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Protein

CREB-regulated transcription coactivator 2

Gene

Crtc2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei627 – 6271Required for ubiquitination and degradationBy similarity

GO - Molecular functioni

  • cAMP response element binding protein binding Source: GO_Central
  • chromatin binding Source: RGD

GO - Biological processi

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi1308903. Crtc2.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • 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.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 691690CREB-regulated transcription coactivator 2PRO_0000318530Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei51 – 511Asymmetric dimethylarginine; by PRMT6By similarity
Modified residuei70 – 701PhosphoserineBy similarity
Modified residuei86 – 861PhosphoserineBy similarity
Modified residuei90 – 901PhosphoserineBy similarity
Modified residuei99 – 991Asymmetric dimethylarginine; by PRMT6By similarity
Modified residuei120 – 1201Asymmetric dimethylarginine; by PRMT6By similarity
Modified residuei123 – 1231Asymmetric dimethylarginine; by PRMT6By similarity
Modified residuei136 – 1361PhosphoserineBy similarity
Modified residuei161 – 1611Asymmetric dimethylarginine; by PRMT6By similarity
Modified residuei168 – 1681Asymmetric dimethylarginine; by PRMT6By similarity
Modified residuei171 – 1711Phosphoserine; by AMPK, MARK2, SIK1 and SIK2By similarity
Modified residuei192 – 1921PhosphothreonineBy similarity
Modified residuei274 – 2741Phosphoserine; by MARK2By similarity
Modified residuei306 – 3061PhosphoserineBy similarity
Modified residuei368 – 3681PhosphoserineBy similarity
Modified residuei393 – 3931PhosphoserineBy similarity
Modified residuei433 – 4331PhosphoserineBy similarity
Modified residuei456 – 4561PhosphoserineBy similarity
Modified residuei488 – 4881PhosphotyrosineBy similarity
Modified residuei489 – 4891PhosphoserineBy similarity
Modified residuei492 – 4921PhosphoserineBy similarity
Modified residuei501 – 5011PhosphothreonineBy similarity
Modified residuei611 – 6111PhosphoserineCombined sources
Modified residuei621 – 6211PhosphoserineBy similarity
Modified residuei622 – 6221PhosphoserineBy 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-274 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-274 promotes interaction with 14-3-3 proteins and translocation to the cytoplasm (By similarity).By similarity
Asymmetric dimethylation of arginine resisues by PRMT6 enhances the association of CRTC2 with CREB on the promoters of gluconeogenic genes.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ3LRZ1.
PRIDEiQ3LRZ1.

PTM databases

iPTMnetiQ3LRZ1.
PhosphoSiteiQ3LRZ1.

Expressioni

Gene expression databases

ExpressionAtlasiQ3LRZ1. differential.
GenevisibleiQ3LRZ1. RN.

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. Interaction with RFWD2/COP1 mediates nuclear export and degradation of CRTC2 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi259674. 3 interactions.
STRINGi10116.ENSRNOP00000021700.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi271 – 28717Nuclear export signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi236 – 2405Poly-Ser
Compositional biasi336 – 41277Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the TORC family.Curated

Phylogenomic databases

eggNOGiENOG410IGNT. Eukaryota.
ENOG410XPDQ. LUCA.
GeneTreeiENSGT00390000010652.
HOGENOMiHOG000111980.
HOVERGENiHBG058314.
InParanoidiQ3LRZ1.
KOiK16333.
PhylomeDBiQ3LRZ1.

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.

Q3LRZ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSGANGPG SATASASNPR KFSEKIALQK QRQAEETAAF EEVMMDIGST
60 70 80 90 100
RLQAQKLRLA YTRSSHYGGS LPNVNQIGCG LAEFQSPLHS PLDSSRSTRH
110 120 130 140 150
HGLVERVQRD PRRMVSPLRR YPRHIDSSPY SPAYLSPPPE SGWRRMMPWG
160 170 180 190 200
NLPAEKGQLF RLPSALNRTS SDSALHTSVM NPNPQDTYPG PTPPSVLPSR
210 220 230 240 250
RGGFLDGEMD AKVPAIEENL VDDKHLLKPW DAKKLSSSSS RPRSCEVPGI
260 270 280 290 300
NIFPSPDQPA NVPVLPPAMS TGGSLPDLTN LHFPPPLPTP LDPEETVYPS
310 320 330 340 350
LSGGNSTTNL THTMTHLGIS GGLGLGPSYD VPGLHSPLSH PSLQSSLSNP
360 370 380 390 400
NLQASLSSPQ PQLQGSHSHP SLPASSLAHH ALPTTSLGHP SLSAPALSSS
410 420 430 440 450
SSSSSTSSPV LSAPPYPAST PGASPRHRRV PLSPLSLPAG PADARRSQQQ
460 470 480 490 500
LPKQFSPTMS PTLSSITQGV PLDTSKLPTD QRLPPYPYSP PSLVIPSHPP
510 520 530 540 550
TPKSLQQLPS QACLVQPSGG QPPGRQPHYG TLYPPGSSGH GQQPYHRPIN
560 570 580 590 600
DFSLGNLEQF NMESPSTSLV LDPPAFSEGP GFLGSEGSVS GPQDSHVLNH
610 620 630 640 650
QNLTHCSRHG SGPNIILTGD SSPGFSKEIA AALAGVPGFE VSASGLELGL
660 670 680 690
GLEDELRMEP LGLEGLTMLS DPCALLPDPA VEDSFRSDRL Q
Length:691
Mass (Da):73,146
Last modified:October 25, 2005 - v1
Checksum:i8CC1DA5B06D890B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ185515 mRNA. Translation: ABA28301.1.
RefSeqiNP_001029067.1. NM_001033895.1.
UniGeneiRn.13599.

Genome annotation databases

EnsembliENSRNOT00000092144; ENSRNOP00000068813; ENSRNOG00000056337.
GeneIDi310615.
KEGGirno:310615.
UCSCiRGD:1308903. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ185515 mRNA. Translation: ABA28301.1.
RefSeqiNP_001029067.1. NM_001033895.1.
UniGeneiRn.13599.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi259674. 3 interactions.
STRINGi10116.ENSRNOP00000021700.

PTM databases

iPTMnetiQ3LRZ1.
PhosphoSiteiQ3LRZ1.

Proteomic databases

PaxDbiQ3LRZ1.
PRIDEiQ3LRZ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000092144; ENSRNOP00000068813; ENSRNOG00000056337.
GeneIDi310615.
KEGGirno:310615.
UCSCiRGD:1308903. rat.

Organism-specific databases

CTDi200186.
RGDi1308903. Crtc2.

Phylogenomic databases

eggNOGiENOG410IGNT. Eukaryota.
ENOG410XPDQ. LUCA.
GeneTreeiENSGT00390000010652.
HOGENOMiHOG000111980.
HOVERGENiHBG058314.
InParanoidiQ3LRZ1.
KOiK16333.
PhylomeDBiQ3LRZ1.

Miscellaneous databases

PROiQ3LRZ1.

Gene expression databases

ExpressionAtlasiQ3LRZ1. differential.
GenevisibleiQ3LRZ1. RN.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "TORC2 in central nervous system."
    Wu H., Miao S., Shen H., Xiong Z.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCRTC2_RAT
AccessioniPrimary (citable) accession number: Q3LRZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 25, 2005
Last modified: July 6, 2016
This is version 70 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.