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UniProtKB/Swiss-Prot entry P27450


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CX32_ARATH
Primary accession number P27450
Secondary accession numbers O81792 Q8VZ07 Q9M068
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on June 21, 2004 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 73)
Name and origin of the protein
Protein name Probable serine/threonine-protein kinase Cx32, chloroplastic [Precursor]
Synonym EC 2.7.11.1
Gene name
OrderedLocusNames: At4g35600
ORFNames: F8D20.110
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1851993 [NCBI, ExPASy, EBI, Israel, Japan]
Meiners S., Xu A., Schindler M.;
"Gap junction protein homologue from Arabidopsis thaliana: evidence for connexins in plants.";
Proc. Natl. Acad. Sci. U.S.A. 88:4119-4122(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
DISCUSSION OF SEQUENCE.
DOI=10.1105/tpc.5.9.998; PubMed=8400879 [NCBI, ExPASy, EBI, Israel, Japan]
Mushegian A.R., Koonin E.V.;
"The proposed plant connexin is a protein kinase-like protein.";
Plant Cell 5:998-999(1993).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND MASS SPECTROMETRY.
DOI=10.1105/tpc.104.023150; PubMed=15308754 [NCBI, ExPASy, EBI, Israel, Japan]
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database.";
Plant Cell 16:2394-2405(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700164-MCP200; PubMed=17586839 [NCBI, ExPASy, EBI, Israel, Japan]
Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
"Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis.";
Mol. Cell. Proteomics 6:1711-1726(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M63234; AAA32850.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031135; CAA20030.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161587; CAB80276.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY065403; AAL38844.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY096501; AAM20151.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39357; A39357.
C85420; C85420.
T04665; T04665.
RefSeq NP_195285.3; -.
UniGene At.57035
3D structure databases
ModBase P27450.
Protein-protein interaction databases
IntAct P27450; -.
Organism-specific databases
GeneFarm 1725; 129.
TAIR At4g35600; -.
Gene expression databases
ArrayExpress P27450; -.
GermOnline AT4G35600; Arabidopsis thaliana.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from InterPro).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P27450.
ProtoNet P27450.
Proteomic databases
ProMEX P27450; -.
Genome annotation databases
GeneID 829712; -.
GenomeReviews CT486007_GR; AT4G35600.
KEGG ath:AT4G35600; -.
NMPDR fig|3702.1.peg.21645; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Chloroplast; Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein; Plastid; Serine/threonine-protein kinase; Transferase; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    42  42     Chloroplast (Potential). 
CHAIN   43   419  377     Probable serine/threonine-protein kinase Cx32, chloroplastic. PRO_0000024321
DOMAIN   86   368  283     Protein kinase. 
NP_BIND   92   100  9     ATP (By similarity). 
COMPBIAS   9    14  6     Poly-Ser. 
ACT_SITE   218   218        Proton acceptor (By similarity). 
BINDING   124   124        ATP (By similarity). 
MOD_RES   117   117        Phosphoserine. 
Sequence information
Length: 419 AA [This is the length of the unprocessed precursor] Molecular weight: 46340 Da [This is the MW of the unprocessed precursor] CRC64: 7C85AB6C38925145 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGACISFFSS SSPSKTGLHS HATTNNHSNG TEFSSTTGAT TNSSVGQQSQ FSDISTGIIS 

        70         80         90        100        110        120 
DSGKLLESPN LKVYNFLDLK TATKNFKPDS MLGQGGFGKV YRGWVDATTL APSRVGSGMI 

       130        140        150        160        170        180 
VAIKRLNSES VQGFAEWRSE VNFLGMLSHR NLVKLLGYCR EDKELLLVYE FMPKGSLESH 

       190        200        210        220        230        240 
LFRRNDPFPW DLRIKIVIGA ARGLAFLHSL QREVIYRDFK ASNILLDSNY DAKLSDFGLA 

       250        260        270        280        290        300 
KLGPADEKSH VTTRIMGTYG YAAPEYMATG HLYVKSDVFA FGVVLLEIMT GLTAHNTKRP 

       310        320        330        340        350        360 
RGQESLVDWL RPELSNKHRV KQIMDKGIKG QYTTKVATEM ARITLSCIEP DPKNRPHMKE 

       370        380        390        400        410 
VVEVLEHIQG LNVVPNRSST KQAVANSSRS SPHHYRYKAG ALGAERKRAT PGRFGSVEK 

P27450 in FASTA format

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View entry in raw text format (no links)
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