Reviewed, UniProtKB/Swiss-Prot P51567 (AFC2_ARATH)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase AFC2
    EC=2.7.12.1

Gene names

Name:	AFC2
Ordered Locus Names:	At4g24740
ORF Names:	F22K18.60

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	mRNA processing Inferred from direct assay. Source: TAIR protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RSZp22	O23646	1	EBI-1792180,EBI-1792215
scl33	Q9SEU4	2	EBI-1792180,EBI-927103
SR45	Q9SEE9	1	EBI-1792180,EBI-1792008

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P51567-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 427	427	Serine/threonine-protein kinase AFC2		PRO_0000085601
Regions
	Domain	98 – 423	326	Protein kinase
	Nucleotide binding	104 – 112	9	ATP By similarity
Sites
	Active site	223	1	Proton acceptor By similarity
	Binding site	127	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 33A1948B8372B374	FASTA	427	49,566
	10 20 30 40 50 60 MEMERVHEFP HTHMDRRPRK RARLGWDVLP QATKAQVGMF CGQEIGNISS FASSGAPSDN 70 80 90 100 110 120 SSSLCVKGVA RNGSPPWRED DKDGHYIFEL GDDLTPRYKI YSKMGEGTFG QVLECWDRER 130 140 150 160 170 180 KEMVAVKIVR GVKKYREAAM IEIEMLQQLG KHDKGGNRCV QIRNWFDYRN HICIVFEKLG 190 200 210 220 230 240 SSLYDFLRKN NYRSFPIDLV REIGWQLLEC VAFMHDLRMI HTDLKPENIL LVSSDYVKIP 250 260 270 280 290 300 EYKGSRLQRD VCYKRVPKSS AIKVIDFGST TYERQDQTYI VSTRHYRAPE VILGLGWSYP 310 320 330 340 350 360 CDVWSVGCII VELCTGEALF QTHENLEHLA MMERVLGPFP QQMLKKVDRH SEKYVRRGRL 370 380 390 400 410 420 DWPDGATSRD SLKAVLKLPR LQNLIMQHVD HSAGELINMV QGLLRFDPSE RITAREALRH PFFARRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"AFC1, a LAMMER kinase from Arabidopsis thaliana, activates STE12-dependent processes in yeast." Bender J., Fink G.R. Proc. Natl. Acad. Sci. U.S.A. 91:12105-12109(1994) [PubMed: 7991592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Landsberg erecta.
[2]	"A.thaliana genes encoding protein kinases of a new family." Kuromori T., Yamamoto M. Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U16177 mRNA. Translation: AAA57118.1. D45353 mRNA. Translation: BAA08214.1. AL035356 Genomic DNA. Translation: CAA22989.1. AL161562 Genomic DNA. Translation: CAB79384.1.
IPI	IPI00543604.
PIR	T05560.
RefSeq	NP_194205.1.
UniGene	At.67573 At.73921
3D structure databases
HSSP	HSSP built from PDB template 1HOW based on UniProtKB Q03656.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51567. 4 interactions.
Genome annotation databases
GeneID	828576.
GenomeReviews	Gene locus AT4G24740 in contig CT486007_GR.
KEGG	ath:AT4G24740.
Organism-specific databases
TAIR	At4g24740.
Phylogenomic databases
OMA	P51567. HYSKSSG.
Enzyme and pathway databases
BRENDA	2.7.12.1. 302.
Gene expression databases
ArrayExpress	P51567.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AFC2_ARATH

Accession

Primary (citable) accession number: P51567

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)