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Protein

CREB-regulated transcription coactivator 2

Gene

CRTC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR).7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei629Required for ubiquitination and degradationBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator
Biological processHost-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-400253 Circadian Clock

SIGNOR Signaling Network Open Resource

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SIGNORi
Q53ET0

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CRTC2
Synonyms:TORC2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000160741.16

Human Gene Nomenclature Database

More...
HGNCi
HGNC:27301 CRTC2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
608972 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q53ET0

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi70S → A: No effect on cAMP- and calcium-regulated phosphorylation. 1
Mutagenesisi171S → 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. 3 Publications1
Mutagenesisi274S → A: Impaired phosphorylation under low glucose conditions and impaired interaction with 14-3-3 proteins; when associated with A-171. 1 Publication1
Mutagenesisi368S → A: Reduced cAMP- and calcium-regulated phosphorylation. 2 Publications1
Mutagenesisi393S → A: No effect on cAMP- and calcium-regulated phosphorylation. 1

Organism-specific databases

DisGeNET

More...
DisGeNETi
200186

Open Targets

More...
OpenTargetsi
ENSG00000160741

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA142672073

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CRTC2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
167009135

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003185282 – 693CREB-regulated transcription coactivator 2Add BLAST692

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1
Modified residuei51Asymmetric dimethylarginine; by PRMT6By similarity1
Modified residuei70PhosphoserineCombined sources1 Publication1
Modified residuei86PhosphoserineCombined sources1
Modified residuei90PhosphoserineCombined sources1 Publication1
Modified residuei99Asymmetric dimethylarginine; by PRMT6By similarity1
Modified residuei120Asymmetric dimethylarginine; by PRMT6By similarity1
Modified residuei123Asymmetric dimethylarginine; by PRMT6By similarity1
Modified residuei136PhosphoserineCombined sources1 Publication1
Modified residuei161Asymmetric dimethylarginine; by PRMT6By similarity1
Modified residuei168Asymmetric dimethylarginine; by PRMT6By similarity1
Modified residuei169PhosphothreonineBy similarity1
Modified residuei171Phosphoserine; by AMPK, MARK2, SIK1 and SIK24 Publications1
Modified residuei192PhosphothreonineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki234Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei274Phosphoserine; by MARK21 Publication1
Modified residuei306Phosphoserine1 Publication1
Modified residuei368Phosphoserine1 Publication1
Modified residuei393Phosphoserine1 Publication1
Modified residuei433PhosphoserineCombined sources1 Publication1
Modified residuei456Phosphoserine1 Publication1
Modified residuei488PhosphotyrosineCombined sources1
Modified residuei489Phosphoserine1 Publication1
Modified residuei490PhosphoserineCombined sources1
Modified residuei492Phosphoserine1 Publication1
Modified residuei501PhosphothreonineCombined sources1
Modified residuei613PhosphoserineCombined sources1 Publication1
Modified residuei623PhosphoserineBy similarity1
Modified residuei624PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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. 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.5 Publications
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, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q53ET0

MaxQB - The MaxQuant DataBase

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MaxQBi
Q53ET0

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q53ET0

PeptideAtlas

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PeptideAtlasi
Q53ET0

PRoteomics IDEntifications database

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PRIDEi
Q53ET0

ProteomicsDB human proteome resource

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ProteomicsDBi
62448

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q53ET0

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q53ET0

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000160741 Expressed in 171 organ(s), highest expression level in small intestine Peyer's patch

CleanEx database of gene expression profiles

More...
CleanExi
HS_CRTC2

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q53ET0 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q53ET0 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA028454
HPA028465

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 and SIK2. Interacts with 14-3-3 proteins, YWHAB and YWHAG. Interaction with COP1 mediates nuclear export and degradation of CRTC2 (By similarity).By similarity
(Microbial infection) Interaction with the human T-cell leukemia virus type 1 (HTLV-1) Tax protein is essential for optimal transcription activation by Tax.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
128308, 38 interactors

Database of interacting proteins

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DIPi
DIP-29950N

Protein interaction database and analysis system

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IntActi
Q53ET0, 19 interactors

Molecular INTeraction database

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MINTi
Q53ET0

STRING: functional protein association networks

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STRINGi
9606.ENSP00000357622

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1693
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q53ET0

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q53ET0

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi271 – 287Nuclear export signalBy similarityAdd BLAST17

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi236 – 240Poly-Ser5
Compositional biasi336 – 408Ser-richAdd BLAST73

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the TORC family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IGNT Eukaryota
ENOG410XPDQ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000010652

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000111980

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG058314

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q53ET0

KEGG Orthology (KO)

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KOi
K16333

Identification of Orthologs from Complete Genome Data

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OMAi
SQACSVQ

Database of Orthologous Groups

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OrthoDBi
EOG091G03YN

Database for complete collections of gene phylogenies

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PhylomeDBi
Q53ET0

TreeFam database of animal gene trees

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TreeFami
TF321571

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR024786 TORC
IPR024785 TORC_C
IPR024784 TORC_M
IPR024783 TORC_N

The PANTHER Classification System

More...
PANTHERi
PTHR13589 PTHR13589, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12886 TORC_C, 1 hit
PF12885 TORC_M, 1 hit
PF12884 TORC_N, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

Q53ET0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATSGANGPG SATASASNPR KFSEKIALQK QRQAEETAAF EEVMMDIGST
60 70 80 90 100
RLQAQKLRLA YTRSSHYGGS LPNVNQIGSG LAEFQSPLHS PLDSSRSTRH
110 120 130 140 150
HGLVERVQRD PRRMVSPLRR YTRHIDSSPY SPAYLSPPPE SSWRRTMAWG
160 170 180 190 200
NFPAEKGQLF RLPSALNRTS SDSALHTSVM NPSPQDTYPG PTPPSILPSR
210 220 230 240 250
RGGILDGEMD PKVPAIEENL LDDKHLLKPW DAKKLSSSSS RPRSCEVPGI
260 270 280 290 300
NIFPSPDQPA NVPVLPPAMN TGGSLPDLTN LHFPPPLPTP LDPEETAYPS
310 320 330 340 350
LSGGNSTSNL THTMTHLGIS RGMGLGPGYD APGLHSPLSH PSLQSSLSNP
360 370 380 390 400
NLQASLSSPQ PQLQGSHSHP SLPASSLARH VLPTTSLGHP SLSAPALSSS
410 420 430 440 450
SSSSSTSSPV LGAPSYPAST PGASPHHRRV PLSPLSLLAG PADARRSQQQ
460 470 480 490 500
LPKQFSPTMS PTLSSITQGV PLDTSKLSTD QRLPPYPYSS PSLVLPTQPH
510 520 530 540 550
TPKSLQQPGL PSQSCSVQSS GGQPPGRQSH YGTPYPPGPS GHGQQSYHRP
560 570 580 590 600
MSDFNLGNLE QFSMESPSAS LVLDPPGFSE GPGFLGGEGP MGGPQDPHTF
610 620 630 640 650
NHQNLTHCSR HGSGPNIILT GDSSPGFSKE IAAALAGVPG FEVSAAGLEL
660 670 680 690
GLGLEDELRM EPLGLEGLNM LSDPCALLPD PAVEESFRSD RLQ
Length:693
Mass (Da):73,302
Last modified:February 5, 2008 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iEE6C52E0ECDC1DF1
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5T4K5Q5T4K5_HUMAN
CREB-regulated transcription coacti...
CRTC2
373Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3KNE6J3KNE6_HUMAN
CREB-regulated transcription coacti...
CRTC2
54Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YDQ8H0YDQ8_HUMAN
CREB-regulated transcription coacti...
CRTC2
481Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti323 – 325MGL → HGP in AAQ98857 (PubMed:14506290).Curated3
Sequence conflicti499P → S in BAD97279 (Ref. 2) Curated1

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

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).1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_038756147M → V. Corresponds to variant dbSNP:rs11264680Ensembl.1
Natural variantiVAR_038757379R → C2 PublicationsCorresponds to variant dbSNP:rs150423770Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AY360172 mRNA Translation: AAQ98857.1
AK223559 mRNA Translation: BAD97279.1
AL358472 Genomic DNA No translation available.
BC028886 mRNA Translation: AAH28886.1
BC053562 mRNA Translation: AAH53562.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS30875.1

NCBI Reference Sequences

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RefSeqi
NP_859066.1, NM_181715.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.406392

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000368633; ENSP00000357622; ENSG00000160741

Database of genes from NCBI RefSeq genomes

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GeneIDi
200186

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:200186

UCSC genome browser

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UCSCi
uc057leo.1 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY360172 mRNA Translation: AAQ98857.1
AK223559 mRNA Translation: BAD97279.1
AL358472 Genomic DNA No translation available.
BC028886 mRNA Translation: AAH28886.1
BC053562 mRNA Translation: AAH53562.1
CCDSiCCDS30875.1
RefSeqiNP_859066.1, NM_181715.2
UniGeneiHs.406392

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HTMX-ray2.00A18-50[»]
ProteinModelPortaliQ53ET0
SMRiQ53ET0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128308, 38 interactors
DIPiDIP-29950N
IntActiQ53ET0, 19 interactors
MINTiQ53ET0
STRINGi9606.ENSP00000357622

PTM databases

iPTMnetiQ53ET0
PhosphoSitePlusiQ53ET0

Polymorphism and mutation databases

BioMutaiCRTC2
DMDMi167009135

Proteomic databases

EPDiQ53ET0
MaxQBiQ53ET0
PaxDbiQ53ET0
PeptideAtlasiQ53ET0
PRIDEiQ53ET0
ProteomicsDBi62448

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368633; ENSP00000357622; ENSG00000160741
GeneIDi200186
KEGGihsa:200186
UCSCiuc057leo.1 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
200186
DisGeNETi200186
EuPathDBiHostDB:ENSG00000160741.16

GeneCards: human genes, protein and diseases

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GeneCardsi
CRTC2
HGNCiHGNC:27301 CRTC2
HPAiHPA028454
HPA028465
MIMi608972 gene
neXtProtiNX_Q53ET0
OpenTargetsiENSG00000160741
PharmGKBiPA142672073

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IGNT Eukaryota
ENOG410XPDQ LUCA
GeneTreeiENSGT00390000010652
HOGENOMiHOG000111980
HOVERGENiHBG058314
InParanoidiQ53ET0
KOiK16333
OMAiSQACSVQ
OrthoDBiEOG091G03YN
PhylomeDBiQ53ET0
TreeFamiTF321571

Enzyme and pathway databases

ReactomeiR-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-400253 Circadian Clock
SIGNORiQ53ET0

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
CRTC2 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
CRTC2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
200186

Protein Ontology

More...
PROi
PR:Q53ET0

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000160741 Expressed in 171 organ(s), highest expression level in small intestine Peyer's patch
CleanExiHS_CRTC2
ExpressionAtlasiQ53ET0 baseline and differential
GenevisibleiQ53ET0 HS

Family and domain databases

InterProiView protein in InterPro
IPR024786 TORC
IPR024785 TORC_C
IPR024784 TORC_M
IPR024783 TORC_N
PANTHERiPTHR13589 PTHR13589, 1 hit
PfamiView protein in Pfam
PF12886 TORC_C, 1 hit
PF12885 TORC_M, 1 hit
PF12884 TORC_N, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCRTC2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q53ET0
Secondary accession number(s): Q6UUV8, Q7Z3X7, Q8N332
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: December 5, 2018
This is version 115 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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