P30274 (CCNA2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	CCNA2
Synonyms:	CCNA

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	430 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.
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 By similarity.
Subcellular location	Nucleus. Cytoplasm. Note: Cytoplasmic when associated with SCAPER By similarity.
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 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 electronic annotation. Source: Compara regulation of cyclin-dependent protein serine/threonine kinase activity Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell female pronucleus Inferred from electronic annotation. Source: Compara male pronucleus Inferred from electronic annotation. Source: Compara nucleus Inferred from sequence or structural similarity. Source: AgBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 430

430

Cyclin-A2

PRO_0000080337

Amino acid modifications

Modified residue

1

1

N-acetylmethionine By similarity

Modified residue

5

1

Phosphoserine By similarity

Experimental info

Sequence conflict

24

1

A → E in CAA48398. Ref.2

Sequence conflict

107

1

Missing in CAA48398. Ref.2

Secondary structure

1

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430

Helix Strand Turn

Details...

Helix

170 – 172

3

Turn

174 – 176

3

Helix

177 – 190

14

Turn

195 – 197

3

Helix

198 – 200

3

Helix

206 – 222

17

Helix

227 – 243

17

Helix

248 – 250

3

Helix

251 – 266

16

Helix

273 – 279

7

Turn

280 – 282

3

Helix

286 – 299

14

Turn

300 – 302

3

Helix

309 – 317

9

Beta strand

320 – 322

3

Helix

325 – 340

16

Helix

342 – 345

4

Helix

350 – 366

17

Helix

372 – 378

7

Helix

382 – 398

17

Helix

399 – 401

3

Helix

406 – 410

5

Helix

414 – 416

3

Helix

419 – 421

3

Sequences

	Sequence		Length	Mass (Da)
	P30274 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: FACA1B8E770E997F	FASTA	430	48,262
	10 20 30 40 50 60 MLGSSAHGPA AREAGSAVTL QQTAFQEDQE NVNPEKAAPA QQPRTRAGLA VLRAGNSRGP 70 80 90 100 110 120 APQRPKTRRV APLKDLPIND EYVPVPPWKA NNKQPAFTIH VDEAEEEIQK RPTESKKSES 130 140 150 160 170 180 EDVLAFNSAV TLPGPRKPLA PLDYPMDGSF ESPHTMEMSV VLEDEKPVSV NEVPDYHEDI 190 200 210 220 230 240 HTYLREMEVK CKPKVGYMKK QPDITNSMRA ILVDWLVEVG EEYKLQNETL HLAVNYIDRF 250 260 270 280 290 300 LSSMSVLRGK LQLVGTAAML LASKFEEIYP PEVAEFVYIT DDTYTKKQVL RMEHLVLKVL 310 320 330 340 350 360 AFDLAAPTIN QFLTQYFLHQ QPANCKVESL AMFLGELSLI DADPYLKYLP SVIAAAAFHL 370 380 390 400 410 420 ALYTVTGQSW PESLVQKTGY TLETLKPCLL DLHQTYLRAP QHAQQSIREK YKNSKYHGVS 430 LLNPPETLNV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Thalamus.
[2]	"Identification of the domains in cyclin A required for binding to, and activation of, p34cdc2 and p32cdk2 protein kinase subunits." Kobayashi H., Stewart E., Poon R., Adamczewski J.P., Gannon J., Hunt T. Mol. Biol. Cell 3:1279-1294(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-430. Tissue: Lymphocyte.
[3]	"The crystal structure of cyclin A." Brown N.R., Noble M.E.M., Endicott J.A., Garman E.F., Wakatsuki S., Mitchell E., Rasmussen B., Hunt T., Johnson L.N. Structure 3:1235-1247(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 179-430.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BC118203 mRNA. Translation: AAI18204.1.
X68321 mRNA. Translation: CAA48398.1.

IPI

IPI00687731.

PIR

S24788.

RefSeq

NP_001068591.1. NM_001075123.1.

UniGene

Bt.87491.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VIN	X-ray	2.00	A	170-429	[»]
2G9X	X-ray	2.50	B/D	170-429	[»]
3BHT	X-ray	2.00	B/D	169-430	[»]
3BHU	X-ray	2.30	B/D	169-430	[»]
3BHV	X-ray	2.10	B/D	169-430	[»]
3DDP	X-ray	2.70	B/D	169-430	[»]
3DDQ	X-ray	1.80	B/D	169-430	[»]
3DOG	X-ray	2.70	B/D	169-430	[»]
3MY5	X-ray	2.10	B/D	169-430	[»]
3TNW	X-ray	2.00	B/D	169-430	[»]
4BCN	X-ray	2.10	D	169-430	[»]
4BCO	X-ray	2.05	B/D	169-429	[»]
4BCQ	X-ray	2.40	B	169-429	[»]
			D	169-430	[»]

ProteinModelPortal

P30274.

SMR

P30274. Positions 169-430.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-693N.

STRING

9913.ENSBTAP00000006503.

Proteomic databases

PRIDE

P30274.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

281667.

KEGG

bta:281667.

Organism-specific databases

CTD

890.

Phylogenomic databases

eggNOG

COG5024.

HOGENOM

HOG000167672.

HOVERGEN

HBG106244.

InParanoid

P30274.

KO

K06627.

OrthoDB

EOG41RPV4.

Enzyme and pathway databases

BioCyc

CATTLE:281667-MONOMER.

Gene expression databases

ArrayExpress

P30274.

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

EvolutionaryTrace

P30274.

NextBio

20805598.

Entry information

Entry name

CCNA2_BOVIN

Accession

Primary (citable) accession number: P30274
Secondary accession number(s): Q17QS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	October 17, 2006
Last modified:	May 29, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program