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ASK3_ARATH
ID   ASK3_ARATH              Reviewed;         163 AA.
AC   Q9SL93;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=SKP1-like protein 3;
DE            Short=AtSK3;
GN   Name=ASK3; OrderedLocusNames=At2g25700; ORFNames=F3N11.15;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12970487; DOI=10.1104/pp.103.024703;
RA   Zhao D., Ni W., Feng B., Han T., Petrasek M.G., Ma H.;
RT   "Members of the Arabidopsis-SKP1-like gene family exhibit a variety of
RT   expression patterns and may play diverse roles in Arabidopsis.";
RL   Plant Physiol. 133:203-217(2003).
RN   [5]
RP   INTERACTION WITH ADO3/FKF1 AND AT3G61590.
RX   PubMed=14749489; DOI=10.1093/pcp/pch009;
RA   Takahashi N., Kuroda H., Kuromori T., Hirayama T., Seki M., Shinozaki K.,
RA   Shimada H., Matsui M.;
RT   "Expression and interaction analysis of Arabidopsis Skp1-related genes.";
RL   Plant Cell Physiol. 45:83-91(2004).
CC   -!- FUNCTION: Involved in ubiquitination and subsequent proteasomal
CC       degradation of target proteins. Together with CUL1, RBX1 and a F-box
CC       protein, it forms a SCF E3 ubiquitin ligase complex. The functional
CC       specificity of this complex depends on the type of F-box protein. In
CC       the SCF complex, it serves as an adapter that links the F-box protein
CC       to CUL1 (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex (By
CC       similarity). Interacts with ADO3/FKF1 and At3g61590. {ECO:0000250,
CC       ECO:0000269|PubMed:14749489}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in siliques.
CC       {ECO:0000269|PubMed:12970487}.
CC   -!- DEVELOPMENTAL STAGE: In flowers, mostly restricted to sepals and
CC       pedicels. {ECO:0000269|PubMed:12970487}.
CC   -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR   EMBL; AC006053; AAD31370.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07739.1; -; Genomic_DNA.
DR   EMBL; AY052700; AAK96604.1; -; mRNA.
DR   EMBL; AY139806; AAM98112.1; -; mRNA.
DR   PIR; F84651; F84651.
DR   RefSeq; NP_565604.1; NM_128129.2.
DR   AlphaFoldDB; Q9SL93; -.
DR   SMR; Q9SL93; -.
DR   BioGRID; 2463; 62.
DR   ComplexPortal; CPX-1430; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK3.
DR   ComplexPortal; CPX-1451; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK3.
DR   ComplexPortal; CPX-1473; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK3.
DR   ComplexPortal; CPX-1494; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK3.
DR   ComplexPortal; CPX-1516; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK3.
DR   ComplexPortal; CPX-1537; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK3.
DR   ComplexPortal; CPX-1559; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK3.
DR   ComplexPortal; CPX-1580; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK3.
DR   IntAct; Q9SL93; 18.
DR   STRING; 3702.AT2G25700.1; -.
DR   PaxDb; Q9SL93; -.
DR   PRIDE; Q9SL93; -.
DR   ProteomicsDB; 246794; -.
DR   EnsemblPlants; AT2G25700.1; AT2G25700.1; AT2G25700.
DR   GeneID; 817111; -.
DR   Gramene; AT2G25700.1; AT2G25700.1; AT2G25700.
DR   KEGG; ath:AT2G25700; -.
DR   Araport; AT2G25700; -.
DR   TAIR; locus:2050281; AT2G25700.
DR   eggNOG; KOG1724; Eukaryota.
DR   HOGENOM; CLU_059252_6_1_1; -.
DR   OMA; WERIPSC; -.
DR   OrthoDB; 1412723at2759; -.
DR   PhylomeDB; Q9SL93; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9SL93; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SL93; baseline and differential.
DR   Genevisible; Q9SL93; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IC:ComplexPortal.
DR   GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IC:ComplexPortal.
DR   GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:ComplexPortal.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009733; P:response to auxin; IC:ComplexPortal.
DR   GO; GO:0009753; P:response to jasmonic acid; IMP:ComplexPortal.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR016897; SKP1.
DR   InterPro; IPR001232; SKP1-like.
DR   InterPro; IPR036296; SKP1-like_dim_sf.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR016072; Skp1_comp_dimer.
DR   InterPro; IPR016073; Skp1_comp_POZ.
DR   PANTHER; PTHR11165; PTHR11165; 1.
DR   Pfam; PF01466; Skp1; 1.
DR   Pfam; PF03931; Skp1_POZ; 1.
DR   PIRSF; PIRSF028729; E3_ubiquit_lig_SCF_Skp; 1.
DR   SMART; SM00512; Skp1; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   SUPFAM; SSF81382; SSF81382; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..163
FT                   /note="SKP1-like protein 3"
FT                   /id="PRO_0000375244"
FT   REGION          105..163
FT                   /note="Interaction with the F-box domain of F-box proteins"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   163 AA;  18365 MW;  8F7C7796CE5CEB4F CRC64;
     MAETKKMIIL KSSDGESFEV EEAVAVESQT IKHMIEDDCV DNGIPLPNVT GAILAKVIEY
     CKKHVEAAAE AGGDKDFYGS TENHELKTWD NDFVKVDHPT LFDLLRAANY LNISGLLDLT
     CKAVADQMRG KTPAQMREHF NIKNDYTPEE EAEVRNENRW AFE
 
 
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