Q9HCD5 (NCOA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	579 AA.
Sequence status	Complete.
Protein existence	Evidence 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.10
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Activator Repressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro aminoacyl-tRNA ligase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 579

579

Nuclear receptor coactivator 5

PRO_0000094411

Regions

Region

1 – 158

158

Transcription repression

Region

458 – 579

122

Transcription activation

Motif

345 – 349

5

LXXLL motif

Compositional bias

7 – 150

144

Arg/Asp-rich (mixed charge)

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.13

Modified residue

3

1

Phosphothreonine Ref.13

Modified residue

9

1

Phosphoserine Ref.13

Modified residue

29

1

Phosphoserine By similarity

Modified residue

34

1

Phosphoserine By similarity

Modified residue

127

1

Phosphotyrosine Ref.9

Modified residue

151

1

Phosphoserine Ref.9

Modified residue

377

1

Phosphoserine Ref.11

Modified residue

378

1

Phosphoserine Ref.12 Ref.14

Modified residue

379

1

Phosphothreonine Ref.13 Ref.14

Modified residue

381

1

Phosphoserine Ref.12 Ref.13 Ref.14

Modified residue

387

1

Phosphoserine Ref.11

Modified residue

404

1

Phosphoserine Ref.8

Modified residue

420

1

Phosphothreonine Ref.8

Natural variations

Natural variant

326

1

E → G.
Corresponds to variant rs11549557 [ dbSNP | Ensembl ].

VAR_053530

Experimental info

Mutagenesis

342

1

I → A: Abolishes E2-inducible strong interaction with ESR1, but not basal interaction. Ref.1

Mutagenesis

348 – 349

2

LL → AA: Abolishes interaction with ESR1.

Secondary structure

1

.

.

.

579

Helix Strand Turn

Details...

Helix

345 – 350

6

Sequences

	Sequence		Length	Mass (Da)
	Q9HCD5 [UniParc]. Last modified February 12, 2003. Version 2. Checksum: D2ADCCEBEE566A91	FASTA	579	65,536
	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

References

	« Hide 'large scale' referencesShow '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: 11113208] [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: 15073177] [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. , 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: 11780052] [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. , 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: 15489334] [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: 10997877] [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: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[8]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404 AND THR-420, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127 AND SER-151, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 17890166] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; RBMX AND PPP1CA, INTERACTION WITH YLPM1.
[11]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-387, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-381, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-9; THR-379 AND SER-381, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378; THR-379 AND SER-381, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[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: 21269460] [Abstract] Cited for: 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.

IPI

IPI00288941.

RefSeq

NP_066018.1. NM_020967.2.

UniGene

Hs.654991.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V95	NMR	-	A	197-313	[»]
2J7X	X-ray	2.10	B	338-354	[»]
2J7Y	X-ray	1.80	B	338-354	[»]

ProteinModelPortal

Q9HCD5.

SMR

Q9HCD5. Positions 197-314.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9HCD5. 3 interactions.

STRING

Q9HCD5.

PTM databases

PhosphoSite

Q9HCD5.

Polymorphism databases

DMDM

28380083.

Proteomic databases

PRIDE

Q9HCD5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000290231; ENSP00000290231; ENSG00000124160.

GeneID

57727.

KEGG

hsa:57727.

UCSC

uc002xrd.1. human.

Organism-specific databases

CTD

57727.

GeneCards

GC20M044690.

H-InvDB

HIX0015876.

HGNC

HGNC:15909. NCOA5.

neXtProt

NX_Q9HCD5.

PharmGKB

PA31474.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00530000064134.

HOGENOM

HBG713301.

HOVERGEN

HBG052585.

InParanoid

Q9HCD5.

OMA

LMRSSTD.

OrthoDB

EOG42BX8N.

PhylomeDB

Q9HCD5.

Gene expression databases

ArrayExpress

Q9HCD5.

Bgee

Q9HCD5.

CleanEx

HS_NCOA5.

Genevestigator

Q9HCD5.

GermOnline

ENSG00000124160. Homo sapiens.

Family and domain databases

InterPro

IPR004154. Anticodon-bd.
[Graphical view]

Gene3D

G3DSA:3.40.50.800. Anticodon_bd. 1 hit.

SUPFAM

SSF52954. Anticodon_bd. 1 hit.

ProtoNet

Search...

Other

NextBio

64672.

PMAP-CutDB

Q9HCD5.

Entry information

Entry name

NCOA5_HUMAN

Accession

Primary (citable) accession number: Q9HCD5
Secondary accession number(s): B2RTV9 , E1P5R0, Q6HA99, Q9H1F2, Q9H2T2, Q9H4Y9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	February 12, 2003
Last modified:	January 25, 2012
This is version 88 of the entry and version 2 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.