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Q3U182

- CRTC2_MOUSE

UniProt

Q3U182 - CRTC2_MOUSE

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Protein
CREB-regulated transcription coactivator 2
Gene
Crtc2, Torc2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates gluconeogenesis as a component of the LKB1/AMPK/TORC2 signaling pathway. Regulates the expression of specific genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells By similarity.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei628 – 6281Required for ubiquitination and degradation

GO - Molecular functioni

  1. cAMP response element binding protein binding Source: InterPro
  2. protein binding Source: MGI
Complete GO annotation...

GO - Biological processi

  1. gluconeogenesis Source: UniProtKB
  2. glucose homeostasis Source: UniProtKB
  3. histone H3-K9 acetylation Source: MGI
  4. positive regulation of CREB transcription factor activity Source: UniProtKB
  5. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  6. protein homotetramerization Source: InterPro
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
CREB-regulated transcription coactivator 2
Alternative name(s):
Transducer of regulated cAMP response element-binding protein 2
Short name:
TORC-2
Short name:
Transducer of CREB protein 2
Gene namesi
Name:Crtc2
Synonyms:Torc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1921593. Crtc2.

Subcellular locationi

Cytoplasm. Nucleus
Note: Translocated from the nucleus to the cytoplasm on interaction of the phosphorylated form with 14-3-3 protein. In response to cAMP levels and glucagon, relocated to the nucleus.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi171 – 1711S → A: Upregulates CREB-mediated gluconeogenic gene expression. No degradation of CRTC2. Loss of SIK2-mediated phosphorylation. 1 Publication
Mutagenesisi213 – 2131K → R: No effect on COP1-mediated degradation of TORC1 under forksolin stimulation.
Mutagenesisi214 – 2141V → A: No interaction with RFWD2/COP1. Inhibition of degradation under exposure to FSK/INS. 1 Publication
Mutagenesisi215 – 2151P → A: No interaction with RFWD2/COP1. Inhibition of degradation under exposure to FSK/INS. 1 Publication
Mutagenesisi628 – 6281K → R: Translocates to the nucleus and no COP1-mediated degradation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 692691CREB-regulated transcription coactivator 2
PRO_0000318529Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei51 – 511Asymmetric dimethylarginine; by PRMT61 Publication
Modified residuei70 – 701Phosphoserine By similarity
Modified residuei86 – 861Phosphoserine By similarity
Modified residuei90 – 901Phosphoserine By similarity
Modified residuei99 – 991Asymmetric dimethylarginine; by PRMT61 Publication
Modified residuei120 – 1201Asymmetric dimethylarginine; by PRMT61 Publication
Modified residuei123 – 1231Asymmetric dimethylarginine; by PRMT61 Publication
Modified residuei136 – 1361Phosphoserine By similarity
Modified residuei161 – 1611Asymmetric dimethylarginine; by PRMT61 Publication
Modified residuei168 – 1681Asymmetric dimethylarginine; by PRMT61 Publication
Modified residuei171 – 1711Phosphoserine; by AMPK, MARK2, SIK1 and SIK23 Publications
Modified residuei192 – 1921Phosphothreonine By similarity
Modified residuei275 – 2751Phosphoserine; by MARK2 By similarity
Modified residuei307 – 3071Phosphoserine By similarity
Modified residuei369 – 3691Phosphoserine By similarity
Modified residuei394 – 3941Phosphoserine By similarity
Modified residuei434 – 4341Phosphoserine By similarity
Modified residuei457 – 4571Phosphoserine By similarity
Modified residuei489 – 4891Phosphotyrosine
Modified residuei490 – 4901Phosphoserine By similarity
Modified residuei493 – 4931Phosphoserine By similarity
Modified residuei502 – 5021Phosphothreonine By similarity
Modified residuei612 – 6121Phosphoserine1 Publication
Modified residuei623 – 6231Phosphoserine By similarity

Post-translational modificationi

Phosphorylation/dephosphorylation states of Ser-171 are required for regulating transduction of CREB activity. TORCs are inactive when phosphorylated, and active when dephosphorylated at this site. This primary site of phosphorylation, is regulated by cAMP and calcium levels and is dependent on the phosphorylation of SIKs (SIK1 and SIK2) by LKB1. Phosphorylation at Ser-275 by MARK2 is induced under low glucose conditions and dephosphorylated in response to glucose influx. Both insulin and AMPK increase this phosphorylation of CRTC2 while glucagon suppresses it. Phosphorylation at Ser-275 promotes interaction with 14-3-3 proteins and translocation to the cytoplasm By similarity.3 Publications
Asymmetric dimethylation of arginine resisues by PRMT6 enhances the association of CRTC2 with CREB on the promoters of gluconeogenic genes.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ3U182.
PaxDbiQ3U182.
PRIDEiQ3U182.

