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Q15596

- NCOA2_HUMAN

UniProt

Q15596 - NCOA2_HUMAN

Protein

Nuclear receptor coactivator 2

Gene

NCOA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 2 (01 May 1997)
      Previous versions | rss
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    Functioni

    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. Involved in the positive regulation of the transcriptional activity of the glucocorticoid receptor NR3C1 by sumoylation enhancer RWDD3.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei869 – 8702Breakpoint for translocation to form KAT6A-NCOA2

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. histone acetyltransferase activity Source: InterPro
    3. ligand-dependent nuclear receptor binding Source: UniProtKB
    4. ligand-dependent nuclear receptor transcription coactivator activity Source: BHF-UCL
    5. nuclear hormone receptor binding Source: UniProtKB
    6. protein binding Source: IntAct
    7. signal transducer activity Source: InterPro
    8. thyroid hormone receptor coactivator activity Source: Ensembl
    9. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    3. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    4. regulation of transcription, DNA-templated Source: UniProtKB
    5. small molecule metabolic process Source: Reactome
    6. transcription, DNA-templated Source: UniProtKB-KW

    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.
    SignaLinkiQ15596.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:NCOA2
    Synonyms:BHLHE75, SRC2, TIF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:7669. NCOA2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi644 – 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. 1 Publication
    Mutagenesisi693 – 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. 1 Publication
    Mutagenesisi748 – 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. 1 Publication
    Mutagenesisi1079 – 10835LLDQL → AADQA: Reduces transcriptional coactivation and disrupts interaction with CREBBP/CBP. 1 Publication
    Mutagenesisi1081 – 10822DQ → AA: Has little effect on transcriptional coactivation. 1 Publication

    Organism-specific databases

    PharmGKBiPA31471.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 14641463Nuclear receptor coactivator 2PRO_0000094402Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei487 – 4871Phosphoserine1 Publication
    Modified residuei493 – 4931Phosphoserine1 Publication
    Modified residuei499 – 4991Phosphoserine1 Publication
    Modified residuei636 – 6361N6-acetyllysineBy similarity
    Modified residuei640 – 6401N6-acetyllysine1 Publication
    Modified residuei699 – 6991PhosphoserineBy similarity
    Modified residuei771 – 7711PhosphoserineBy similarity
    Modified residuei780 – 7801N6-acetyllysine1 Publication
    Modified residuei785 – 7851N6-acetyllysine1 Publication
    Modified residuei851 – 8511Phosphoserine1 Publication
    Modified residuei854 – 8541Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15596.
    PaxDbiQ15596.
    PRIDEiQ15596.

    PTM databases

    PhosphoSiteiQ15596.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15596.
    BgeeiQ15596.
    CleanExiHS_NCOA2.
    GenevestigatoriQ15596.

    Interactioni

    Subunit structurei

    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). Interacts with RWDD3.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP102752EBI-81236,EBI-608057
    DDX17Q928412EBI-81236,EBI-746012
    ESR1P033728EBI-81236,EBI-78473

    Protein-protein interaction databases

    BioGridi115761. 60 interactions.
    DIPiDIP-5997N.
    IntActiQ15596. 12 interactions.
    MINTiMINT-122867.
    STRINGi9606.ENSP00000399968.

    Structurei

    Secondary structure

    1
    1464
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi688 – 6947
    Beta strandi739 – 7413
    Helixi743 – 7508

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    4POHX-ray2.30B686-698[»]
    4POJX-ray2.00B686-698[»]
    4PP3X-ray2.00B686-698[»]
    4PP5X-ray2.00B686-698[»]
    4PP6X-ray2.20C/D688-696[»]
    4PPPX-ray2.69C/D688-696[»]
    4PPSX-ray1.93C/D687-698[»]
    ProteinModelPortaliQ15596.
    SMRiQ15596. Positions 30-376, 1071-1115.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15596.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 8358bHLHPROSITE-ProRule annotationAdd
    BLAST
    Domaini119 – 18365PASPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni691 – 74353CASP8AP2-bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi641 – 6455LXXLL motif 1
    Motifi690 – 6945LXXLL motif 2
    Motifi745 – 7495LXXLL motif 3
    Motifi878 – 8825LXXLL motif 4
    Motifi1079 – 10879LLXXLXXXL motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1254 – 12607Poly-Gln

    Domaini

    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.1 Publication
    The LLXXLXXXL motif is involved in transcriptional coactivation and CREBBP/CBP binding.1 Publication
    Contains 2 C-terminal transcription activation domains (AD1 and AD2) that can function independently.1 Publication

    Sequence similaritiesi

    Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation
    Contains 1 PAS (PER-ARNT-SIM) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG315556.
    HOGENOMiHOG000230947.
    HOVERGENiHBG052583.
    InParanoidiQ15596.
    KOiK11255.
    OMAiTGMIGSN.
    OrthoDBiEOG72JWFB.
    PhylomeDBiQ15596.
    TreeFamiTF332652.

    Family and domain databases

    Gene3Di4.10.280.10. 1 hit.
    4.10.630.10. 2 hits.
    InterProiIPR011598. 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]
    PANTHERiPTHR10684. PTHR10684. 1 hit.
    PTHR10684:SF2. PTHR10684:SF2. 1 hit.
    PfamiPF07469. DUF1518. 1 hit.
    PF08815. Nuc_rec_co-act. 1 hit.
    PF00989. PAS. 1 hit.
    PF08832. SRC-1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038181. Nuclear_receptor_coactivator. 1 hit.
    SMARTiSM00353. HLH. 1 hit.
    SM00086. PAC. 1 hit.
    SM00091. PAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF47459. SSF47459. 1 hit.
    SSF55785. SSF55785. 2 hits.
    SSF69125. SSF69125. 1 hit.
    PROSITEiPS50888. BHLH. 1 hit.
    PS50112. PAS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q15596-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRNTEKRNRE QENKYIEELA     50
    ELIFANFNDI DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS 100
    DVSSTGQGVI DKDALGPMML EALDGFFFVV NLEGNVVFVS ENVTQYLRYN 150
    QEELMNKSVY SILHVGDHTE FVKNLLPKSI VNGGSWSGEP PRRNSHTFNC 200
    RMLVKPLPDS EEEGHDNQEA HQKYETMQCF AVSQPKSIKE EGEDLQSCLI 250
    CVARRVPMKE RPVLPSSESF TTRQDLQGKI TSLDTSTMRA AMKPGWEDLV 300
    RRCIQKFHAQ HEGESVSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ 350
    TKSKLIRSQT TNEPQLVISL HMLHREQNVC VMNPDLTGQT MGKPLNPISS 400
    NSPAHQALCS GNPGQDMTLS SNINFPINGP KEQMGMPMGR FGGSGGMNHV 450
    SGMQATTPQG SNYALKMNSP SQSSPGMNPG QPTSMLSPRH RMSPGVAGSP 500
    RIPPSQFSPA GSLHSPVGVC SSTGNSHSYT NSSLNALQAL SEGHGVSLGS 550
    SLASPDLKMG NLQNSPVNMN PPPLSKMGSL DSKDCFGLYG EPSEGTTGQA 600
    ESSCHPGEQK ETNDPNLPPA VSSERADGQS RLHDSKGQTK LLQLLTTKSD 650
    QMEPSPLASS LSDTNKDSTG SLPGSGSTHG TSLKEKHKIL HRLLQDSSSP 700
    VDLAKLTAEA TGKDLSQESS STAPGSEVTI KQEPVSPKKK ENALLRYLLD 750
    KDDTKDIGLP EITPKLERLD SKTDPASNTK LIAMKTEKEE MSFEPGDQPG 800
    SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP AGSVDKQAII NDLMQLTAEN 850
    SPVTPVGAQK TALRISQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG 900
    PFPPIRNSSP YSVIPQPGMM GNQGMIGNQG NLGNSSTGMI GNSASRPTMP 950
    SGEWAPQSSA VRVTCAATTS AMNRPVQGGM IRNPAASIPM RPSSQPGQRQ 1000
    TLQSQVMNIG PSELEMNMGG PQYSQQQAPP NQTAPWPESI LPIDQASFAS 1050
    QNRQPFGSSP DDLLCPHPAA ESPSDEGALL DQLYLALRNF DGLEEIDRAL 1100
    GIPELVSQSQ AVDPEQFSSQ DSNIMLEQKA PVFPQQYASQ AQMAQGSYSP 1150
    MQDPNFHTMG QRPSYATLRM QPRPGLRPTG LVQNQPNQLR LQLQHRLQAQ 1200
    QNRQPLMNQI SNVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR 1250
    QMHQQQQVQQ RTLMMRGQGL NMTPSMVAPS GMPATMSNPR IPQANAQQFP 1300
    FPPNYGISQQ PDPGFTGATT PQSPLMSPRM AHTQSPMMQQ SQANPAYQAP 1350
    SDINGWAQGN MGGNSMFSQQ SPPHFGQQAN TSMYSNNMNI NVSMATNTGG 1400
    MSSMNQMTGQ ISMTSVTSVP TSGLSSMGPE QVNDPALRGG NLFPNQLPGM 1450
    DMIKQEGDTT RKYC 1464
    Length:1,464
    Mass (Da):159,157
    Last modified:May 1, 1997 - v2
    Checksum:i0A61AA5D1878304B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1282 – 12821M → I.1 Publication
    Corresponds to variant rs2228591 [ dbSNP | Ensembl ].
    VAR_024546

