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UniProtKB/Swiss-Prot entry P20248


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CCNA2_HUMAN
Primary accession number P20248
Secondary accession numbers Q2M3U6 Q4W5P4 Q6LER8
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on February 1, 1991 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 88)
Name and origin of the protein
Protein name Cyclin-A2
Synonym Cyclin-A
Gene name
Name: CCNA2
Synonyms: CCN1, CCNA
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/343555a0; PubMed=1967822 [NCBI, ExPASy, EBI, Israel, Japan]
Wang J., Chenivesse X., Henglein B., Brechot C.;
"Hepatitis B virus integration in a cyclin A gene in a hepatocellular carcinoma.";
Nature 343:555-557(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8202514 [NCBI, ExPASy, EBI, Israel, Japan]
Henglein B., Chenivesse X., Wang D., Eick D., Brechot C.;
"Structure and cell cycle-regulated transcription of the human cyclin A gene.";
Proc. Natl. Acad. Sci. U.S.A. 91:5490-5494(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-163.
Rieder M.J., Livingston R.J., Braun A.C., Montoya M.A., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-163.
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH SCAPER, AND SUBCELLULAR LOCATION.
DOI=10.1083/jcb.200701166; PubMed=17698606 [NCBI, ExPASy, EBI, Israel, Japan]
Tsang W.Y., Wang L., Chen Z., Sanchez I., Dynlacht B.D.;
"SCAPER, a novel cyclin A-interacting protein that regulates cell cycle progression.";
J. Cell Biol. 178:621-633(2007).
[8]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 COMPLEXED WITH CDK2.
DOI=10.1038/376313a0; PubMed=7630397 [NCBI, ExPASy, EBI, Israel, Japan]
Jeffrey P.D., Russo A.A., Polyak K., Gibbs E., Hurwitz J., Massague J., Pavletich N.P.;
"Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex.";
Nature 376:313-320(1995).
[9]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 IN CDK2/KIP1 COMPLEX.
DOI=10.1038/382325a0; PubMed=8684460 [NCBI, ExPASy, EBI, Israel, Japan]
Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.;
"Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex.";
Nature 382:325-331(1996).
[10]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 173-432 COMPLEXED WITH CDK2.
DOI=10.1038/nsb0896-696; PubMed=8756328 [NCBI, ExPASy, EBI, Israel, Japan]
Russo A.A., Jeffrey P.D., Pavletich N.P.;
"Structural basis of cyclin-dependent kinase activation by phosphorylation.";
Nat. Struct. Biol. 3:696-700(1996).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X51688; CAA35986.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X68303; CAA48375.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR407692; CAG28620.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF518006; AAM54042.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC079341; AAY40969.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC104783; AAI04784.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC104787; AAI04788.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S08277; S08277.
RefSeq NP_001228.1; -.
UniGene Hs.58974
3D structure databases
PDB
1E9H; X-ray; 2.50 A; B/D=175-432.[ExPASy / RCSB / EBI]
1FIN; X-ray; 2.30 A; B/D=173-432.[ExPASy / RCSB / EBI]
1FVV; X-ray; 2.80 A; B/D=173-432.[ExPASy / RCSB / EBI]
1GY3; X-ray; 2.70 A; B/D=175-432.[ExPASy / RCSB / EBI]
