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Q15596 (NCOA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 2

Short name=NCoA-2
Alternative name(s):
Class E basic helix-loop-helix protein 75
Short name=bHLHe75
Transcriptional intermediary factor 2
Short name=hTIF2
Gene names
Name:NCOA2
Synonyms:BHLHE75, SRC2, TIF2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional coactivator for steroid receptors and nuclear receptors. Coactivator of the steroid binding domain (AF-2) but not of the modulating N-terminal domain (AF-1). Required with NCOA1 to control energy balance between white and brown adipose tissues. Critical regulator of glucose metabolism regulation, acts as RORA coactivator to specifically modulate G6PC expression. Ref.4

Subunit structure

Present in a complex containing NCOA3, IKKA, IKKB, IKBKG and CREBBP. Interacts (via C-terminus) with CREBBP. Interacts with ESR1, HIF1A, NCOA1, APEX, NR3C1, NR3C2, CARM1, RARA, and RXRA. Present in a complex containing CARM1 and EP300/P300. Interacts with CASP8AP2 and TTLL5/STAMP. Interacts with PSMB9 and DDX5. Interacts (via LXXLL 1, 2 and 3 motifs) with RORA and RORC (via AF-2 motif). Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.14

Subcellular location

Nucleus.

Domain

Contains four Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The LXXLL motifs are essential for the association with nuclear receptors and are, at least in part, functionally redundant. Ref.4

The LLXXLXXXL motif is involved in transcriptional coactivation and CREBBP/CBP binding. Ref.4

Contains 2 C-terminal transcription activation domains (AD1 and AD2) that can function independently. Ref.4

Involvement in disease

Chromosomal aberrations involving NCOA2 may be a cause of acute myeloid leukemias. Inversion inv8(p11;q13) generates the KAT6A-NCOA2 oncogene, which consists of the N-terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription activation.

Sequence similarities

Belongs to the SRC/p160 nuclear receptor coactivator family.

Contains 1 bHLH (basic helix-loop-helix) domain.

Contains 1 PAS (PER-ARNT-SIM) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular lipid metabolic process

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

histone acetyltransferase activity

Inferred from electronic annotation. Source: InterPro

ligand-dependent nuclear receptor binding

Inferred from physical interaction PubMed 18798693. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from direct assay PubMed 17363140. Source: BHF-UCL

nuclear hormone receptor binding

Inferred from physical interaction Ref.6. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8PubMed 11265755PubMed 15563469. Source: IntAct

signal transducer activity

Inferred from electronic annotation. Source: InterPro

thyroid hormone receptor coactivator activity

Inferred from electronic annotation. Source: Ensembl

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17
Chain2 – 14641463Nuclear receptor coactivator 2
PRO_0000094402

Regions

Domain26 – 8358bHLH
Domain119 – 18365PAS
Region691 – 74353CASP8AP2-binding By similarity
Motif641 – 6455LXXLL motif 1
Motif690 – 6945LXXLL motif 2
Motif745 – 7495LXXLL motif 3
Motif878 – 8825LXXLL motif 4
Motif1079 – 10879LLXXLXXXL motif
Compositional bias1254 – 12607Poly-Gln

Sites

Site869 – 8702Breakpoint for translocation to form KAT6A-NCOA2

Amino acid modifications

Modified residue21N-acetylserine Ref.17
Modified residue4871Phosphoserine Ref.20
Modified residue4931Phosphoserine Ref.20
Modified residue4991Phosphoserine Ref.20
Modified residue6361N6-acetyllysine By similarity
Modified residue6401N6-acetyllysine Ref.19
Modified residue6991Phosphoserine By similarity
Modified residue7711Phosphoserine By similarity
Modified residue7801N6-acetyllysine Ref.19
Modified residue7851N6-acetyllysine Ref.19
Modified residue8511Phosphoserine Ref.20
Modified residue8541Phosphothreonine Ref.20

Natural variations

Natural variant12821M → I. Ref.2
Corresponds to variant rs2228591 [ dbSNP | Ensembl ].
VAR_024546

Experimental info

Mutagenesis644 – 6452LL → AA: By itself, does not affect nuclear receptor binding or transcriptional coactivation. Abrogates ligand-induced nuclear receptor binding and transactivation; when associated with 693-A-A-694 and 748-A-A-749.
Mutagenesis693 – 6942LL → AA: By itself, does not affect nuclear receptor binding or transcriptional coactivation. Abrogates ligand-induced nuclear receptor binding and transactivation; when associated with 644-A-A-665 and 748-A-A-749.
Mutagenesis748 – 7492LL → AA: By itself, does not affect nuclear receptor binding or transcriptional coactivation. Abrogates ligand-induced nuclear receptor binding and transactivation; when associated with 644-A-A-665 and 693-A-A-694.
Mutagenesis1079 – 10835LLDQL → AADQA: Reduces transcriptional coactivation and disrupts interaction with CREBBP/CBP. Ref.4
Mutagenesis1081 – 10822DQ → AA: Has little effect on transcriptional coactivation.

Secondary structure

....... 1464
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15596 [UniParc].

Last modified May 1, 1997. Version 2.
Checksum: 0A61AA5D1878304B

FASTA1,464159,157
        10         20         30         40         50         60 
MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRNTEKRNRE QENKYIEELA ELIFANFNDI 

        70         80         90        100        110        120 
DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS DVSSTGQGVI DKDALGPMML 

       130        140        150        160        170        180 
EALDGFFFVV NLEGNVVFVS ENVTQYLRYN QEELMNKSVY SILHVGDHTE FVKNLLPKSI 

       190        200        210        220        230        240 
VNGGSWSGEP PRRNSHTFNC RMLVKPLPDS EEEGHDNQEA HQKYETMQCF AVSQPKSIKE 

       250        260        270        280        290        300 
EGEDLQSCLI CVARRVPMKE RPVLPSSESF TTRQDLQGKI TSLDTSTMRA AMKPGWEDLV 

       310        320        330        340        350        360 
RRCIQKFHAQ HEGESVSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ TKSKLIRSQT 

       370        380        390        400        410        420 
TNEPQLVISL HMLHREQNVC VMNPDLTGQT MGKPLNPISS NSPAHQALCS GNPGQDMTLS 

       430        440        450        460        470        480 
SNINFPINGP KEQMGMPMGR FGGSGGMNHV SGMQATTPQG SNYALKMNSP SQSSPGMNPG 

       490        500        510        520        530        540 
QPTSMLSPRH RMSPGVAGSP RIPPSQFSPA GSLHSPVGVC SSTGNSHSYT NSSLNALQAL 

       550        560        570        580        590        600 
SEGHGVSLGS SLASPDLKMG NLQNSPVNMN PPPLSKMGSL DSKDCFGLYG EPSEGTTGQA 

       610        620        630        640        650        660 
ESSCHPGEQK ETNDPNLPPA VSSERADGQS RLHDSKGQTK LLQLLTTKSD QMEPSPLASS 

       670        680        690        700        710        720 
LSDTNKDSTG SLPGSGSTHG TSLKEKHKIL HRLLQDSSSP VDLAKLTAEA TGKDLSQESS 

       730        740        750        760        770        780 
STAPGSEVTI KQEPVSPKKK ENALLRYLLD KDDTKDIGLP EITPKLERLD SKTDPASNTK 

       790        800        810        820        830        840 
LIAMKTEKEE MSFEPGDQPG SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP AGSVDKQAII 

       850        860        870        880        890        900 
NDLMQLTAEN SPVTPVGAQK TALRISQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG 

       910        920        930        940        950        960 
PFPPIRNSSP YSVIPQPGMM GNQGMIGNQG NLGNSSTGMI GNSASRPTMP SGEWAPQSSA 

       970        980        990       1000       1010       1020 
VRVTCAATTS AMNRPVQGGM IRNPAASIPM RPSSQPGQRQ TLQSQVMNIG PSELEMNMGG 

      1030       1040       1050       1060       1070       1080 
PQYSQQQAPP NQTAPWPESI LPIDQASFAS QNRQPFGSSP DDLLCPHPAA ESPSDEGALL 

      1090       1100       1110       1120       1130       1140 
DQLYLALRNF DGLEEIDRAL GIPELVSQSQ AVDPEQFSSQ DSNIMLEQKA PVFPQQYASQ 

      1150       1160       1170       1180       1190       1200 
AQMAQGSYSP MQDPNFHTMG QRPSYATLRM QPRPGLRPTG LVQNQPNQLR LQLQHRLQAQ 

      1210       1220       1230       1240       1250       1260 
QNRQPLMNQI SNVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR QMHQQQQVQQ 

      1270       1280       1290       1300       1310       1320 
RTLMMRGQGL NMTPSMVAPS GMPATMSNPR IPQANAQQFP FPPNYGISQQ PDPGFTGATT 

      1330       1340       1350       1360       1370       1380 
PQSPLMSPRM AHTQSPMMQQ SQANPAYQAP SDINGWAQGN MGGNSMFSQQ SPPHFGQQAN 

      1390       1400       1410       1420       1430       1440 
TSMYSNNMNI NVSMATNTGG MSSMNQMTGQ ISMTSVTSVP TSGLSSMGPE QVNDPALRGG 

      1450       1460 
NLFPNQLPGM DMIKQEGDTT RKYC 

« Hide

References

« Hide 'large scale' references
[1]"TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors."
Voegel J.J., Heine M.J.S., Zechel C., Chambon P., Gronemeyer H.
EMBO J. 15:3667-3675(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"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], VARIANT ILE-1282.
[3]"A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia."
Carapeti M., Aguiar R.C.T., Goldman J.M., Cross N.C.P.
Blood 91:3127-3133(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 870-939, CHROMOSOMAL TRANSLOCATION WITH KAT6A.
[4]"The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways."
Voegel J.J., Heine M.J.S., Tini M., Vivat V., Chambon P., Gronemeyer H.
EMBO J. 17:507-519(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CREBBP; ESR1; RARA AND RXRA, DOMAIN, MUTAGENESIS OF 644-LEU-LEU-645; 693-LEU-LEU-694; 748-LEU-LEU-749; 1079-LEU--LEU-1083 AND 1081-ASP-GLN-1082.
[5]"Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex."
Fryer C.J., Archer T.K.
Nature 393:88-91(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR3C1.
[6]"Coactivators for the orphan nuclear receptor RORalpha."
Atkins G.B., Hu X., Guenther M.G., Rachez C., Freedman L.P., Lazar M.A.
Mol. Endocrinol. 13:1550-1557(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RORA.
[7]"Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha."
Carrero P., Okamoto K., Coumailleau P., O'Brien S., Tanaka H., Poellinger L.
Mol. Cell. Biol. 20:402-415(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIF1A; NCOA1 AND APEX.
[8]"A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor alpha coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA."
Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S., Arao Y., Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y., Kato S.
EMBO J. 20:1341-1352(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX5.
[9]"Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase."
Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J., O'Malley B.W.
Mol. Cell. Biol. 22:3549-3561(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COACTIVATOR COMPLEX CONTAINING CREBBP; NCOA3; IKKA; IKKB AND IKBKG.
[10]"MOZ-TIF2-induced acute myeloid leukemia requires the MOZ nucleosome binding motif and TIF2-mediated recruitment of CBP."
Deguchi K., Ayton P.M., Carapeti M., Kutok J.L., Snyder C.S., Williams I.R., Cross N.C.P., Glass C.K., Cleary M.L., Gilliland D.G.
Cancer Cell 3:259-271(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH KAT6A.
[11]"MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by impairment of CBP function."
Kindle K.B., Troke P.J.F., Collins H.M., Matsuda S., Bossi D., Bellodi C., Kalkhoven E., Salomoni P., Pelicci P.G., Minucci S., Heery D.M.
Mol. Cell. Biol. 25:988-1002(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH KAT6A.
[12]"The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription."
Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R., Sun X., Shang Y.
EMBO J. 25:4223-4233(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSMB9.
[13]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"STAMP, a novel predicted factor assisting TIF2 actions in glucocorticoid receptor-mediated induction and repression."
He Y., Simons S.S. Jr.
Mol. Cell. Biol. 27:1467-1485(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TTLL5.
Tissue: Testis.
[15]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[18]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-640; LYS-780 AND LYS-785, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487; SER-493; SER-499; SER-851 AND THR-854, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X97674 mRNA. Translation: CAA66263.1.
BC114383 mRNA. Translation: AAI14384.1.
CCDSCCDS47872.1.
RefSeqNP_006531.1. NM_006540.2.
XP_005251185.1. XM_005251128.2.
XP_005251186.1. XM_005251129.2.
XP_005251187.1. XM_005251130.2.
XP_005251188.1. XM_005251131.2.
XP_005251189.1. XM_005251132.2.
UniGeneHs.446678.
Hs.595378.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GWQX-ray2.45C/D688-696[»]
1GWRX-ray2.40C/D742-750[»]
1M2ZX-ray2.50B/E734-754[»]
1MV9X-ray1.90B686-698[»]
1MVCX-ray1.90B686-698[»]
1MZNX-ray1.90B/D/F/H686-698[»]
1P93X-ray2.70E/F/G/H740-751[»]
1T63X-ray2.07B740-753[»]
1T65X-ray1.66B686-698[»]
1UHLX-ray2.90C/D687-696[»]
1YOKX-ray2.50B/C740-753[»]
1ZDTX-ray2.10P/Q741-752[»]
1ZDUX-ray2.50P/Q741-751[»]
1ZKYX-ray2.25C/D686-698[»]
2AO6X-ray1.89B740-753[»]
2B1VX-ray1.80C/D686-698[»]
2B1ZX-ray1.78C/D686-698[»]
2B23X-ray2.10C/D686-698[»]
2FAIX-ray2.10C/D686-698[»]
2G44X-ray2.65C/D686-698[»]
2G5OX-ray2.30C/D686-698[»]
2P15X-ray1.94C/D686-698[»]
2P1TX-ray1.80B686-698[»]
2P1UX-ray2.20B686-698[»]
2P1VX-ray2.20B686-698[»]
2Q7JX-ray1.90B740-753[»]
2Q7LX-ray1.92B740-753[»]
2ZXZX-ray3.00B686-698[»]
2ZY0X-ray2.90B/D686-698[»]
3A9EX-ray2.75I686-698[»]
3CLDX-ray2.84C/H740-751[»]
3DZUX-ray3.20E/G685-697[»]
3DZYX-ray3.10E/G685-697[»]
3E00X-ray3.10E/G685-697[»]
3E7CX-ray2.15D/H741-751[»]
3E94X-ray1.90B686-698[»]
3ERDX-ray2.03C/D686-698[»]
3FUGX-ray2.00B686-698[»]
3GN8X-ray2.50C/E734-754[»]
3K22X-ray2.10D/H740-751[»]
3K23X-ray3.00D/E/F740-751[»]
3KWYX-ray2.30B686-698[»]
3KYTX-ray2.35C686-697[»]
3L0EX-ray2.30B740-751[»]
3L0JX-ray2.40C688-697[»]
3L0LX-ray1.74C/E685-697[»]
3O1DX-ray2.40B686-698[»]
3O1EX-ray2.50B686-698[»]
3OAPX-ray2.05B686-696[»]
3OZJX-ray2.10B/D686-696[»]
3PCUX-ray2.00B687-696[»]
3PLZX-ray1.75C/D740-753[»]
3Q95X-ray2.05C/D686-698[»]
3Q97X-ray2.10C/D686-698[»]
3R5MX-ray2.80B/D687-696[»]
3UP0X-ray1.60P/Q740-753[»]
3UP3X-ray1.25P741-754[»]
4CSJX-ray2.30B741-753[»]
4DOSX-ray2.00B/C740-753[»]
4E2JX-ray2.50C/E741-752[»]
4FHHX-ray2.33B686-698[»]
4FHIX-ray2.40B686-698[»]
4IA1X-ray2.44B686-698[»]
4IA2X-ray2.95B686-698[»]
4IA3X-ray2.70B686-698[»]
4IA7X-ray2.70B686-698[»]
4IQRX-ray2.90I/J/K/L685-697[»]
4IU7X-ray2.29C/D687-696[»]
4IUIX-ray2.30C/D687-696[»]
4IV2X-ray2.14C/D687-696[»]
4IV4X-ray2.30C/D687-696[»]
4IVWX-ray2.06C/D687-696[»]
4IVYX-ray1.95C/D687-696[»]
4IW6X-ray1.98C/D687-696[»]
4IW8X-ray2.04C/D687-696[»]
4IWCX-ray2.24C/D687-696[»]
4IWFX-ray1.93C/D687-696[»]
4K4JX-ray2.00B686-698[»]
4K6IX-ray2.10B686-698[»]
4M8EX-ray2.40B686-696[»]
4M8HX-ray2.20B686-696[»]
4NIEX-ray2.01C/D686-697[»]
4NQAX-ray3.10C/D/J/K686-698[»]
4P6WX-ray1.95B741-752[»]
4P6XX-ray2.50B/D/F/H/J/L740-753[»]
4PP6X-ray2.20C/D688-696[»]
4PPPX-ray2.69C/D688-696[»]
4PPSX-ray1.93C/D687-698[»]
ProteinModelPortalQ15596.
SMRQ15596. Positions 30-376, 1071-1115.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115761. 60 interactions.
DIPDIP-5997N.
IntActQ15596. 12 interactions.
MINTMINT-122867.
STRING9606.ENSP00000399968.

Chemistry

ChEMBLCHEMBL2095163.

PTM databases

PhosphoSiteQ15596.

Polymorphism databases

DMDM13626594.

Proteomic databases

MaxQBQ15596.
PaxDbQ15596.
PRIDEQ15596.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000452400; ENSP00000399968; ENSG00000140396.
GeneID10499.
KEGGhsa:10499.
UCSCuc003xyn.1. human.

Organism-specific databases

CTD10499.
GeneCardsGC08M071016.
HGNCHGNC:7669. NCOA2.
MIM601993. gene.
neXtProtNX_Q15596.
PharmGKBPA31471.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG315556.
HOGENOMHOG000230947.
HOVERGENHBG052583.
InParanoidQ15596.
KOK11255.
OMATGMIGSN.
OrthoDBEOG72JWFB.
PhylomeDBQ15596.
TreeFamTF332652.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111217. Metabolism.
SignaLinkQ15596.

Gene expression databases

ArrayExpressQ15596.
BgeeQ15596.
CleanExHS_NCOA2.
GenevestigatorQ15596.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProIPR011598. bHLH_dom.
IPR010011. DUF1518.
IPR028822. NCOA2.
IPR009110. Nuc_rcpt_coact.
IPR014920. Nuc_rcpt_coact_Ncoa-typ.
IPR017426. Nuclear_rcpt_coactivator.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR014935. SRC-1.
IPR008955. Src1_rcpt_coact.
[Graphical view]
PANTHERPTHR10684. PTHR10684. 1 hit.
PTHR10684:SF2. PTHR10684:SF2. 1 hit.
PfamPF07469. DUF1518. 1 hit.
PF08815. Nuc_rec_co-act. 1 hit.
PF00989. PAS. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view]
PIRSFPIRSF038181. Nuclear_receptor_coactivator. 1 hit.
SMARTSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNCOA2. human.
EvolutionaryTraceQ15596.
GeneWikiNuclear_receptor_coactivator_2.
GenomeRNAi10499.
NextBio39840.
PROQ15596.
SOURCESearch...

Entry information

Entry nameNCOA2_HUMAN
AccessionPrimary (citable) accession number: Q15596
Secondary accession number(s): Q14CD2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 160 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 8

Human chromosome 8: entries, gene names and cross-references to MIM