Q9Y2X3 (NOP58_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleolar protein 58

Alternative name(s):
Nucleolar protein 5

Gene names

Name:	NOP58
Synonyms:	NOL5, NOP5
ORF Names:	HSPC120

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for 60S ribosomal subunit biogenesis By similarity.
Subunit structure	Interacts with NOLC1/Nopp140 By similarity. Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Ref.1
Subcellular location	Nucleus › nucleolus Ref.1 Ref.7.
Tissue specificity	Ubiquitous.
Post-translational modification	Sumoylation is essential for high-affinity binding to snoRNAs. Ref.13
Sequence similarities	Belongs to the NOP5/NOP56 family. Contains 1 Nop domain.

Ontologies

Keywords
Biological process	Ribosome biogenesis
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell growth Traceable author statement Ref.2. Source: UniProtKB rRNA processing Traceable author statement Ref.2. Source: UniProtKB snRNP protein import into nucleus Inferred from sequence or structural similarity PubMed 10679015. Source: UniProtKB
Cellular_component	Cajal body Inferred from direct assay PubMed 16687569. Source: BHF-UCL box C/D snoRNP complex Non-traceable author statement PubMed 17636026. Source: BHF-UCL cytoplasm Inferred from direct assay. Source: HPA pre-snoRNP complex Inferred from direct assay PubMed 17636026. Source: BHF-UCL
Molecular_function	snoRNA binding Inferred from direct assay PubMed 17636026. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 529	529	Nucleolar protein 58		PRO_0000219023
Regions
	Domain	282 – 400	119	Nop
	Compositional bias	441 – 524	84	Lys-rich
Amino acid modifications
	Modified residue	109	1	Phosphoserine Ref.9
	Modified residue	351	1	Phosphoserine Ref.11 Ref.14
	Modified residue	483	1	Phosphoserine Ref.14
	Modified residue	502	1	Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16
	Modified residue	514	1	Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16
	Cross-link	467		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13
	Cross-link	497		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13
Natural variations
	Natural variant	387	1	N → T. Corresponds to variant rs34748654 [ dbSNP | Ensembl ].		VAR_059461
	Natural variant	389	1	A → P. Corresponds to variant rs34458926 [ dbSNP | Ensembl ].		VAR_059462
	Natural variant	400	1	D → A. Corresponds to variant rs35900977 [ dbSNP | Ensembl ].		VAR_059463
	Natural variant	508	1	T → P. Corresponds to variant rs34523815 [ dbSNP | Ensembl ].		VAR_059464
Experimental info
	Sequence conflict	2	1	L → M in CAB55989. Ref.5
	Sequence conflict	129	1	G → V in CAB55989. Ref.5
	Sequence conflict	202 – 221	20	LTYCK…YASAK → YHTASVYRKLAIGRLCLCQ in AAF29084. Ref.6
	Sequence conflict	235 – 260	26	KAAAE…HLCTQ → EGSCRDIHGNRGFRRRYLQY SASLHP in AAF29084. Ref.6
	Sequence conflict	280	1	M → V in CAB55989. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9Y2X3 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 27CD73CFF5B9A556	FASTA	529	59,578
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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.
[14]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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].
[16]	"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, MASS SPECTROMETRY.

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.
IPI	IPI00006379.
PIR	T17299.
RefSeq	NP_057018.1. NM_015934.3.
UniGene	Hs.471104.
3D structure databases
ProteinModelPortal	Q9Y2X3.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y2X3. 11 interactions.
STRING	9606.ENSP00000264279.
PTM databases
PhosphoSite	Q9Y2X3.
Polymorphism databases
DMDM	17380155.
2D gel databases
SWISS-2DPAGE	Q9Y2X3.
Proteomic databases
PaxDb	Q9Y2X3.
PeptideAtlas	Q9Y2X3.
PRIDE	Q9Y2X3.
Protocols and materials databases
DNASU	51602.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264279; ENSP00000264279; ENSG00000055044.
GeneID	51602.
KEGG	hsa:51602.
UCSC	uc002uzb.3. human.
Organism-specific databases
CTD	51602.
GeneCards	GC02P203130.
HGNC	HGNC:29926. NOP58.
HPA	HPA018472. HPA021062.
neXtProt	NX_Q9Y2X3.
PharmGKB	PA164724092.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1498.
HOGENOM	HOG000196310.
InParanoid	Q9Y2X3.
KO	K14565.
OMA	DAHEQLA.
OrthoDB	EOG451DQQ.
PhylomeDB	Q9Y2X3.
Gene expression databases
ArrayExpress	Q9Y2X3.
Bgee	Q9Y2X3.
Genevestigator	Q9Y2X3.
GermOnline	ENSG00000055044. Homo sapiens.
Family and domain databases
InterPro	IPR012974. NOP5_N. IPR002687. Nop_dom. IPR012976. NOSIC. [Graphical view]
Pfam	PF01798. Nop. 1 hit. PF08156. NOP5NT. 1 hit. PF08060. NOSIC. 1 hit. [Graphical view]
SMART	SM00931. NOSIC. 1 hit. [Graphical view]
PROSITE	PS51358. NOP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	NOP58. human.
GenomeRNAi	51602.
NextBio	55479.

Entry information

Entry name

NOP58_HUMAN

Accession

Primary (citable) accession number: Q9Y2X3
Secondary accession number(s): Q53SA4 , Q6PK08, Q9P036, Q9UFN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.