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Entry version 202 (05 Jun 2019)
Sequence version 2 (02 Nov 2010)
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Protein

Cyclin-A2

Gene

CCNA2

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

Cyclin which controls both the G1/S and the G2/M transition phases of the cell cycle. Functions through the formation of specific serine/threonine protein kinase holoenzyme complexes with the cyclin-dependent protein kinases CDK1 or CDK2. The cyclin subunit confers the substrate specificity of these complexes and differentially interacts with and activates CDK1 and CDK2 throughout the cell cycle.1 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

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 functionCyclin
Biological processCell cycle, Cell division, Host-virus interaction, Mitosis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1362300 Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1
R-HSA-1538133 G0 and Early G1
R-HSA-170145 Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-176408 Regulation of APC/C activators between G1/S and early anaphase
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-6804116 TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-6804757 Regulation of TP53 Degradation
R-HSA-68911 G2 Phase
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69273 Cyclin A/B1/B2 associated events during G2/M transition
R-HSA-69563 p53-Dependent G1 DNA Damage Response
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P20248

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P20248

<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:
Cyclin-A2Imported
Short name:
Cyclin-A1 Publication
Alternative name(s):
Cyclin A1 Publication
<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:CCNA2Imported
Synonyms:CCN1Imported, CCNAImported
<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 4

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:1578 CCNA2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
123835 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P20248

<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 & Seán O’Donoghue; 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

Organism-specific databases

DisGeNET

More...
DisGeNETi
890

Open Targets

More...
OpenTargetsi
ENSG00000145386

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA94

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2582

Drug and drug target database

More...
DrugBanki
DB08463 (2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-ol
DB07137 (2S)-N-[(3Z)-5-CYCLOPROPYL-3H-PYRAZOL-3-YLIDENE]-2-[4-(2-OXOIMIDAZOLIDIN-1-YL)PHENYL]PROPANAMIDE
DB06948 2-ANILINO-6-CYCLOHEXYLMETHOXYPURINE
DB08248 3-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)-BENZENESULFONAMIDE
DB08309 3-({2-[(4-{[6-(CYCLOHEXYLMETHOXY)-9H-PURIN-2-YL]AMINO}PHENYL)SULFONYL]ETHYL}AMINO)PROPAN-1-OL
DB08241 4-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)--BENZAMIDE
DB08572 4-{[4-AMINO-6-(CYCLOHEXYLMETHOXY)-5-NITROSOPYRIMIDIN-2-YL]AMINO}BENZAMIDE
DB07203 6-CYCLOHEXYLMETHOXY-2-(3'-CHLOROANILINO) PURINE
DB08233 6-CYCLOHEXYLMETHYLOXY-2-(4'-HYDROXYANILINO)PURINE
DB02407 6-O-Cyclohexylmethyl Guanine
DB02833 [4-(2-Amino-4-Methyl-Thiazol-5-Yl)-Pyrimidin-2-Yl]-(3-Nitro-Phenyl)-Amine
DB06944 N-(3-cyclopropyl-1H-pyrazol-5-yl)-2-(2-naphthyl)acetamide
DB07126 O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO) PURINE

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CCNA2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
311033358

<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_00000803381 – 432Cyclin-A2Add BLAST432

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 residuei1N-acetylmethionineCombined sources1
Modified residuei5PhosphoserineCombined sources1
Modified residuei55PhosphoserineCombined 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

Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-promoting complex (APC/C), leading to its degradation by the proteasome. Deubiquitinated and stabilized by USP37 enables entry into S phase.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P20248

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P20248

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P20248

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

More...
PaxDbi
P20248

PeptideAtlas

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PeptideAtlasi
P20248

PRoteomics IDEntifications database

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PRIDEi
P20248

ProteomicsDB human proteome resource

More...
ProteomicsDBi
53735

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P20248

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

More...
PhosphoSitePlusi
P20248

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P20248

<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 the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Accumulates steadily during G2 and is abruptly destroyed at mitosis. Not detected during the G1 phase of the cell cycle. It accumulates during the DNA synthesis/S phase and disappears as cells progress into mitosis, between prophase and metaphase (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000145386 Expressed in 192 organ(s), highest expression level in oocyte

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P20248 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB000114
HPA020626

<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

Interacts with the CDK1 and CDK2 protein kinases to form serine/threonine kinase holoenzyme complexes (PubMed:1312467, PubMed:7630397, PubMed:8684460, PubMed:8756328). Interacts with CDK1 (hyperphosphorylated form in G1 and underphosphorylated forms in S and G2) (PubMed:1312467). Interacts with CDK2; the interaction increases from G1 to G2 (PubMed:1312467). Interacts (associated with CDK2 but not with CDK1) with SCAPER; regulates the activity of CCNA2/CDK2 by transiently maintaining CCNA2 in the cytoplasm (PubMed:17698606). Forms a ternary complex with CDK2 and CDKN1B; CDKN1B inhibits the kinase activity of CDK2 through conformational rearrangements (PubMed:8684460). Interacts with INCA1 (PubMed:21540187).6 Publications
(Microbial infection) Interacts with human cytomegalovirus protein UL32.1 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)

More...
BioGridi
107331, 124 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2004 Cyclin A2-CDK1 complex
CPX-2006 Cyclin A2-CDK2 complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P20248

Database of interacting proteins

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DIPi
DIP-638N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P20248

Protein interaction database and analysis system

More...
IntActi
P20248, 56 interactors

Molecular INTeraction database

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MINTi
P20248

STRING: functional protein association networks

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STRINGi
9606.ENSP00000274026

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P20248

<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

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P20248

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P20248

<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

<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 cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0654 Eukaryota
COG5024 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155372

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000167672

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P20248

KEGG Orthology (KO)

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KOi
K06627

Identification of Orthologs from Complete Genome Data

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OMAi
TMDISIV

Database of Orthologous Groups

More...
OrthoDBi
993640at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P20248

TreeFam database of animal gene trees

More...
TreeFami
TF101002

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00043 CYCLIN, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR039361 Cyclin
IPR032447 Cyclin-A_N
IPR013763 Cyclin-like
IPR036915 Cyclin-like_sf
IPR004367 Cyclin_C-dom
IPR006671 Cyclin_N

The PANTHER Classification System

More...
PANTHERi
PTHR10177 PTHR10177, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02984 Cyclin_C, 1 hit
PF00134 Cyclin_N, 1 hit
PF16500 Cyclin_N2, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001771 Cyclin_A_B_D_E, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00385 CYCLIN, 2 hits
SM01332 Cyclin_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47954 SSF47954, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00292 CYCLINS, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

P20248-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLGNSAPGPA TREAGSALLA LQQTALQEDQ ENINPEKAAP VQQPRTRAAL
60 70 80 90 100
AVLKSGNPRG LAQQQRPKTR RVAPLKDLPV NDEHVTVPPW KANSKQPAFT
110 120 130 140 150
IHVDEAEKEA QKKPAESQKI EREDALAFNS AISLPGPRKP LVPLDYPMDG
160 170 180 190 200
SFESPHTMDM SIILEDEKPV SVNEVPDYHE DIHTYLREME VKCKPKVGYM
210 220 230 240 250
KKQPDITNSM RAILVDWLVE VGEEYKLQNE TLHLAVNYID RFLSSMSVLR
260 270 280 290 300
GKLQLVGTAA MLLASKFEEI YPPEVAEFVY ITDDTYTKKQ VLRMEHLVLK
310 320 330 340 350
VLTFDLAAPT VNQFLTQYFL HQQPANCKVE SLAMFLGELS LIDADPYLKY
360 370 380 390 400
LPSVIAGAAF HLALYTVTGQ SWPESLIRKT GYTLESLKPC LMDLHQTYLK
410 420 430
APQHAQQSIR EKYKNSKYHG VSLLNPPETL NL
Length:432
Mass (Da):48,551
Last modified:November 2, 2010 - 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:i97763A2897DD35F4
GO

