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Q9HCD5 (NCOA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. 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:
Nuclear receptor coactivator 5

Short name=NCoA-5
Alternative name(s):
Coactivator independent of AF-2
Short name=CIA
Gene names
Name:NCOA5
Synonyms:KIAA1637
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2). Ref.2

Subunit structure

Binds HTATIP2/TIP30. Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and PPP1CA. Ref.1 Ref.2 Ref.9

Subcellular location

Nucleus.

Tissue specificity

Widely expressed.

Domain

Contains one Leu-Xaa-Xaa-Leu-Leu (LxxLL) motif that is essential for the association with nuclear receptors.

Sequence caution

The sequence AAG36793.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Nr1d2Q606742EBI-2863498,EBI-5326205From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579Nuclear receptor coactivator 5
PRO_0000094411

Regions

Region1 – 158158Transcription repression
Region458 – 579122Transcription activation
Motif345 – 3495LXXLL motif
Compositional bias7 – 150144Arg/Asp-rich (mixed charge)

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11 Ref.13 Ref.15
Modified residue31Phosphothreonine Ref.13
Modified residue91Phosphoserine Ref.13 Ref.15
Modified residue291Phosphoserine Ref.13
Modified residue341Phosphoserine Ref.13
Modified residue1261Phosphoserine Ref.15
Modified residue1511Phosphoserine Ref.8
Modified residue3781Phosphoserine Ref.13
Modified residue3811Phosphoserine Ref.10 Ref.12 Ref.13 Ref.15
Modified residue3941Phosphothreonine Ref.15
Modified residue3951Phosphoserine Ref.15
Modified residue3981Phosphoserine Ref.15

Natural variations

Natural variant3261E → G.
Corresponds to variant rs11549557 [ dbSNP | Ensembl ].
VAR_053530

Experimental info

Mutagenesis3421I → A: Abolishes E2-inducible strong interaction with ESR1, but not basal interaction. Ref.1
Mutagenesis348 – 3492LL → AA: Abolishes interaction with ESR1.

Secondary structure

......................... 579
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HCD5 [UniParc].

Last modified February 12, 2003. Version 2.
Checksum: D2ADCCEBEE566A91

FASTA57965,536
        10         20         30         40         50         60 
MNTAPSRPSP TRRDPYGFGD SRDSRRDRSP IRGSPRREPR DGRNGRDARD SRDIRDPRDL 

        70         80         90        100        110        120 
RDHRHSRDLR DHRDSRSVRD VRDVRDLRDF RDLRDSRDFR DQRDPMYDRY RDMRDSRDPM 

       130        140        150        160        170        180 
YRREGSYDRY LRMDDYCRRK DDSYFDRYRD SFDGRGPPGP ESQSRAKERL KREERRREEL 

       190        200        210        220        230        240 
YRQYFEEIQR RFDAERPVDC SVIVVNKQTK DYAESVGRKV RDLGMVVDLI FLNTEVSLSQ 

       250        260        270        280        290        300 
ALEDVSRGGS PFAIVITQQH QIHRSCTVNI MFGTPQEHRN MPQADAMVLV ARNYERYKNE 

       310        320        330        340        350        360 
CREKEREEIA RQAAKMADEA ILQERERGGP EEGVRGGHPP AIQSLINLLA DNRYLTAEET 

       370        380        390        400        410        420 
DKIINYLRER KERLMRSSTD SLPGPISRQP LGATSGASLK TQPSSQPLQS GQVLPSATPT 

       430        440        450        460        470        480 
PSAPPTSQQE LQAKILSLFN SGTVTANSSS ASPSVAAGNT PNQNFSTAAN SQPQQRSQAS 

       490        500        510        520        530        540 
GNQPPSILGQ GGSAQNMGPR PGAPSQGLFG QPSSRLAPAS NMTSQRPVSS TGINFDNPSV 

       550        560        570 
QKALDTLIQS GPALSHLVSQ TTAQMGQPQA PMGSYQRHY 

« Hide

References

« Hide 'large scale' references
[1]"CIA, a novel estrogen receptor coactivator with a bifunctional nuclear receptor interacting determinant."
Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F., Giguere V.
Mol. Cell. Biol. 21:343-353(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ESR1; ESR2 AND NR1D2, MUTAGENESIS OF ILE-342 AND 348-LEU-LEU-349.
Tissue: Fetal kidney.
[2]"TIP30 interacts with an estrogen receptor alpha-interacting coactivator CIA and regulates c-myc transcription."
Jiang C., Ito M., Piening V., Bruck K., Roeder R.G., Xiao H.
J. Biol. Chem. 279:27781-27789(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 86-91 AND 280-292, FUNCTION, INTERACTION WITH HTATIP2.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [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].
Tissue: Brain.
[6]"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-579.
Tissue: Brain.
[7]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[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-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G."
Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.
Biochim. Biophys. Acta 1774:1339-1350(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; RBMX AND PPP1CA, INTERACTION WITH YLPM1.
[10]"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-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-9; SER-29; SER-34; SER-378 AND SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-126; SER-381; THR-394; SER-395 AND SER-398, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Solution structure of anticodon binding domain from nuclear receptor coactivator 5 (human KIAA1637 protein)."
RIKEN structural genomics initiative (RSGI)
Submitted (JUL-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 197-313.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF230533 mRNA. Translation: AAG36793.1. Different initiation.
AF470686 mRNA. Translation: AAO33457.1.
AL035662, AL162458 Genomic DNA. Translation: CAI42972.1.
AL162458, AL035662 Genomic DNA. Translation: CAH74052.1.
CH471077 Genomic DNA. Translation: EAW75765.1.
CH471077 Genomic DNA. Translation: EAW75769.1.
BC140836 mRNA. Translation: AAI40837.1.
BC151133 mRNA. Translation: AAI51134.1.
AB046857 mRNA. Translation: BAB13463.1.
RefSeqNP_066018.1. NM_020967.2.
UniGeneHs.654991.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V95NMR-A197-313[»]
2J7XX-ray2.10B338-354[»]
2J7YX-ray1.80B338-354[»]
ProteinModelPortalQ9HCD5.
SMRQ9HCD5. Positions 197-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121747. 13 interactions.
IntActQ9HCD5. 7 interactions.
STRING9606.ENSP00000290231.

PTM databases

PhosphoSiteQ9HCD5.

Polymorphism databases

DMDM28380083.

Proteomic databases

PaxDbQ9HCD5.
PRIDEQ9HCD5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290231; ENSP00000290231; ENSG00000124160.
GeneID57727.
KEGGhsa:57727.
UCSCuc002xrd.3. human.

Organism-specific databases

CTD57727.
GeneCardsGC20M044690.
HGNCHGNC:15909. NCOA5.
HPAHPA050231.
neXtProtNX_Q9HCD5.
PharmGKBPA31474.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG147049.
HOVERGENHBG052585.
InParanoidQ9HCD5.
OMAGSARNMG.
OrthoDBEOG7GTT6B.
PhylomeDBQ9HCD5.
TreeFamTF324704.

Gene expression databases

ArrayExpressQ9HCD5.
BgeeQ9HCD5.
CleanExHS_NCOA5.
GenevestigatorQ9HCD5.

Family and domain databases

Gene3D3.40.50.800. 1 hit.
InterProIPR004154. Anticodon-bd.
[Graphical view]
SUPFAMSSF52954. SSF52954. 1 hit.
ProtoNetSearch...

Other

ChiTaRSNCOA5. human.
EvolutionaryTraceQ9HCD5.
GeneWikiNCOA5.
GenomeRNAi57727.
NextBio64672.
PMAP-CutDBQ9HCD5.
PROQ9HCD5.

Entry information

Entry nameNCOA5_HUMAN
AccessionPrimary (citable) accession number: Q9HCD5
Secondary accession number(s): B2RTV9 expand/collapse secondary AC list , E1P5R0, Q6HA99, Q9H1F2, Q9H2T2, Q9H4Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: February 12, 2003
Last modified: April 16, 2014
This is version 107 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 20

Human chromosome 20: entries, gene names and cross-references to MIM