ASK5_ARATH
ID ASK5_ARATH Reviewed; 153 AA.
AC Q9M1X4;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=SKP1-like protein 5;
DE Short=AtSK5;
GN Name=ASK5; OrderedLocusNames=At3g60020; ORFNames=F24G16.290, T2O9.2;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH PP2A13.
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 [5]
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).
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 PP2A13. {ECO:0000250,
CC ECO:0000269|PubMed:12169662}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Restricted to inflorescences, especially in the
CC inflorescence meristem (IM). {ECO:0000269|PubMed:12970487}.
CC -!- DEVELOPMENTAL STAGE: In young buds, confined to sepals and pedicels.
CC {ECO:0000269|PubMed:12970487}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR EMBL; AL138647; CAB75821.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80003.1; -; Genomic_DNA.
DR EMBL; DQ056631; AAY78779.1; -; mRNA.
DR PIR; T47826; T47826.
DR RefSeq; NP_567091.1; NM_115865.2.
DR AlphaFoldDB; Q9M1X4; -.
DR SMR; Q9M1X4; -.
DR BioGRID; 10486; 13.
DR ComplexPortal; CPX-1432; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK5.
DR ComplexPortal; CPX-1453; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK5.
DR ComplexPortal; CPX-1475; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK5.
DR ComplexPortal; CPX-1496; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK5.
DR ComplexPortal; CPX-1518; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK5.
DR ComplexPortal; CPX-1539; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK5.
DR ComplexPortal; CPX-1561; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK5.
DR ComplexPortal; CPX-1582; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK5.
DR IntAct; Q9M1X4; 1.
DR STRING; 3702.AT3G60020.1; -.
DR PaxDb; Q9M1X4; -.
DR PRIDE; Q9M1X4; -.
DR EnsemblPlants; AT3G60020.1; AT3G60020.1; AT3G60020.
DR GeneID; 825172; -.
DR Gramene; AT3G60020.1; AT3G60020.1; AT3G60020.
DR KEGG; ath:AT3G60020; -.
DR Araport; AT3G60020; -.
DR TAIR; locus:2080542; AT3G60020.
DR eggNOG; KOG1724; Eukaryota.
DR HOGENOM; CLU_059252_6_1_1; -.
DR OMA; MAEDECA; -.
DR OrthoDB; 1412723at2759; -.
DR PhylomeDB; Q9M1X4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9M1X4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1X4; baseline and differential.
DR Genevisible; Q9M1X4; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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..153
FT /note="SKP1-like protein 5"
FT /id="PRO_0000375246"
FT REGION 90..153
FT /note="Interaction with the F-box domain of F-box proteins"
FT /evidence="ECO:0000250"
SQ SEQUENCE 153 AA; 17444 MW; 580F970133356105 CRC64;
MSTKIMLKSS DGKSFEIDED VARKSIAINH MVEDGCATDV IPLRNVTSKI LKIVIDYCEK
HVKSKEEEDL KEWDADFMKT IETTILFDVM MAANYLNIQS LLDLTCKTVS DLLQADLLSG
KTPDEIRAHF NIENDLTAEE VAKIREENQW AFQ
