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Q14686 (NCOA6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. 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 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 names
Name:NCOA6
Synonyms:AIB3, KIAA0181, RAP250, TRBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2063 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.1 Ref.2 Ref.3 Ref.4 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17

Subcellular location

Nucleus.

Tissue specificity

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

Domain

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.

Post-translational modification

Phosphorylated by PRKDC. Ref.4 Ref.15

Phosphorylation on Ser-884 leads to a strong decrease in binding to ESR1 and ESR2.

Miscellaneous

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

Sequence caution

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.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombination

Non-traceable author statement Ref.11. Source: UniProtKB

DNA repair

Non-traceable author statement Ref.11. Source: UniProtKB

DNA replication

Non-traceable author statement Ref.11. Source: UniProtKB

DNA-templated transcription, initiation

Inferred from direct assay Ref.1. Source: UniProtKB

brain development

Inferred from sequence or structural similarity. Source: UniProtKB

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cellular response to DNA damage stimulus

Inferred from direct assay Ref.17. Source: MGI

glucocorticoid receptor signaling pathway

Non-traceable author statement Ref.11. Source: UniProtKB

heart development

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular estrogen receptor signaling pathway

Non-traceable author statement Ref.11. Source: UniProtKB

labyrinthine layer blood vessel development

Inferred from electronic annotation. Source: Ensembl

myeloid cell differentiation

Inferred from direct assay PubMed 11302752. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.11. Source: UniProtKB

positive regulation of transcription, DNA-templated

Traceable author statement PubMed 12519782. Source: UniProtKB

response to hormone

Traceable author statement Ref.11. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componenthistone methyltransferase complex

Inferred from direct assay Ref.17. Source: MGI

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

transcription factor complex

Traceable author statement Ref.11. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.12. Source: UniProtKB

estrogen receptor binding

Traceable author statement Ref.11. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from physical interaction Ref.11. Source: UniProtKB

retinoid X receptor binding

Traceable author statement Ref.11. Source: UniProtKB

thyroid hormone receptor binding

Inferred from direct assay Ref.11. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.1Ref.11. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20632063Nuclear receptor coactivator 6
PRO_0000094413

Regions

Region1 – 13101310NCOA1-binding region
Region1 – 10571057CREBBP-binding region
Region1 – 928928TBP/GTF2A-binding region
Region773 – 927155NCOA6IP-binding region
Region1641 – 2063423EP300/CRSP3-binding region
Motif887 – 8915LXXLL motif 1
Motif1491 – 14955LXXLL motif 2
Compositional bias227 – 1041815Gln-rich
Compositional bias372 – 3776Poly-Pro
Compositional bias913 – 9186Poly-Lys

Amino acid modifications

Modified residue8841Phosphoserine; by MAPK; in vitro
Modified residue13211Phosphothreonine
Modified residue18191N6-acetyllysine By similarity
Modified residue18221N6-acetyllysine By similarity

Natural variations

Natural variant5121P → L.
Corresponds to variant rs6060031 [ dbSNP | Ensembl ].
VAR_027874
Natural variant9551N → S. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5
Corresponds to variant rs17092079 [ dbSNP | Ensembl ].
VAR_027875
Natural variant10601P → S in a breast cancer sample; somatic mutation. Ref.18
VAR_036551
Natural variant11911S → R in a breast cancer sample; somatic mutation. Ref.18
VAR_036552
Natural variant19951I → V.
Corresponds to variant rs6060022 [ dbSNP | Ensembl ].
VAR_027876

Experimental info

Mutagenesis883 – 89412TSPLL…LLQSD → ENPLLVNLLQFI: Reduced binding to THRB, RXRA, ESR2 and ESR1. Ref.15
Mutagenesis883 – 89412TSPLL…LLQSD → NLPLLVNLLQHT: Reduced binding to THRB, RXRA, ESR2 and ESR1. Ref.15
Mutagenesis883 – 89412TSPLL…LLQSD → VNPLLVNLLQFI: Reduced binding to THRB, RXRA, ESR2 and ESR1. Ref.15
Mutagenesis883 – 8842TS → SY: Strong increase in binding to THRB, RXRA and ESR2, but dramatic decrease in binding to ESR1.
Mutagenesis884 – 89411SPLLVNLLQSD → NPLLVNLLQLL: Reduced binding to THRB, RXRA, ESR2 and ESR1.

Sequences

Sequence LengthMass (Da)Tools
Q14686 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 73219502F5138427

FASTA2,063219,145
        10         20         30         40         50         60 
MVLDDLPNLE DIYTSLCSST MEDSEMDFDS GLEDDDTKSD SILEDSTIFV AFKGNIDDKD 

        70         80         90        100        110        120 
FKWKLDAILK NVPNLLHMES SKLKVQKVEP WNSVRVTFNI PREAAERLRI LAQSNNQQLR 

       130        140        150        160        170        180 
DLGILSVQIE GEGAINLALA QNRSQDVRMN GPMGAGNSVR MEAGFPMASG PGIIRMNNPA 

       190        200        210        220        230        240 
TVMIPPGGNV SSSMMAPGPN PELQPRTPRP ASQSDAMDPL LSGLHIQQQS HPSGSLAPPH 

       250        260        270        280        290        300 
HPMQPVSVNR QMNPANFPQL QQQQQQQQQQ QQQQQQQQQQ QQQQQLQARP PQQHQQQQPQ 

       310        320        330        340        350        360 
GIRPQFTAPT QVPVPPGWNQ LPSGALQPPP AQGSLGTMTA NQGWKKAPLP GPMQQQLQAR 

       370        380        390        400        410        420 
PSLATVQTPS HPPPPYPFGS QQASQAHTNF PQMSNPGQFT APQMKSLQGG PSRVPTPLQQ 

       430        440        450        460        470        480 
PHLTNKSPAS SPSSFQQGSP ASSPTVNQTQ QQMGPRPPQN NPLPQGFQQP VSSPGRNPMV 

       490        500        510        520        530        540 
QQGNVPPNFM VMQQQPPNQG PQSLHPGLGG MPKRLPPGFS AGQANPNFMQ GQVPSTTATT 

       550        560        570        580        590        600 
PGNSGAPQLQ ANQNVQHAGG QGAGPPQNQM QVSHGPPNMM QPSLMGIHGN MNNQQAGTSG 

       610        620        630        640        650        660 
VPQVNLSNMQ GQPQQGPPSQ LMGMHQQIVP SQGQMVQQQG TLNPQNPMIL SRAQLMPQGQ 

       670        680        690        700        710        720 
MMVNPPSQNL GPSPQRMTPP KQMLSQQGPQ MMAPHNQMMG PQGQVLLQQN PMIEQIMTNQ 

       730        740        750        760        770        780 
MQGNKQQFNT QNQSNVMPGP AQIMRGPTPN MQGNMVQFTG QMSGQMLPQQ GPVNNSPSQV 

       790        800        810        820        830        840 
MGIQGQVLRP PGPSPHMAQQ HGDPATTANN DVSLSQMMPD VSIQQTNMVP PHVQAMQGNS 

       850        860        870        880        890        900 
ASGNHFSGHG MSFNAPFSGA PNGNQMSCGQ NPGFPVNKDV TLTSPLLVNL LQSDISAGHF 

       910        920        930        940        950        960 
GVNNKQNNTN ANKPKKKKPP RKKKNSQQDL NTPDTRPAGL EEADQPPLPG EQGINLDNSG 

       970        980        990       1000       1010       1020 
PKLPEFSNRP PGYPSQPVEQ RPLQQMPPQL MQHVAPPPQP PQQQPQPQLP QQQQPPPPSQ 

      1030       1040       1050       1060       1070       1080 
PQSQQQQQQQ QQMMMMLMMQ QDPKSVRLPV SQNVHPPRGP LNPDSQRMPM QQSGSVPVMV 

      1090       1100       1110       1120       1130       1140 
SLQGPASVPP SPDKQRMPMP VNTPLGSNSR KMVYQESPQN PSSSPLAEMA SLPEASGSEA 

      1150       1160       1170       1180       1190       1200 
PSVPGGPNNM PSHVVLPQNQ LMMTGPKPGP SPLSATQGAT PQQPPVNSLP SSHGHHFPNV 

      1210       1220       1230       1240       1250       1260 
AAPTQTSRPK TPNRASPRPY YPQTPNNRPP STEPSEISLS PERLNASIAG LFPPQINIPL 

      1270       1280       1290       1300       1310       1320 
PPRPNLNRGF DQQGLNPTTL KAIGQAPSNL TMNPSNFATP QTHKLDSVVV NSGKQSNSGA 

      1330       1340       1350       1360       1370       1380 
TKRASPSNSR RSSPGSSRKT TPSPGRQNSK APKLTLASQT NAALLQNVEL PRNVLVSPTP 

      1390       1400       1410       1420       1430       1440 
LANPPVPGSF PNNSGLNPQN STVSVAAVGG VVEDNKESLN VPQDSDCQNS QSRKEQVNIE 

      1450       1460       1470       1480       1490       1500 
LKAVPAQEVK MVVPEDQSKK DGQPSDPNKL PSVEENKNLV SPAMREAPTS LSQLLDNSGA 

      1510       1520       1530       1540       1550       1560 
PNVTIKPPGL TDLEVTPPVV SGEDLKKASV IPTLQDLSSS KEPSNSLNLP HSNELCSSLV 

      1570       1580       1590       1600       1610       1620 
HPELSEVSSN VAPSIPPVMS RPVSSSSIST PLPPNQITVF VTSNPITTSA NTSAALPTHL 

      1630       1640       1650       1660       1670       1680 
QSALMSTVVT MPNAGSKVMV SEGQSAAQSN ARPQFITPVF INSSSIIQVM KGSQPSTIPA 

      1690       1700       1710       1720       1730       1740 
APLTTNSGLM PPSVAVVGPL HIPQNIKFSS APVPPNALSS SPAPNIQTGR PLVLSSRATP 

      1750       1760       1770       1780       1790       1800 
VQLPSPPCTS SPVVPSHPPV QQVKELNPDE ASPQVNTSAD QNTLPSSQST TMVSPLLTNS 

      1810       1820       1830       1840       1850       1860 
PGSSGNRRSP VSSSKGKGKV DKIGQILLTK ACKKVTGSLE KGEEQYGADG ETEGQGLDTT 

      1870       1880       1890       1900       1910       1920 
APGLMGTEQL STELDSKTPT PPAPTLLKMT SSPVGPGTAS AGPSLPGGAL PTSVRSIVTT 

      1930       1940       1950       1960       1970       1980 
LVPSELISAV PTTKSNHGGI ASESLAGGLV EEKVGSHPEL LPSIAPSQNL VSKETSTTAL 

      1990       2000       2010       2020       2030       2040 
QASVARPELE VNAAIVSGQS SEPKEIVEKS KIPGRRNSRT EEPTVASESV ENGHRKRSSR 

      2050       2060 
PASASSSTKD ITSAVQSKRR KSK 

« Hide

References

« Hide 'large scale' references
[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. 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].
[8]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].
[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.
[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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-1060 AND ARG-1191.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001229468.1. NM_001242539.1.
NP_054790.2. NM_014071.3.
XP_005260405.1. XM_005260348.2.
UniGeneHs.368971.
Hs.736403.

3D structure databases

ProteinModelPortalQ14686.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116691. 78 interactions.
DIPDIP-30934N.
IntActQ14686. 31 interactions.
MINTMINT-1194462.
STRING9606.ENSP00000351894.

PTM databases

PhosphoSiteQ14686.

Polymorphism databases

DMDM116242672.

Proteomic databases

PaxDbQ14686.
PRIDEQ14686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359003; ENSP00000351894; ENSG00000198646.
ENST00000374796; ENSP00000363929; ENSG00000198646.
GeneID23054.
KEGGhsa:23054.
UCSCuc002xav.3. human.

Organism-specific databases

CTD23054.
GeneCardsGC20M033302.
H-InvDBHIX0015752.
HGNCHGNC:15936. NCOA6.
HPAHPA004198.
MIM605299. gene.
neXtProtNX_Q14686.
PharmGKBPA31475.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG052586.
InParanoidQ14686.
KOK14971.
OMANARPQFI.
OrthoDBEOG7W9RSX.
PhylomeDBQ14686.
TreeFamTF332639.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeQ14686.
CleanExHS_NCOA6.
GenevestigatorQ14686.

Family and domain databases

InterProIPR026638. NCOA6.
[Graphical view]
PANTHERPTHR15690. PTHR15690. 1 hit.
ProtoNetSearch...

Other

ChiTaRSNCOA6. human.
GeneWikiNCOA6.
GenomeRNAi23054.
NextBio44111.
PROQ14686.
SOURCESearch...

Entry information

Entry nameNCOA6_HUMAN
AccessionPrimary (citable) accession number: Q14686
Secondary accession number(s): A6NLF1 expand/collapse secondary AC list , B2RMN5, E1P5P7, Q9NTZ9, Q9UH74, Q9UK86
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 123 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

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 20

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