Reviewed, UniProtKB/Swiss-Prot Q944A7 (Y4523_ARATH)

Names and origin

Protein names

Recommended name:
    Putative serine/threonine-protein kinase At4g35230
    EC=2.7.11.1

Gene names

Ordered Locus Names:	At4g35230
ORF Names:	F23E12.210

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	512 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Cell membrane; Lipid-anchor Potential.
Sequence similarities	Contains 1 protein kinase domain.
Sequence caution	The sequence CAA18746.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB80240.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	brassinosteroid mediated signaling Inferred from direct assay. Source: TAIR protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	plasma membrane Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
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 protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRI1	O22476	4	EBI-1797846,EBI-1797828

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Potential
	Chain	2 – 512	511	Putative serine/threonine-protein kinase At4g35230		PRO_0000324844
Regions
	Domain	76 – 331	256	Protein kinase
	Nucleotide binding	82 – 90	9	ATP By similarity
	Coiled coil	483 – 508	26	Potential
	Compositional bias	30 – 54	25	Gly-rich
Sites
	Active site	198	1	Proton acceptor By similarity
	Binding site	104	1	ATP By similarity
Amino acid modifications
	Modified residue	230	1	Phosphoserine Ref.3
	Lipidation	2	1	N-myristoyl glycine Potential
	Lipidation	3	1	S-palmitoyl cysteine Potential
	Lipidation	4	1	S-palmitoyl cysteine Potential

Sequences

	Sequence		Length	Mass (Da)
	Q944A7-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 3087B726C5049864	FASTA	512	56,818
	10 20 30 40 50 60 MGCCQSLFSG DNPLGKDGVQ PQPLSQNNHG GATTADNGGS GGASGVGGGG GGGGIPSFSE 70 80 90 100 110 120 FSFADLKAAT NNFSSDNIVS ESGEKAPNLV YKGRLQNRRW IAVKKFTKMA WPEPKQFAEE 130 140 150 160 170 180 AWGVGKLRHN RLANLIGYCC DGDERLLVAE FMPNDTLAKH LFHWENQTIE WAMRLRVGYY 190 200 210 220 230 240 IAEALDYCST EGRPLYHDLN AYRVLFDEDG DPRLSCFGLM KNSRDGKSYS TNLAYTPPEY 250 260 270 280 290 300 LRNGRVTPES VTYSFGTVLL DLLSGKHIPP SHALDMIRGK NIILLMDSHL EGKFSTEEAT 310 320 330 340 350 360 VVVELASQCL QYEPRERPNT KDLVATLAPL QTKSDVPSYV MLGIKKQEEA PSTPQRPLSP 370 380 390 400 410 420 LGEACSRMDL TAIHQILVMT HYRDDEGTNE LSFQEWTQQM KDMLDARKRG DQSFREKDFK 430 440 450 460 470 480 TAIDCYSQFI DVGTMVSPTV FGRRSLCYLL CDQPDAALRD AMQAQCVYPD WPTAFYMQSV 490 500 510 ALAKLNMNTD AADMLNEAAQ LEEKRQRGGR GS

References

[1]	"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.
[2]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis." Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X. Mol. Cell. Proteomics 6:1711-1726(2007) [PubMed: 17586839] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL022604 Genomic DNA. Translation: CAA18746.1. Sequence problems. AL161587 Genomic DNA. Translation: CAB80240.1. Sequence problems. AF439824 mRNA. Translation: AAL27496.1. AY142063 mRNA. Translation: AAM98327.1.
IPI	IPI00530358.
PIR	T06134.
RefSeq	NP_567980.1.
UniGene	At.19802
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q944A7. 1 interaction.
Proteomic databases
PRIDE	Q944A7.
Genome annotation databases
GeneID	829676.
GenomeReviews	Gene locus AT4G35230 in contig CT486007_GR.
KEGG	ath:AT4G35230.
NMPDR	fig|3702.1.peg.21600.
Organism-specific databases
GeneFarm	1675. 123.
TAIR	At4g35230.
Phylogenomic databases
OMA	Q944A7. THYRDDE.
Enzyme and pathway databases
BRENDA	2.7.11.1. 302.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR011990. TPR-like_helical. IPR001245. Tyr_pkinase. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 1 hit.
Pfam	PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Y4523_ARATH

Accession

Primary (citable) accession number: Q944A7
Secondary accession number(s): O65504

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)