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 conflicti156H → R in CAG28620 (Ref. 3) Curated1

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_018819163I → VCombined sources7 PublicationsCorresponds to variant dbSNP:rs769242Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X51688 mRNA Translation: CAA35986.1
X68303 Genomic DNA Translation: CAA48375.1
CR407692 mRNA Translation: CAG28620.1
AF518006 Genomic DNA Translation: AAM54042.1
AK291931 mRNA Translation: BAF84620.1
AC079341 Genomic DNA Translation: AAY40969.1
CH471056 Genomic DNA Translation: EAX05246.1
BC104783 mRNA Translation: AAI04784.1
BC104787 mRNA Translation: AAI04788.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS3723.1

Protein sequence database of the Protein Information Resource

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PIRi
S08277

NCBI Reference Sequences

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RefSeqi
NP_001228.1, NM_001237.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000274026; ENSP00000274026; ENSG00000145386
ENST00000618014; ENSP00000481380; ENSG00000145386

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
890

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:890

UCSC genome browser

More...
UCSCi
uc003iec.5 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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51688 mRNA Translation: CAA35986.1
X68303 Genomic DNA Translation: CAA48375.1
CR407692 mRNA Translation: CAG28620.1
AF518006 Genomic DNA Translation: AAM54042.1
AK291931 mRNA Translation: BAF84620.1
AC079341 Genomic DNA Translation: AAY40969.1
CH471056 Genomic DNA Translation: EAX05246.1
BC104783 mRNA Translation: AAI04784.1
BC104787 mRNA Translation: AAI04788.1
CCDSiCCDS3723.1
PIRiS08277
RefSeqiNP_001228.1, NM_001237.4

