NCOA2 | ENSG00000140396 | NCBI 10499

Details for: NCOA2

Gene ID: 10499

Symbol: NCOA2

Ensembl ID: ENSG00000140396

Description: nuclear receptor coactivator 2

Associated with

Activated pkn1 stimulates transcription of ar (androgen receptor) regulated genes klk2 and klk3
(R-HSA-5625886)
Activation of gene expression by srebf (srebp)
(R-HSA-2426168)
Bile acid and bile salt metabolism
(R-HSA-194068)
Biological oxidations
(R-HSA-211859)
Bmal1:clock,npas2 activates circadian gene expression
(R-HSA-1368108)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to chemical stress
(R-HSA-9711123)
Chromatin modifying enzymes
(R-HSA-3247509)
Chromatin organization
(R-HSA-4839726)
Circadian clock
(R-HSA-400253)
Cytochrome p450 - arranged by substrate type
(R-HSA-211897)
Cytoprotection by hmox1
(R-HSA-9707564)
Developmental biology
(R-HSA-1266738)
Endogenous sterols
(R-HSA-211976)
Esr-mediated signaling
(R-HSA-8939211)
Estrogen-dependent gene expression
(R-HSA-9018519)
Hats acetylate histones
(R-HSA-3214847)
Heme signaling
(R-HSA-9707616)
Metabolism
(R-HSA-1430728)
Metabolism of lipids
(R-HSA-556833)
Metabolism of proteins
(R-HSA-392499)
Metabolism of steroids
(R-HSA-8957322)
Mitochondrial biogenesis
(R-HSA-1592230)
Organelle biogenesis and maintenance
(R-HSA-1852241)
Phase i - functionalization of compounds
(R-HSA-211945)
Post-translational protein modification
(R-HSA-597592)
Ppara activates gene expression
(R-HSA-1989781)
Recycling of bile acids and salts
(R-HSA-159418)
Regulation of cholesterol biosynthesis by srebp (srebf)
(R-HSA-1655829)
Regulation of lipid metabolism by pparalpha
(R-HSA-400206)
Rho gtpase effectors
(R-HSA-195258)
Rho gtpases activate pkns
(R-HSA-5625740)
Rora activates gene expression
(R-HSA-1368082)
Signaling by nuclear receptors
(R-HSA-9006931)
Signaling by rho gtpases
(R-HSA-194315)
Signaling by rho gtpases, miro gtpases and rhobtb3
(R-HSA-9716542)
Signal transduction
(R-HSA-162582)
Sumo e3 ligases sumoylate target proteins
(R-HSA-3108232)
Sumoylation
(R-HSA-2990846)
Sumoylation of transcription cofactors
(R-HSA-3899300)
Synthesis of bile acids and bile salts
(R-HSA-192105)
Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
(R-HSA-193368)
Synthesis of bile acids and bile salts via 27-hydroxycholesterol
(R-HSA-193807)
Transcriptional activation of mitochondrial biogenesis
(R-HSA-2151201)
Transcriptional regulation of white adipocyte differentiation
(R-HSA-381340)
Aryl hydrocarbon receptor binding
(GO:0017162)
Cellular response to hormone stimulus
(GO:0032870)
Cellular response to thyroglobulin triiodothyronine
(GO:1904017)
Chromatin
(GO:0000785)
Chromatin binding
(GO:0003682)
Circadian regulation of gene expression
(GO:0032922)
Cytoplasm
(GO:0005737)
Locomotor rhythm
(GO:0045475)
Mrna transcription by rna polymerase ii
(GO:0042789)
Negative regulation of transcription by rna polymerase ii
(GO:0000122)
Nuclear body
(GO:0016604)
Nuclear receptor binding
(GO:0016922)
Nuclear receptor coactivator activity
(GO:0030374)
Nucleoplasm
(GO:0005654)
Nucleus
(GO:0005634)
Peroxisome proliferator activated receptor signaling pathway
(GO:0035357)
Positive regulation of adipose tissue development
(GO:1904179)
Positive regulation of transcription by rna polymerase ii
(GO:0045944)
Protein-containing complex
(GO:0032991)
Protein binding
(GO:0005515)
Protein dimerization activity
(GO:0046983)
Protein domain specific binding
(GO:0019904)
Regulation of cellular response to insulin stimulus
(GO:1900076)
Regulation of dna-templated transcription
(GO:0006355)
Regulation of glucose metabolic process
(GO:0010906)
Regulation of lipid metabolic process
(GO:0019216)
Response to progesterone
(GO:0032570)
Rna polymerase ii cis-regulatory region sequence-specific dna binding
(GO:0000978)
Rna polymerase ii intronic transcription regulatory region sequence-specific dna binding
(GO:0001162)
Rna polymerase ii transcription regulator complex
(GO:0090575)
Transcription coactivator activity
(GO:0003713)
Transcription regulator complex
(GO:0005667)

Other Information

Proteins

Nuclear receptor coactivator 2
B4DPW8_HUMAN

Genular Protein ID: 950094546

Symbol: NCOA2_HUMAN

Name: Nuclear receptor coactivator 2

UniProtKB Accession Codes:

Q15596 Q14CD2

Database IDs:

Citations:

PubMed ID: 8670870

Title: TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors.

PubMed ID: 8670870

DOI: 10.1002/j.1460-2075.1996.tb00736.x

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9558366

Title: A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia.

PubMed ID: 9558366

PubMed ID: 9430642

Title: The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways.

PubMed ID: 9430642

DOI: 10.1093/emboj/17.2.507

PubMed ID: 9590696

Title: Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex.

PubMed ID: 9590696

DOI: 10.1038/30032

PubMed ID: 10478845

Title: Coactivators for the orphan nuclear receptor RORalpha.

PubMed ID: 10478845

DOI: 10.1210/mend.13.9.0343

PubMed ID: 10594042

Title: Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha.

PubMed ID: 10594042

DOI: 10.1128/mcb.20.1.402-415.2000

PubMed ID: 11250900

Title: 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.

PubMed ID: 11250900

DOI: 10.1093/emboj/20.6.1341

PubMed ID: 11971985

Title: Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase.

PubMed ID: 11971985

DOI: 10.1128/mcb.22.10.3549-3561.2002

PubMed ID: 12676584

Title: MOZ-TIF2-induced acute myeloid leukemia requires the MOZ nucleosome binding motif and TIF2-mediated recruitment of CBP.

PubMed ID: 12676584

DOI: 10.1016/s1535-6108(03)00051-5

PubMed ID: 15657427

Title: MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by impairment of CBP function.

PubMed ID: 15657427

DOI: 10.1128/mcb.25.3.988-1002.2005

PubMed ID: 16957778

Title: The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription.

PubMed ID: 16957778

DOI: 10.1038/sj.emboj.7601306

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17116691

Title: STAMP, a novel predicted factor assisting TIF2 actions in glucocorticoid receptor-mediated induction and repression.

PubMed ID: 17116691

DOI: 10.1128/mcb.01360-06

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18690216

Title: Cytosporone B is an agonist for nuclear orphan receptor Nur77.

PubMed ID: 18690216

DOI: 10.1038/nchembio.106

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19481530

Title: GPS2 is required for cholesterol efflux by triggering histone demethylation, LXR recruitment, and coregulator assembly at the ABCG1 locus.

PubMed ID: 19481530

DOI: 10.1016/j.molcel.2009.05.006

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23508108

Title: RSUME enhances glucocorticoid receptor SUMOylation and transcriptional activity.

PubMed ID: 23508108

DOI: 10.1128/mcb.01470-12

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

Sequence Information:

Length: 1464
Mass: 159157
Checksum: 0A61AA5D1878304B
Sequence:

MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRNTEKRNRE QENKYIEELA ELIFANFNDI 
DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS DVSSTGQGVI DKDALGPMML 
EALDGFFFVV NLEGNVVFVS ENVTQYLRYN QEELMNKSVY SILHVGDHTE FVKNLLPKSI 
VNGGSWSGEP PRRNSHTFNC RMLVKPLPDS EEEGHDNQEA HQKYETMQCF AVSQPKSIKE 
EGEDLQSCLI CVARRVPMKE RPVLPSSESF TTRQDLQGKI TSLDTSTMRA AMKPGWEDLV 
RRCIQKFHAQ HEGESVSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ TKSKLIRSQT 
TNEPQLVISL HMLHREQNVC VMNPDLTGQT MGKPLNPISS NSPAHQALCS GNPGQDMTLS 
SNINFPINGP KEQMGMPMGR FGGSGGMNHV SGMQATTPQG SNYALKMNSP SQSSPGMNPG 
QPTSMLSPRH RMSPGVAGSP RIPPSQFSPA GSLHSPVGVC SSTGNSHSYT NSSLNALQAL 
SEGHGVSLGS SLASPDLKMG NLQNSPVNMN PPPLSKMGSL DSKDCFGLYG EPSEGTTGQA 
ESSCHPGEQK ETNDPNLPPA VSSERADGQS RLHDSKGQTK LLQLLTTKSD QMEPSPLASS 
LSDTNKDSTG SLPGSGSTHG TSLKEKHKIL HRLLQDSSSP VDLAKLTAEA TGKDLSQESS 
STAPGSEVTI KQEPVSPKKK ENALLRYLLD KDDTKDIGLP EITPKLERLD SKTDPASNTK 
LIAMKTEKEE MSFEPGDQPG SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP AGSVDKQAII 
NDLMQLTAEN SPVTPVGAQK TALRISQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG 
PFPPIRNSSP YSVIPQPGMM GNQGMIGNQG NLGNSSTGMI GNSASRPTMP SGEWAPQSSA 
VRVTCAATTS AMNRPVQGGM IRNPAASIPM RPSSQPGQRQ TLQSQVMNIG PSELEMNMGG 
PQYSQQQAPP NQTAPWPESI LPIDQASFAS QNRQPFGSSP DDLLCPHPAA ESPSDEGALL 
DQLYLALRNF DGLEEIDRAL GIPELVSQSQ AVDPEQFSSQ DSNIMLEQKA PVFPQQYASQ 
AQMAQGSYSP MQDPNFHTMG QRPSYATLRM QPRPGLRPTG LVQNQPNQLR LQLQHRLQAQ 
QNRQPLMNQI SNVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR QMHQQQQVQQ 
RTLMMRGQGL NMTPSMVAPS GMPATMSNPR IPQANAQQFP FPPNYGISQQ PDPGFTGATT 
PQSPLMSPRM AHTQSPMMQQ SQANPAYQAP SDINGWAQGN MGGNSMFSQQ SPPHFGQQAN 
TSMYSNNMNI NVSMATNTGG MSSMNQMTGQ ISMTSVTSVP TSGLSSMGPE QVNDPALRGG 
NLFPNQLPGM DMIKQEGDTT RKYC

Genular Protein ID: 2387121203

Symbol: B4DPW8_HUMAN

Name: N/A

UniProtKB Accession Codes:

B4DPW8

Database IDs:

Sequence Information:

Length: 552
Mass: 60131
Checksum: 043279D67E98DE7E
Sequence:

MQLTAENSPV TPVGAQKTAL RISQSRMIGN SASRPTMPSG EWAPQSSAVR VTCAATTSAM 
NRPVQGGMIR NPAASIPMRP SSQPGQRQTL QSQVMNTGPS ELEMNMGGPQ YSQQQAPPNQ 
TAPWPESILP IDQASFASQN RQPFGSSPDD LLCPHPAAES PSDEGALLDQ LYLALRNFDG 
LEEIDRALGI PELVSQSQAV DPEQFSSQDS NIMLEQKAPV FPQQYASQAQ MAQGSYSPMQ 
DPNFHTMGQR PSYATLRMQP RPGLRPTGLV QNQPNQLRLQ LQHRLQAQQN RQPLMNQISN 
VSNVNLTLRP GVPTQAPINA QMLAQRQREI LNQHLRQRQM HQQQQVQQRT LMMRGQGLNM 
TPSMVAPSGM PATMSNPRIP QANAQQFPFP PNYGISQQPD PGFTGATTPQ SPLMSPRMAH 
TQSPMMQQSQ ANPAYQAPSD INGWAQGNMG GNSMFSQQSP PHFGQQANTS MYSNNMNINV 
STATNTGGMS SMNQMTGQIS MTSVTSVPTS GLSSMGPEQV NDPALRGGNL FPNQLPGMDM 
IKQEGDTTRK YC

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: NCOA2

Associated with

Other Information

TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. PubMed ID: 8670870

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia. PubMed ID: 9558366

The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways. PubMed ID: 9430642

Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. PubMed ID: 9590696

Coactivators for the orphan nuclear receptor RORalpha. PubMed ID: 10478845

Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. PubMed ID: 10594042

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. PubMed ID: 11250900

Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase. PubMed ID: 11971985

MOZ-TIF2-induced acute myeloid leukemia requires the MOZ nucleosome binding motif and TIF2-mediated recruitment of CBP. PubMed ID: 12676584

MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by impairment of CBP function. PubMed ID: 15657427

The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription. PubMed ID: 16957778

A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PubMed ID: 16964243

STAMP, a novel predicted factor assisting TIF2 actions in glucocorticoid receptor-mediated induction and repression. PubMed ID: 17116691

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PubMed ID: 18691976

Cytosporone B is an agonist for nuclear orphan receptor Nur77. PubMed ID: 18690216

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

GPS2 is required for cholesterol efflux by triggering histone demethylation, LXR recruitment, and coregulator assembly at the ABCG1 locus. PubMed ID: 19481530

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

RSUME enhances glucocorticoid receptor SUMOylation and transcriptional activity. PubMed ID: 23508108

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. PubMed ID: 24129315

Uncovering global SUMOylation signaling networks in a site-specific manner. PubMed ID: 25218447

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733