P51943 (CCNA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclin-A2
Short name=Cyclin-A

Gene names

Name:	Ccna2
Synonyms:	Ccna, Cyca

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.6
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. In the testis, interacts only with CDK2. When associated with CDK2 (but not with CDK1), interacts with SCAPER By similarity.
Subcellular location	Nucleus. Cytoplasm. Note: Cytoplasmic when associated with SCAPER By similarity.
Tissue specificity	Ubiquitous. In the testis, expressed in germ cells and in the ovary, in both germline and somatic cells.
Developmental stage	Accumulates steadily during G2 and is abruptly destroyed at mitosis. Expressed in spermatogonia and is most abundant in preleptotene spermatocytes, cells which will enter the meiotic pathway.
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 process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Nucleus
Molecular function	Cyclin
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Ras protein signal transduction Inferred from electronic annotation. Source: Compara cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription, DNA-dependent Inferred from mutant phenotype PubMed 16137671. Source: MGI regulation of cyclin-dependent protein serine/threonine kinase activity Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from direct assay PubMed 15159393. Source: MGI female pronucleus Inferred from direct assay PubMed 16137671. Source: MGI male pronucleus Inferred from direct assay PubMed 16137671. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cdk1	P11440	2	EBI-846980,EBI-846949
Cdk2	P97377	3	EBI-846980,EBI-847048

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 422

422

Cyclin-A2

PRO_0000080340

Amino acid modifications

Modified residue

1

1

N-acetylmethionine By similarity

Modified residue

5

1

Phosphoserine By similarity

Experimental info

Sequence conflict

127

1

G → A in CAA81331. Ref.1

Sequence conflict

127

1

G → A in CAA53212. Ref.2

Sequence conflict

391

1

A → P in CAA53212. Ref.2

Secondary structure

1

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422

Helix Strand Turn

Details...

Helix

166 – 182

17

Helix

189 – 192

4

Helix

198 – 214

17

Helix

219 – 235

17

Helix

240 – 242

3

Helix

243 – 258

16

Helix

265 – 271

7

Beta strand

274 – 276

3

Helix

278 – 291

14

Turn

292 – 294

3

Helix

301 – 308

8

Helix

309 – 311

3

Beta strand

312 – 314

3

Helix

317 – 332

16

Helix

334 – 337

4

Helix

342 – 358

17

Helix

364 – 370

7

Helix

374 – 390

17

Helix

391 – 393

3

Helix

398 – 402

5

Helix

406 – 408

3

Helix

411 – 413

3

Sequences

	Sequence		Length	Mass (Da)
	P51943 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 1818B92552E4D0D1	FASTA	422	47,269
	10 20 30 40 50 60 MPGTSRHSGR DAGSALLSLH QEDQENVNPE KLAPAQQPRA QAVLKAGNVR GPAPQQKLKT 70 80 90 100 110 120 RRVAPLKDLP INDEHVTAGP SWKAVSKQPA FTIHVDEAEE TQKRPAELKE TECEDALAFN 130 140 150 160 170 180 AAVSLPGARK PLTPLDYPMD GSFESPHAMD MSIVLEDKPV NVNEVPDYQE DIHTYLREME 190 200 210 220 230 240 VKCKPKVGYM KRQPDITNSM RAILVDWLVE VGEEYKLQNE TLHLAVNYID RFLSSMSVLR 250 260 270 280 290 300 GKLQLVGTAA MLLASKFEEI YPPEVAEFVY ITDDTYSKKQ VLRMEHLVLK VLAFDLAAPT 310 320 330 340 350 360 VNQFLTQYFL HLQPANCKVE SLAMFLGELS LIDADPYLKY LPSLIAGAAF HLALYTVTGQ 370 380 390 400 410 420 SWPESLAQQT GYTLESLKPC LVDLHQTYLK APQHAQQSIR EKYKHSKYHS VSLLNPPETL SV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The developmentally restricted pattern of expression in the male germ line of a murine cyclin A, cyclin A2, suggests roles in both mitotic and meiotic cell cycles." Ravnik S.E., Wolgemuth D.J. Dev. Biol. 173:69-78(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A distinct cyclin A is expressed in germ cells in the mouse." Sweeney C., Murphy M., Kubelka M., Ravnik S.E., Hawkins C.F., Wolgemuth D.J., Carrington M. Development 122:53-64(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Thymus.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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].
[6]	"Regulation of meiosis during mammalian spermatogenesis: the A-type cyclins and their associated cyclin-dependent kinases are differentially expressed in the germ-cell lineage." Ravnik S.E., Wolgemuth D.J. Dev. Biol. 207:408-418(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: Swiss Webster.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z26580 mRNA. Translation: CAA81331.1.
X75483 mRNA. Translation: CAA53212.1.
AK044924 mRNA. Translation: BAC32144.1.
CH466530 Genomic DNA. Translation: EDL35081.1.
BC052730 mRNA. Translation: AAH52730.1.

IPI

IPI00128671.

PIR

S37280.
S38501.

RefSeq

NP_033958.2. NM_009828.2.

UniGene

Mm.4189.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QHR	X-ray	2.17	B/D	163-422	[»]
3QHW	X-ray	1.91	B/D	163-422	[»]
4I3Z	X-ray	2.05	B/D	165-421	[»]
4II5	X-ray	2.15	B/D	165-422	[»]

ProteinModelPortal

P51943.

SMR

P51943. Positions 163-422.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-45864N.

IntAct

P51943. 3 interactions.

STRING

10090.ENSMUSP00000029270.

PTM databases

PhosphoSite

P51943.

Proteomic databases

PaxDb

P51943.

PRIDE

P51943.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000029270; ENSMUSP00000029270; ENSMUSG00000027715.

GeneID

12428.

KEGG

mmu:12428.

Organism-specific databases

CTD

890.

MGI

MGI:108069. Ccna2.

Phylogenomic databases

eggNOG

COG5024.

GeneTree

ENSGT00560000076692.

HOGENOM

HOG000167672.

HOVERGEN

HBG106244.

InParanoid

Q8BRG1.

KO

K06627.

OMA

NPEKAAP.

OrthoDB

EOG41RPV4.

Enzyme and pathway databases

Reactome

REACT_118161. Cell Cycle.

Gene expression databases

ArrayExpress

P51943.

Bgee

P51943.

CleanEx

MM_CCNA2.

Genevestigator

P51943.

GermOnline

ENSMUSG00000027715. Mus musculus.

Family and domain databases

Gene3D

1.10.472.10. 2 hits.

InterPro

IPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]

Pfam

PF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]

PIRSF

PIRSF001771. Cyclin_A_B_D_E. 1 hit.

SMART

SM00385. CYCLIN. 2 hits.
[Graphical view]

SUPFAM

SSF47954. Cyclin_like. 2 hits.

PROSITE

PS00292. CYCLINS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CCNA2. mouse.

NextBio

281244.

SOURCE

Search...

Entry information

Entry name

CCNA2_MOUSE

Accession

Primary (citable) accession number: P51943
Secondary accession number(s): Q61459, Q8BRG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program