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97674 mRNA. Translation: CAA66263.1.
    BC114383 mRNA. Translation: AAI14384.1.
    CCDSiCCDS47872.1.
    RefSeqiNP_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.
    UniGeneiHs.446678.
    Hs.595378.

    Genome annotation databases

    EnsembliENST00000452400; ENSP00000399968; ENSG00000140396.
    GeneIDi10499.
    KEGGihsa:10499.
    UCSCiuc003xyn.1. human.

    Polymorphism databases

    DMDMi13626594.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97674 mRNA. Translation: CAA66263.1 .
    BC114383 mRNA. Translation: AAI14384.1 .
    CCDSi CCDS47872.1.
    RefSeqi NP_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.
    UniGenei Hs.446678.
    Hs.595378.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GWQ X-ray 2.45 C/D 688-696 [» ]
    1GWR X-ray 2.40 C/D 742-750 [» ]
    1M2Z X-ray 2.50 B/E 734-754 [» ]
    1MV9 X-ray 1.90 B 686-698 [» ]
    1MVC X-ray 1.90 B 686-698 [» ]
    1MZN X-ray 1.90 B/D/F/H 686-698 [» ]
    1P93 X-ray 2.70 E/F/G/H 740-751 [» ]
    1T63 X-ray 2.07 B 740-753 [» ]
    1T65 X-ray 1.66 B 686-698 [» ]
    1UHL X-ray 2.90 C/D 687-696 [» ]
    1YOK X-ray 2.50 B/C 740-753 [» ]
    1ZDT X-ray 2.10 P/Q 741-752 [» ]
    1ZDU X-ray 2.50 P/Q 741-751 [» ]
    1ZKY X-ray 2.25 C/D 686-698 [» ]
    2AO6 X-ray 1.89 B 740-753 [» ]
    2B1V X-ray 1.80 C/D 686-698 [» ]
    2B1Z X-ray 1.78 C/D 686-698 [» ]
    2B23 X-ray 2.10 C/D 686-698 [» ]
    2FAI X-ray 2.10 C/D 686-698 [» ]
    2G44 X-ray 2.65 C/D 686-698 [» ]
    2G5O X-ray 2.30 C/D 686-698 [» ]
    2P15 X-ray 1.94 C/D 686-698 [» ]
    2P1T X-ray 1.80 B 686-698 [» ]
    2P1U X-ray 2.20 B 686-698 [» ]
    2P1V X-ray 2.20 B 686-698 [» ]
    2Q7J X-ray 1.90 B 740-753 [» ]
    2Q7L X-ray 1.92 B 740-753 [» ]
    2ZXZ X-ray 3.00 B 686-698 [» ]
    2ZY0 X-ray 2.90 B/D 686-698 [» ]
    3A9E X-ray 2.75 I 686-698 [» ]
    3CLD X-ray 2.84 C/H 740-751 [» ]
    3DZU X-ray 3.20 E/G 685-697 [» ]
    3DZY X-ray 3.10 E/G 685-697 [» ]
    3E00 X-ray 3.10 E/G 685-697 [» ]
    3E7C X-ray 2.15 D/H 741-751 [» ]
    3E94 X-ray 1.90 B 686-698 [» ]
    3ERD X-ray 2.03 C/D 686-698 [» ]
    3FUG X-ray 2.00 B 686-698 [» ]
    3GN8 X-ray 2.50 C/E 734-754 [» ]