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
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
1E9HX-ray2.50B/D175-432[»]
1FINX-ray2.30B/D173-432[»]
1FVVX-ray2.80B/D173-432[»]
1GY3X-ray2.70B/D175-432[»]
1H1PX-ray2.10B/D175-432[»]
1H1QX-ray2.50B/D175-432[»]
1H1RX-ray2.00B/D175-432[»]
1H1SX-ray2.00B/D175-432[»]
1H24X-ray2.50B/D174-432[»]
1H25X-ray2.50B/D174-432[»]
1H26X-ray2.24B/D174-432[»]
1H27X-ray2.20B/D174-432[»]
1H28X-ray2.80B/D174-432[»]
1JSTX-ray2.60B/D175-432[»]
1JSUX-ray2.30B173-432[»]
1OGUX-ray2.60B/D174-432[»]
1OI9X-ray2.10B/D174-432[»]
1OIUX-ray2.00B/D174-432[»]
1OIYX-ray2.40B/D174-432[»]
1OKVX-ray2.40B/D173-432[»]
1OKWX-ray2.50B/D173-432[»]
1OL1X-ray2.90B/D173-432[»]
1OL2X-ray2.60B/D173-432[»]
1P5EX-ray2.22B/D175-432[»]
1PKDX-ray2.30B/D175-432[»]
1QMZX-ray2.20B/D174-432[»]
1URCX-ray2.60B/D173-432[»]
1VYWX-ray2.30B/D174-432[»]
2BKZX-ray2.60B/D174-432[»]
2BPMX-ray2.40B/D174-432[»]
2C4GX-ray2.70B/D173-432[»]
2C5NX-ray2.10B/D174-432[»]
2C5OX-ray2.10B/D173-432[»]
2C5VX-ray2.90B/D174-432[»]
2C5XX-ray2.90B/D174-432[»]
2C6TX-ray2.61B/D175-432[»]
2CCHX-ray1.70B/D173-432[»]
2CCIX-ray2.70B/D175-432[»]
2CJMX-ray2.30B/D175-432[»]
2I40X-ray2.80B/D173-432[»]
2IW6X-ray2.30B/D174-432[»]
2IW8X-ray2.30B/D174-432[»]
2IW9X-ray2.00B/D174-432[»]
2UUEX-ray2.06B/D174-432[»]
2UZBX-ray2.70B/D175-432[»]
2UZDX-ray2.72B/D175-432[»]
2UZEX-ray2.40B/D175-432[»]
2UZLX-ray2.40B/D175-432[»]
2V22X-ray2.60B/D174-432[»]
2WEVX-ray2.30B/D173-432[»]
2WFYX-ray2.53B/D173-432[»]
2WHBX-ray2.90B/D173-432[»]
2WIHX-ray2.50B/D173-432[»]
2WIPX-ray2.80B/D173-432[»]
2WMAX-ray2.80B/D174-432[»]
2WMBX-ray2.60B/D174-432[»]
2WPAX-ray2.51B/D173-432[»]
2WXVX-ray2.60B/D173-432[»]
2X1NX-ray2.75B/D172-432[»]
3EIDX-ray3.15B/D173-432[»]
3EJ1X-ray3.22B/D173-432[»]
3EOCX-ray3.20B/D173-432[»]
3F5XX-ray2.40B/D177-432[»]
4BCKX-ray2.05B/D171-432[»]
4BCMX-ray2.45B/D171-432[»]
4BCNX-ray2.10B171-432[»]
D171-431[»]
4BCPX-ray2.26B/D171-432[»]
4CFMX-ray2.85B/D175-432[»]
4CFNX-ray2.20B/D175-432[»]
4CFUX-ray2.20B172-432[»]
D173-432[»]
4CFVX-ray2.00B/D172-432[»]
4CFWX-ray2.45B/D175-432[»]
4CFXX-ray3.50B/D173-432[»]
4EOIX-ray2.00B/D175-432[»]
4EOJX-ray1.65B/D175-432[»]
4EOKX-ray2.57B/D175-432[»]
4EOLX-ray2.40B/D175-432[»]
4EOMX-ray2.10B/D175-432[»]
4EONX-ray2.40B/D175-432[»]
4EOOX-ray2.10B/D175-432[»]
4EOPX-ray1.99B/D175-432[»]
4EOQX-ray2.15B/D175-432[»]
4EORX-ray2.20B/D175-432[»]
4EOSX-ray2.57B/D175-432[»]
4FX3X-ray2.75B/D175-432[»]
5CYIX-ray2.00B/D174-432[»]
5IF1X-ray2.61B/D174-432[»]
5LMKX-ray2.40B/D175-432[»]
5NEVX-ray2.97B/D174-432[»]
6ATHX-ray1.82B173-432[»]
SMRiP20248
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107331, 124 interactors
ComplexPortaliCPX-2004 Cyclin A2-CDK1 complex
CPX-2006 Cyclin A2-CDK2 complex
CORUMiP20248
DIPiDIP-638N
ELMiP20248
IntActiP20248, 56 interactors
MINTiP20248
STRINGi9606.ENSP00000274026

Chemistry databases

BindingDBiP20248
ChEMBLiCHEMBL2582
DrugBankiDB08463 (2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-ol
DB07137 (2S)-N-[(3Z)-5-CYCLOPROPYL-3H-PYRAZOL-3-YLIDENE]-2-[4-(2-OXOIMIDAZOLIDIN-1-YL)PHENYL]PROPANAMIDE
DB06948 2-ANILINO-6-CYCLOHEXYLMETHOXYPURINE
DB08248 3-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)-BENZENESULFONAMIDE
DB08309 3-({2-[(4-{[6-(CYCLOHEXYLMETHOXY)-9H-PURIN-2-YL]AMINO}PHENYL)SULFONYL]ETHYL}AMINO)PROPAN-1-OL
DB08241 4-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)--BENZAMIDE
DB08572 4-{[4-AMINO-6-(CYCLOHEXYLMETHOXY)-5-NITROSOPYRIMIDIN-2-YL]AMINO}BENZAMIDE
DB07203 6-CYCLOHEXYLMETHOXY-2-(3'-CHLOROANILINO) PURINE
DB08233 6-CYCLOHEXYLMETHYLOXY-2-(4'-HYDROXYANILINO)PURINE
DB02407 6-O-Cyclohexylmethyl Guanine
DB02833 [4-(2-Amino-4-Methyl-Thiazol-5-Yl)-Pyrimidin-2-Yl]-(3-Nitro-Phenyl)-Amine
DB06944 N-(3-cyclopropyl-1H-pyrazol-5-yl)-2-(2-naphthyl)acetamide
DB07126 O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO) PURINE

PTM databases

iPTMnetiP20248
PhosphoSitePlusiP20248

Polymorphism and mutation databases

BioMutaiCCNA2
DMDMi311033358

Proteomic databases

EPDiP20248
jPOSTiP20248
MaxQBiP20248
PaxDbiP20248
PeptideAtlasiP20248
PRIDEiP20248
ProteomicsDBi53735

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000274026; ENSP00000274026; ENSG00000145386
ENST00000618014; ENSP00000481380; ENSG00000145386
GeneIDi890
KEGGihsa:890
UCSCiuc003iec.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
890
DisGeNETi890

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CCNA2
HGNCiHGNC:1578 CCNA2
HPAiCAB000114
HPA020626
MIMi123835 gene
neXtProtiNX_P20248
OpenTargetsiENSG00000145386
PharmGKBiPA94

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0654 Eukaryota
COG5024 LUCA
GeneTreeiENSGT00940000155372
HOGENOMiHOG000167672
InParanoidiP20248
KOiK06627
OMAiTMDISIV
OrthoDBi993640at2759
PhylomeDBiP20248
TreeFamiTF101002

Enzyme and pathway databases

ReactomeiR-HSA-1362300 Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1
R-HSA-1538133 G0 and Early G1
R-HSA-170145 Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-176408 Regulation of APC/C activators between G1/S and early anaphase
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-6804116 TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-6804757 Regulation of TP53 Degradation
R-HSA-68911 G2 Phase
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69273 Cyclin A/B1/B2 associated events during G2/M transition
R-HSA-69563 p53-Dependent G1 DNA Damage Response
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
SignaLinkiP20248
SIGNORiP20248

Miscellaneous databases

EvolutionaryTraceiP20248

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Cyclin_A2

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

More...
GenomeRNAii
890
PMAP-CutDBiP20248

Protein Ontology

More...
PROi
PR:P20248

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000145386 Expressed in 192 organ(s), highest expression level in oocyte
GenevisibleiP20248 HS

Family and domain databases

CDDicd00043 CYCLIN, 2 hits
InterProiView protein in InterPro
IPR039361 Cyclin
IPR032447 Cyclin-A_N
IPR013763 Cyclin-like
IPR036915 Cyclin-like_sf
IPR004367 Cyclin_C-dom
IPR006671 Cyclin_N
PANTHERiPTHR10177 PTHR10177, 1 hit
PfamiView protein in Pfam
PF02984 Cyclin_C, 1 hit
PF00134 Cyclin_N, 1 hit
PF16500 Cyclin_N2, 1 hit
PIRSFiPIRSF001771 Cyclin_A_B_D_E, 1 hit
SMARTiView protein in SMART
SM00385 CYCLIN, 2 hits
SM01332 Cyclin_C, 1 hit
SUPFAMiSSF47954 SSF47954, 2 hits
PROSITEiView protein in PROSITE
PS00292 CYCLINS, 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 nameiCCNA2_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: P20248
Secondary accession number(s): A8K7B6
, Q2M3U6, Q4W5P4, Q6LER8
<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 1, 1991
Last sequence update: November 2, 2010
Last modified: June 5, 2019
This is version 202 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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