1H1P; X-ray; 2.10 A; B/D=175-432.[ExPASy / RCSB / EBI]
1H1Q; X-ray; 2.50 A; B/D=175-432.[ExPASy / RCSB / EBI]
1H1R; X-ray; 2.00 A; B/D=175-432.[ExPASy / RCSB / EBI]
1H1S; X-ray; 2.00 A; B/D=175-432.[ExPASy / RCSB / EBI]
1H24; X-ray; 2.50 A; B/D=174-432.[ExPASy / RCSB / EBI]
1H25; X-ray; 2.50 A; B/D=174-432.[ExPASy / RCSB / EBI]
1H26; X-ray; 2.24 A; B/D=174-432.[ExPASy / RCSB / EBI]
1H27; X-ray; 2.20 A; B/D=174-432.[ExPASy / RCSB / EBI]
1H28; X-ray; 2.80 A; B/D=174-432.[ExPASy / RCSB / EBI]
1JST; X-ray; 2.60 A; B/D=175-432.[ExPASy / RCSB / EBI]
1JSU; X-ray; 2.30 A; B=173-432.[ExPASy / RCSB / EBI]
1OGU; X-ray; 2.60 A; B/D=174-432.[ExPASy / RCSB / EBI]
1OI9; X-ray; 2.10 A; B/D=174-432.[ExPASy / RCSB / EBI]
1OIU; X-ray; 2.00 A; B/D=174-432.[ExPASy / RCSB / EBI]
1OIY; X-ray; 2.40 A; B/D=174-432.[ExPASy / RCSB / EBI]
1OKV; X-ray; 2.40 A; B/D=173-432.[ExPASy / RCSB / EBI]
1OKW; X-ray; 2.50 A; B/D=173-432.[ExPASy / RCSB / EBI]
1OL1; X-ray; 2.90 A; B/D=173-432.[ExPASy / RCSB / EBI]
1OL2; X-ray; 2.60 A; B/D=173-432.[ExPASy / RCSB / EBI]
1P5E; X-ray; 2.22 A; B/D=175-432.[ExPASy / RCSB / EBI]
1PKD; X-ray; 2.30 A; B/D=175-432.[ExPASy / RCSB / EBI]
1QMZ; X-ray; 2.20 A; B/D=174-432.[ExPASy / RCSB / EBI]
1URC; X-ray; 2.60 A; B/D=173-432.[ExPASy / RCSB / EBI]
1VYW; X-ray; 2.30 A; B/D=173-432.[ExPASy / RCSB / EBI]
2BKZ; X-ray; 2.60 A; B/D=173-432.[ExPASy / RCSB / EBI]
2BPM; X-ray; 2.40 A; B/D=173-432.[ExPASy / RCSB / EBI]
2C4G; X-ray; 2.70 A; B/D=173-432.[ExPASy / RCSB / EBI]
2C5N; X-ray; 2.10 A; B/D=174-432.[ExPASy / RCSB / EBI]
2C5O; X-ray; 2.10 A; B/D=173-432.[ExPASy / RCSB / EBI]
2C5P; X-ray; 2.30 A; B/D=173-432.[ExPASy / RCSB / EBI]
2C5V; X-ray; 2.90 A; B/D=174-432.[ExPASy / RCSB / EBI]
2C5X; X-ray; 2.90 A; B/D=174-432.[ExPASy / RCSB / EBI]
2C6T; X-ray; 2.61 A; B/D=175-432.[ExPASy / RCSB / EBI]
2CCH; X-ray; 1.70 A; B/D=173-432.[ExPASy / RCSB / EBI]
2CCI; X-ray; 2.70 A; B/D=175-432.[ExPASy / RCSB / EBI]
2CJM; X-ray; 2.30 A; B/D=175-432.[ExPASy / RCSB / EBI]
2I40; X-ray; 2.80 A; B/D=173-432.[ExPASy / RCSB / EBI]
2IW6; X-ray; 2.30 A; B/D=174-432.[ExPASy / RCSB / EBI]
2IW8; X-ray; 2.30 A; B/D=174-432.[ExPASy / RCSB / EBI]
2IW9; X-ray; 2.00 A; B/D=174-432.[ExPASy / RCSB / EBI]
2UUE; X-ray; 2.06 A; B/D=174-432.[ExPASy / RCSB / EBI]
2UZB; X-ray; 2.70 A; B/D=175-432.[ExPASy / RCSB / EBI]
2UZD; X-ray; 2.72 A; B/D=175-432.[ExPASy / RCSB / EBI]
2UZE; X-ray; 2.40 A; B/D=175-432.[ExPASy / RCSB / EBI]
2UZL; X-ray; 2.40 A; B/D=175-432.[ExPASy / RCSB / EBI]
2V22; X-ray; 2.60 A; B/D=174-432.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1E9H; -.
1FIN; -.
1FVV; -.
1GY3; -.
1H1P; -.
1H1Q; -.
1H1R; -.
1H1S; -.
1H24; -.
1H25; -.
1H26; -.
1H27; -.
1H28; -.
1JST; -.
1JSU; -.
1OGU; -.
1OI9; -.
1OIU; -.
1OIY; -.
1OKV; -.
1OKW; -.
1OL1; -.
1OL2; -.
1P5E; -.
1PKD; -.
1QMZ; -.
1URC; -.
1VYW; -.
2BKZ; -.
2BPM; -.
2C4G; -.
2C5N; -.
2C5O; -.
2C5P; -.
2C5V; -.
2C5X; -.
2C6T; -.
2CCH; -.
2CCI; -.
2CJM; -.
2I40; -.
2IW6; -.
2IW8; -.
2IW9; -.
2UUE; -.
2UZB; -.
2UZD; -.
2UZE; -.
2UZL; -.
2V22; -.
ModBase P20248.
Protein-protein interaction databases
DIP DIP:638N; -.
IntAct P20248; -.
Enzyme and pathway databases
Reactome REACT_152; Cell Cycle, Mitotic.
REACT_383; DNA Replication.
REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Polymorphism databases
NIEHS-SNPs CCNA2.
