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Q61026

- NCOA2_MOUSE

UniProt

Q61026 - NCOA2_MOUSE

Protein

Nuclear receptor coactivator 2

Gene

Ncoa2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      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 RWDD3.4 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. negative regulation of transcription, DNA-templated Source: MGI
    2. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    3. positive regulation of receptor activity Source: GOC
    4. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    5. regulation of glucose metabolic process Source: UniProtKB
    6. regulation of transcription, DNA-templated Source: MGI
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_118837. Rora activates circadian gene expression.
    REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_198351. RORA activates circadian gene expression.
    REACT_198352. REV-ERBA represses gene expression.
    REACT_198602. PPARA activates gene expression.
    REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor coactivator 2
    Short name:
    NCoA-2
    Alternative name(s):
    Glucocorticoid receptor-interacting protein 1
    Short name:
    GRIP-1
    Steroid receptor coactivator 2
    Short name:
    SRC-2
    Transcriptional intermediary factor 2
    Gene namesi
    Name:Ncoa2
    Synonyms:Grip1, Src2, Tif2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1276533. Ncoa2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nucleoplasm Source: Reactome
    3. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Animals show a glycogenopathy resembling to Von Gierke's disease with impaired growth, fasting hypoglycemia, and an increase in concentrations of triglycerides, cholesterol, free fatty acids, ketone bodies, uric acid and lactic acid in the plasma during fating. They also have increased liver glycogen stores and hepatic steatosis.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi644 – 6452LL → AA: Abolishes interaction with RORC; when associated with 689-A--A-694 and 744-A--A-749. 1 Publication
    Mutagenesisi689 – 6946ILHRLL → AAHRAA: Abolishes interaction with RORC; when associated with 644-A-A-645 and 744-A--A-749. 1 Publication
    Mutagenesisi744 – 7496LLRYLL → AARAA: Abolishes interaction with RORC; when associated with 644-A-A-645 and 689-A--A-694. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 14621461Nuclear receptor coactivator 2PRO_0000094403Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ61026.
    PRIDEiQ61026.

    PTM databases

    PhosphoSiteiQ61026.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ61026.
    BgeeiQ61026.
    CleanExiMM_GRIP1.
    MM_NCOA2.
    GenevestigatoriQ61026.

    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 RWDD3.6 Publications

    Protein-protein interaction databases

    BioGridi201708. 12 interactions.
    DIPiDIP-5979N.
    IntActiQ61026. 4 interactions.
    MINTiMINT-236676.

    Structurei

    Secondary structure

    1
    1462
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi689 – 6946
    Helixi743 – 7497

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L2IX-ray1.95C/D686-698[»]
    1OSVX-ray2.50C/D/E741-752[»]
    1WM0X-ray2.90Y684-697[»]
    2Q6JX-ray2.70C/D686-698[»]
    2QA6X-ray2.60C/D686-698[»]
    2QA8X-ray1.85C/D686-698[»]
    2QABX-ray1.89C/D686-698[»]
    2QGTX-ray2.15C/D686-698[»]
    2QGWX-ray2.39C/D686-698[»]
    2QH6X-ray2.70C/D686-698[»]
    2QPYX-ray2.50B744-753[»]
    2QR9X-ray2.00C/D686-698[»]
    2QSEX-ray1.85C/D686-698[»]
    2QXMX-ray2.30C/D686-698[»]
    2QZOX-ray1.72C/D686-698[»]
    3MNEX-ray1.96B740-752[»]
    3MNOX-ray1.55B740-752[»]
    3MNPX-ray1.50B740-752[»]
    ProteinModelPortaliQ61026.
    SMRiQ61026. Positions 28-376, 1071-1113.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ61026.

    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-bindingAdd
    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

    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 (PubMed:16148126).1 Publication
    The LLXXLXXXL motif is involved in transcriptional coactivation and CREBBP/CBP binding.By similarity

    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.
    GeneTreeiENSGT00530000063109.
    HOGENOMiHOG000230947.
    HOVERGENiHBG052583.
    InParanoidiQ61026.
    KOiK11255.
    OMAiTGMIGSN.
    OrthoDBiEOG72JWFB.
    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.

    Q61026-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRSTEKRNRE QENKYIEELA     50
    ELIFANFNDI DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS 100
    DVSSTGQGVI DKDALGPMML EALDGFFFVV NLEGSVVFVS ENVTQYLRYN 150
    QEELMNKSVY SILHVGDHTE FVKNLLPKSM VNGGSWSGEP PRRSSHTFNC 200
    RMLVKPLPDS EEEGHDSQEA HQKYEAMQCF AVSQPKSIKE EGEDLQSCLI 250
    CVARRVPMKE RPTLPSSESF TTRQDLQGKI TSLDTSTMRA AMKPGWEDLV 300
    RRCIQKFHTQ HEGESLSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ 350
    TKSKLIRSQT TNEPQLVISL HMLHREQNVC VMNPDLTGQA MGKPLNPISS 400
    SSPAHQALCS GNPGQDMTLG SNINFPMNGP KEQMGMPMGR FGGSGGMNHV 450
    SGMQATTPQG SNYALKMNSP SQSSPGMNPG QASSVLSPRQ RMSPGVAGSP 500
    RIPPSQFSPA GSLHSPVGVC SSTGNSHSYT NSSLNALQAL SEGHGVSLGS 550
    SLASPDLKMG NLQNSPVNMN PPPLSKMGSL DSKDCFGLYG EPSEGTTGQA 600
    EASCHPEEQK GPNDSSMPQA ASGDRAEGHS RLHDSKGQTK LLQLLTTKSD 650
    QMEPSPLPSS LSDTNKDSTG SLPGPGSTHG TSLKEKHKIL HRLLQDSSSP 700
    VDLAKLTAEA TGKELSQESS STAPGSEVTV KQEPASPKKK ENALLRYLLD 750
    KDDTKDIGLP EITPKLERLD SKTDPASNTK LIAMKTVKEE VSFEPSDQPG 800
    SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP TGSVDKQAII NDLMQLTADS 850
    SPVPPAGAQK AALRMSQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG 900
    PFPPIRNSSP YSVIPQPGMM GNQGMLGSQG NLGNNSTGMI GSSTSRPSMP 950
    SGEWAPQSPA VRVTCAATTG AMNRPVQGGM IRNPTASIPM RANSQPGQRQ 1000
    MLQSQVMNIG PSELEMNMGG PQYNQQQAPP NQTAPWPESI LPIDQASFAS 1050
    QNRQPFGSSP DDLLCPHPAA ESPSDEGALL DQLYLALRNF DGLEEIDRAL 1100
    GIPELVSQSQ AVDAEQFSSQ ESSIMLEQKP PVFPQQYASQ AQMAQGGYNP 1150
    MQDPNFHTMG QRPNYTTLRM QPRPGLRPTG IVQNQPNQLR LQLQHRLQAQ 1200
    QNRQPLMNQI SSVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR 1250
    QMQQQVQQRT LMMRGQGLNV TPSMVAPAGL PAAMSNPRIP QANAQQFPFP 1300
    PNYGISQQPD PGFTGATTPQ SPLMSPRMAH TQSPMMQQSQ ANPAYQPTSD 1350
    MNGWAQGSMG GNSMFSQQSP PHFGQQANTS MYSNNMNISV SMATNTGGLS 1400
    SMNQMTGQMS MTSVTSVPTS GLPSMGPEQV NDPALRGGNL FPNQLPGMDM 1450
    IKQEGDASRK YC 1462
    Length:1,462
    Mass (Da):158,466
    Last modified:July 27, 2011 - v3
    Checksum:i619462FF1ACC6067
    GO

    Sequence cautioni

    The sequence AAB61575.1 differs from that shown. Reason: Frameshift at positions 251, 256, 302, 321, 959, 964 and 983.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511E → D in AAC53151. (PubMed:9111344)Curated
    Sequence conflicti140 – 1412SE → FR in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti194 – 1941S → T in AAC53151. (PubMed:9111344)Curated
    Sequence conflicti256 – 2561V → I in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti286 – 2861S → T in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti420 – 4201G → S in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti512 – 5121S → N in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti594 – 5941E → K in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti607 – 6082EE → KK in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti864 – 8641R → C in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti869 – 8691T → S in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti884 – 8841N → Y in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti972 – 9721M → K in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti980 – 9801M → K in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti991 – 9911R → G in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti996 – 9961P → L in AAB61575. (PubMed:9192892)Curated
    Sequence conflicti1407 – 14071G → C in AAC53151. (PubMed:9111344)Curated
    Sequence conflicti1446 – 14461P → L in AAB61575. (PubMed:9192892)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39060 mRNA. Translation: AAC53151.1.
    AF000582 mRNA. Translation: AAB61575.1. Frameshift.
    AC091248 Genomic DNA. No translation available.
    AC121538 Genomic DNA. No translation available.
    CCDSiCCDS35515.1.
    PIRiT30193.
    T42639.
    RefSeqiNP_032704.2. NM_008678.2.
    XP_006495528.1. XM_006495465.1.
    XP_006495529.1. XM_006495466.1.
    XP_006495530.1. XM_006495467.1.
    XP_006495531.1. XM_006495468.1.
    UniGeneiMm.2537.

    Genome annotation databases

    EnsembliENSMUST00000006037; ENSMUSP00000006037; ENSMUSG00000005886.
    GeneIDi17978.
    KEGGimmu:17978.
    UCSCiuc007aim.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39060 mRNA. Translation: AAC53151.1 .
    AF000582 mRNA. Translation: AAB61575.1 . Frameshift.
    AC091248 Genomic DNA. No translation available.
    AC121538 Genomic DNA. No translation available.
    CCDSi CCDS35515.1.
    PIRi T30193.
    T42639.
    RefSeqi NP_032704.2. NM_008678.2.
    XP_006495528.1. XM_006495465.1.
    XP_006495529.1. XM_006495466.1.
    XP_006495530.1. XM_006495467.1.
    XP_006495531.1. XM_006495468.1.
    UniGenei Mm.2537.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1L2I X-ray 1.95 C/D 686-698 [» ]
    1OSV X-ray 2.50 C/D/E 741-752 [» ]
    1WM0 X-ray 2.90 Y 684-697 [» ]
    2Q6J X-ray 2.70 C/D 686-698 [» ]
    2QA6 X-ray 2.60 C/D 686-698 [» ]
    2QA8 X-ray 1.85 C/D 686-698 [» ]
    2QAB X-ray 1.89 C/D 686-698 [» ]
    2QGT X-ray 2.15 C/D 686-698 [» ]
    2QGW X-ray 2.39 C/D 686-698 [» ]
    2QH6 X-ray 2.70 C/D 686-698 [» ]
    2QPY X-ray 2.50 B 744-753 [» ]
    2QR9 X-ray 2.00 C/D 686-698 [» ]
    2QSE X-ray 1.85 C/D 686-698 [» ]
    2QXM X-ray 2.30 C/D 686-698 [» ]
    2QZO X-ray 1.72 C/D 686-698 [» ]
    3MNE X-ray 1.96 B 740-752 [» ]
    3MNO X-ray 1.55 B 740-752 [» ]
    3MNP X-ray 1.50 B 740-752 [» ]
    ProteinModelPortali Q61026.
    SMRi Q61026. Positions 28-376, 1071-1113.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201708. 12 interactions.
    DIPi DIP-5979N.
    IntActi Q61026. 4 interactions.
    MINTi MINT-236676.

    PTM databases

    PhosphoSitei Q61026.

    Proteomic databases

    PaxDbi Q61026.
    PRIDEi Q61026.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000006037 ; ENSMUSP00000006037 ; ENSMUSG00000005886 .
    GeneIDi 17978.
    KEGGi mmu:17978.
    UCSCi uc007aim.1. mouse.

    Organism-specific databases

    CTDi 10499.
    MGIi MGI:1276533. Ncoa2.

    Phylogenomic databases

    eggNOGi NOG315556.
    GeneTreei ENSGT00530000063109.
    HOGENOMi HOG000230947.
    HOVERGENi HBG052583.
    InParanoidi Q61026.
    KOi K11255.
    OMAi TGMIGSN.
    OrthoDBi EOG72JWFB.
    TreeFami TF332652.

    Enzyme and pathway databases

    Reactomei REACT_118837. Rora activates circadian gene expression.
    REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_198351. RORA activates circadian gene expression.
    REACT_198352. REV-ERBA represses gene expression.
    REACT_198602. PPARA activates gene expression.
    REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Miscellaneous databases

    ChiTaRSi NCOA2. mouse.
    EvolutionaryTracei Q61026.
    NextBioi 292941.
    PROi Q61026.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61026.
    Bgeei Q61026.
    CleanExi MM_GRIP1.
    MM_NCOA2.
    Genevestigatori Q61026.

    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. "GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors."
      Hong H., Kohli K., Garabedian M.J., Stallcup M.R.
      Mol. Cell. Biol. 17:2735-2744(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NR3C2.
      Strain: ICR.
      Tissue: Brain.
    2. "The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function."
      Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., Rosenfeld M.G.
      Nature 387:677-684(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors."
      Hong H., Kohli K., Trivedi A., Johnson D.L., Stallcup M.R.
      Proc. Natl. Acad. Sci. U.S.A. 93:4948-4952(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 322-1119.
      Strain: ICR.
      Tissue: Embryo.
    5. "Regulation of transcription by a protein methyltransferase."
      Chen D., Ma H., Hong H., Koh S.S., Huang S.-M., Schurter B.T., Aswad D.W., Stallcup M.R.
      Science 284:2174-2177(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CARM1.
    6. "SRC-1 and TIF2 control energy balance between white and brown adipose tissues."
      Picard F., Gehin M., Annicotte J.-S., Rocchi S., Champy M.-F., O'Malley B.W., Chambon P., Auwerx J.
      Cell 111:931-941(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities."
      Lee Y.-H., Koh S.S., Zhang X., Cheng X., Stallcup M.R.
      Mol. Cell. Biol. 22:3621-3632(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH EP300 AND NCOA2.
    8. "Tumor necrosis factor alpha receptor- and Fas-associated FLASH inhibit transcriptional activity of the glucocorticoid receptor by binding to and interfering with its interaction with p160 type nuclear receptor coactivators."
      Kino T., Chrousos G.P.
      J. Biol. Chem. 278:3023-3029(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CASP8AP2.
    9. "RORgammat recruits steroid receptor coactivators to ensure thymocyte survival."
      Xie H., Sadim M.S., Sun Z.
      J. Immunol. 175:3800-3809(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS COACTIVATOR, INTERACTION WITH RORC, DOMAIN, MUTAGENESIS OF 644-L-L-645; 689-L--L-694; 744-L--L-749.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    12. "Absence of the SRC-2 coactivator results in a glycogenopathy resembling Von Gierke's disease."
      Chopra A.R., Louet J.F., Saha P., An J., Demayo F., Xu J., York B., Karpen S., Finegold M., Moore D., Chan L., Newgard C.B., O'Malley B.W.
      Science 322:1395-1399(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN GLUCOSE METABOLISM REGULATION, INTERACTION WITH RORA, DISRUPTION PHENOTYPE.
    13. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493; SER-699 AND SER-771, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: INTERACTS WITH RORA AND RORC.
    15. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-636; LYS-640; LYS-780 AND LYS-785, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiNCOA2_MOUSE
    AccessioniPrimary (citable) accession number: Q61026
    Secondary accession number(s): E9QMH9, O09001, P97759
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 146 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3