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Protein ACTIVITY OF BC1 COMPLEX KINASE 1, chloroplastic (ABC1-LIKE KINASE 1) (EC 2.7.-.-) (EC 2.7.11.1) (Protein ABC1-LIKE KINASE RELATED TO CHLOROPHYLL DEGRADATION AND OXIDATIVE STRESS 1) (AtACDO1) (Protein BLEACHING AND DWARF IN RED LIGHT 1) (Protein PROTON GRADIENT REGULATION 6)

 AB1K1_ARATH             Reviewed;         682 AA.
Q8RWG1; O49588;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
22-NOV-2017, entry version 111.
RecName: Full=Protein ACTIVITY OF BC1 COMPLEX KINASE 1, chloroplastic {ECO:0000303|PubMed:23673981};
Short=ABC1-LIKE KINASE 1 {ECO:0000303|PubMed:23673981};
EC=2.7.-.- {ECO:0000255|PROSITE-ProRule:PRU00159};
EC=2.7.11.1 {ECO:0000269|PubMed:24267661};
AltName: Full=Protein ABC1-LIKE KINASE RELATED TO CHLOROPHYLL DEGRADATION AND OXIDATIVE STRESS 1 {ECO:0000303|PubMed:22447966};
Short=AtACDO1 {ECO:0000303|PubMed:22447966};
AltName: Full=Protein BLEACHING AND DWARF IN RED LIGHT 1 {ECO:0000303|PubMed:25882344};
AltName: Full=Protein PROTON GRADIENT REGULATION 6 {ECO:0000303|PubMed:24267661};
Flags: Precursor;
Name=ABC1K1 {ECO:0000303|PubMed:23673981};
Synonyms=ACDO1 {ECO:0000303|PubMed:22447966},
BDR1 {ECO:0000303|PubMed:25882344},
PGR6 {ECO:0000303|PubMed:24267661};
OrderedLocusNames=At4g31390 {ECO:0000312|Araport:AT4G31390};
ORFNames=F3L17.6 {ECO:0000312|EMBL:CAB79857.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
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).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=16461379; DOI=10.1104/pp.105.076083;
Ytterberg A.J., Peltier J.-B., van Wijk K.J.;
"Protein profiling of plastoglobules in chloroplasts and chromoplasts.
A surprising site for differential accumulation of metabolic
enzymes.";
Plant Physiol. 140:984-997(2006).
[5]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INDUCTION BY METHYL VIOLOGEN.
STRAIN=cv. Columbia;
PubMed=22447966; DOI=10.1093/jxb/ers072;
Yang S., Zeng X., Li T., Liu M., Zhang S., Gao S., Wang Y., Peng C.,
Li L., Yang C.;
"AtACDO1, an ABC1-like kinase gene, is involved in chlorophyll
degradation and the response to photooxidative stress in
Arabidopsis.";
J. Exp. Bot. 63:3959-3973(2012).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=22274653; DOI=10.1104/pp.111.193144;
Lundquist P.K., Poliakov A., Bhuiyan N.H., Zybailov B., Sun Q.,
van Wijk K.J.;
"The functional network of the Arabidopsis plastoglobule proteome
based on quantitative proteomics and genome-wide coexpression
analysis.";
Plant Physiol. 158:1172-1192(2012).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH ABC1K3.
STRAIN=cv. Columbia;
PubMed=23673981; DOI=10.1105/tpc.113.111120;
Lundquist P.K., Poliakov A., Giacomelli L., Friso G., Appel M.,
McQuinn R.P., Krasnoff S.B., Rowland E., Ponnala L., Sun Q.,
van Wijk K.J.;
"Loss of plastoglobule kinases ABC1K1 and ABC1K3 causes conditional
degreening, modified prenyl-lipids, and recruitment of the jasmonic
acid pathway.";
Plant Cell 25:1818-1839(2013).
[8]
FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
STRAIN=cv. Columbia;
PubMed=24267661; DOI=10.1111/tpj.12385;
Martinis J., Glauser G., Valimareanu S., Stettler M., Zeeman S.C.,
Yamamoto H., Shikanai T., Kessler F.;
"ABC1K1/PGR6 kinase: a regulatory link between photosynthetic activity
and chloroplast metabolism.";
Plant J. 77:269-283(2014).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=25882344; DOI=10.1016/j.molp.2015.04.003;
Huang H., Yang M., Su Y., Qu L., Deng X.W.;
"Arabidopsis atypical kinases ABC1K1 and ABC1K3 act oppositely to cope
with photodamage under red light.";
Mol. Plant 8:1122-1124(2015).
