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P20248 (CCNA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-A2

Short name=Cyclin-A
Gene names
Name:CCNA2
Synonyms:CCN1, CCNA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 CDK1 and CDK2 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 CDK1), interacts with SCAPER. Ref.9

Subcellular location

Nucleus. Cytoplasm. Note: Cytoplasmic when associated with SCAPER. Ref.9

Developmental stage

Accumulates steadily during G2 and is abruptly destroyed at mitosis.

Post-translational modification

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 By similarity.

Sequence similarities

Belongs to the cyclin family. Cyclin AB subfamily.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   Molecular functionCyclin
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

Ras protein signal transduction

Inferred from expression pattern PubMed 9054499. Source: BHF-UCL

mitotic G2 DNA damage checkpoint

Traceable author statement PubMed 1312467. Source: ProtInc

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

organ regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

regulation of G2/M transition of mitotic cell cycle

Inferred from electronic annotation. Source: InterPro

regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to glucagon

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 23791195. Source: MGI

female pronucleus

Inferred from electronic annotation. Source: Ensembl

male pronucleus

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 16109376. Source: MGI

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 11141566PubMed 12244298PubMed 12941338PubMed 15189033PubMed 15239650PubMed 15890360PubMed 16209941PubMed 17254966PubMed 21952639PubMed 23455922PubMed 23602568PubMed 8411358Ref.15Ref.16. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Cyclin-A2
PRO_0000080338

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10
Modified residue51Phosphoserine Ref.10
Modified residue551Phosphoserine Ref.10

Natural variations

Natural variant1631I → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.17
Corresponds to variant rs769242 [ dbSNP | Ensembl ].
VAR_018819

Experimental info

Sequence conflict1561H → R in CAG28620. Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P20248 [UniParc].

Last modified November 2, 2010. Version 2.
Checksum: 97763A2897DD35F4

FASTA43248,551
        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 SIILEDEKPV 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

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-163.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-163.
[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], VARIANT VAL-163.
[4]NIEHS SNPs program
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-163.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-163.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-163.
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-163.
Tissue: Brain.
[9]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCAPER, SUBCELLULAR LOCATION.
[10]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry."
Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G., Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.
Mol. Cell 42:511-523(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP37.
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 COMPLEXED WITH CDK2.
[15]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 IN CDK2/KIP1 COMPLEX.
[16]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 173-432 COMPLEXED WITH CDK2.
[17]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3723.1.
PIRS08277.
RefSeqNP_001228.1. NM_001237.3.
UniGeneHs.58974.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
4CFNX-ray2.20B/D175-432[»]
4CFWX-ray2.45B/D175-432[»]
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[»]
ProteinModelPortalP20248.
SMRP20248. Positions 176-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107331. 71 interactions.
DIPDIP-638N.
IntActP20248. 27 interactions.
MINTMINT-141826.
STRING9606.ENSP00000274026.

Chemistry

BindingDBP20248.
ChEMBLCHEMBL2582.

PTM databases

PhosphoSiteP20248.

Polymorphism databases

DMDM311033358.

Proteomic databases

MaxQBP20248.
PaxDbP20248.
PRIDEP20248.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274026; ENSP00000274026; ENSG00000145386.
GeneID890.
KEGGhsa:890.
UCSCuc003iec.4. human.

Organism-specific databases

CTD890.
GeneCardsGC04M122737.
HGNCHGNC:1578. CCNA2.
HPACAB000114.
HPA020626.
MIM123835. gene.
neXtProtNX_P20248.
PharmGKBPA94.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5024.
HOGENOMHOG000167672.
HOVERGENHBG106244.
InParanoidP20248.
KOK06627.
OMANPEKAAP.
OrthoDBEOG7G7KQ0.
PhylomeDBP20248.
TreeFamTF101002.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_383. DNA Replication.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
SignaLinkP20248.

Gene expression databases

BgeeP20248.
CleanExHS_CCNA2.
GenevestigatorP20248.

Family and domain databases

Gene3D1.10.472.10. 2 hits.
InterProIPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E/F.
IPR015453. Cyclin_A_chordates.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERPTHR10177:SF69. PTHR10177:SF69. 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]
SUPFAMSSF47954. SSF47954. 2 hits.
PROSITEPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20248.
GeneWikiCyclin_A2.
GenomeRNAi890.
NextBio3682.
PMAP-CutDBP20248.
PROP20248.
SOURCESearch...

Entry information

Entry nameCCNA2_HUMAN
AccessionPrimary (citable) accession number: P20248
Secondary accession number(s): A8K7B6 expand/collapse secondary AC list , Q2M3U6, Q4W5P4, Q6LER8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM