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Q61026 (NCOA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ncoa2
Synonyms:Grip1, Src2, Tif2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.9 Ref.12

Subunit structure

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). Ref.1 Ref.5 Ref.7 Ref.8 Ref.9 Ref.12

Subcellular location

Nucleus.

Tissue specificity

Ubiquitous.

Domain

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 (Ref.9). Ref.9

The LLXXLXXXL motif is involved in transcriptional coactivation and CREBBP/CBP binding By similarity. Ref.9

Contains 2 C-terminal transcription activation domains (AD1 and AD2) that can function independently By similarity. Ref.9

Disruption phenotype

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. Ref.12

Sequence similarities

Belongs to the SRC/p160 nuclear receptor coactivator family.

Contains 1 bHLH (basic helix-loop-helix) domain.

Contains 1 PAS (PER-ARNT-SIM) domain.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.4. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.4. Source: MGI

positive regulation of receptor activity

Inferred from direct assay PubMed 15072553. Source: GOC

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 15383530. Source: MGI

regulation of glucose metabolic process

Inferred from mutant phenotype Ref.12. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11675124PubMed 12130539. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11675124. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 11675124PubMed 12130539. Source: MGI

   Molecular_functionchromatin binding

Inferred from direct assay PubMed 16109736. Source: MGI

histone acetyltransferase activity

Inferred from electronic annotation. Source: InterPro

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from direct assay PubMed 15072553. Source: MGI

receptor binding

Inferred from direct assay Ref.4. Source: MGI

signal transducer activity

Inferred from electronic annotation. Source: InterPro

thyroid hormone receptor coactivator activity

Inferred from direct assay PubMed 15072553. Source: MGI

transcription coactivator activity

Inferred from direct assay Ref.9. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.9. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 14621461Nuclear receptor coactivator 2
PRO_0000094403

Regions

Domain26 – 8358bHLH
Domain119 – 18365PAS
Region691 – 74353CASP8AP2-binding
Motif641 – 6455LXXLL motif 1
Motif690 – 6945LXXLL motif 2
Motif745 – 7495LXXLL motif 3
Motif878 – 8825LXXLL motif 4
Motif1079 – 10879LLXXLXXXL motif

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue4871Phosphoserine By similarity
Modified residue4931Phosphoserine Ref.13
Modified residue4991Phosphoserine By similarity
Modified residue6361N6-acetyllysine Ref.15
Modified residue6401N6-acetyllysine Ref.15
Modified residue6991Phosphoserine Ref.13
Modified residue7711Phosphoserine Ref.13
Modified residue7801N6-acetyllysine Ref.15
Modified residue7851N6-acetyllysine Ref.15
Modified residue8511Phosphoserine By similarity

Experimental info

Mutagenesis644 – 6452LL → AA: Abolishes interaction with RORC; when associated with 689-A--A-694 and 744-A--A-749. Ref.9
Mutagenesis689 – 6946ILHRLL → AAHRAA: Abolishes interaction with RORC; when associated with 644-A-A-645 and 744-A--A-749. Ref.9
Mutagenesis744 – 7496LLRYLL → AARAA: Abolishes interaction with RORC; when associated with 644-A-A-645 and 689-A--A-694. Ref.9
Sequence conflict511E → D in AAC53151. Ref.1
Sequence conflict140 – 1412SE → FR in AAB61575. Ref.2
Sequence conflict1941S → T in AAC53151. Ref.1
Sequence conflict2561V → I in AAB61575. Ref.2
Sequence conflict2861S → T in AAB61575. Ref.2
Sequence conflict4201G → S in AAB61575. Ref.2
Sequence conflict5121S → N in AAB61575. Ref.2
Sequence conflict5941E → K in AAB61575. Ref.2
Sequence conflict607 – 6082EE → KK in AAB61575. Ref.2
Sequence conflict8641R → C in AAB61575. Ref.2
Sequence conflict8691T → S in AAB61575. Ref.2
Sequence conflict8841N → Y in AAB61575. Ref.2
Sequence conflict9721M → K in AAB61575. Ref.2
Sequence conflict9801M → K in AAB61575. Ref.2
Sequence conflict9911R → G in AAB61575. Ref.2
Sequence conflict9961P → L in AAB61575. Ref.2
Sequence conflict14071G → C in AAC53151. Ref.1
Sequence conflict14461P → L in AAB61575. Ref.2

Secondary structure

..... 1462
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q61026 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 619462FF1ACC6067

FASTA1,462158,466
        10         20         30         40         50         60 
MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRSTEKRNRE QENKYIEELA ELIFANFNDI 

        70         80         90        100        110        120 
DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS DVSSTGQGVI DKDALGPMML 

       130        140        150        160        170        180 
EALDGFFFVV NLEGSVVFVS ENVTQYLRYN QEELMNKSVY SILHVGDHTE FVKNLLPKSM 

       190        200        210        220        230        240 
VNGGSWSGEP PRRSSHTFNC RMLVKPLPDS EEEGHDSQEA HQKYEAMQCF AVSQPKSIKE 

       250        260        270        280        290        300 
EGEDLQSCLI CVARRVPMKE RPTLPSSESF TTRQDLQGKI TSLDTSTMRA AMKPGWEDLV 

       310        320        330        340        350        360 
RRCIQKFHTQ HEGESLSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ TKSKLIRSQT 

       370        380        390        400        410        420 
TNEPQLVISL HMLHREQNVC VMNPDLTGQA MGKPLNPISS SSPAHQALCS GNPGQDMTLG 

       430        440        450        460        470        480 
SNINFPMNGP KEQMGMPMGR FGGSGGMNHV SGMQATTPQG SNYALKMNSP SQSSPGMNPG 

       490        500        510        520        530        540 
QASSVLSPRQ RMSPGVAGSP RIPPSQFSPA GSLHSPVGVC SSTGNSHSYT NSSLNALQAL 

       550        560        570        580        590        600 
SEGHGVSLGS SLASPDLKMG NLQNSPVNMN PPPLSKMGSL DSKDCFGLYG EPSEGTTGQA 

       610        620        630        640        650        660 
EASCHPEEQK GPNDSSMPQA ASGDRAEGHS RLHDSKGQTK LLQLLTTKSD QMEPSPLPSS 

       670        680        690        700        710        720 
LSDTNKDSTG SLPGPGSTHG TSLKEKHKIL HRLLQDSSSP VDLAKLTAEA TGKELSQESS 

       730        740        750        760        770        780 
STAPGSEVTV KQEPASPKKK ENALLRYLLD KDDTKDIGLP EITPKLERLD SKTDPASNTK 

       790        800        810        820        830        840 
LIAMKTVKEE VSFEPSDQPG SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP TGSVDKQAII 

       850        860        870        880        890        900 
NDLMQLTADS SPVPPAGAQK AALRMSQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG 

       910        920        930        940        950        960 
PFPPIRNSSP YSVIPQPGMM GNQGMLGSQG NLGNNSTGMI GSSTSRPSMP SGEWAPQSPA 

       970        980        990       1000       1010       1020 
VRVTCAATTG AMNRPVQGGM IRNPTASIPM RANSQPGQRQ MLQSQVMNIG PSELEMNMGG 

      1030       1040       1050       1060       1070       1080 
PQYNQQQAPP NQTAPWPESI LPIDQASFAS QNRQPFGSSP DDLLCPHPAA ESPSDEGALL 

      1090       1100       1110       1120       1130       1140 
DQLYLALRNF DGLEEIDRAL GIPELVSQSQ AVDAEQFSSQ ESSIMLEQKP PVFPQQYASQ 

      1150       1160       1170       1180       1190       1200 
AQMAQGGYNP MQDPNFHTMG QRPNYTTLRM QPRPGLRPTG IVQNQPNQLR LQLQHRLQAQ 

      1210       1220       1230       1240       1250       1260 
QNRQPLMNQI SSVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR QMQQQVQQRT 

      1270       1280       1290       1300       1310       1320 
LMMRGQGLNV TPSMVAPAGL PAAMSNPRIP QANAQQFPFP PNYGISQQPD PGFTGATTPQ 

      1330       1340       1350       1360       1370       1380 
SPLMSPRMAH TQSPMMQQSQ ANPAYQPTSD MNGWAQGSMG GNSMFSQQSP PHFGQQANTS 

      1390       1400       1410       1420       1430       1440 
MYSNNMNISV SMATNTGGLS SMNQMTGQMS MTSVTSVPTS GLPSMGPEQV NDPALRGGNL 

      1450       1460 
FPNQLPGMDM IKQEGDASRK YC 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[11]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"Suppression of TH17 differentiation and autoimmunity by a synthetic ROR ligand."
Solt L.A., Kumar N., Nuhant P., Wang Y., Lauer J.L., Liu J., Istrate M.A., Kamenecka T.M., Roush W.R., Vidovic D., Schuerer S.C., Xu J., Wagoner G., Drew P.D., Griffin P.R., Burris T.P.
Nature 472:491-494(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U39060 mRNA. Translation: AAC53151.1.
AF000582 mRNA. Translation: AAB61575.1. Frameshift.
AC091248 Genomic DNA. No translation available.
AC121538 Genomic DNA. No translation available.
PIRT30193.
T42639.
RefSeqNP_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.
UniGeneMm.2537.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ61026.
SMRQ61026. Positions 34-376, 1071-1113.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201708. 12 interactions.
DIPDIP-5979N.
IntActQ61026. 4 interactions.
MINTMINT-236676.

PTM databases

PhosphoSiteQ61026.

Proteomic databases

PaxDbQ61026.
PRIDEQ61026.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006037; ENSMUSP00000006037; ENSMUSG00000005886.
GeneID17978.
KEGGmmu:17978.
UCSCuc007aim.1. mouse.

Organism-specific databases

CTD10499.
MGIMGI:1276533. Ncoa2.

Phylogenomic databases

eggNOGNOG315556.
GeneTreeENSGT00530000063109.
HOGENOMHOG000230947.
HOVERGENHBG052583.
InParanoidQ61026.
KOK11255.
OMATGMIGSN.
OrthoDBEOG72JWFB.
TreeFamTF332652.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Gene expression databases

ArrayExpressQ61026.
BgeeQ61026.
CleanExMM_GRIP1.
MM_NCOA2.
GenevestigatorQ61026.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProIPR011598. 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]
PANTHERPTHR10684. PTHR10684. 1 hit.
PTHR10684:SF2. PTHR10684:SF2. 1 hit.
PfamPF07469. DUF1518. 1 hit.
PF08815. Nuc_rec_co-act. 1 hit.
PF00989. PAS. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view]
PIRSFPIRSF038181. Nuclear_receptor_coactivator. 1 hit.
SMARTSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNCOA2. mouse.
EvolutionaryTraceQ61026.
NextBio292941.
PROQ61026.
SOURCESearch...

Entry information

Entry nameNCOA2_MOUSE
AccessionPrimary (citable) accession number: Q61026
Secondary accession number(s): E9QMH9, O09001, P97759
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot