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Q15596

- NCOA2_HUMAN

UniProt

Q15596 - NCOA2_HUMAN

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Protein

Nuclear receptor coactivator 2

Gene

NCOA2

Organism
Homo sapiens (Human)
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 RWDD3.2 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. signal transducer activity Source: InterPro
  7. thyroid hormone receptor coactivator activity Source: Ensembl
  8. 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 glucose metabolic process Source: Ensembl
  5. regulation of transcription, DNA-templated Source: UniProtKB
  6. small molecule metabolic process Source: Reactome
  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_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
Complete GO annotation...

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

BgeeiQ15596.
CleanExiHS_NCOA2.
ExpressionAtlasiQ15596. baseline and differential.
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. 63 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[»]
4Q0AX-ray1.90D687-695[»]
ProteinModelPortaliQ15596.
SMRiQ15596. Positions 34-376, 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.
GeneTreeiENSGT00530000063109.
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

        10         20         30         40         50
MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRNTEKRNRE QENKYIEELA
60 70 80 90 100
ELIFANFNDI DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS
110 120 130 140 150
DVSSTGQGVI DKDALGPMML EALDGFFFVV NLEGNVVFVS ENVTQYLRYN
160 170 180 190 200
QEELMNKSVY SILHVGDHTE FVKNLLPKSI VNGGSWSGEP PRRNSHTFNC
210 220 230 240 250
RMLVKPLPDS EEEGHDNQEA HQKYETMQCF AVSQPKSIKE EGEDLQSCLI
260 270 280 290 300
CVARRVPMKE RPVLPSSESF TTRQDLQGKI TSLDTSTMRA AMKPGWEDLV
310 320 330 340 350
RRCIQKFHAQ HEGESVSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ
360 370 380 390 400
TKSKLIRSQT TNEPQLVISL HMLHREQNVC VMNPDLTGQT MGKPLNPISS
410 420 430 440 450
NSPAHQALCS GNPGQDMTLS SNINFPINGP KEQMGMPMGR FGGSGGMNHV
460 470 480 490 500
SGMQATTPQG SNYALKMNSP SQSSPGMNPG QPTSMLSPRH 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
ESSCHPGEQK ETNDPNLPPA VSSERADGQS RLHDSKGQTK LLQLLTTKSD
660 670 680 690 700
QMEPSPLASS LSDTNKDSTG SLPGSGSTHG TSLKEKHKIL HRLLQDSSSP
710 720 730 740 750
VDLAKLTAEA TGKDLSQESS STAPGSEVTI KQEPVSPKKK ENALLRYLLD
760 770 780 790 800
KDDTKDIGLP EITPKLERLD SKTDPASNTK LIAMKTEKEE MSFEPGDQPG
810 820 830 840 850
SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP AGSVDKQAII NDLMQLTAEN
860 870 880 890 900
SPVTPVGAQK TALRISQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG
910 920 930 940 950
PFPPIRNSSP YSVIPQPGMM GNQGMIGNQG NLGNSSTGMI GNSASRPTMP
960 970 980 990 1000
SGEWAPQSSA VRVTCAATTS AMNRPVQGGM IRNPAASIPM RPSSQPGQRQ
1010 1020 1030 1040 1050
TLQSQVMNIG PSELEMNMGG PQYSQQQAPP NQTAPWPESI LPIDQASFAS
1060 1070 1080 1090 1100
QNRQPFGSSP DDLLCPHPAA ESPSDEGALL DQLYLALRNF DGLEEIDRAL
1110 1120 1130 1140 1150
GIPELVSQSQ AVDPEQFSSQ DSNIMLEQKA PVFPQQYASQ AQMAQGSYSP
1160 1170 1180 1190 1200
MQDPNFHTMG QRPSYATLRM QPRPGLRPTG LVQNQPNQLR LQLQHRLQAQ
1210 1220 1230 1240 1250
QNRQPLMNQI SNVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR
1260 1270 1280 1290 1300
QMHQQQQVQQ RTLMMRGQGL NMTPSMVAPS GMPATMSNPR IPQANAQQFP
1310 1320 1330 1340 1350
FPPNYGISQQ PDPGFTGATT PQSPLMSPRM AHTQSPMMQQ SQANPAYQAP
1360 1370 1380 1390 1400
SDINGWAQGN MGGNSMFSQQ SPPHFGQQAN TSMYSNNMNI NVSMATNTGG
1410 1420 1430 1440 1450
MSSMNQMTGQ ISMTSVTSVP TSGLSSMGPE QVNDPALRGG NLFPNQLPGM
1460
DMIKQEGDTT RKYC
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 [» ]
4Q0A X-ray 1.90 D 687-695 [» ]
ProteinModelPortali Q15596.
SMRi Q15596. Positions 34-376, 1071-1115.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115761. 63 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.
GeneTreei ENSGT00530000063109.
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

Bgeei Q15596.
CleanExi HS_NCOA2.
ExpressionAtlasi Q15596. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 163 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