Expressioni

Gene expression databases

ArrayExpressiQ3U182.
BgeeiQ3U182.
CleanExiMM_CRTC2.
GenevestigatoriQ3U182.

Interactioni

Subunit structurei

Binds, as a tetramer, through its N-terminal region, with the bZIP domain of CREB1. 'Arg-314' in the bZIP domain of CREB1 is essential for this interaction. Interaction, via its C-terminal, with TAF4, enhances recruitment of TAF4 to CREB1 By similarity. Interacts with PPP3CA/calcineurin alpha, SIK2 and 14-3-3 proteins, YWHAB and YWHAG By similarity. Interaction with RFWD2/COP1 mediates nuclear export and degradation of CRTC2.1 Publication

Protein-protein interaction databases

DIPiDIP-46162N.
IntActiQ3U182. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ3U182.
SMRiQ3U182. Positions 20-47.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni209 – 2157Required for interaction with RFWD2/COP1
Regioni272 – 28817Nuclear export signal By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi237 – 2415Poly-Ser
Compositional biasi337 – 41377Ser-rich
Add
BLAST

Sequence similaritiesi

Belongs to the TORC family.

Phylogenomic databases

eggNOGiNOG74259.
GeneTreeiENSGT00390000010652.
HOGENOMiHOG000111980.
HOVERGENiHBG058314.
InParanoidiQ3U182.
KOiK16333.
OMAiTHCSRHG.
OrthoDBiEOG7MKW5P.
PhylomeDBiQ3U182.
TreeFamiTF321571.

Family and domain databases

InterProiIPR024786. TORC.
IPR024785. TORC_C.
IPR024784. TORC_M.
IPR024783. TORC_N.
[Graphical view]
PANTHERiPTHR13589. PTHR13589. 1 hit.
PfamiPF12886. TORC_C. 1 hit.
PF12885. TORC_M. 1 hit.
PF12884. TORC_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3U182-1 [UniParc]FASTAAdd to Basket

« Hide

MATSGANGPG SATASASNPR KFSEKIALQK QRQAEETAAF EEVMMDIGST    50
RLQAQKLRLA YTRSSHYGGS LPNVNQIGCG LAEFQSPLHS PLDSSRSTRH 100
HGLVERVQRD ARRMVSPLRR YPRHIDSSPY SPAYLSPPPE SGWRRMMPWG 150
NLPAEKGQLF RLPSALNRTS SDSALHTSVM NPNPQDTYPG PTPPSVLPSR 200
RGGGFLDGEM DAKVPAIEEN VVDDKHLLKP WDAKKLSSSS SRPRSCEVPG 250
INIFPSPDQP ANVPVLPPAM NTGGSLPDLT NLHFPPPLPT PLDPEETVYP 300
SLSGGNSTTN LTHTMTHLGI SGGLGLGPSY DVPGLHSPLS HPSLQSSLSN 350
PNLQASLSSP QPQLQGSHSH PSLPASSLAH HALPTTSLGH PSLSAPALSS 400
SSSSSSTSSP VLSAPPYPAS TPGASPRHRR VPLSPLSLPA GPADARRSQQ 450
QLPKQFSPTM SPTLSSITQG VPLDTSKLPT DQRLPPYPYS PPSLVIPTHP 500
PTPKSLQQLP SQACLVQPSG GQPPGRQPHY GALYPPGSSG HGQQPYHRPI 550
NDFSLGNLEQ FNMESPSTSL VLDPPAFSEG PGFLGSEGSM SGPQDPHVLN 600
HQNLTHCSRH GSGPNIILTG DSSPGFSKEI AAALAGVPGF EVSASGLELG 650
LGLEDELRME PLGLEGLTML SDPCALLPDP AVEDSFRSDR LQ 692
Length:692
Mass (Da):73,216
Last modified:February 5, 2008 - v2
Checksum:i5BCBC416D45CFAD8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951S → G in BAE33618. 1 Publication
Sequence conflicti203 – 2031G → R in BAE42818. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK156192 mRNA. Translation: BAE33618.1.
AK172084 mRNA. Translation: BAE42818.1.
BC023831 mRNA. Translation: AAH23831.1.
BC032183 mRNA. Translation: AAH32183.1.
BC033300 mRNA. Translation: AAH33300.1.
CCDSiCCDS38501.1.
RefSeqiNP_083157.1. NM_028881.2.
UniGeneiMm.35627.

