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NEK6_ORYSJ
ID   NEK6_ORYSJ              Reviewed;         534 AA.
AC   Q6YY75; A0A0P0VL88; B9F0T5; Q0DZY9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Serine/threonine-protein kinase Nek6 {ECO:0000305};
DE            EC=2.7.11.1 {ECO:0000305};
DE   AltName: Full=NimA-related protein kinase 6 {ECO:0000303|PubMed:17886359};
DE   AltName: Full=OsNek6 {ECO:0000303|PubMed:17886359};
GN   Name=NEK6 {ECO:0000303|PubMed:17886359};
GN   OrderedLocusNames=Os02g0590800 {ECO:0000312|EMBL:BAS79503.1},
GN   LOC_Os02g37830 {ECO:0000305};
GN   ORFNames=OsJ_07328 {ECO:0000312|EMBL:EEE57277.1},
GN   OSJNBa0006O15.28 {ECO:0000312|EMBL:BAD17425.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   FUNCTION, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17886359; DOI=10.1111/j.1365-313x.2007.03161.x;
RA   Vigneault F., Lachance D., Cloutier M., Pelletier G., Levasseur C.,
RA   Seguin A.;
RT   "Members of the plant NIMA-related kinases are involved in organ
RT   development and vascularization in poplar, Arabidopsis and rice.";
RL   Plant J. 51:575-588(2007).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=19224952; DOI=10.1093/pcp/pcp026;
RA   Fujii S., Yamada M., Toriyama K.;
RT   "Cytoplasmic male sterility-related protein kinase, OsNek3, is regulated
RT   downstream of mitochondrial protein phosphatase 2C, DCW11.";
RL   Plant Cell Physiol. 50:828-837(2009).
RN   [7]
RP   INTERACTION WITH DIS1, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX   PubMed=21719639; DOI=10.1104/pp.111.180893;
RA   Ning Y., Jantasuriyarat C., Zhao Q., Zhang H., Chen S., Liu J., Liu L.,
RA   Tang S., Park C.H., Wang X., Liu X., Dai L., Xie Q., Wang G.L.;
RT   "The SINA E3 ligase OsDIS1 negatively regulates drought response in rice.";
RL   Plant Physiol. 157:242-255(2011).
CC   -!- FUNCTION: May be involved in plant development processes.
CC       {ECO:0000305|PubMed:17886359}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Interacts with DIS1. {ECO:0000269|PubMed:21719639}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21719639}.
CC       Note=Localizes in cytoplasmic spots associated with tubulin.
CC       {ECO:0000269|PubMed:21719639}.
CC   -!- TISSUE SPECIFICITY: Expressed in anthers, pistils and leaves.
CC       {ECO:0000269|PubMed:19224952}.
CC   -!- PTM: Ubiquitinated by the E3 ligase DIS1. Ubiquitination of NEK6 leads
CC       to its degradation via the 26S proteasome-dependent pathway.
CC       {ECO:0000269|PubMed:21719639}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD17425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF09199.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAS79503.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP005640; BAD17425.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008208; BAF09199.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014958; BAS79503.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM000139; EEE57277.1; -; Genomic_DNA.
DR   RefSeq; XP_015626426.1; XM_015770940.1.
DR   AlphaFoldDB; Q6YY75; -.
DR   SMR; Q6YY75; -.
DR   STRING; 4530.OS02T0590800-00; -.
DR   PaxDb; Q6YY75; -.
DR   PRIDE; Q6YY75; -.
DR   GeneID; 4329828; -.
DR   KEGG; osa:4329828; -.
DR   eggNOG; KOG0589; Eukaryota.
DR   HOGENOM; CLU_000288_128_3_1; -.
DR   InParanoid; Q6YY75; -.
DR   OrthoDB; 70360at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6YY75; OS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT   CHAIN           1..534
FT                   /note="Serine/threonine-protein kinase Nek6"
FT                   /id="PRO_0000314050"
FT   DOMAIN          4..257
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          278..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        129
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   534 AA;  59497 MW;  8EAC4403B7BF4062 CRC64;
     MEQYEVVEQI GRGAYGSAYL VVHKGERKRY VMKKIRLSKQ NDKFQRTAYQ EMSLMASLSN
     PYIVEYKDGW VDEGTSACIV TSYCEGGDMA ERIKKARGVL FSEERVCRWF TQLLLALDYL
     HCNRVLHRDL KCSNILLTKD NNIRLADFGL AKLLMEDLAS TIVGTPNYMC PEILADIPYG
     YKSDIWSLGC CMFEILAHRP AFKAADMASL INKINRSSIS PMPPIYSSSL KQIVKSMLRK
     NPEHRPTAGE LLRHPYLQPY LAESCSCSPI YLPVKPTKSN LGDKQQSRKP GSGRKRIIKT
     NGSSEALETA AEQAVDTRDN STYISDVSTV GTQDACISQV SVDPQARNKA YQNIDDLTLF
     QQIEENLMTI TDRQIDEAIF LKAVRTSSTV DVVPVSGAIQ KPNEAPIPKE ELTIGVVQEQ
     RKEVKAHTHQ GSKPGTGDVP IVTEESSPKS AVKLAHSDST PAEWDHLNIV QQRADALESL
     LELCAKLLKQ ERLEELAGVL RPFGEGAVSS RETAIWLTKS LMTPPKLEGS PKLT
 
 
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