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Q61026

- NCOA2_MOUSE

UniProt

Q61026 - NCOA2_MOUSE

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Protein

Nuclear receptor coactivator 2

Gene
Ncoa2, Grip1, Src2, Tif2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.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
Complete GO annotation...

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
Complete GO annotation...

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 – 11Removed By similarity
Chaini2 – 14621461Nuclear receptor coactivator 2PRO_0000094403Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei487 – 4871Phosphoserine By similarity
Modified residuei493 – 4931Phosphoserine1 Publication
Modified residuei499 – 4991Phosphoserine By 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 – 8511Phosphoserine By 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).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.

Miscellaneous databases

EvolutionaryTraceiQ61026.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 8358bHLHAdd
BLAST
Domaini119 – 18365PASAdd
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.1 Publication
Contains 2 C-terminal transcription activation domains (AD1 and AD2) that can function independently (By similarity).1 Publication

Sequence similaritiesi

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511E → D in AAC53151. 1 Publication
Sequence conflicti140 – 1412SE → FR in AAB61575. 1 Publication
Sequence conflicti194 – 1941S → T in AAC53151. 1 Publication
Sequence conflicti256 – 2561V → I in AAB61575. 1 Publication
Sequence conflicti286 – 2861S → T in AAB61575. 1 Publication
Sequence conflicti420 – 4201G → S in AAB61575. 1 Publication
Sequence conflicti512 – 5121S → N in AAB61575. 1 Publication
Sequence conflicti594 – 5941E → K in AAB61575. 1 Publication
Sequence conflicti607 – 6082EE → KK in AAB61575. 1 Publication
Sequence conflicti864 – 8641R → C in AAB61575. 1 Publication
Sequence conflicti869 – 8691T → S in AAB61575. 1 Publication
Sequence conflicti884 – 8841N → Y in AAB61575. 1 Publication
Sequence conflicti972 – 9721M → K in AAB61575. 1 Publication
Sequence conflicti980 – 9801M → K in AAB61575. 1 Publication
Sequence conflicti991 – 9911R → G in AAB61575. 1 Publication
Sequence conflicti996 – 9961P → L in AAB61575. 1 Publication
Sequence conflicti1407 – 14071G → C in AAC53151. 1 Publication
Sequence conflicti1446 – 14461P → L in AAB61575. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 145 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

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