    3K22 X-ray 2.10 D/H 740-751 [» ]
    3K23 X-ray 3.00 D/E/F 740-751 [» ]
    3KWY X-ray 2.30 B 686-698 [» ]
    3KYT X-ray 2.35 C 686-697 [» ]
    3L0E X-ray 2.30 B 740-751 [» ]
    3L0J X-ray 2.40 C 688-697 [» ]
    3L0L X-ray 1.74 C/E 685-697 [» ]
    3O1D X-ray 2.40 B 686-698 [» ]
    3O1E X-ray 2.50 B 686-698 [» ]
    3OAP X-ray 2.05 B 686-696 [» ]
    3OZJ X-ray 2.10 B/D 686-696 [» ]
    3PCU X-ray 2.00 B 687-696 [» ]
    3PLZ X-ray 1.75 C/D 740-753 [» ]
    3Q95 X-ray 2.05 C/D 686-698 [» ]
    3Q97 X-ray 2.10 C/D 686-698 [» ]
    3R5M X-ray 2.80 B/D 687-696 [» ]
    3UP0 X-ray 1.60 P/Q 740-753 [» ]
    3UP3 X-ray 1.25 P 741-754 [» ]
    4CSJ X-ray 2.30 B 741-753 [» ]
    4DOS X-ray 2.00 B/C 740-753 [» ]
    4E2J X-ray 2.50 C/E 741-752 [» ]
    4FHH X-ray 2.33 B 686-698 [» ]
    4FHI X-ray 2.40 B 686-698 [» ]
    4IA1 X-ray 2.44 B 686-698 [» ]
    4IA2 X-ray 2.95 B 686-698 [» ]
    4IA3 X-ray 2.70 B 686-698 [» ]
    4IA7 X-ray 2.70 B 686-698 [» ]
    4IQR X-ray 2.90 I/J/K/L 685-697 [» ]
    4IU7 X-ray 2.29 C/D 687-696 [» ]
    4IUI X-ray 2.30 C/D 687-696 [» ]
    4IV2 X-ray 2.14 C/D 687-696 [» ]
    4IV4 X-ray 2.30 C/D 687-696 [» ]
    4IVW X-ray 2.06 C/D 687-696 [» ]
    4IVY X-ray 1.95 C/D 687-696 [» ]
    4IW6 X-ray 1.98 C/D 687-696 [» ]
    4IW8 X-ray 2.04 C/D 687-696 [» ]
    4IWC X-ray 2.24 C/D 687-696 [» ]
    4IWF X-ray 1.93 C/D 687-696 [» ]
    4K4J X-ray 2.00 B 686-698 [» ]
    4K6I X-ray 2.10 B 686-698 [» ]
    4M8E X-ray 2.40 B 686-696 [» ]
    4M8H X-ray 2.20 B 686-696 [» ]
    4NIE X-ray 2.01 C/D 686-697 [» ]
    4NQA X-ray 3.10 C/D/J/K 686-698 [» ]
    4P6W X-ray 1.95 B 741-752 [» ]
    4P6X X-ray 2.50 B/D/F/H/J/L 740-753 [» ]
    4POH X-ray 2.30 B 686-698 [» ]
    4POJ X-ray 2.00 B 686-698 [» ]
    4PP3 X-ray 2.00 B 686-698 [» ]
    4PP5 X-ray 2.00 B 686-698 [» ]
    4PP6 X-ray 2.20 C/D 688-696 [» ]
    4PPP X-ray 2.69 C/D 688-696 [» ]
    4PPS X-ray 1.93 C/D 687-698 [» ]
    ProteinModelPortali Q15596.
    SMRi Q15596. Positions 30-376, 1071-1115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115761. 60 interactions.
    DIPi DIP-5997N.
    IntActi Q15596. 12 interactions.
    MINTi MINT-122867.
    STRINGi 9606.ENSP00000399968.

