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Q53ET0 (CRTC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CRTC2
Synonyms:TORC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length693 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 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. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR). Ref.1 Ref.5 Ref.6 Ref.8 Ref.9 Ref.11 Ref.12

Subunit structure

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 the human T-cell leukemia virus type 1 (HTLV-1) Tax protein is essential for optimal transcription activation by Tax. Interaction with RFWD2/COP1 mediates nuclear export and degradation of CRTC2 By similarity. Ref.6 Ref.9 Ref.14

Subcellular location

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. Ref.6 Ref.7 Ref.8

Tissue specificity

Most abundantly expressed in the thymus. Present in both B and T-lymphocytes. Highly expressed in HEK293T cells and in insulinomas. High levels also in spleen, ovary, muscle and lung, with highest levels in muscle. Lower levels found in brain, colon, heart, kidney, prostate, small intestine and stomach. Weak expression in liver and pancreas. Ref.5 Ref.6 Ref.11

Post-translational modification

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. Both insulin and AMPK increase this phosphorylation of CRTC2 while glucagon suppresses it. Phosphorylation at Ser-274 by MARK2 is induced under low glucose conditions and dephosphorylated in response to glucose influx. Phosphorylation at Ser-274 promotes interaction with 14-3-3 proteins and translocation to the cytoplasm. Ref.6 Ref.7 Ref.8 Ref.12 Ref.14

Polymorphism

Variant Cys-379, under a dominant model, linked to a recessive mutation in LKB1, may be associated with susceptibility to type II or non-insulin-dependent diabetes mellitus (NIDDM).

Sequence similarities

Belongs to the TORC family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.16
Chain2 – 693692CREB-regulated transcription coactivator 2
PRO_0000318528

Regions

Motif271 – 28717Nuclear export signal By similarity
Compositional bias236 – 2405Poly-Ser
Compositional bias336 – 40873Ser-rich

Sites

Site6291Required for ubiquitination and degradation By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.16 Ref.21
Modified residue701Phosphoserine Ref.6 Ref.15 Ref.17
Modified residue861Phosphoserine Ref.15 Ref.17
Modified residue901Phosphoserine Ref.6 Ref.15 Ref.17
Modified residue1361Phosphoserine Ref.6 Ref.15
Modified residue1711Phosphoserine; by AMPK, MARK2, SIK1 and SIK2 Ref.6 Ref.8 Ref.12 Ref.14
Modified residue1921Phosphothreonine Ref.17
Modified residue2741Phosphoserine; by MARK2 Ref.14
Modified residue3061Phosphoserine Ref.6
Modified residue3681Phosphoserine Ref.6
Modified residue3931Phosphoserine Ref.6
Modified residue4331Phosphoserine Ref.6 Ref.10 Ref.13 Ref.15 Ref.17
Modified residue4561Phosphoserine Ref.6
Modified residue4881Phosphotyrosine Ref.17
Modified residue4891Phosphoserine Ref.6
Modified residue4901Phosphoserine Ref.17
Modified residue4921Phosphoserine Ref.6
Modified residue5011Phosphothreonine Ref.15 Ref.18
Modified residue6131Phosphoserine Ref.6 Ref.15 Ref.17 Ref.18
Modified residue6241Phosphoserine Ref.15 Ref.17 Ref.18

Natural variations

Natural variant1471M → V.
Corresponds to variant rs11264680 [ dbSNP | Ensembl ].
VAR_038756
Natural variant3791R → C. Ref.1 Ref.22
Corresponds to variant rs150423770 [ dbSNP | Ensembl ].
VAR_038757

Experimental info

Mutagenesis701S → A: No effect on cAMP- and calcium-regulated phosphorylation.
Mutagenesis1711S → A: Loss of cAMP- and calcium-regulated phosphorylation. Greatly reduced interaction with 14-3-3 proteins. Impaired phosphorylation under low glucose conditions and impaired interaction with 14-3-3 proteins; when associated with A-274. Ref.6 Ref.8 Ref.14
Mutagenesis2741S → A: Impaired phosphorylation under low glucose conditions and impaired interaction with 14-3-3 proteins; when associated with A-171. Ref.14
Mutagenesis3681S → A: Reduced cAMP- and calcium-regulated phosphorylation. Ref.6 Ref.14
Mutagenesis3931S → A: No effect on cAMP- and calcium-regulated phosphorylation.
Sequence conflict323 – 3253MGL → HGP in AAQ98857. Ref.1
Sequence conflict4991P → S in BAD97279. Ref.2

Secondary structure

... 693
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q53ET0 [UniParc].

Last modified February 5, 2008. Version 2.
Checksum: EE6C52E0ECDC1DF1

FASTA69373,302
        10         20         30         40         50         60 
MATSGANGPG SATASASNPR KFSEKIALQK QRQAEETAAF EEVMMDIGST RLQAQKLRLA 

        70         80         90        100        110        120 
YTRSSHYGGS LPNVNQIGSG LAEFQSPLHS PLDSSRSTRH HGLVERVQRD PRRMVSPLRR 

       130        140        150        160        170        180 
YTRHIDSSPY SPAYLSPPPE SSWRRTMAWG NFPAEKGQLF RLPSALNRTS SDSALHTSVM 

       190        200        210        220        230        240 
NPSPQDTYPG PTPPSILPSR RGGILDGEMD PKVPAIEENL LDDKHLLKPW DAKKLSSSSS 

       250        260        270        280        290        300 
RPRSCEVPGI NIFPSPDQPA NVPVLPPAMN TGGSLPDLTN LHFPPPLPTP LDPEETAYPS 

       310        320        330        340        350        360 
LSGGNSTSNL THTMTHLGIS RGMGLGPGYD APGLHSPLSH PSLQSSLSNP NLQASLSSPQ 

       370        380        390        400        410        420 
PQLQGSHSHP SLPASSLARH VLPTTSLGHP SLSAPALSSS SSSSSTSSPV LGAPSYPAST 

       430        440        450        460        470        480 
PGASPHHRRV PLSPLSLLAG PADARRSQQQ LPKQFSPTMS PTLSSITQGV PLDTSKLSTD 

       490        500        510        520        530        540 
QRLPPYPYSS PSLVLPTQPH TPKSLQQPGL PSQSCSVQSS GGQPPGRQSH YGTPYPPGPS 

       550        560        570        580        590        600 
GHGQQSYHRP MSDFNLGNLE QFSMESPSAS LVLDPPGFSE GPGFLGGEGP MGGPQDPHTF 

       610        620        630        640        650        660 
NHQNLTHCSR HGSGPNIILT GDSSPGFSKE IAAALAGVPG FEVSAAGLEL GLGLEDELRM 

       670        680        690 
EPLGLEGLNM LSDPCALLPD PAVEESFRSD RLQ 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells."
Iourgenko V., Zhang W., Mickanin C., Daly I., Jiang C., Hexham J.M., Orth A.P., Miraglia L., Meltzer J., Garza D., Chirn G.-W., McWhinnie E., Cohen D., Skelton J., Terry R., Yu Y., Bodian D., Buxton F.P. expand/collapse author list , Zhu J., Song C., Labow M.A.
Proc. Natl. Acad. Sci. U.S.A. 100:12147-12152(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CYS-379, FUNCTION.
[2]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Tissue: Brain.
[4]"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].
Tissue: PNS.
[5]"TORCs: transducers of regulated CREB activity."
Conkright M.D., Canettieri G., Screaton R., Guzman E., Miraglia L., Hogenesch J.B., Montminy M.
Mol. Cell 12:413-423(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[6]"The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector."
Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G., Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H., Okamoto M., Montminy M.
Cell 119:61-74(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CREB1; SIK2; PPP3CA; YWHAB AND YWHAG, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, PHOSPHORYLATION AT SER-70; SER-90; SER-136; SER-171; SER-306; SER-368; SER-393; SER-433; SER-456; SER-489; SER-492 AND SER-613, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-171 AND SER-368.
[7]"Activation of cAMP response element-mediated gene expression by regulated nuclear transport of TORC proteins."
Bittinger M.A., McWhinnie E., Meltzer J., Iourgenko V., Latario B., Liu X., Chen C.H., Song C., Garza D., Labow M.
Curr. Biol. 14:2156-2161(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[8]"Silencing the constitutive active transcription factor CREB by the LKB1-SIK signaling cascade."
Katoh Y., Takemori H., Lin X.-Z., Tamura M., Muraoka M., Satoh T., Tsuchiya Y., Min L., Doi J., Miyauchi A., Witters L.A., Nakamura H., Okamoto M.
FEBS J. 273:2730-2748(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-171, MUTAGENESIS OF SER-171.
[9]"TORC1 and TORC2 coactivators are required for tax activation of the human T-cell leukemia virus type 1 long terminal repeats."
Siu Y.-T., Chin K.-T., Siu K.-L., Yee Wai Choy E., Jeang K.-T., Jin D.-Y.
J. Virol. 80:7052-7059(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTLV-1 TAX, FUNCTION.
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Transducer of regulated CREB-binding proteins (TORCs) induce PGC-1alpha transcription and mitochondrial biogenesis in muscle cells."
Wu Z., Huang X., Feng Y., Handschin C., Feng Y., Gullicksen P.S., Bare O., Labow M., Spiegelman B., Stevenson S.C.
Proc. Natl. Acad. Sci. U.S.A. 103:14379-14384(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]"Dephosphorylation of TORC initiates expression of the StAR gene."
Takemori H., Kanematsu M., Kajimura J., Hatano O., Katoh Y., Lin X.-Z., Min L., Yamazaki T., Doi J., Okamoto M.
Mol. Cell. Endocrinol. 265:196-204(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-171.
[13]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Glucose controls CREB activity in islet cells via regulated phosphorylation of TORC2."
Jansson D., Ng A.C., Fu A., Depatie C., Al Azzabi M., Screaton R.A.
Proc. Natl. Acad. Sci. U.S.A. 105:10161-10166(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-171 AND SER-274, INTERACTION WITH 14-3-3, MUTAGENESIS OF SER-171; SER-274 AND SER-368.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-86; SER-90; SER-136; SER-433; THR-501; SER-613 AND SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[17]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-86; SER-90; THR-192; SER-433; TYR-488; SER-490; SER-613 AND SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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 THR-501; SER-613 AND SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Single nucleotide polymorphisms in genes encoding LKB1 (STK11), TORC2 (CRTC2) and AMPK alpha2-subunit (PRKAA2) and risk of type 2 diabetes."
Keshavarz P., Inoue H., Nakamura N., Yoshikawa T., Tanahashi T., Itakura M.
Mol. Genet. Metab. 93:200-209(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-379, INVOLVEMENT IN SUSCEPTIBILITY TO NIDDM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY360172 mRNA. Translation: AAQ98857.1.
AK223559 mRNA. Translation: BAD97279.1.
AL358472 Genomic DNA. Translation: CAI14017.1.
BC053562 mRNA. Translation: AAH53562.1.
RefSeqNP_859066.1. NM_181715.2.
UniGeneHs.406392.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4HTMX-ray2.00A18-50[»]
ProteinModelPortalQ53ET0.
SMRQ53ET0. Positions 20-47.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128308. 10 interactions.
DIPDIP-29950N.
IntActQ53ET0. 5 interactions.
MINTMINT-1631979.
STRING9606.ENSP00000305873.

PTM databases

PhosphoSiteQ53ET0.

Polymorphism databases

DMDM167009135.

Proteomic databases

PaxDbQ53ET0.
PRIDEQ53ET0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368633; ENSP00000357622; ENSG00000160741.
GeneID200186.
KEGGhsa:200186.
UCSCuc021pab.1. human.

Organism-specific databases

CTD200186.
GeneCardsGC01M153920.
HGNCHGNC:27301. CRTC2.
HPAHPA028454.
HPA028465.
MIM608972. gene.
neXtProtNX_Q53ET0.
PharmGKBPA142672073.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG74259.
HOGENOMHOG000111980.
HOVERGENHBG058314.
InParanoidQ53ET0.
KOK16333.
OMATHCSRHG.
OrthoDBEOG7MKW5P.
PhylomeDBQ53ET0.
TreeFamTF321571.

Gene expression databases

ArrayExpressQ53ET0.
BgeeQ53ET0.
CleanExHS_CRTC2.
GenevestigatorQ53ET0.

Family and domain databases

InterProIPR024786. TORC.
IPR024785. TORC_C.
IPR024784. TORC_M.
IPR024783. TORC_N.
[Graphical view]
PANTHERPTHR13589. PTHR13589. 1 hit.
PfamPF12886. TORC_C. 1 hit.
PF12885. TORC_M. 1 hit.
PF12884. TORC_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCRTC2.
GenomeRNAi200186.
NextBio89862.
PROQ53ET0.
SOURCESearch...

Entry information

Entry nameCRTC2_HUMAN
AccessionPrimary (citable) accession number: Q53ET0
Secondary accession number(s): Q6UUV8, Q7Z3X7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: April 16, 2014
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM