Reviewed, UniProtKB/Swiss-Prot Q14686 (NCOA6_HUMAN)

Names and origin

Protein names

Recommended name:
    Nuclear receptor coactivator 6
Alternative name(s):
    Amplified in breast cancer protein 3
    Cancer-amplified transcriptional coactivator ASC-2
    Activating signal cointegrator 2
      Short name=ASC-2
    Peroxisome proliferator-activated receptor-interacting protein
      Short name=PPAR-interacting protein
      Short name=PRIP
    Nuclear receptor-activating protein, 250 kDa
    Nuclear receptor coactivator RAP250
      Short name=NRC RAP250
    Thyroid hormone receptor-binding protein

Gene names

Name:	NCOA6
Synonyms:	AIB3, KIAA0181, RAP250, TRBP

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	2063 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 MLL3/MLL4 complex, at least composed of MLL3, MLL4, ASH2L, RBBP5, DPY30, WDR5, NCOA6, UTX, PAXIP1/PTIP and C16orf53/PA1. Some fraction of the complex contains MLL2 instead of MLL4 and is named MLL2/MLL3 complex. Interacts with ZNF335.
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. 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
Molecular function	Activator
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	DNA recombination Ref.10 Non-traceable author statement. Source: UniProtKB DNA repair Ref.10 Non-traceable author statement. Source: UniProtKB DNA replication Ref.10 Non-traceable author statement. Source: UniProtKB brain development Inferred from sequence or structural similarity. Source: UniProtKB estrogen receptor signaling pathway Ref.10 Non-traceable author statement. Source: UniProtKB glucocorticoid receptor signaling pathway Ref.10 Non-traceable author statement. Source: UniProtKB heart development Inferred from sequence or structural similarity. Source: UniProtKB in utero embryonic development Inferred from sequence or structural similarity. Source: UniProtKB myeloid cell differentiation Inferred from direct assay. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Ref.10 Inferred from direct assay. Source: UniProtKB response to hormone stimulus Ref.10 Traceable author statement. Source: UniProtKB transcription initiation from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	transcription factor complex Ref.10 Traceable author statement. Source: UniProtKB
Molecular function	chromatin binding Inferred from sequence or structural similarity. Source: UniProtKB estrogen receptor binding Ref.10 Traceable author statement. Source: UniProtKB ligand-dependent nuclear receptor transcription coactivator activity Ref.10 Inferred from physical interaction. Source: UniProtKB retinoid X receptor binding Ref.10 Traceable author statement. Source: UniProtKB thyroid hormone receptor binding Ref.10 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AR	P10275	1	EBI-78670,EBI-608057
CREBBP	Q92793	1	EBI-78670,EBI-81215
PRMT2	P55345	1	EBI-78670,EBI-78458
RB1	P06400	2	EBI-78670,EBI-491274

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2063	2063	Nuclear receptor coactivator 6		PRO_0000094413
Regions
	Region	1 – 1310	1310	NCOA1-binding region
	Region	1 – 1057	1057	CREBBP-binding region
	Region	1 – 928	928	TBP/GTF2A-binding region
	Region	773 – 927	155	NCOA6IP-binding region
	Region	1641 – 2063	423	EP300/CRSP3-binding region
	Motif	887 – 891	5	LXXLL motif 1
	Motif	1491 – 1495	5	LXXLL motif 2
	Compositional bias	227 – 1041	815	Gln-rich
	Compositional bias	372 – 377	6	Poly-Pro
	Compositional bias	913 – 918	6	Poly-Lys
Amino acid modifications
	Modified residue	884	1	Phosphoserine; by MAPK; in vitro
	Modified residue	1321	1	Phosphothreonine
Natural variations
	Natural variant	512	1	P → L: dbSNP rs6060031.		VAR_027874
	Natural variant	955	1	N → S: dbSNP rs17092079.		VAR_027875
	Natural variant	1060	1	P → S in a breast cancer sample; somatic mutation.		VAR_036551
	Natural variant	1191	1	S → R in a breast cancer sample; somatic mutation.		VAR_036552
	Natural variant	1995	1	I → V: dbSNP rs6060022.		VAR_027876
Experimental info
	Mutagenesis	883 – 894	12	TSPLL…LLQSD → ENPLLVNLLQFI: Reduced binding to THRB, RXRA, ESR2 and ESR1
	Mutagenesis	883 – 894	12	TSPLL…LLQSD → NLPLLVNLLQHT: Reduced binding to THRB, RXRA, ESR2 and ESR1
	Mutagenesis	883 – 894	12	TSPLL…LLQSD → SYPLLVNLLQSD: Strong increase in binding to THRB, RXRA and ESR2, but dramatic decrease in binding to ESR1
	Mutagenesis	883 – 894	12	TSPLL…LLQSD → TNPLLVNLLQLL: Reduced binding to THRB, RXRA, ESR2 and ESR1
	Mutagenesis	883 – 894	12	TSPLL…LLQSD → VNPLLVNLLQFI: Reduced binding to THRB, RXRA, ESR2 and ESR1

Sequences

	Sequence		Length	Mass (Da)
	Q14686-1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 73219502F5138427	FASTA	2,063	219,145
	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

References

	« Hide 'large scale' referencesShow '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: 10567404] [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: 10866662] [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: 10681503] [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: 10823961] [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: 8724849] [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: 12168954] [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: 11780052] [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. , 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]	"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: 11517327] [Abstract] Cited for: INTERACTION WITH NCOA6IP.
[10]	"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: 11443112] [Abstract] Cited for: INTERACTION WITH RBM14.
[11]	"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: 12039952] [Abstract] Cited for: INTERACTION WITH PRMT2.
[12]	"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: 12215545] [Abstract] Cited for: INTERACTION WITH ZNF335.
[13]	"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: 12482968] [Abstract] Cited for: INTERACTION WITH MLL3 AND THE MLL3/MLL4 COMPLEX. Tissue: Cervix carcinoma.
[14]	"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: 11773444] [Abstract] Cited for: MUTAGENESIS OF 883-THR--GLU-894, PHOSPHORYLATION.
[15]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1321, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"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: 17500065] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL3/MLL4 COMPLEX.
[17]	"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. , 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: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-1060 AND ARG-1191.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
RefSeq	NP_054790.2.
UniGene	Hs.368971
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14686.
PTM databases
PhosphoSite	Q14686.
Genome annotation databases
Ensembl	ENSG00000198646. Homo sapiens. [Contig view]
GeneID	23054.
KEGG	hsa:23054.
Organism-specific databases
H-InvDB	HIX0015752.
HGNC	HGNC:15936. NCOA6.
HPA	HPA004198.
MIM	605299. gene.
PharmGKB	PA31475.
HUGE	Search...
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q14686.
HOVERGEN	Q14686.
Gene expression databases
CleanEx	HS_NCOA6.
GermOnline	ENSG00000198646. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other Resources
LinkHub	Q14686.
NextBio	44111.
SOURCE	Search...