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P78316 (NOP14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleolar protein 14
Alternative name(s):
Nucleolar complex protein 14
Gene names
Name:NOP14
Synonyms:C4orf9, NOL14
ORF Names:RES4-25
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length857 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm By similarity.

Subunit structure

Component of the ribosomal small subunit (SSU) processome By similarity.

Subcellular location

Nucleusnucleolus By similarity.

Sequence similarities

Belongs to the NOP14 family.

Sequence caution

The sequence AAB97011.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processRibosome biogenesis
rRNA processing
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from sequence or structural similarity. Source: UniProtKB

endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from sequence or structural similarity. Source: UniProtKB

endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from sequence or structural similarity. Source: UniProtKB

maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from sequence or structural similarity. Source: UniProtKB

rRNA processing

Inferred from sequence or structural similarity. Source: UniProtKB

ribosomal small subunit biogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_component90S preribosome

Inferred from sequence or structural similarity. Source: UniProtKB

Noc4p-Nop14p complex

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

small-subunit processome

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

snoRNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P78316-1)

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 2 (identifier: P78316-2)

The sequence of this isoform differs from the canonical sequence as follows:
     772-819: KVLEFGRKQG...DNQFLARMQL → SNSRPQVIHLPWPPNYRCEPQHPAKKVIFFRVIML
     820-857: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 857857Nucleolar protein 14
PRO_0000137155

Amino acid modifications

Modified residue961Phosphoserine Ref.6 Ref.9 Ref.10 Ref.12
Modified residue1461Phosphoserine Ref.5 Ref.7 Ref.9 Ref.10 Ref.12
Modified residue1481Phosphoserine Ref.5 Ref.7 Ref.9 Ref.10
Modified residue3491Phosphoserine Ref.12

Natural variations

Alternative sequence772 – 81948KVLEF…ARMQL → SNSRPQVIHLPWPPNYRCEP QHPAKKVIFFRVIML in isoform 2.
VSP_018021
Alternative sequence820 – 85738Missing in isoform 2.
VSP_018022
Natural variant3801L → S. Ref.2
Corresponds to variant rs2515960 [ dbSNP | Ensembl ].
VAR_053540
Natural variant7161Q → R.
Corresponds to variant rs1054090 [ dbSNP | Ensembl ].
VAR_060075

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 7, 2004. Version 3.
Checksum: CDADFB91083DBB75

FASTA85797,668
        10         20         30         40         50         60 
MAKAKKVGAR RKASGAPAGA RGGPAKANSN PFEVKVNRQK FQILGRKTRH DVGLPGVSRA 

        70         80         90        100        110        120 
RALRKRTQTL LKEYKERDKS NVFRDKRFGE YNSNMSPEEK MMKRFALEQQ RHHEKKSIYN 

       130        140        150        160        170        180 
LNEDEELTHY GQSLADIEKH NDIVDSDSDA EDRGTLSAEL TAAHFGGGGG LLHKKTQQEG 

       190        200        210        220        230        240 
EEREKPKSRK ELIEELIAKS KQEKRERQAQ REDALELTEK LDQDWKEIQT LLSHKTPKSE 

       250        260        270        280        290        300 
NRDKKEKPKP DAYDMMVREL GFEMKAQPSN RMKTEAELAK EEQEHLRKLE AERLRRMLGK 

       310        320        330        340        350        360 
DEDENVKKPK HMSADDLNDG FVLDKDDRRL LSYKDGKMNV EEDVQEEQSK EASDPESNEE 

       370        380        390        400        410        420 
EGDSSGGEDT EESDSPDSHL DLESNVESEE ENEKPAKEQR QTPGKGLISG KERAGKATRD 

       430        440        450        460        470        480 
ELPYTFAAPE SYEELRSLLL GRSMEEQLLV VERIQKCNHP SLAEGNKAKL EKLFGFLLEY 

       490        500        510        520        530        540 
VGDLATDDPP DLTVIDKLVV HLYHLCQMFP ESASDAIKFV LRDAMHEMEE MIETKGRAAL 

       550        560        570        580        590        600 
PGLDVLIYLK ITGLLFPTSD FWHPVVTPAL VCLSQLLTKC PILSLQDVVK GLFVCCLFLE 

       610        620        630        640        650        660 
YVALSQRFIP ELINFLLGIL YIATPNKASQ GSTLVHPFRA LGKNSELLVV SAREDVATWQ 

       670        680        690        700        710        720 
QSSLSLRWAS RLRAPTSTEA NHIRLSCLAV GLALLKRCVL MYGSLPSFHA IMGPLQALLT 

       730        740        750        760        770        780 
DHLADCSHPQ ELQELCQSTL TEMESQKQLC RPLTCEKSKP VPLKLFTPRL VKVLEFGRKQ 

       790        800        810        820        830        840 
GSSKEEQERK RLIHKHKREF KGAVREIRKD NQFLARMQLS EIMERDAERK RKVKQLFNSL 

       850 
ATQEGEWKAL KRKKFKK 

« Hide

Isoform 2 [UniParc].

Checksum: B7EEF5F61E6D6390
Show »

FASTA80691,385

References

« Hide 'large scale' references
[1]"Exon trapping and sequence-based methods of gene finding in transcript mapping of human 4p16.3."
Pribill I., Barnes G.T., Chen J., Church D., Buckler A., Baxendale S., Bates G.P., Lehrach H., Gusella M.J., Duyao M.P., Ambrose C.M., Gusella J.F., MacDonald M.E.
Somat. Cell Mol. Genet. 23:413-427(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]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], VARIANT SER-380.
[3]"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] (ISOFORMS 1 AND 2).
Tissue: Cervix and Colon.
[4]"The primary structure and genomic organization of five novel transcripts located close to the Huntington's disease gene on human chromosome 4p16.3."
Hadano S., Ishida Y., Ikeda J.-E.
DNA Res. 5:177-186(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 140-857 (ISOFORM 1).
Tissue: Brain.
[5]"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-146 AND SER-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"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-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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-146 AND SER-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"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].
[9]"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-96; SER-146 AND SER-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"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-96; SER-146 AND SER-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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-96; SER-146 AND SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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
AF040965 mRNA. Translation: AAB97011.1. Different initiation.
CH471131 Genomic DNA. Translation: EAW82489.1.
CH471131 Genomic DNA. Translation: EAW82491.1.
CH471131 Genomic DNA. Translation: EAW82492.1.
BC026035 mRNA. Translation: AAH26035.1.
BC053635 mRNA. Translation: AAH53635.1.
AB000467 mRNA. Translation: BAA19121.1.
PIRJE0188.
RefSeqNP_003694.1. NM_003703.1.
UniGeneHs.627133.

3D structure databases

ProteinModelPortalP78316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114162. 8 interactions.
MINTMINT-3022939.
STRING9606.ENSP00000315674.

PTM databases

PhosphoSiteP78316.

Polymorphism databases

DMDM56404449.

Proteomic databases

PaxDbP78316.
PRIDEP78316.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314262; ENSP00000315674; ENSG00000087269. [P78316-1]
ENST00000398071; ENSP00000381146; ENSG00000087269. [P78316-2]
ENST00000416614; ENSP00000405068; ENSG00000087269. [P78316-1]
GeneID8602.
KEGGhsa:8602.
UCSCuc003ggj.1. human. [P78316-1]

Organism-specific databases

CTD8602.
GeneCardsGC04M002910.
H-InvDBHIX0004040.
HGNCHGNC:16821. NOP14.
HPAHPA039596.
HPA055652.
MIM611526. gene.
neXtProtNX_P78316.
PharmGKBPA164723982.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242520.
HOGENOMHOG000285983.
HOVERGENHBG052649.
InParanoidP78316.
KOK14766.
OMAKHYDPDR.
OrthoDBEOG78PV8T.
PhylomeDBP78316.
TreeFamTF105698.

Gene expression databases

ArrayExpressP78316.
BgeeP78316.
CleanExHS_NOP14.
GenevestigatorP78316.

Family and domain databases

InterProIPR007276. Nop14.
[Graphical view]
PANTHERPTHR23183. PTHR23183. 1 hit.
PfamPF04147. Nop14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi8602.
NextBio32233.
PMAP-CutDBP78316.
PROP78316.
SOURCESearch...

Entry information

Entry nameNOP14_HUMAN
AccessionPrimary (citable) accession number: P78316
Secondary accession number(s): D3DVR6 expand/collapse secondary AC list , Q7LGI5, Q7Z6K0, Q8TBR6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 7, 2004
Last modified: April 16, 2014
This is version 110 of the entry and version 3 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 4

Human chromosome 4: entries, gene names and cross-references to MIM