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Protein

Cell cycle and apoptosis regulator protein 2

Gene

Ccar2

Organism
Mus musculus (Mouse)
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

Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis (By similarity). As part of a histone H3-specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). Inhibits SUV39H1 methyltransferase activity. Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress (By similarity) Regulates the circadian expression of the core clock components NR1D1 and ARNTL/BMAL1. Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation. Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1 (PubMed:24415752). Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization (PubMed:21030595). Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2 (PubMed:25732823). Represses the ligand-dependent transcriptional activation function of ESR2. Positively regulates the beta-catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway. Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3. Represses the transcriptional activator activity of BRCA1. Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro (By similarity).By similarity1 Publication

<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

  • enzyme binding Source: MGI
  • enzyme inhibitor activity Source: UniProtKB
  • nuclear receptor transcription coactivator activity Source: GO_Central
  • RNA polymerase II complex binding Source: UniProtKB

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, Metalloenzyme inhibitor, Repressor
Biological processApoptosis, Biological rhythms, Cell cycle, DNA damage, mRNA processing, mRNA splicing, Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-3371453 Regulation of HSF1-mediated heat shock response

<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:
Cell cycle and apoptosis regulator protein 2
Alternative name(s):
Cell division cycle and apoptosis regulator 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:Ccar2
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 14

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:2444228 Ccar2

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice mimic a fasted state and therefore, display an increased production of glucose. Display elevated levels of PCK1 and are glucose-intolerant in both a normal and a high-fat diet (PubMed:24415752). Mice develop more tumors including lymphomas, liver tumors, lung tumors (PubMed:25732823).2 Publications

Keywords - Diseasei

Tumor suppressor

<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 ‘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_00000508141 – 922Cell cycle and apoptosis regulator protein 2Add BLAST922

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 residuei35PhosphothreonineBy similarity1
Modified residuei112N6-acetyllysine; by KAT8By similarity1
Modified residuei123N6-methyllysineBy similarity1
Modified residuei124PhosphoserineBy similarity1
Modified residuei180Omega-N-methylarginineBy similarity1
Modified residuei215N6-acetyllysine; by KAT8By similarity1
Modified residuei483PhosphothreonineBy similarity1
Modified residuei568PhosphoserineBy similarity1
<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-linki590Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3); alternateBy similarity
Cross-linki590Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei612PhosphoserineCombined sources1
Modified residuei626PhosphoserineBy similarity1
Modified residuei674PhosphoserineCombined sources1
Modified residuei677PhosphoserineCombined sources1
Modified residuei680PhosphoserineCombined sources1
Modified residuei684PhosphotyrosineCombined sources1
Modified residuei686PhosphoserineCombined sources1
Modified residuei807PhosphoserineBy similarity1
Modified residuei896PhosphothreonineBy similarity1

<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

Acetylation at Lys-112 and Lys-215 by KAT8 prevents inhibitory binding to SIRT1 and increases its deacetylase activity.By similarity
Genotoxic stress induces its sumoylation and sumoylation promotes the SIRT1-CCAR2 interaction which in turn inhibits SIRT1-mediated deacetylation of p53/TP53. Sumoylation leads to transcriptional activation of p53/TP53 by sequestering SIRT1 from p53/TP53. Desumoylated by SENP1.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q8VDP4

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q8VDP4

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

More...
PaxDbi
Q8VDP4

PeptideAtlas

More...
PeptideAtlasi
Q8VDP4

PRoteomics IDEntifications database

More...
PRIDEi
Q8VDP4

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8VDP4

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

More...
PhosphoSitePlusi
Q8VDP4

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000033712 Expressed in 251 organ(s), highest expression level in dorsal pancreas

CleanEx database of gene expression profiles

More...
CleanExi
MM_2610301G19RIK

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8VDP4 MM

<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

Component of the DBIRD complex. Interacts with ZNF326/ZIRD; the interaction is direct. Interacts (via N-terminus) with SIRT1, which inhibits the deacetylation of substrates. Interacts (via N-terminus) with SUV39H1; this interaction abolishes the interaction with SIRT1. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with NR1D1. Interacts (via N-terminus) with ESR1 and ESR2. Interacts (via N-terminus) with HDAC3 (via C-terminus). Interacts with HDAC1 and MED2F. Interacts with MCC. Interacts (via N-terminus) with NR1H2 and NR1H3 in a ligand-independent manner. Interacts with CSNK2A1. Interacts (via N-terminus) with p53/TP53. Interacts (via N-terminus) with BRCA1 (via the BRCT domains). Interacts (via N-terminus) with CHEK2 (via protein kinase domain). Interacts with PSEM3. Interacts (via N-terminus) with PSIA3 and SENP1. The sumoylated form shows a preferential interaction with SIRT1 as compared to its unmodified form (By similarity).By similarity5 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
230123, 5 interactors