Genome annotation databases

EnsembliENSMUST00000029545; ENSMUSP00000029545; ENSMUSG00000027936.
GeneIDi74343.
KEGGimmu:74343.
UCSCiuc008qbt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK156192 mRNA. Translation: BAE33618.1 .
AK172084 mRNA. Translation: BAE42818.1 .
BC023831 mRNA. Translation: AAH23831.1 .
BC032183 mRNA. Translation: AAH32183.1 .
BC033300 mRNA. Translation: AAH33300.1 .
CCDSi CCDS38501.1.
RefSeqi NP_083157.1. NM_028881.2.
UniGenei Mm.35627.

3D structure databases

ProteinModelPortali Q3U182.
SMRi Q3U182. Positions 20-47.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-46162N.
IntActi Q3U182. 1 interaction.

Proteomic databases

MaxQBi Q3U182.
PaxDbi Q3U182.
PRIDEi Q3U182.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029545 ; ENSMUSP00000029545 ; ENSMUSG00000027936 .
GeneIDi 74343.
KEGGi mmu:74343.
UCSCi uc008qbt.2. mouse.

Organism-specific databases

CTDi 200186.
MGIi MGI:1921593. Crtc2.

Phylogenomic databases

eggNOGi NOG74259.
GeneTreei ENSGT00390000010652.
HOGENOMi HOG000111980.
HOVERGENi HBG058314.
InParanoidi Q3U182.
KOi K16333.
OMAi THCSRHG.
OrthoDBi EOG7MKW5P.
PhylomeDBi Q3U182.
TreeFami TF321571.

Miscellaneous databases

NextBioi 340497.
PROi Q3U182.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q3U182.
Bgeei Q3U182.
CleanExi MM_CRTC2.
Genevestigatori Q3U182.

Family and domain databases

InterProi IPR024786. TORC.
IPR024785. TORC_C.
IPR024784. TORC_M.
IPR024783. TORC_N.
[Graphical view ]
PANTHERi PTHR13589. PTHR13589. 1 hit.
Pfami PF12886. TORC_C. 1 hit.
PF12885. TORC_M. 1 hit.
PF12884. TORC_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Spleen.
  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].
    Strain: FVB/N.
    Tissue: Liver, Mammary tumor and Salivary gland.
  3. Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-171, TISSUE SPECIFICITY.
  4. "The kinase LKB1 mediates glucose homeostasis in liver and therapeutic effects of metformin."
    Shaw R.J., Lamia K.A., Vasquez D., Koo S.-H., Bardeesy N., Depinho R.A., Montminy M., Cantley L.C.
    Science 310:1642-1646(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-171, SUBCELLULAR LOCATION.
  5. "Insulin modulates gluconeogenesis by inhibition of the coactivator TORC2."
    Dentin R., Liu Y., Koo S.-H., Hedrick S., Vargas T., Heredia J., Yates J. III, Montminy M.
    Nature 449:366-369(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RFWD2, PHOSPHORYLATION AT SER-171, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-171; VAL-214; PRO-215 AND LYS-628.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Arginine methylation of CRTC2 is critical in the transcriptional control of hepatic glucose metabolism."
    Han H.S., Jung C.Y., Yoon Y.S., Choi S., Choi D., Kang G., Park K.G., Kim S.T., Koo S.H.
    Sci. Signal. 7:RA19-RA19(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-51; ARG-99; ARG-120; ARG-123; ARG-161 AND ARG-168.

Entry informationi

Entry nameiCRTC2_MOUSE
AccessioniPrimary (citable) accession number: Q3U182
Secondary accession number(s): Q3TA52, Q8BH09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: September 3, 2014
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi