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Protein

UPF0568 protein C14orf166

Gene

C14orf166

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

Functioni

RNA-binding protein involved in modulation of mRNA transcription by Polymerase II. In case of infection by influenza virus A, is involved in viral replication. Component of the tRNA-splicing ligase complex and is required for tRNA ligation (PubMed:24870230). May be required for RNA transport (PubMed:24608264).3 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA polymerase II core binding Source: UniProtKB

GO - Biological processi

  • gene expression Source: Reactome
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • RNA transport Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • tRNA processing Source: Reactome
  • tRNA splicing, via endonucleolytic cleavage and ligation Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-6784531. tRNA processing in the nucleus.

Names & Taxonomyi

Protein namesi
Recommended name:
UPF0568 protein C14orf166
Alternative name(s):
CLE7 homolog
Short name:
CLE
Gene namesi
ORF Names:CGI-99
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:23169. C14orf166.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB-SubCell
  • microtubule organizing center Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • tRNA-splicing ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134953268.

Polymorphism and mutation databases

BioMutaiC14orf166.
DMDMi20138086.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 244244UPF0568 protein C14orf166PRO_0000089956Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201N6-acetyllysineCombined sources
Modified residuei62 – 621N6-acetyllysineCombined sources
Modified residuei98 – 981N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9Y224.
MaxQBiQ9Y224.
PaxDbiQ9Y224.
PRIDEiQ9Y224.
TopDownProteomicsiQ9Y224.

2D gel databases

REPRODUCTION-2DPAGEQ9Y224.

PTM databases

iPTMnetiQ9Y224.
PhosphoSiteiQ9Y224.
SwissPalmiQ9Y224.

Expressioni

Tissue specificityi

Widely expressed. Expressed at high level in heart and skeletal muscle. Expressed at intermediate level in liver, pancreas, fetal brain and fetal lung. Weakly expressed in adult brain, adult lung, placenta, fetal liver and fetal kidney. Overexpressed in many brain tumors.1 Publication

Gene expression databases

BgeeiQ9Y224.
CleanExiHS_C14orf166.
ExpressionAtlasiQ9Y224. baseline and differential.
GenevisibleiQ9Y224. HS.

Organism-specific databases

HPAiHPA039824.

Interactioni

Subunit structurei

Homodimer (Probable). Interacts with NIN; which may prevent phosphorylation of NIN. Interacts with POLR2A. Component of a tRNA-splicing ligase complex with FAM98B, DDX1 and RTCB. Interacts with influenza A virus RNA polymerase subunits PA, PB1 and PB2, and nucleocapsid NP. Interacts with hepatitis C virus core protein p19.Curated8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1104547,EBI-1104547
FAM98AQ8NCA53EBI-1104547,EBI-1210765
NINQ8N4C64EBI-1104547,EBI-1164022
PAP313434EBI-1104547,EBI-5800362From a different organism.
PAQ670203EBI-1104547,EBI-11514477From a different organism.

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • RNA polymerase II core binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119650. 77 interactions.
IntActiQ9Y224. 35 interactions.
MINTiMINT-3083992.
STRINGi9606.ENSP00000261700.

Structurei

3D structure databases

ProteinModelPortaliQ9Y224.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UPF0568 family.Curated

Phylogenomic databases

eggNOGiKOG4380. Eukaryota.
ENOG410XRFT. LUCA.
GeneTreeiENSGT00390000005163.
HOGENOMiHOG000039763.
HOVERGENiHBG051035.
InParanoidiQ9Y224.
KOiK15433.
OMAiPFDKGND.
OrthoDBiEOG7MH108.
PhylomeDBiQ9Y224.
TreeFamiTF323606.

Family and domain databases

InterProiIPR019265. UPF0568.
[Graphical view]
PANTHERiPTHR15924. PTHR15924. 1 hit.
PfamiPF10036. RLL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y224-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRRKLTALD YHNPAGFNCK DETEFRNFIV WLEDQKIRHY KIEDRGNLRN
60 70 80 90 100
IHSSDWPKFF EKYLRDVNCP FKIQDRQEAI DWLLGLAVRL EYGDNAEKYK
110 120 130 140 150
DLVPDNSKTA DNATKNAEPL INLDVNNPDF KAGVMALANL LQIQRHDDYL
160 170 180 190 200
VMLKAIRILV QERLTQDAVA KANQTKEGLP VALDKHILGF DTGDAVLNEA
210 220 230 240
AQILRLLHIE ELRELQTKIN EAIVAVQAII ADPKTDHRLG KVGR
Length:244
Mass (Da):28,068
Last modified:November 1, 1999 - v1
Checksum:iEB2C3C5577A09A2A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF100755 mRNA. Translation: AAD43019.1.
AF151857 mRNA. Translation: AAD34094.1.
BC001722 mRNA. Translation: AAH01722.1.
CCDSiCCDS9705.1.
RefSeqiNP_057123.1. NM_016039.2.
UniGeneiHs.534457.