-!- FUNCTION: Kinase that can phosphorylates the tocopherol cyclase
VTE1, a key enzyme of tocopherol (vitamin E) metabolism and
involved in the recycling of oxidated alpha-tocopherol quinone,
possibly stabilizing it at plastoglobules. Regulates also
plastoglobule protein composition (PubMed:24267661). Prevents
photodamage of chloroplasts under continuous red light, thus
working in opposition to ABC1K3 (PubMed:25882344). Together with
ABC1K1, contributes to plastoglobule (PG) function in prenyl-lipid
metabolism, stress response, and thylakoid remodeling
(PubMed:23673981, PubMed:24267661). Involved in chlorophyll
degradation and in the maintenance of the number of chlorophyll-
binding photosynthetic thylakoid membranes (PubMed:22447966).
Ensures photosynthetic electron transport by regulating the
homeostasis of plastoquinone, beta-carotene and xanthophyll
lutein, as well as membrane antioxidant tocopherol metabolism
(PubMed:24267661). Seems to affect specifically stability or
turnover of D1 protein, product of psbA, one of the four core
subunits of the photosystem II (PSII) (PubMed:25882344). Required
for photooxidative stress responses, including the induction of
oxidative stress response genes (e.g. FSD1, CSD1, CAT1, and
UTG71C1), to prevent photosystem II core and chlorophyll
degradations (PubMed:22447966, PubMed:23673981, PubMed:24267661).
{ECO:0000269|PubMed:22447966, ECO:0000269|PubMed:23673981,
ECO:0000269|PubMed:24267661, ECO:0000269|PubMed:25882344}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:24267661}.
-!- SUBUNIT: Interacts with ABC1K3 in plastoglobules (PG).
{ECO:0000269|PubMed:23673981}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
{ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653}.
Plastid, chloroplast {ECO:0000269|PubMed:22447966}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8RWG1-1; Sequence=Displayed;
Name=2;
IsoId=Q8RWG1-2; Sequence=VSP_025072;
Note=Derived from EST data. No experimental confirmation
available. {ECO:0000312|EMBL:AEE85904.1};
-!- TISSUE SPECIFICITY: Expressed in all tissues (e.g. especially in
leaves) at all developmental stages from seed germination to
flowering, except in the root tips. {ECO:0000269|PubMed:22447966}.
-!- INDUCTION: Up-regulated by methyl viologen (paraquat, MV)
treatment, an herbicide triggering photooxidative stress.
{ECO:0000269|PubMed:22447966}.
-!- DISRUPTION PHENOTYPE: High chlorophyll fluorescence and reduced
non-photochemical quenching (NPQ) caused by defects in
photosynthetic electron transport. Specifically deficient in the
electron carrier plastoquinone, as well as in beta-carotene and
the xanthophyll lutein, and defective in membrane antioxidant
tocopherol metabolism. Altered plastoglobule protein composition
(PubMed:24267661). Abnormal development with albino cotyledons and
paler mesophyll cells leading to yellow-green leaves due to
reduced contents of carotenoids and chlorophyll, as well as
changes in the numbers of chlorophyll-binding proteins of the
photosynthetic complexes (PubMed:22447966, PubMed:24267661,
PubMed:25882344). In bdr1-1 and bdr1-2, increased accumulation of
anthocyanin under red and blue light conditions. Exposure to red
light for 5 days leads to dwarf plants with pale green rosette
leaves. Reduced level of D1 protein, product of psbA, one of the
four core subunits of the photosystem II (PSII) (PubMed:25882344).
Increased levels of chlorophyll degradation products such as
chlorophyllide (Chlide) a and pheophorbide a. Stronger
photosynthetic and metabolic perturbations in response to high
light stress and methyl viologen (paraquat, MV), an herbicide
triggering photooxidative stress, strongly affecting carbohydrate
metabolism (PubMed:22447966, PubMed:24267661). However, the mutant
acclimates to high light after 7 days together with a recovery of
carotenoid levels and a drastic alteration in the starch-to-
sucrose ratio (PubMed:24267661). Lower transcript levels of the
oxidative stress response genes FSD1, CSD1, CAT1, and UTG71C1
after MV treatment (PubMed:22447966). Conditional light stress
phenotype in the double mutant abc1k1 abc1k3 that displays rapid
chlorosis upon high light stress and slower, but irreversible,
senescence-like phenotype during moderate light stress, drought or
nitrogen limitation, but not cold stress. This senescence-like
phenotype is associated with the degradation of the photosystem II
core and up-regulation of chlorophyll degradation. Modified
prenyl-lipid composition in plastoglobules (PG) probably due to
reduced VTE1 activity and loss of CCD4. Abnormal recruitement of
plastid jasmonate biosynthesis enzymes in PG (PubMed:23673981).
{ECO:0000269|PubMed:22447966, ECO:0000269|PubMed:23673981,
ECO:0000269|PubMed:24267661, ECO:0000269|PubMed:25882344}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK
protein kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA16542.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB79857.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AL021633; CAA16542.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161578; CAB79857.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE85903.1; -; Genomic_DNA.
EMBL; CP002687; AEE85904.1; -; Genomic_DNA.
EMBL; AY093113; AAM13112.1; -; mRNA.
EMBL; BT008424; AAP37783.1; -; mRNA.
PIR; T04506; T04506.
RefSeq; NP_001031763.1; NM_001036686.1. [Q8RWG1-2]
RefSeq; NP_194867.2; NM_119288.3. [Q8RWG1-1]
UniGene; At.44818; -.
ProteinModelPortal; Q8RWG1; -.
SMR; Q8RWG1; -.
STRING; 3702.AT4G31390.1; -.
PaxDb; Q8RWG1; -.
PRIDE; Q8RWG1; -.
EnsemblPlants; AT4G31390.1; AT4G31390.1; AT4G31390. [Q8RWG1-1]
EnsemblPlants; AT4G31390.2; AT4G31390.2; AT4G31390. [Q8RWG1-2]
GeneID; 829266; -.
Gramene; AT4G31390.1; AT4G31390.1; AT4G31390.
Gramene; AT4G31390.2; AT4G31390.2; AT4G31390.
KEGG; ath:AT4G31390; -.
Araport; AT4G31390; -.
TAIR; locus:2128116; AT4G31390.
eggNOG; KOG1235; Eukaryota.
eggNOG; COG0661; LUCA.
HOGENOM; HOG000232962; -.
InParanoid; Q8RWG1; -.
OMA; ICFTLQP; -.
OrthoDB; EOG093603W7; -.
PhylomeDB; Q8RWG1; -.
BioCyc; ARA:GQT-2246-MONOMER; -.
PRO; PR:Q8RWG1; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q8RWG1; baseline and differential.
Genevisible; Q8RWG1; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0010287; C:plastoglobule; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0006995; P:cellular response to nitrogen starvation; IMP:UniProtKB.
GO; GO:0015996; P:chlorophyll catabolic process; IMP:TAIR.
GO; GO:0009767; P:photosynthetic electron transport chain; IMP:UniProtKB.
GO; GO:0080177; P:plastoglobule organization; IMP:UniProtKB.
GO; GO:1904143; P:positive regulation of carotenoid biosynthetic process; IMP:UniProtKB.
GO; GO:1902326; P:positive regulation of chlorophyll biosynthetic process; IMP:UniProtKB.
GO; GO:0031540; P:regulation of anthocyanin biosynthetic process; IMP:UniProtKB.
GO; GO:0010109; P:regulation of photosynthesis; IMP:UniProtKB.
GO; GO:1902171; P:regulation of tocopherol cyclase activity; IDA:UniProtKB.
GO; GO:0009637; P:response to blue light; IMP:UniProtKB.
GO; GO:1901562; P:response to paraquat; IEP:UniProtKB.
GO; GO:0080183; P:response to photooxidative stress; IMP:UniProtKB.
GO; GO:0010114; P:response to red light; IMP:UniProtKB.
GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
GO; GO:0010027; P:thylakoid membrane organization; IMP:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR004147; UbiB_dom.
Pfam; PF03109; ABC1; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Chloroplast; Complete proteome;
Kinase; Nucleotide-binding; Plastid; Reference proteome;
Stress response; Transferase; Transit peptide.
TRANSIT 1 79 Chloroplast. {ECO:0000255}.
CHAIN 80 682 Protein ACTIVITY OF BC1 COMPLEX KINASE 1,
chloroplastic.
/FTId=PRO_0000286524.
DOMAIN 236 567 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 242 250 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 400 400 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 265 265 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
VAR_SEQ 321 345 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_025072.
SEQUENCE 682 AA; 76757 MW; E31B0AC7C7812F38 CRC64;
MESIHCNSLL NPNFSLNQRR RRINHAVLNR RDALLRSLNA VELRRSRTFS AVRTSNFSVT
AAATDVGGRN STDASVMTTA MSGVERGVRV GKSSSALEQL DIERGVCVPF RKYSPETVRS
KVLESRGAVV SLVSRGVEIV WTLGLYWSTL TYDFLVGRDE EVVPFRARQL RNLLCNLGPS
FIKAGQVLAN RPDIIREDYM NELCILQDDV PPFPNEVAFN IIEEELGQPL ENIFSKISSQ
TIAAASLGQV YRATLRATGE DVAIKVQRPQ IEPIIYRDLF LFRTLASFLN GFSLQKLGCN
AELIVDEFGE KLLEELDYTL EARNIEDFLE NFKDDPTVKI PGVYKNLCGP RVLVMEWIDG
IRCTDPQAIK DAGIDLNGFL TVGVSAALRQ LLEFGLFHGD PHPGNIFAMQ DGRIAYVDFG
NVAVLSQQNK QILIDAVVHA VNEDYGEMAN DFTRLGFLAK DTDVSPIVPA LEAIWQNSAG
KGLADFNFRS VTGQFNKLVY DFPIRIPERF SLVIRSLLTQ EGICFTLKPD FKFLEVAYPY
VAKRLLTDPN PALRERLIQV LFKDGVFQWK RLENLLSLAK ENVAKMSSNP NLRVKRVESK
LDLTDTIKDG ARLFLLDEGI RRKLILALTE DSKLHVEELV DVYRLVEDEV DIPTLAMQVV
QDLPNVFRDF VLSWSNSVLS DR


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EIAAB24970 Leucine zipper- and sterile alpha motif kinase ZAK,Mitogen-activated protein kinase kinase kinase MLT,Mixed lineage kinase-related kinase,MLK-like mitogen-activated protein triple kinase,MLK-related k
EIAAB31337 Homo sapiens,Human,PKN2,PRK2,PRKCL2,Protein kinase C-like 2,Protein-kinase C-related kinase 2,Serine_threonine-protein kinase N2
EIAAB31338 Homo sapiens,Human,PKN3,PKNBETA,Protein kinase PKN-beta,Protein-kinase C-related kinase 3,Serine_threonine-protein kinase N3
EIAAB40326 Pancreatic serine_threonine-protein kinase,Pask,PS_TK,PSTK1,Rat,Rattus norvegicus,Serine_threonine-protein kinase 39,Spak,STE20_SPS1-related proline-alanine-rich protein kinase,Ste-20-related kinase,S
EIAAB24861 c-Jun N-terminal kinase 3,Homo sapiens,Human,JNK3,JNK3A,MAP kinase 10,MAP kinase p49 3F12,MAPK 10,MAPK10,Mitogen-activated protein kinase 10,PRKM10,Stress-activated protein kinase JNK3
EIAAB31339 Mouse,Mus musculus,Pkn3,Pknbeta,Protein kinase PKN-beta,Protein-kinase C-related kinase 3,Serine_threonine-protein kinase N3
EIAAB24863 c-Jun N-terminal kinase 3,Jnk3,MAP kinase 10,MAP kinase p49 3F12,MAPK 10,Mapk10,Mitogen-activated protein kinase 10,Mouse,Mus musculus,Prkm10,Serk2,Stress-activated protein kinase JNK3
EIAAB26898 Homo sapiens,Human,NEK6,Never in mitosis A-related kinase 6,NimA-related protein kinase 6,Protein kinase SID6-1512,Serine_threonine-protein kinase Nek6
EIAAB31336 Mouse,Mus musculus,Pkn2,Prkcl2,Protein kinase C-like 2,Protein-kinase C-related kinase 2,Serine_threonine-protein kinase N2
EIAAB40306 Homo sapiens,Human,Serine_threonine-protein kinase 25,SOK1,SOK-1,Ste20_oxidant stress response kinase 1,Ste20-like kinase,Sterile 20_oxidant stress-response kinase 1,STK25,YSK1
EIAAB40307 Mouse,Mus musculus,Serine_threonine-protein kinase 25,Sok1,SOK-1,Ste20_oxidant stress response kinase 1,Ste20-like kinase,Sterile 20_oxidant stress-response kinase 1,Stk25


 

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