Organism-specific databases
H-InvDB HIX0031483; -.
HGNC HGNC:1578; CCNA2.
GenAtlas CCNA2.
HPA CAB000114; -.
MIM 123835; gene. [NCBI / EBI]
PharmGKB PA94; -.
GeneCards P20248.
Gene expression databases
CleanEx HS_CCNA2; -.
GermOnline ENSG00000145386; Homo sapiens.
Ontologies
GO
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0007095; Biological process: mitotic cell cycle G2/M transition DNA damage checkpoint (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR015453; CycA.
IPR006670; Cyclin.
IPR014400; Cyclin_A_B_D_E.
IPR004367; Cyclin_C.
IPR006671; Cyclin_N.
IPR013763; Cyclin_related.
Graphical view of domain structure.
Gene3D G3DSA:1.10.472.10; Cyclin_related; 1.
PANTHER PTHR10177:SF23; CycA; 1.
Pfam PF02984; Cyclin_C; 1.
PF00134; Cyclin_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001771; Cyclin_A_B_D_E; 1.
SMART SM00385; CYCLIN; 2.
SMART graphical view of domain structure.
PROSITE PS00292; CYCLINS; 1.
BLOCKS P20248.
Genome annotation databases
Ensembl ENSG00000145386; Homo sapiens. [Contig view]
GeneID 890; -.
KEGG hsa:890; -.
Phylogenomic databases
HOGENOM P20248; -.
HOVERGEN P20248; -.
Other
LinkHub P20248; -.
SOURCE CCNA2; Homo sapiens.
ProtoNet P20248.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell cycle; Cell division; Cyclin; Cytoplasm; Mitosis; Nucleus; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   432  432     Cyclin-A2. PRO_0000080338
VARIANT   163   163  1     V -> I (in dbSNP:rs769242 [NCBI]). VAR_018819 
CONFLICT   156   156        H -> R (in Ref. 3; CAG28620). 
HELIX   176   178  3      
HELIX   179   193  15      
TURN   197   202  6      
HELIX   208   225  18      
HELIX   229   242  14      
HELIX   250   252  3      
HELIX   253   268  16      
STRAND   269   271  3      
HELIX   275   280  6      
TURN   281   284  4      
HELIX   288   302  15      
HELIX   311   319  9      
HELIX   327   340  14      
HELIX   344   347  4      
HELIX   352   368  17      
HELIX   374   380  7      
HELIX   384   399  16      
HELIX   401   403  3      
HELIX   408   412  5      
HELIX   416   418  3      
HELIX   421   423  3      
Sequence information
Length: 432 AA [This is the length of the unprocessed precursor] Molecular weight: 48537 Da [This is the MW of the unprocessed precursor] CRC64: 977EA71797DB671B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLGNSAPGPA TREAGSALLA LQQTALQEDQ ENINPEKAAP VQQPRTRAAL AVLKSGNPRG 

        70         80         90        100        110        120 
LAQQQRPKTR RVAPLKDLPV NDEHVTVPPW KANSKQPAFT IHVDEAEKEA QKKPAESQKI 

       130        140        150        160        170        180 
EREDALAFNS AISLPGPRKP LVPLDYPMDG SFESPHTMDM SIVLEDEKPV SVNEVPDYHE 

       190        200        210        220        230        240 
DIHTYLREME VKCKPKVGYM KKQPDITNSM RAILVDWLVE VGEEYKLQNE TLHLAVNYID 

       250        260        270        280        290        300 
RFLSSMSVLR GKLQLVGTAA MLLASKFEEI YPPEVAEFVY ITDDTYTKKQ VLRMEHLVLK 

       310        320        330        340        350        360 
VLTFDLAAPT VNQFLTQYFL HQQPANCKVE SLAMFLGELS LIDADPYLKY LPSVIAGAAF 

       370        380        390        400        410        420 
HLALYTVTGQ SWPESLIRKT GYTLESLKPC LMDLHQTYLK APQHAQQSIR EKYKNSKYHG 

       430 
VSLLNPPETL NL 

P20248 in FASTA format

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