Genome annotation databases

EnsembliENST00000261700; ENSP00000261700; ENSG00000087302.
GeneIDi51637.
KEGGihsa:51637.
UCSCiuc010aod.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF100755 mRNA. Translation: AAD43019.1.
AF151857 mRNA. Translation: AAD34094.1.
BC001722 mRNA. Translation: AAH01722.1.
CCDSiCCDS9705.1.
RefSeqiNP_057123.1. NM_016039.2.
UniGeneiHs.534457.

3D structure databases

ProteinModelPortaliQ9Y224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119650. 77 interactions.
IntActiQ9Y224. 35 interactions.
MINTiMINT-3083992.
STRINGi9606.ENSP00000261700.

PTM databases

iPTMnetiQ9Y224.
PhosphoSiteiQ9Y224.
SwissPalmiQ9Y224.

Polymorphism and mutation databases

BioMutaiC14orf166.
DMDMi20138086.

2D gel databases

REPRODUCTION-2DPAGEQ9Y224.

Proteomic databases

EPDiQ9Y224.
MaxQBiQ9Y224.
PaxDbiQ9Y224.
PRIDEiQ9Y224.
TopDownProteomicsiQ9Y224.

Protocols and materials databases

DNASUi51637.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261700; ENSP00000261700; ENSG00000087302.
GeneIDi51637.
KEGGihsa:51637.
UCSCiuc010aod.4. human.

Organism-specific databases

CTDi51637.
GeneCardsiC14orf166.
H-InvDBHIX0131233.
HGNCiHGNC:23169. C14orf166.
HPAiHPA039824.
MIMi610858. gene.
neXtProtiNX_Q9Y224.
PharmGKBiPA134953268.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4380. Eukaryota.
ENOG410XRFT. LUCA.
GeneTreeiENSGT00390000005163.
HOGENOMiHOG000039763.
HOVERGENiHBG051035.
InParanoidiQ9Y224.
KOiK15433.
OMAiPFDKGND.
OrthoDBiEOG7MH108.
PhylomeDBiQ9Y224.
TreeFamiTF323606.

Enzyme and pathway databases

ReactomeiR-HSA-6784531. tRNA processing in the nucleus.

Miscellaneous databases

ChiTaRSiC14orf166. human.
GeneWikiiC14orf166.
GenomeRNAii51637.
NextBioi55573.
PROiQ9Y224.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y224.
CleanExiHS_C14orf166.
ExpressionAtlasiQ9Y224. baseline and differential.
GenevisibleiQ9Y224. HS.

Family and domain databases

InterProiIPR019265. UPF0568.
[Graphical view]
PANTHERiPTHR15924. PTHR15924. 1 hit.
PfamiPF10036. RLL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pituitary.
  2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
    Tissue: Muscle.
  4. "PA subunit from influenza virus polymerase complex interacts with a cellular protein with homology to a family of transcriptional activators."
    Huarte M., Sanz-Ezquerro J.J., Roncal F., Ortin J., Nieto A.
    J. Virol. 75:8597-8604(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INFLUENZA A VIRUS PA.
  5. "A novel ninein-interaction protein, CGI-99, blocks ninein phosphorylation by GSK3beta and is highly expressed in brain tumors."
    Howng S.-L., Hsu H.-C., Cheng T.-S., Lee Y.-L., Chang L.-K., Lu P.-J., Hong Y.-R.
    FEBS Lett. 566:162-168(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NIN.
  6. "hCLE/CGI-99, a human protein that interacts with the influenza virus polymerase, is a mRNA transcription modulator."
    Perez-Gonzalez A., Rodriguez A., Huarte M., Salanueva I.J., Nieto A.
    J. Mol. Biol. 362:887-900(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH POLR2A.
  7. "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-20; LYS-62 AND LYS-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Identification of hnRNPH1, NF45, and C14orf166 as novel host interacting partners of the mature hepatitis C virus core protein."
    Lee J.W., Liao P.C., Young K.C., Chang C.L., Chen S.S., Chang T.T., Lai M.D., Wang S.W.
    J. Proteome Res. 10:4522-4534(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEPATITIS C VIRUS CORE PROTEIN P19.
  10. "Cellular human CLE/C14orf166 protein interacts with influenza virus polymerase and is required for viral replication."
    Rodriguez A., Perez-Gonzalez A., Nieto A.
    J. Virol. 85:12062-12066(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INFLUENZA VIRUS PA; PB1; PB2 AND NP.
  11. Cited for: IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Analysis of orthologous groups reveals archease and DDX1 as tRNA splicing factors."
    Popow J., Jurkin J., Schleiffer A., Martinez J.
    Nature 511:104-107(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX.
  14. "hCLE/C14orf166 associates with DDX1-HSPC117-FAM98B in a novel transcription-dependent shuttling RNA-transporting complex."
    Perez-Gonzalez A., Pazo A., Navajas R., Ciordia S., Rodriguez-Frandsen A., Nieto A.
    PLoS ONE 9:E90957-E90957(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH FAM98B; DDX1 AND RTCB, RNA-BINDING, FUNCTION.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCN166_HUMAN
AccessioniPrimary (citable) accession number: Q9Y224
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: November 1, 1999
Last modified: April 13, 2016
This is version 130 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families
  4. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.