Protein interaction database and analysis system

More...
IntActi
Q8VDP4, 10 interactors

Molecular INTeraction database

More...
MINTi
Q8VDP4

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000036924

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q8VDP4

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

More...
SMRi
Q8VDP4

Database of comparative protein structure models

More...
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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni609 – 669Interaction with MCCBy similarityAdd BLAST61
Regioni703 – 922Interaction with NR1D1By similarityAdd BLAST220

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili573 – 596Sequence analysisAdd BLAST24
Coiled coili828 – 898Sequence analysisAdd BLAST71

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4246 Eukaryota
ENOG4111FW4 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00530000063672

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000113184

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG081843

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8VDP4

Identification of Orthologs from Complete Genome Data

More...
OMAi
PLQLEMQ

Database of Orthologous Groups

More...
OrthoDBi
EOG091G03QV

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8VDP4

TreeFam database of animal gene trees

More...
TreeFami
TF316387

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR025224 CCAR1/CCAR2
IPR028811 CCAR2
IPR025954 DBC1/CARP1_inactive_NUDIX_dom
IPR011992 EF-hand-dom_pair
IPR025223 S1-like_RNA-bd_dom

The PANTHER Classification System

More...
PANTHERi
PTHR14304 PTHR14304, 1 hit
PTHR14304:SF12 PTHR14304:SF12, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF14443 DBC1, 1 hit
PF14444 S1-like, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01122 DBC1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47473 SSF47473, 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>Sequencei

<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.

Q8VDP4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQFKRQRIN PLPGGRNFSG AASTSLLGPP PGLLTPPVAT DLSQNARHLQ
60 70 80 90 100
SGEKQRVFTG IVTSLHDYFG VVDEEVFFQL SVVKGRLPQL GEKVLVKAAY
110 120 130 140 150
NPGQAVPWNA VKVQTLSNQP LLKSPAPPLL HVAALGQKQG ILGAQPQLIF
160 170 180 190 200
QPHRIPPLFP QKPLSLFQTS HTLHLSHLNR FPARGPHGRL DQGRSDDYDS
210 220 230 240 250
KKRKQRAGGE PWGAKKPRHD LSPYRVHLTP YTVDSPTCDF LELQRRYRSL
260 270 280 290 300
LVPSDFLSVH LSWLSAFPLG QPFSLHHPSR IQVSSEKEAA PDTGAEPSPE
310 320 330 340 350
DSDPTYSSKV LLLSSPGLEE FYRCCMLFVD DMAEPRETPE HPLKQLKFLL
360 370 380 390 400
GRKEEEAVLV GGEWSPSLDG LDPQADPQVL VRTAIRCAQA QTGIDLSTCT
410 420 430 440 450
KWWRFAEFQY LQPGPPRQLH TVVVYLPDVW TIMPTLEEWE ALCQQKATEA
460 470 480 490 500
APQPHEASGE AEATEQAPDV SEQADTSKQN TETMEATTQQ DVDTDLPEAP
510 520 530 540 550
PPPLEPAVMA RPRCVNLSLY GIVEDRRPKE RISFEVVVLA ELFVEMLQRD
560 570 580 590 600
FGYRIYKTLL SLPEKVVSPP EPEKEEAAKE DAVKEEEAVK EEAVKVSKDE
610 620 630 640 650
VQNEGTAAES DSPLKEDGLL PKRPSSGGEE EEKARGEAAE DLCEMALDPD
660 670 680 690 700
LLLLRDDGED EFAGAKLEET EVRSVASNQS EMEYSSLQDM PKELDPSTVL
710 720 730 740 750
PLDCLLAFVF FDANWCGYLH RRDLERVLLT LGIRLSAEQA KQLVSRVVAQ
760 770 780 790 800
NICQYRSLQY SRAEVLDDGL PEDVLFGNLD LLPPSGKSTK PGAAPTEHKG
810 820 830 840 850
LVPHNGSLIN VGSLLQRAEQ QDSGRLYLEN KIHTLELKLE ESHNRFSATE
860 870 880 890 900
VTNKTLAAEM QELRARLAEA EETARTAERQ KNQLQRQMQD FRRRLTPLHL
910 920
EMQRIVEKAD SWVEKEEPTP SN
Length:922
Mass (Da):103,002
Last modified:March 1, 2004 - 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:i19F43ECEE58F461C
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAC27420 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC34139 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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 conflicti527 – 529RPK → HAS in AAH25471 (PubMed:15489334).Curated3
Sequence conflicti720H → L in AAH38346 (PubMed:15489334).Curated1
Sequence conflicti812G → R in BAC27420 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AK031472 mRNA Translation: BAC27420.1 Different initiation.
AK050238 mRNA Translation: BAC34139.2 Different initiation.
BC021475 mRNA Translation: AAH21475.2
BC025471 mRNA Translation: AAH25471.1
BC038346 mRNA Translation: AAH38346.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS49534.1

NCBI Reference Sequences

More...
RefSeqi
NP_666167.3, NM_146055.3
XP_006518959.1, XM_006518896.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.218284

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000035612; ENSMUSP00000036924; ENSMUSG00000033712

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
219158

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:219158

UCSC genome browser

More...
UCSCi
uc007unf.1 mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031472 mRNA Translation: BAC27420.1 Different initiation.
AK050238 mRNA Translation: BAC34139.2 Different initiation.
BC021475 mRNA Translation: AAH21475.2
BC025471 mRNA Translation: AAH25471.1
BC038346 mRNA Translation: AAH38346.1
CCDSiCCDS49534.1
RefSeqiNP_666167.3, NM_146055.3
XP_006518959.1, XM_006518896.3
UniGeneiMm.218284

3D structure databases

ProteinModelPortaliQ8VDP4
SMRiQ8VDP4
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230123, 5 interactors
IntActiQ8VDP4, 10 interactors
MINTiQ8VDP4
STRINGi10090.ENSMUSP00000036924

PTM databases

iPTMnetiQ8VDP4
PhosphoSitePlusiQ8VDP4

Proteomic databases

EPDiQ8VDP4
MaxQBiQ8VDP4
PaxDbiQ8VDP4
PeptideAtlasiQ8VDP4
PRIDEiQ8VDP4

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035612; ENSMUSP00000036924; ENSMUSG00000033712
GeneIDi219158
KEGGimmu:219158
UCSCiuc007unf.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
57805
MGIiMGI:2444228 Ccar2

Phylogenomic databases

eggNOGiKOG4246 Eukaryota
ENOG4111FW4 LUCA
GeneTreeiENSGT00530000063672
HOGENOMiHOG000113184
HOVERGENiHBG081843
InParanoidiQ8VDP4
OMAiPLQLEMQ
OrthoDBiEOG091G03QV
PhylomeDBiQ8VDP4
TreeFamiTF316387

Enzyme and pathway databases

ReactomeiR-MMU-3371453 Regulation of HSF1-mediated heat shock response

Miscellaneous databases

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

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ChiTaRSi
Ccar2 mouse

Protein Ontology

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PROi
PR:Q8VDP4

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000033712 Expressed in 251 organ(s), highest expression level in dorsal pancreas
CleanExiMM_2610301G19RIK
GenevisibleiQ8VDP4 MM

Family and domain databases

InterProiView protein in InterPro
IPR025224 CCAR1/CCAR2
IPR028811 CCAR2
IPR025954 DBC1/CARP1_inactive_NUDIX_dom
IPR011992 EF-hand-dom_pair
IPR025223 S1-like_RNA-bd_dom
PANTHERiPTHR14304 PTHR14304, 1 hit
PTHR14304:SF12 PTHR14304:SF12, 1 hit
PfamiView protein in Pfam
PF14443 DBC1, 1 hit
PF14444 S1-like, 1 hit
SMARTiView protein in SMART
SM01122 DBC1, 1 hit
SUPFAMiSSF47473 SSF47473, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiCCAR2_MOUSE
<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: Q8VDP4
Secondary accession number(s): Q6PIB1
, Q8BWR5, Q8C0F0, Q8R3G6
<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: January 24, 2006
Last sequence update: March 1, 2004
Last modified: November 7, 2018
This is version 132 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

<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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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