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Reviewed, UniProtKB/Swiss-Prot P20248 (CCNA2_HUMAN)

Last modified June 16, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cyclin-A2
      Short name=Cyclin-A
Gene names
Name: CCNA2
Synonyms: CCN1, CCNA
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.

Subunit structure

Interacts with the CDK2 and CDC2 protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. When associated with CDK2 (but not with CDC2), interacts with SCAPER. Ref.7

Subcellular location

Nucleus. Cytoplasm. Note: Cytoplasmic when associated with SCAPER. Ref.7

Developmental stage

Accumulates steadily during G2 and is abruptly destroyed at mitosis.

Sequence similarities

Belongs to the cyclin family. Cyclin AB subfamily.

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Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   Molecular functionCyclin
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle G2/M transition DNA damage checkpoint

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from Experiment. Source: Reactome

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDKN1AP389361EBI-457097,EBI-375077
CDKN1BP465274EBI-457097,EBI-519280

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Cyclin-A2
PRO_0000080338

Natural variations

Natural variant1631V → I: dbSNP rs769242. Ref.4 Ref.5
VAR_018819

Experimental info

Sequence conflict1561H → R in CAG28620. Ref.3

Secondary structure

1 ....................................... 432
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P20248-1 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 977EA71797DB671B

FASTA43248,537
        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

« Hide

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References

« Hide 'large scale' references
[1]"Hepatitis B virus integration in a cyclin A gene in a hepatocellular carcinoma."
Wang J., Chenivesse X., Henglein B., Brechot C.
Nature 343:555-557(1990) [PubMed: 1967822] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure and cell cycle-regulated transcription of the human cyclin A gene."
Henglein B., Chenivesse X., Wang D., Eick D., Brechot C.
Proc. Natl. Acad. Sci. U.S.A. 91:5490-5494(1994) [PubMed: 8202514] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]NIEHS SNPs program
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-163.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-163.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"SCAPER, a novel cyclin A-interacting protein that regulates cell cycle progression."
Tsang W.Y., Wang L., Chen Z., Sanchez I., Dynlacht B.D.
J. Cell Biol. 178:621-633(2007) [PubMed: 17698606] [Abstract]
Cited for: INTERACTION WITH SCAPER, SUBCELLULAR LOCATION.
[8]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]"Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex."
Jeffrey P.D., Russo A.A., Polyak K., Gibbs E., Hurwitz J., Massague J., Pavletich N.P.
Nature 376:313-320(1995) [PubMed: 7630397] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 COMPLEXED WITH CDK2.
[10]"Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex."
Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.
Nature 382:325-331(1996) [PubMed: 8684460] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 IN CDK2/KIP1 COMPLEX.
[11]"Structural basis of cyclin-dependent kinase activation by phosphorylation."
Russo A.A., Jeffrey P.D., Pavletich N.P.
Nat. Struct. Biol. 3:696-700(1996) [PubMed: 8756328] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 173-432 COMPLEXED WITH CDK2.
+Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases

X51688 mRNA. Translation: CAA35986.1.
X68303 Genomic DNA. Translation: CAA48375.1.
CR407692 mRNA. Translation: CAG28620.1.
AF518006 Genomic DNA. Translation: AAM54042.1.
AC079341 Genomic DNA. Translation: AAY40969.1.
BC104783 mRNA. Translation: AAI04784.1.
BC104787 mRNA. Translation: AAI04788.1.
IPIIPI00022865.
PIRS08277.
RefSeqNP_001228.1.
UniGeneHs.58974

3D structure databases

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/D173-432[»]
2BKZX-ray2.60B/D173-432[»]
2BPMX-ray2.40B/D174-432[»]
2C4GX-ray2.70B/D173-432[»]
2C5NX-ray2.10B/D174-432[»]
2C5OX-ray2.10B/D173-432[»]
2C5PX-ray2.30B/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[»]
3EIDX-ray3.15B/D173-432[»]
3EJ1X-ray3.22B/D173-432[»]
3EOCX-ray3.20B/D173-432[»]
3F5XX-ray2.40B/D177-432[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:638N.
IntActP20248. 11 interactions.

PTM databases

PhosphoSiteP20248.

Proteomic databases

PRIDEP20248.

Genome annotation databases

EnsemblENSG00000145386. Homo sapiens. [Contig view]
GeneID890.
KEGGhsa:890.

Organism-specific databases

GeneCardsGC04M123018.
H-InvDBHIX0031483.
HGNCHGNC:1578. CCNA2.
HPACAB000114.
MIM123835. gene.
PharmGKBPA94.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP20248.
HOVERGENP20248.

Enzyme and pathway databases

Pathway_Interaction_DBil2_stat5pathway. IL2 signaling events mediated by STAT5.
prlsignalingeventspathway. Signaling events mediated by PRL.
ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_383. DNA Replication.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.

Gene expression databases

BgeeP20248.
CleanExHS_CCNA2.
GermOnlineENSG00000145386. Homo sapiens.

Family and domain databases

InterProIPR015453. CycA.
IPR006670. Cyclin.
IPR014400. Cyclin_A_B_D_E.
IPR004367. Cyclin_C.
IPR006671. Cyclin_N.
IPR013763. Cyclin_related.
[Graphical view]
Gene3DG3DSA:1.10.472.10. Cyclin_related. 1 hit.
PANTHERPTHR10177:SF23. CycA. 1 hit.
PfamPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFPIRSF001771. Cyclin_A_B_D_E. 1 hit.
SMARTSM00385. CYCLIN. 2 hits.
[Graphical view]
PROSITEPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio3682.
PMAP-CutDBP20248.
SOURCESearch...

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Entry information

Entry nameCCNA2_HUMAN
AccessionPrimary (citable) accession number: P20248
Secondary accession number(s): Q2M3U6, Q4W5P4, Q6LER8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 16, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents