Q53ET0 (CRTC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CRTC2
Synonyms:	TORC2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	693 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from sequence or structural similarity. Source: UniProtKB glucose homeostasis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of CREB transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB protein homotetramerization Inferred from electronic annotation. Source: InterPro transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA
Molecular_function	cAMP response element binding protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SIK1	P57059	1	EBI-1181987,EBI-1181640
SIK3	Q9Y2K2	1	EBI-1181987,EBI-1181460

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 693

693

CREB-regulated transcription coactivator 2

PRO_0000318528

Regions

Motif

271 – 287

17

Nuclear export signal By similarity

Compositional bias

236 – 240

5

Poly-Ser

Compositional bias

336 – 408

73

Ser-rich

Sites

Site

629

1

Required for ubiquitination and degradation By similarity

Amino acid modifications

Modified residue

70

1

Phosphoserine Ref.6 Ref.15 Ref.16

Modified residue

86

1

Phosphoserine Ref.15 Ref.16

Modified residue

90

1

Phosphoserine Ref.6 Ref.15 Ref.16

Modified residue

136

1

Phosphoserine Ref.6 Ref.15

Modified residue

169

1

Phosphothreonine By similarity

Modified residue

171

1

Phosphoserine; by AMPK, MARK2, SIK1 and SIK2 Ref.6 Ref.8 Ref.12 Ref.14

Modified residue

177

1

Phosphothreonine By similarity

Modified residue

192

1

Phosphothreonine Ref.16

Modified residue

274

1

Phosphoserine; by MARK2 Ref.14

Modified residue

306

1

Phosphoserine Ref.6

Modified residue

368

1

Phosphoserine Ref.6

Modified residue

393

1

Phosphoserine Ref.6

Modified residue

433

1

Phosphoserine Ref.6 Ref.10 Ref.13 Ref.15 Ref.16

Modified residue

456

1

Phosphoserine Ref.6

Modified residue

488

1

Phosphotyrosine Ref.16

Modified residue

489

1

Phosphoserine Ref.6

Modified residue

490

1

Phosphoserine Ref.16

Modified residue

492

1

Phosphoserine Ref.6

Modified residue

501

1

Phosphothreonine Ref.15 Ref.17

Modified residue

613

1

Phosphoserine Ref.6 Ref.15 Ref.16 Ref.17

Modified residue

624

1

Phosphoserine Ref.15 Ref.16 Ref.17

Natural variations

Natural variant

147

1

M → V.
Corresponds to variant rs11264680 [ dbSNP | Ensembl ].

VAR_038756

Natural variant

379

1

R → C. Ref.1 Ref.20

VAR_038757

Experimental info

Mutagenesis

70

1

S → A: No effect on cAMP- and calcium-regulated phosphorylation.

Mutagenesis

171

1

S → 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

Mutagenesis

274

1

S → A: Impaired phosphorylation under low glucose conditions and impaired interaction with 14-3-3 proteins; when associated with A-171. Ref.14

Mutagenesis

368

1

S → A: Reduced cAMP- and calcium-regulated phosphorylation. Ref.6 Ref.14

Mutagenesis

393

1

S → A: No effect on cAMP- and calcium-regulated phosphorylation.

Sequence conflict

323 – 325

3

MGL → HGP in AAQ98857. Ref.1

Sequence conflict

499

1

P → S in BAD97279. Ref.2

Secondary structure

1

.

.

.

693

Helix Strand Turn

Details...

Helix

21 – 45

25

Sequences

	Sequence		Length	Mass (Da)
	Q53ET0 [UniParc]. Last modified February 5, 2008. Version 2. Checksum: EE6C52E0ECDC1DF1	FASTA	693	73,302
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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].
[19]	"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].
[20]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00783502.

RefSeq

NP_859066.1. NM_181715.2.

UniGene

Hs.406392.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4HTM	X-ray	2.00	A	18-50	[»]

ProteinModelPortal

Q53ET0.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29950N.

IntAct

Q53ET0. 3 interactions.

MINT

MINT-1631979.

STRING

9606.ENSP00000305873.

PTM databases

PhosphoSite

Q53ET0.

Polymorphism databases

DMDM

167009135.

Proteomic databases

PaxDb

Q53ET0.

PRIDE

Q53ET0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368633; ENSP00000357622; ENSG00000160741.

GeneID

200186.

KEGG

hsa:200186.

UCSC

uc021pab.1. human.

Organism-specific databases

CTD

200186.

GeneCards

GC01M153920.

HGNC

HGNC:27301. CRTC2.

HPA

HPA028454.
HPA028465.

MIM

608972. gene.

neXtProt

NX_Q53ET0.

PharmGKB

PA142672073.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG74259.

HOGENOM

HOG000111980.

HOVERGEN

HBG058314.

InParanoid

Q53ET0.

KO

K16333.

OMA

THCSRHG.

OrthoDB

EOG4RBQJC.

Gene expression databases

ArrayExpress

Q53ET0.

Bgee

Q53ET0.

CleanEx

HS_CRTC2.

Genevestigator

Q53ET0.

Family and domain databases

InterPro

IPR024786. TORC.
IPR024785. TORC_C.
IPR024784. TORC_M.
IPR024783. TORC_N.
[Graphical view]

PANTHER

PTHR13589. PTHR13589. 1 hit.

Pfam

PF12886. TORC_C. 1 hit.
PF12885. TORC_M. 1 hit.
PF12884. TORC_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

200186.

NextBio

89862.

SOURCE

Search...

Entry information

Entry name

CRTC2_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.