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Q14978 (NOLC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleolar and coiled-body phosphoprotein 1
Alternative name(s):
140 kDa nucleolar phosphoprotein
Short name=Nopp140
Hepatitis C virus NS5A-transactivated protein 13
Short name=HCV NS5A-transactivated protein 13
Nucleolar 130 kDa protein
Nucleolar phosphoprotein p130
Gene names
Name:NOLC1
Synonyms:KIAA0035, NS5ATP13
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length699 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Related to nucleologenesis, may play a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus. It has intrinsic GTPase and ATPase activities. May play an important role in transcription catalyzed by RNA polymerase I.

Subunit structure

Interacts with RNA polymerase I 194 kDa subunit (RPA194) and with casein kinase-II.

Subcellular location

Nucleusnucleolus. Cytoplasm. Note: Shuttles between the nucleolus and the cytoplasm. At telophase it begins to assemble into granular-like pre-nucleolar bodies which are subsequently relocated to nucleoli at the early G1-phase.

Post-translational modification

Undergoes rapid and massive phosphorylation/dephosphorylation cycles on CK2 and PKC sites. There is evidence suggesting that CDK1 kinase phosphorylates p130 at the M-phase.

Sequence similarities

Contains 1 LisH domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARRB1P494073EBI-396155,EBI-743313
ARRB2P321213EBI-396155,EBI-714559
gagP045912EBI-396155,EBI-6179719From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: Q14978-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Beta (identifier: Q14978-2)

The sequence of this isoform differs from the canonical sequence as follows:
     241-241: K → KVWTITSVRAE
Isoform 3 (identifier: Q14978-3)

The sequence of this isoform differs from the canonical sequence as follows:
     58-59: LK → LNR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 699699Nucleolar and coiled-body phosphoprotein 1
PRO_0000096942

Regions

Domain10 – 4233LisH
Repeat84 – 9512Acidic serine cluster 1
Repeat125 – 13612Acidic serine cluster 2
Repeat167 – 17812Acidic serine cluster 3
Repeat221 – 23212Acidic serine cluster 4
Repeat264 – 27512Acidic serine cluster 5
Repeat325 – 33612Acidic serine cluster 6
Repeat363 – 37513Acidic serine cluster 7
Repeat425 – 43612Acidic serine cluster 8
Repeat470 – 48112Acidic serine cluster 9
Repeat519 – 52911Acidic serine cluster 10
Repeat555 – 56612Acidic serine cluster 11
Region84 – 56648311 X 12 AA approximate repeats of an acidic serine cluster
Region204 – 382179Interacts with RPA194
Motif68 – 8215Nuclear localization signal Potential
Motif384 – 587204Nuclear localization signal Potential
Motif601 – 61717Nuclear localization signal Potential

Amino acid modifications

Modified residue331N6-acetyllysine Ref.18
Modified residue871Phosphoserine Ref.14
Modified residue901Phosphoserine Ref.14
Modified residue911Phosphoserine Ref.14
Modified residue3661Phosphoserine Ref.14
Modified residue3971Phosphoserine Ref.19 Ref.21
Modified residue4151N6-acetyllysine Ref.18
Modified residue5081Phosphoserine Ref.13 Ref.14 Ref.19
Modified residue5381Phosphoserine Ref.11 Ref.13 Ref.19 Ref.21
Modified residue5631Phosphoserine Ref.11 Ref.15 Ref.19
Modified residue5801Phosphoserine Ref.14 Ref.19
Modified residue5821Phosphoserine Ref.14 Ref.19
Modified residue6071Phosphothreonine Ref.10 Ref.12 Ref.13
Modified residue6101Phosphothreonine Ref.10 Ref.12 Ref.13
Modified residue6221Phosphoserine Ref.21
Modified residue6431Phosphoserine Ref.12 Ref.13 Ref.19 Ref.21
Modified residue6631N6-acetyllysine Ref.18
Modified residue6861Phosphoserine Ref.14
Modified residue6981Phosphoserine Ref.11 Ref.12 Ref.14 Ref.17 Ref.19 Ref.21

Natural variations

Alternative sequence58 – 592LK → LNR in isoform 3.
VSP_035415
Alternative sequence2411K → KVWTITSVRAE in isoform Beta.
VSP_004338
Natural variant4121G → V.
Corresponds to variant rs11191224 [ dbSNP | Ensembl ].
VAR_031677
Natural variant4561S → P. Ref.6
Corresponds to variant rs1049455 [ dbSNP | Ensembl ].
VAR_031678

Experimental info

Sequence conflict31D → A in BAA04803. Ref.6
Sequence conflict1331S → R in CAA84063. Ref.1
Sequence conflict291 – 2922SV → YA in CAA84063. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 7C5C4F25677E2E61

FASTA69973,603
        10         20         30         40         50         60 
MADAGIRRVV PSDLYPLVLG FLRDNQLSEV ANKFAKATGA TQQDANASSL LDIYSFWLKS 

        70         80         90        100        110        120 
AKVPERKLQA NGPVAKKAKK KASSSDSEDS SEEEEEVQGP PAKKAAVPAK RVGLPPGKAA 

       130        140        150        160        170        180 
AKASESSSSE ESSDDDDEED QKKQPVQKGV KPQAKAAKAP PKKAKSSDSD SDSSSEDEPP 

       190        200        210        220        230        240 
KNQKPKITPV TVKAQTKAPP KPARAAPKIA NGKAASSSSS SSSSSSSDDS EEEKAAATPK 

       250        260        270        280        290        300 
KTVPKKQVVA KAPVKAATTP TRKSSSSEDS SSDEEEEQKK PMKNKPGPYS SVPPPSAPPP 

       310        320        330        340        350        360 
KKSLGTQPPK KAVEKQQPVE SSEDSSDESD SSSEEEKKPP TKAVVSKATT KPPPAKKAAE 

       370        380        390        400        410        420 
SSSDSSDSDS SEDDEAPSKP AGTTKNSSNK PAVTTKSPAV KPAAAPKQPV GGGQKLLTRK 

       430        440        450        460        470        480 
ADSSSSEEES SSSEEEKTKK MVATTKPKAT AKAALSLPAK QAPQGSRDSS SDSDSSSSEE 

       490        500        510        520        530        540 
EEEKTSKSAV KKKPQKVAGG AAPSKPASAK KGKAESSNSS SSDDSSEEEE EKLKGKGSPR 

       550        560        570        580        590        600 
PQAPKANGTS ALTAQNGKAA KNSEEEEEEK KKAAVVVSKS GSLKKRKQNE AAKEAETPQA 

       610        620        630        640        650        660 
KKIKLQTPNT FPKRKKGEKR ASSPFRRVRE EEIEVDSRVA DNSFDAKRGA AGDWGERANQ 

       670        680        690 
VLKFTKGKSF RHEKTKKKRG SYRGGSISVQ VNSIKFDSE 

« Hide

Isoform Beta [UniParc].

Checksum: 5A02742A231255AB
Show »

FASTA70974,747
Isoform 3 [UniParc].

Checksum: 5F8699563FBA24A9
Show »

FASTA70073,745

References

« Hide 'large scale' references
[1]"Cell-cycle-dependent alterations of a highly phosphorylated nucleolar protein p130 are associated with nucleologenesis."
Pai C.-Y., Chen H.-K., Sheu H.-L., Yeh N.-H.
J. Cell Sci. 108:1911-1920(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
Tissue: Leukemia.
[2]Ying Z.L., Hong D., Jun C.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 3).
Tissue: Lung.
[6]"Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-699 (ISOFORM BETA), VARIANT PRO-456.
Tissue: Bone marrow.
[7]"Cell proliferation-dependent expression of two isoforms of the nucleolar phosphoprotein p130."
Pai C.-Y., Yeh N.-H.
Biochem. Biophys. Res. Commun. 221:581-587(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[8]"The nucleolar phosphoprotein P130 is a GTPase/ATPase with intrinsic property to form large complexes triggered by F- and Mg2+."
Chen H.-K., Yeh N.-H.
Biochem. Biophys. Res. Commun. 230:370-375(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"Human Nopp140, which interacts with RNA polymerase I: implications for rRNA gene transcription and nucleolar structural organization."
Chen H.-K., Pai C.-Y., Huang J.-Y., Yeh N.-H.
Mol. Cell. Biol. 19:8536-8546(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[10]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607 AND THR-610, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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-538; SER-563 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607; THR-610; SER-643 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508; SER-538; THR-607; THR-610 AND SER-643, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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-87; SER-90; SER-91; SER-366; SER-508; SER-580; SER-582; SER-686 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[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]"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-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-415 AND LYS-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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-397; SER-508; SER-538; SER-563; SER-580; SER-582; SER-643 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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].
[21]"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-397; SER-538; SER-622; SER-643 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z34289 mRNA. Translation: CAA84063.1.
AY820769 mRNA. Translation: AAV67777.1.
AL500527 Genomic DNA. Translation: CAH72220.1.
CH471066 Genomic DNA. Translation: EAW49714.1.
CH471066 Genomic DNA. Translation: EAW49715.1.
BC001883 mRNA. Translation: AAH01883.1.
D21262 mRNA. Translation: BAA04803.1.
CCDSCCDS65925.1. [Q14978-3]
CCDS65926.1. [Q14978-2]
CCDS7530.1. [Q14978-1]
PIRI38073.
RefSeqNP_001271317.1. NM_001284388.1. [Q14978-2]
NP_001271318.1. NM_001284389.1. [Q14978-3]
NP_004732.2. NM_004741.4. [Q14978-1]
UniGeneHs.523238.

3D structure databases

ProteinModelPortalQ14978.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114654. 58 interactions.
IntActQ14978. 13 interactions.
MINTMINT-111465.
STRING9606.ENSP00000359024.

PTM databases

PhosphoSiteQ14978.

Polymorphism databases

DMDM145559503.

Proteomic databases

MaxQBQ14978.
PaxDbQ14978.
PRIDEQ14978.

Protocols and materials databases

DNASU9221.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000405356; ENSP00000385410; ENSG00000166197. [Q14978-2]
ENST00000488254; ENSP00000475080; ENSG00000166197. [Q14978-3]
ENST00000605788; ENSP00000474710; ENSG00000166197. [Q14978-1]
GeneID9221.
KEGGhsa:9221.
UCSCuc001kuo.2. human. [Q14978-1]
uc001kup.2. human. [Q14978-2]
uc001kuq.2. human. [Q14978-3]

Organism-specific databases

CTD9221.
GeneCardsGC10P103902.
H-InvDBHIX0009150.
HGNCHGNC:15608. NOLC1.
HPAHPA037366.
HPA050388.
MIM602394. gene.
neXtProtNX_Q14978.
PharmGKBPA31679.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG318801.
HOGENOMHOG000113823.
HOVERGENHBG075370.
OMAMSIIQDL.
OrthoDBEOG7GTT6H.
PhylomeDBQ14978.
TreeFamTF341730.

Gene expression databases

ArrayExpressQ14978.
BgeeQ14978.
CleanExHS_NOLC1.
GenevestigatorQ14978.

Family and domain databases

InterProIPR006594. LisH_dimerisation.
IPR007718. SRP40_C.
[Graphical view]
PfamPF05022. SRP40_C. 1 hit.
[Graphical view]
SMARTSM00667. LisH. 1 hit.
[Graphical view]
PROSITEPS50896. LISH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNOLC1. human.
GeneWikiNucleolar_phosphoprotein_p130.
GenomeRNAi9221.
NextBio34571.
PROQ14978.
SOURCESearch...

Entry information

Entry nameNOLC1_HUMAN
AccessionPrimary (citable) accession number: Q14978
Secondary accession number(s): Q15030, Q5VV70, Q9BUV3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: April 17, 2007
Last modified: July 9, 2014
This is version 139 of the entry and version 2 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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 10

Human chromosome 10: entries, gene names and cross-references to MIM