ASK18_ARATH
ID ASK18_ARATH Reviewed; 158 AA.
AC Q9SY65; F4I4A0; Q8LC82;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=SKP1-like protein 18;
DE Short=AtSK18;
GN Name=ASK18; OrderedLocusNames=At1g10230; ORFNames=F14N23.11;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH EBF1 AND AT4G38940.
RX PubMed=12169662; DOI=10.1073/pnas.162339999;
RA Gagne J.M., Downes B.P., Shiu S.-H., Durski A.M., Vierstra R.D.;
RT "The F-box subunit of the SCF E3 complex is encoded by a diverse
RT superfamily of genes in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11519-11524(2002).
RN [6]
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 [7]
RP TISSUE SPECIFICITY, AND INTERACTION WITH AT3G61590 AND AT5G49610.
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).
RN [8]
RP INTERACTION WITH SKP2A.
RX PubMed=18036202; DOI=10.1111/j.1365-313x.2007.03378.x;
RA Jurado S., Diaz-Trivino S., Abraham Z., Manzano C., Gutierrez C.,
RA del Pozo C.;
RT "SKP2A, an F-box protein that regulates cell division, is degraded via the
RT ubiquitin pathway.";
RL Plant J. 53:828-841(2008).
RN [9]
RP INTERACTION WITH CPR1/CPR30.
RX PubMed=19682297; DOI=10.1111/j.1365-313x.2009.03995.x;
RA Gou M., Su N., Zheng J., Huai J., Wu G., Zhao J., He J., Tang D., Yang S.,
RA Wang G.;
RT "An F-box gene, CPR30, functions as a negative regulator of the defense
RT response in Arabidopsis.";
RL Plant J. 60:757-770(2009).
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 CPR1/CPR30, EBF1, SKP2A, At3g61590,
CC At4g38940 and At5g49610. {ECO:0000250, ECO:0000269|PubMed:12169662,
CC ECO:0000269|PubMed:14749489, ECO:0000269|PubMed:18036202,
CC ECO:0000269|PubMed:19682297}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings, roots, leaves, floral
CC stems, inflorescences, pollen, and siliques.
CC {ECO:0000269|PubMed:12970487, ECO:0000269|PubMed:14749489}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the pith and vascular bundle
CC in the stem. Found in the pedicel of young buds. In siliques, mostly
CC expressed in inner epidermis of the valve.
CC {ECO:0000269|PubMed:12970487}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD32873.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO22641.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO42455.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005489; AAD32873.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE28557.2; -; Genomic_DNA.
DR EMBL; BT002822; AAO22641.1; ALT_INIT; mRNA.
DR EMBL; BT004461; AAO42455.1; ALT_INIT; mRNA.
DR EMBL; AY086743; AAM63794.1; -; mRNA.
DR PIR; G86236; G86236.
DR RefSeq; NP_563864.2; NM_100897.3.
DR AlphaFoldDB; Q9SY65; -.
DR SMR; Q9SY65; -.
DR BioGRID; 22802; 45.
DR ComplexPortal; CPX-1445; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK18.
DR ComplexPortal; CPX-1466; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK18.
DR ComplexPortal; CPX-1488; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK18.
DR ComplexPortal; CPX-1511; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK18.
DR ComplexPortal; CPX-1531; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK18.
DR ComplexPortal; CPX-1552; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK18.
DR ComplexPortal; CPX-1574; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK18.
DR ComplexPortal; CPX-1595; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK18.
DR IntAct; Q9SY65; 12.
DR STRING; 3702.AT1G10230.1; -.
DR PaxDb; Q9SY65; -.
DR PRIDE; Q9SY65; -.
DR ProteomicsDB; 246686; -.
DR EnsemblPlants; AT1G10230.1; AT1G10230.1; AT1G10230.
DR GeneID; 837562; -.
DR Gramene; AT1G10230.1; AT1G10230.1; AT1G10230.
DR KEGG; ath:AT1G10230; -.
DR Araport; AT1G10230; -.
DR eggNOG; KOG1724; Eukaryota.
DR HOGENOM; CLU_059252_5_0_1; -.
DR InParanoid; Q9SY65; -.
DR OMA; DSWDAKF; -.
DR OrthoDB; 1412723at2759; -.
DR PhylomeDB; Q9SY65; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SY65; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SY65; baseline and differential.
DR Genevisible; Q9SY65; 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..158
FT /note="SKP1-like protein 18"
FT /id="PRO_0000375259"
FT REGION 99..157
FT /note="Interaction with the F-box domain of F-box proteins"
FT /evidence="ECO:0000250"
FT CONFLICT 152
FT /note="N -> S (in Ref. 4; AAM63794)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 18163 MW; 5DF3C1D971B73981 CRC64;
MSSNKILLTS SDGESFEIDE AVARKFLIIV HMMEDNCAGE AIPLENVTGD ILSKIIEYAK
MHVNEPSEED EDEEAKKNLD SWDAKFMEKL DLETIFKIIL AANYLNFEGL LGFASQTVAD
YIKDKTPEEV REIFNIENDF TPEEEEEIRK ENAWTFNE