    Chemistry

    ChEMBLi CHEMBL2095163.

    PTM databases

    PhosphoSitei Q15596.

    Polymorphism databases

    DMDMi 13626594.

    Proteomic databases

    MaxQBi Q15596.
    PaxDbi Q15596.
    PRIDEi Q15596.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000452400 ; ENSP00000399968 ; ENSG00000140396 .
    GeneIDi 10499.
    KEGGi hsa:10499.
    UCSCi uc003xyn.1. human.

    Organism-specific databases

    CTDi 10499.
    GeneCardsi GC08M071016.
    HGNCi HGNC:7669. NCOA2.
    MIMi 601993. gene.
    neXtProti NX_Q15596.
    PharmGKBi PA31471.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG315556.
    HOGENOMi HOG000230947.
    HOVERGENi HBG052583.
    InParanoidi Q15596.
    KOi K11255.
    OMAi TGMIGSN.
    OrthoDBi EOG72JWFB.
    PhylomeDBi Q15596.
    TreeFami TF332652.

    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.
    SignaLinki Q15596.

    Miscellaneous databases

    ChiTaRSi NCOA2. human.
    EvolutionaryTracei Q15596.
    GeneWikii Nuclear_receptor_coactivator_2.
    GenomeRNAii 10499.
    NextBioi 39840.
    PROi Q15596.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15596.
    Bgeei Q15596.
    CleanExi HS_NCOA2.
    Genevestigatori Q15596.

    Family and domain databases

    Gene3Di 4.10.280.10. 1 hit.
    4.10.630.10. 2 hits.
    InterProi IPR011598. 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 ]
    PANTHERi PTHR10684. PTHR10684. 1 hit.
    PTHR10684:SF2. PTHR10684:SF2. 1 hit.
    Pfami PF07469. DUF1518. 1 hit.
    PF08815. Nuc_rec_co-act. 1 hit.
    PF00989. PAS. 1 hit.
    PF08832. SRC-1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038181. Nuclear_receptor_coactivator. 1 hit.
    SMARTi SM00353. HLH. 1 hit.
    SM00086. PAC. 1 hit.
    SM00091. PAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47459. SSF47459. 1 hit.
    SSF55785. SSF55785. 2 hits.
    SSF69125. SSF69125. 1 hit.
    PROSITEi PS50888. BHLH. 1 hit.
    PS50112. PAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: FUNCTION, INTERACTION WITH RWDD3 AND NR3C1.

    Entry informationi

    Entry nameiNCOA2_HUMAN
    AccessioniPrimary (citable) accession number: Q15596
    Secondary accession number(s): Q14CD2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 162 of the entry and version 2 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3