHLCTQ VIEISEYRTQ LYEYLQNRMM AIAPNVTVMV GELVGARLIA 

       310        320        330        340        350        360 
HAGSLLNLAK HAASTVQILG AEKALFRALK SRRDTPKYGL IYHASLVGQT SPKHKGKISR 

       370        380        390        400        410        420 
MLAAKTVLAI RYDAFGEDSS SAMGVENRAK LEARLRTLED RGIRKISGTG KALAKTEKYE 

       430        440        450        460        470        480 
HKSEVKTYDP SGDSTLPTCS KKRKIEQVDK EDEITEKKAK KAKIKVKVEE EEEEKVAEEE 

       490        500        510        520 
ETSVKKKKKR GKKKHIKEEP LSEEEPCTST AIASPEKKKK KKKKRENED 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2353.1.
PIRT17299.
RefSeqNP_057018.1. NM_015934.3.
UniGeneHs.471104.

3D structure databases

ProteinModelPortalQ9Y2X3.
SMRQ9Y2X3. Positions 142-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119631. 71 interactions.
IntActQ9Y2X3. 22 interactions.
MINTMINT-3085086.
STRING9606.ENSP00000264279.

PTM databases

PhosphoSiteQ9Y2X3.

Polymorphism databases

DMDM17380155.

2D gel databases

SWISS-2DPAGEQ9Y2X3.

Proteomic databases

MaxQBQ9Y2X3.
PaxDbQ9Y2X3.
PeptideAtlasQ9Y2X3.
PRIDEQ9Y2X3.

Protocols and materials databases

DNASU51602.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264279; ENSP00000264279; ENSG00000055044.
GeneID51602.
KEGGhsa:51602.
UCSCuc002uzb.3. human.

Organism-specific databases

CTD51602.
GeneCardsGC02P203130.
HGNCHGNC:29926. NOP58.
HPAHPA018472.
HPA021062.
neXtProtNX_Q9Y2X3.
PharmGKBPA164724092.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1498.
HOGENOMHOG000196310.
InParanoidQ9Y2X3.
KOK14565.
OMAKNRMTAI.
OrthoDBEOG7T7GT0.
PhylomeDBQ9Y2X3.
TreeFamTF105688.

Gene expression databases

ArrayExpressQ9Y2X3.
BgeeQ9Y2X3.
GenevestigatorQ9Y2X3.

Family and domain databases

InterProIPR012974. NOP5_N.
IPR002687. Nop_dom.
IPR012976. NOSIC.
[Graphical view]
PfamPF01798. Nop. 1 hit.
PF08156. NOP5NT. 1 hit.
PF08060. NOSIC. 1 hit.
[Graphical view]
SMARTSM00931. NOSIC. 1 hit.
[Graphical view]
PROSITEPS51358. NOP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNOP58. human.
GeneWikiNOP5/NOP58.
GenomeRNAi51602.
NextBio55479.
PROQ9Y2X3.

Entry information

Entry nameNOP58_HUMAN
AccessionPrimary (citable) accession number: Q9Y2X3
Secondary accession number(s): Q53SA4 expand/collapse secondary AC list , Q6PK08, Q9P036, Q9UFN3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM