SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q14686

- NCOA6_HUMAN

UniProt

Q14686 - NCOA6_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Nuclear receptor coactivator 6
Gene
NCOA6, AIB3, KIAA0181, RAP250, TRBP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Coactivates expression in an agonist- and AF2-dependent manner. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ERs), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Probably functions as a general coactivator, rather than just a nuclear receptor coactivator. May also be involved in the coactivation of the NF-kappa-B pathway. May coactivate expression via a remodeling of chromatin and its interaction with histone acetyltransferase proteins.

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. enzyme binding Source: UniProtKB
  3. estrogen receptor binding Source: UniProtKB
  4. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. retinoid X receptor binding Source: UniProtKB
  7. thyroid hormone receptor binding Source: UniProtKB
  8. transcription coactivator activity Source: UniProtKB

GO - Biological processi

  1. DNA recombination Source: UniProtKB
  2. DNA repair Source: UniProtKB
  3. DNA replication Source: UniProtKB
  4. DNA-templated transcription, initiation Source: UniProtKB
  5. brain development Source: UniProtKB
  6. cellular lipid metabolic process Source: Reactome
  7. cellular response to DNA damage stimulus Source: MGI
  8. glucocorticoid receptor signaling pathway Source: UniProtKB
  9. heart development Source: UniProtKB
  10. intracellular estrogen receptor signaling pathway Source: UniProtKB
  11. labyrinthine layer blood vessel development Source: Ensembl
  12. myeloid cell differentiation Source: UniProtKB
  13. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  14. positive regulation of transcription, DNA-templated Source: UniProtKB
  15. response to hormone Source: UniProtKB
  16. small molecule metabolic process Source: Reactome
  17. transcription initiation from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118789. REV-ERBA represses gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_24941. Circadian Clock.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor coactivator 6
Alternative name(s):
Activating signal cointegrator 2
Short name:
ASC-2
Amplified in breast cancer protein 3
Cancer-amplified transcriptional coactivator ASC-2
Nuclear receptor coactivator RAP250
Short name:
NRC RAP250
Nuclear receptor-activating protein, 250 kDa
Peroxisome proliferator-activated receptor-interacting protein
Short name:
PPAR-interacting protein
Short name:
PRIP
Thyroid hormone receptor-binding protein
Gene namesi
Name:NCOA6
Synonyms:AIB3, KIAA0181, RAP250, TRBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:15936. NCOA6.

Subcellular locationi

GO - Cellular componenti

  1. histone methyltransferase complex Source: MGI
  2. intracellular membrane-bounded organelle Source: HPA
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. transcription factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi883 – 89412TSPLL…LLQSD → ENPLLVNLLQFI: Reduced binding to THRB, RXRA, ESR2 and ESR1. 1 Publication
Add
BLAST
Mutagenesisi883 – 89412TSPLL…LLQSD → NLPLLVNLLQHT: Reduced binding to THRB, RXRA, ESR2 and ESR1. 1 Publication
Add
BLAST
Mutagenesisi883 – 89412TSPLL…LLQSD → VNPLLVNLLQFI: Reduced binding to THRB, RXRA, ESR2 and ESR1. 1 Publication
Add
BLAST
Mutagenesisi883 – 8842TS → SY: Strong increase in binding to THRB, RXRA and ESR2, but dramatic decrease in binding to ESR1.
Mutagenesisi884 – 89411SPLLVNLLQSD → NPLLVNLLQLL: Reduced binding to THRB, RXRA, ESR2 and ESR1.
Add
BLAST

Organism-specific databases

PharmGKBiPA31475.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20632063Nuclear receptor coactivator 6
PRO_0000094413Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei884 – 8841Phosphoserine; by MAPK; in vitro1 Publication
Modified residuei1321 – 13211Phosphothreonine
Modified residuei1819 – 18191N6-acetyllysine By similarity
Modified residuei1822 – 18221N6-acetyllysine By similarity

Post-translational modificationi

Phosphorylated by PRKDC.2 Publications
Phosphorylation on Ser-884 leads to a strong decrease in binding to ESR1 and ESR2.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ14686.
PaxDbiQ14686.
PRIDEiQ14686.

PTM databases

PhosphoSiteiQ14686.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in brain, prostate, testis and ovary; weakly expressed in lung, thymus and small intestine.

Gene expression databases

BgeeiQ14686.
CleanExiHS_NCOA6.
GenevestigatoriQ14686.

Organism-specific databases

HPAiHPA004198.

Interactioni

Subunit structurei

Monomer and homodimer. Interacts with RBM39 By similarity. Interacts in vitro with the basal transcription factors GTF2A and TBP, suggesting an autonomous transactivation function. Interacts with NCOA1, CRSP3, RBM14, the histone acetyltransferases EP300 and CREBBP, and with the methyltransferases NCOA6IP and PRMT2/HRMT1L1. Component of the MLL2/3 complex (also named ASCOM complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin. Interacts with ZNF335; may enhance ligand-dependent transcriptional activation by nuclear hormone receptors.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARP102752EBI-78670,EBI-608057
ASH2LQ9UBL37EBI-78670,EBI-540797
CREBBPQ927932EBI-78670,EBI-81215
KMT2CQ8NEZ45EBI-78670,EBI-1042997
KMT2DO146866EBI-78670,EBI-996065
RB1P064003EBI-78670,EBI-491274
WDR5P619642EBI-78670,EBI-540834

Protein-protein interaction databases

BioGridi116691. 78 interactions.
DIPiDIP-30934N.
IntActiQ14686. 31 interactions.
MINTiMINT-1194462.
STRINGi9606.ENSP00000351894.

Structurei

3D structure databases

ProteinModelPortaliQ14686.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 13101310NCOA1-binding region
Add
BLAST
Regioni1 – 10571057CREBBP-binding region
Add
BLAST
Regioni1 – 928928TBP/GTF2A-binding region
Add
BLAST
Regioni773 – 927155NCOA6IP-binding region
Add
BLAST
Regioni1641 – 2063423EP300/CRSP3-binding region
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi887 – 8915LXXLL motif 1
Motifi1491 – 14955LXXLL motif 2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi227 – 1041815Gln-rich
Add
BLAST
Compositional biasi372 – 3776Poly-Pro
Compositional biasi913 – 9186Poly-Lys

Domaini

Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Only motif 1 is essential for the association with nuclear receptors, while adjacent Ser-884 displays selectivity for nuclear receptors.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG12793.
HOVERGENiHBG052586.
InParanoidiQ14686.
KOiK14971.
OMAiNARPQFI.
OrthoDBiEOG7W9RSX.
PhylomeDBiQ14686.
TreeFamiTF332639.

Family and domain databases

InterProiIPR026638. NCOA6.
[Graphical view]
PANTHERiPTHR15690. PTHR15690. 1 hit.

Sequencei

Sequence statusi: Complete.

Q14686-1 [UniParc]FASTAAdd to Basket

« Hide

MVLDDLPNLE DIYTSLCSST MEDSEMDFDS GLEDDDTKSD SILEDSTIFV     50
AFKGNIDDKD FKWKLDAILK NVPNLLHMES SKLKVQKVEP WNSVRVTFNI 100
PREAAERLRI LAQSNNQQLR DLGILSVQIE GEGAINLALA QNRSQDVRMN 150
GPMGAGNSVR MEAGFPMASG PGIIRMNNPA TVMIPPGGNV SSSMMAPGPN 200
PELQPRTPRP ASQSDAMDPL LSGLHIQQQS HPSGSLAPPH HPMQPVSVNR 250
QMNPANFPQL QQQQQQQQQQ QQQQQQQQQQ QQQQQLQARP PQQHQQQQPQ 300
GIRPQFTAPT QVPVPPGWNQ LPSGALQPPP AQGSLGTMTA NQGWKKAPLP 350
GPMQQQLQAR PSLATVQTPS HPPPPYPFGS QQASQAHTNF PQMSNPGQFT 400
APQMKSLQGG PSRVPTPLQQ PHLTNKSPAS SPSSFQQGSP ASSPTVNQTQ 450
QQMGPRPPQN NPLPQGFQQP VSSPGRNPMV QQGNVPPNFM VMQQQPPNQG 500
PQSLHPGLGG MPKRLPPGFS AGQANPNFMQ GQVPSTTATT PGNSGAPQLQ 550
ANQNVQHAGG QGAGPPQNQM QVSHGPPNMM QPSLMGIHGN MNNQQAGTSG 600
VPQVNLSNMQ GQPQQGPPSQ LMGMHQQIVP SQGQMVQQQG TLNPQNPMIL 650
SRAQLMPQGQ MMVNPPSQNL GPSPQRMTPP KQMLSQQGPQ MMAPHNQMMG 700
PQGQVLLQQN PMIEQIMTNQ MQGNKQQFNT QNQSNVMPGP AQIMRGPTPN 750
MQGNMVQFTG QMSGQMLPQQ GPVNNSPSQV MGIQGQVLRP PGPSPHMAQQ 800
HGDPATTANN DVSLSQMMPD VSIQQTNMVP PHVQAMQGNS ASGNHFSGHG 850
MSFNAPFSGA PNGNQMSCGQ NPGFPVNKDV TLTSPLLVNL LQSDISAGHF 900
GVNNKQNNTN ANKPKKKKPP RKKKNSQQDL NTPDTRPAGL EEADQPPLPG 950
EQGINLDNSG PKLPEFSNRP PGYPSQPVEQ RPLQQMPPQL MQHVAPPPQP 1000
PQQQPQPQLP QQQQPPPPSQ PQSQQQQQQQ QQMMMMLMMQ QDPKSVRLPV 1050
SQNVHPPRGP LNPDSQRMPM QQSGSVPVMV SLQGPASVPP SPDKQRMPMP 1100
VNTPLGSNSR KMVYQESPQN PSSSPLAEMA SLPEASGSEA PSVPGGPNNM 1150
PSHVVLPQNQ LMMTGPKPGP SPLSATQGAT PQQPPVNSLP SSHGHHFPNV 1200
AAPTQTSRPK TPNRASPRPY YPQTPNNRPP STEPSEISLS PERLNASIAG 1250
LFPPQINIPL PPRPNLNRGF DQQGLNPTTL KAIGQAPSNL TMNPSNFATP 1300
QTHKLDSVVV NSGKQSNSGA TKRASPSNSR RSSPGSSRKT TPSPGRQNSK 1350
APKLTLASQT NAALLQNVEL PRNVLVSPTP LANPPVPGSF PNNSGLNPQN 1400
STVSVAAVGG VVEDNKESLN VPQDSDCQNS QSRKEQVNIE LKAVPAQEVK 1450
MVVPEDQSKK DGQPSDPNKL PSVEENKNLV SPAMREAPTS LSQLLDNSGA 1500
PNVTIKPPGL TDLEVTPPVV SGEDLKKASV IPTLQDLSSS KEPSNSLNLP 1550
HSNELCSSLV HPELSEVSSN VAPSIPPVMS RPVSSSSIST PLPPNQITVF 1600
VTSNPITTSA NTSAALPTHL QSALMSTVVT MPNAGSKVMV SEGQSAAQSN 1650
ARPQFITPVF INSSSIIQVM KGSQPSTIPA APLTTNSGLM PPSVAVVGPL 1700
HIPQNIKFSS APVPPNALSS SPAPNIQTGR PLVLSSRATP VQLPSPPCTS 1750
SPVVPSHPPV QQVKELNPDE ASPQVNTSAD QNTLPSSQST TMVSPLLTNS 1800
PGSSGNRRSP VSSSKGKGKV DKIGQILLTK ACKKVTGSLE KGEEQYGADG 1850
ETEGQGLDTT APGLMGTEQL STELDSKTPT PPAPTLLKMT SSPVGPGTAS 1900
AGPSLPGGAL PTSVRSIVTT LVPSELISAV PTTKSNHGGI ASESLAGGLV 1950
EEKVGSHPEL LPSIAPSQNL VSKETSTTAL QASVARPELE VNAAIVSGQS 2000
SEPKEIVEKS KIPGRRNSRT EEPTVASESV ENGHRKRSSR PASASSSTKD 2050
ITSAVQSKRR KSK 2063
Length:2,063
Mass (Da):219,145
Last modified:October 17, 2006 - v3
Checksum:i73219502F5138427
GO

Sequence cautioni

The sequence AAF16403.1 differs from that shown. Reason: Frameshift at position 88.
The sequence BAA11498.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti512 – 5121P → L.
Corresponds to variant rs6060031 [ dbSNP | Ensembl ].
VAR_027874
Natural varianti955 – 9551N → S.5 Publications
Corresponds to variant rs17092079 [ dbSNP | Ensembl ].
VAR_027875
Natural varianti1060 – 10601P → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_036551
Natural varianti1191 – 11911S → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_036552
Natural varianti1995 – 19951I → V.
Corresponds to variant rs6060022 [ dbSNP | Ensembl ].
VAR_027876

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF177388 mRNA. Translation: AAF13595.1.
AF208227 mRNA. Translation: AAF16403.1. Frameshift.
AF245115 mRNA. Translation: AAF78480.1.
AF128458 mRNA. Translation: AAF37003.1.
AF171667 mRNA. Translation: AAF71829.1.
D80003 mRNA. Translation: BAA11498.2. Different initiation.
AL109824 Genomic DNA. Translation: CAB92721.2.
CH471077 Genomic DNA. Translation: EAW76254.1.
CH471077 Genomic DNA. Translation: EAW76255.1.
BC136272 mRNA. Translation: AAI36273.1.
CCDSiCCDS13241.1.
RefSeqiNP_001229468.1. NM_001242539.1.
NP_054790.2. NM_014071.3.
XP_005260405.1. XM_005260348.2.
UniGeneiHs.368971.
Hs.736403.

Genome annotation databases

EnsembliENST00000359003; ENSP00000351894; ENSG00000198646.
ENST00000374796; ENSP00000363929; ENSG00000198646.
GeneIDi23054.
KEGGihsa:23054.
UCSCiuc002xav.3. human.

Polymorphism databases

DMDMi116242672.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF177388 mRNA. Translation: AAF13595.1 .
AF208227 mRNA. Translation: AAF16403.1 . Frameshift.
AF245115 mRNA. Translation: AAF78480.1 .
AF128458 mRNA. Translation: AAF37003.1 .
AF171667 mRNA. Translation: AAF71829.1 .
D80003 mRNA. Translation: BAA11498.2 . Different initiation.
AL109824 Genomic DNA. Translation: CAB92721.2 .
CH471077 Genomic DNA. Translation: EAW76254.1 .
CH471077 Genomic DNA. Translation: EAW76255.1 .
BC136272 mRNA. Translation: AAI36273.1 .
CCDSi CCDS13241.1.
RefSeqi NP_001229468.1. NM_001242539.1.
NP_054790.2. NM_014071.3.
XP_005260405.1. XM_005260348.2.
UniGenei Hs.368971.
Hs.736403.

3D structure databases

ProteinModelPortali Q14686.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116691. 78 interactions.
DIPi DIP-30934N.
IntActi Q14686. 31 interactions.
MINTi MINT-1194462.
STRINGi 9606.ENSP00000351894.

PTM databases

PhosphoSitei Q14686.

Polymorphism databases

DMDMi 116242672.

Proteomic databases

MaxQBi Q14686.
PaxDbi Q14686.
PRIDEi Q14686.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359003 ; ENSP00000351894 ; ENSG00000198646 .
ENST00000374796 ; ENSP00000363929 ; ENSG00000198646 .
GeneIDi 23054.
KEGGi hsa:23054.
UCSCi uc002xav.3. human.

Organism-specific databases

CTDi 23054.
GeneCardsi GC20M033302.
H-InvDB HIX0015752.
HGNCi HGNC:15936. NCOA6.
HPAi HPA004198.
MIMi 605299. gene.
neXtProti NX_Q14686.
PharmGKBi PA31475.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOVERGENi HBG052586.
InParanoidi Q14686.
KOi K14971.
OMAi NARPQFI.
OrthoDBi EOG7W9RSX.
PhylomeDBi Q14686.
TreeFami TF332639.

Enzyme and pathway databases

Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118789. REV-ERBA represses gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_24941. Circadian Clock.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

ChiTaRSi NCOA6. human.
GeneWikii NCOA6.
GenomeRNAii 23054.
NextBioi 44111.
PROi Q14686.
SOURCEi Search...

Gene expression databases

Bgeei Q14686.
CleanExi HS_NCOA6.
Genevestigatori Q14686.

Family and domain databases

InterProi IPR026638. NCOA6.
[Graphical view ]
PANTHERi PTHR15690. PTHR15690. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo."
    Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.
    J. Biol. Chem. 274:34283-34293(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CREBBP; NCOA1; GTF2A; TBP; RXRA; ESR1; RARA AND THRA, VARIANT SER-955.
  2. "A new family of nuclear receptor coregulators that integrates nuclear receptor signaling through CBP."
    Mahajan M.A., Samuels H.H.
    Mol. Cell. Biol. 20:5048-5063(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], HOMODIMERIZATION, INTERACTION WITH CREBBP; RXRA; ESR1; NR3C1; RARA; VDR AND THRA, VARIANT SER-955.
  3. "Cloning and characterization of RAP250, a nuclear receptor coactivator."
    Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.
    J. Biol. Chem. 275:5308-5317(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PPARA; PPARG; ESR1; ESR2 AND THR, VARIANT SER-955.
    Tissue: Testis.
  4. "Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator."
    Ko L., Cardona G.R., Chin W.W.
    Proc. Natl. Acad. Sci. U.S.A. 97:6212-6217(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION BY PRKDC, INTERACTION WITH THR; RAR; EP300 AND CRSP3, VARIANT SER-955.
    Tissue: Lymphocyte.
  5. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
    DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-955.
    Tissue: Bone marrow.
  6. "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.
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Cerebellum.
  10. "Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function."
    Zhu Y.-J., Qi C., Cao W.-Q., Yeldandi A.V., Rao M.S., Reddy J.K.
    Proc. Natl. Acad. Sci. U.S.A. 98:10380-10385(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA6IP.
  11. "Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM)."
    Iwasaki T., Chin W.W., Ko L.
    J. Biol. Chem. 276:33375-33383(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBM14.
  12. "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha."
    Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.
    J. Biol. Chem. 277:28624-28630(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRMT2.
  13. "NRC-interacting factor 1 is a novel cotransducer that interacts with and regulates the activity of the nuclear hormone receptor coactivator NRC."
    Mahajan M.A., Murray A., Samuels H.H.
    Mol. Cell. Biol. 22:6883-6894(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZNF335.
  14. "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins."
    Goo Y.-H., Sohn Y.C., Kim D.-H., Kim S.-W., Kang M.-J., Jung D.-J., Kwak E., Barlev N.A., Berger S.L., Chow V.T., Roeder R.G., Azorsa D.O., Meltzer P.S., Suh P.-G., Song E.J., Lee K.-J., Lee Y.C., Lee J.W.
    Mol. Cell. Biol. 23:140-149(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
    Tissue: Cervix carcinoma.
  15. "Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs."
    Ko L., Cardona G.R., Iwasaki T., Bramlett K.S., Burris T.P., Chin W.W.
    Mol. Endocrinol. 16:128-140(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 883-THR--GLU-894, PHOSPHORYLATION AT SER-884.
  16. "Coactivator as a target gene specificity determinant for histone H3 lysine 4 methyltransferases."
    Lee S., Lee D.K., Dou Y., Lee J., Lee B., Kwak E., Kong Y.Y., Lee S.K., Roeder R.G., Lee J.W.
    Proc. Natl. Acad. Sci. U.S.A. 103:15392-15397(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
  17. "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex."
    Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T., Dressler G.R., Copeland T.D., Kalkum M., Ge K.
    J. Biol. Chem. 282:20395-20406(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL2/3 COMPLEX.
  18. Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-1060 AND ARG-1191.

Entry informationi

Entry nameiNCOA6_HUMAN
AccessioniPrimary (citable) accession number: Q14686
Secondary accession number(s): A6NLF1
, B2RMN5, E1P5P7, Q9NTZ9, Q9UH74, Q9UK86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 127 of the entry and version 3 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

Miscellaneous

Frequently amplified or overexpressed in colon, breast and lung cancers.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

Similar proteinsi