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Reviewed, UniProtKB/Swiss-Prot P51567 (AFC2_ARATH)

Last modified February 9, 2010. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Serine/threonine-protein kinase AFC2
    EC=2.7.12.1
Gene names
Name: AFC2
Ordered Locus Names: At4g24740
ORF Names: F22K18.60
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Serine/threonine-protein kinase AFC2
PRO_0000085601

Regions

Domain98 – 423326Protein kinase
Nucleotide binding104 – 1129ATP By similarity

Sites

Active site2231Proton acceptor By similarity
Binding site1271ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 33A1948B8372B374

FASTA42749,566
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16177 mRNA. Translation: AAA57118.1.
D45353 mRNA. Translation: BAA08214.1.
AL035356 Genomic DNA. Translation: CAA22989.1.
AL161562 Genomic DNA. Translation: CAB79384.1.
IPIIPI00543604.
PIRT05560.
RefSeqNP_194205.1.
UniGeneAt.67573
At.73921

3D structure databases

SMRP51567. Positions 84-425.
ModBaseSearch...

Protein-protein interaction databases

IntActP51567. 4 interactions.
STRINGP51567.

Genome annotation databases

GeneID828576.
GenomeReviewsGene locus AT4G24740 in contig CT486007_GR.
KEGGath:AT4G24740.

Organism-specific databases

TAIRAt4g24740.

Phylogenomic databases

eggNOGKOG0671.
HOGENOMHBG755340.
InParanoidP51567.
OMAGPAEMYQ.
PhylomeDBP51567.

Enzyme and pathway databases

BRENDA2.7.12.1. 302.

Gene expression databases

ArrayExpressP51567.
GenevestigatorP51567.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAFC2_ARATH
AccessionPrimary (citable) accession number: P51567
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 9, 2010
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

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