Q3EDL4 (Y1154_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable serine/threonine-protein kinase At1g01540
EC=2.7.11.1

Gene names

Ordered Locus Names:	At1g01540
ORF Names:	F22L4.8

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	472 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Membrane; Single-pass membrane protein Potential.
Post-translational modification	Phosphorylation level varies significantly during early response to general elicitors.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.
Sequence caution	The sequence AAK56254.1 differs from that shown. Reason: Erroneous termination at position 473. Translated as stop. The sequence AAM16225.1 differs from that shown. Reason: Erroneous termination at position 473. Translated as stop.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein autophosphorylation Inferred from direct assay. Source: TAIR
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.5Ref.6. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay. Source: TAIR
Complete GO annotation...

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: Q3EDL4-1)

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 – 472	472	Probable serine/threonine-protein kinase At1g01540		PRO_0000302048
Regions
	Transmembrane	24 – 44	21	Helical; Potential
	Domain	154 – 431	278	Protein kinase
	Nucleotide binding	160 – 168	9	ATP By similarity
Sites
	Active site	280	1	Proton acceptor By similarity
	Binding site	182	1	ATP By similarity
Amino acid modifications
	Modified residue	67	1	Phosphothreonine Ref.5 Ref.6 Ref.7
	Modified residue	71	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: FA5E5AED90C5862D	FASTA	472	52,325
	10 20 30 40 50 60 MSVYDAAFLN TELSKPTSIF GLRLWVVIGI LLGSLIVIAL FLLSLCLTSR RKNRKPRADF 70 80 90 100 110 120 ASAAIATPPI SKEIKEIVPA QNQSVPAEIQ VDIGKIEHRV VFSDRVSSGE SRGTASASET 130 140 150 160 170 180 ASYSGSGNCG PEVSHLGWGR WYTLRELEAA TNGLCEENVI GEGGYGIVYR GILTDGTKVA 190 200 210 220 230 240 VKNLLNNRGQ AEKEFKVEVE VIGRVRHKNL VRLLGYCVEG AYRMLVYDFV DNGNLEQWIH 250 260 270 280 290 300 GDVGDVSPLT WDIRMNIILG MAKGLAYLHE GLEPKVVHRD IKSSNILLDR QWNAKVSDFG 310 320 330 340 350 360 LAKLLGSESS YVTTRVMGTF GYVAPEYACT GMLNEKSDIY SFGILIMEII TGRNPVDYSR 370 380 390 400 410 420 PQGETNLVDW LKSMVGNRRS EEVVDPKIPE PPSSKALKRV LLVALRCVDP DANKRPKMGH 430 440 450 460 470 IIHMLEAEDL LYRDERRTTR DHGSRERQET AVVAAGSESG ESGSRHHQQK QR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of a 40-kb Arabidopsis thaliana genomic region located at the top of chromosome 1." Terryn N., Gielen J., De Keyser A., Van Den Daele H., Ardiles W., Neyt P., De Clercq R., Coppieters J., Dehais P., Villarroel R., Rouze P., van Montagu M. Gene 215:11-17(1998) [PubMed: 9666060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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.
[5]	"Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry." Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C. Mol. Cell. Proteomics 2:1234-1243(2003) [PubMed: 14506206] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-67 AND SER-71, MASS SPECTROMETRY. Strain: cv. La-0.
[6]	"Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis." Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H. Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed: 17317660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-67, MASS SPECTROMETRY. Strain: cv. Columbia.
[7]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-67, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Web resources

PlantP kinase Classification PPC

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y12776 Genomic DNA. Translation: CAA73303.1. AC061957 Genomic DNA. Translation: AAF81312.1. CP002684 Genomic DNA. Translation: AEE27302.1. AF332429 mRNA. Translation: AAG48792.1. AF367265 mRNA. Translation: AAK56254.1. Sequence problems. AY093964 mRNA. Translation: AAM16225.1. Sequence problems.
IPI	IPI00528543.
PIR	A86146.
RefSeq	NP_171661.1. NM_100036.4.
UniGene	At.24027.
3D structure databases
ProteinModelPortal	Q3EDL4.
SMR	Q3EDL4. Positions 144-428.
ModBase	Search...
Proteomic databases
PRIDE	Q3EDL4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G01540.2; AT1G01540.2; AT1G01540.
GeneID	839533.
GenomeReviews	Gene locus AT1G01540 in contig CT485782_GR.
KEGG	ath:AT1G01540.
NMPDR	fig|3702.1.peg.263.
Organism-specific databases
GeneFarm	2081. 166.
TAIR	At1g01540.
Phylogenomic databases
HOGENOM	HBG755340.
InParanoid	Q3EDL4.
OMA	VIGRVRH.
PhylomeDB	Q3EDL4.
ProtClustDB	CLSN2682866.
Gene expression databases
Genevestigator	Q3EDL4.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Y1154_ARATH

Accession

Primary (citable) accession number: Q3EDL4
Secondary accession number(s): O23699, Q94KD9, Q9LMM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	September 21, 2011
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program