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Q61026

- NCOA2_MOUSE

UniProt

Q61026 - NCOA2_MOUSE

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Protein

Nuclear receptor coactivator 2

Gene

Ncoa2

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. 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. receptor binding Source: MGI
  5. signal transducer activity Source: InterPro
  6. thyroid hormone receptor coactivator activity Source: MGI
  7. transcription coactivator activity Source: UniProtKB
  8. 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 – 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

MaxQBiQ61026.
PaxDbiQ61026.
PRIDEiQ61026.

PTM databases

PhosphoSiteiQ61026.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ61026.
CleanExiMM_GRIP1.
MM_NCOA2.
ExpressionAtlasiQ61026. baseline and differential.
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 34-376, 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

        10         20         30         40         50
MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRSTEKRNRE QENKYIEELA
60 70 80 90 100
ELIFANFNDI DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS
110 120 130 140 150
DVSSTGQGVI DKDALGPMML EALDGFFFVV NLEGSVVFVS ENVTQYLRYN
160 170 180 190 200
QEELMNKSVY SILHVGDHTE FVKNLLPKSM VNGGSWSGEP PRRSSHTFNC
210 220 230 240 250
RMLVKPLPDS EEEGHDSQEA HQKYEAMQCF AVSQPKSIKE EGEDLQSCLI
260 270 280 290 300
CVARRVPMKE RPTLPSSESF TTRQDLQGKI TSLDTSTMRA AMKPGWEDLV
310 320 330 340 350
RRCIQKFHTQ HEGESLSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ
360 370 380 390 400
TKSKLIRSQT TNEPQLVISL HMLHREQNVC VMNPDLTGQA MGKPLNPISS
410 420 430 440 450
SSPAHQALCS GNPGQDMTLG SNINFPMNGP KEQMGMPMGR FGGSGGMNHV
460 470 480 490 500
SGMQATTPQG SNYALKMNSP SQSSPGMNPG QASSVLSPRQ RMSPGVAGSP
510 520 530 540 550
RIPPSQFSPA GSLHSPVGVC SSTGNSHSYT NSSLNALQAL SEGHGVSLGS
560 570 580 590 600
SLASPDLKMG NLQNSPVNMN PPPLSKMGSL DSKDCFGLYG EPSEGTTGQA
610 620 630 640 650
EASCHPEEQK GPNDSSMPQA ASGDRAEGHS RLHDSKGQTK LLQLLTTKSD
660 670 680 690 700
QMEPSPLPSS LSDTNKDSTG SLPGPGSTHG TSLKEKHKIL HRLLQDSSSP
710 720 730 740 750
VDLAKLTAEA TGKELSQESS STAPGSEVTV KQEPASPKKK ENALLRYLLD
760 770 780 790 800
KDDTKDIGLP EITPKLERLD SKTDPASNTK LIAMKTVKEE VSFEPSDQPG
810 820 830 840 850
SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP TGSVDKQAII NDLMQLTADS
860 870 880 890 900
SPVPPAGAQK AALRMSQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG
910 920 930 940 950
PFPPIRNSSP YSVIPQPGMM GNQGMLGSQG NLGNNSTGMI GSSTSRPSMP
960 970 980 990 1000
SGEWAPQSPA VRVTCAATTG AMNRPVQGGM IRNPTASIPM RANSQPGQRQ
1010 1020 1030 1040 1050
MLQSQVMNIG PSELEMNMGG PQYNQQQAPP NQTAPWPESI LPIDQASFAS
1060 1070 1080 1090 1100
QNRQPFGSSP DDLLCPHPAA ESPSDEGALL DQLYLALRNF DGLEEIDRAL
1110 1120 1130 1140 1150
GIPELVSQSQ AVDAEQFSSQ ESSIMLEQKP PVFPQQYASQ AQMAQGGYNP
1160 1170 1180 1190 1200
MQDPNFHTMG QRPNYTTLRM QPRPGLRPTG IVQNQPNQLR LQLQHRLQAQ
1210 1220 1230 1240 1250
QNRQPLMNQI SSVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR
1260 1270 1280 1290 1300
QMQQQVQQRT LMMRGQGLNV TPSMVAPAGL PAAMSNPRIP QANAQQFPFP
1310 1320 1330 1340 1350
PNYGISQQPD PGFTGATTPQ SPLMSPRMAH TQSPMMQQSQ ANPAYQPTSD
1360 1370 1380 1390 1400
MNGWAQGSMG GNSMFSQQSP PHFGQQANTS MYSNNMNISV SMATNTGGLS
1410 1420 1430 1440 1450
SMNQMTGQMS MTSVTSVPTS GLPSMGPEQV NDPALRGGNL FPNQLPGMDM
1460
IKQEGDASRK YC
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 34-376, 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

MaxQBi Q61026.
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

Bgeei Q61026.
CleanExi MM_GRIP1.
MM_NCOA2.
ExpressionAtlasi Q61026. baseline and differential.
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: October 29, 2014
This is version 147 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