ASK11_ARATH
ID ASK11_ARATH Reviewed; 152 AA.
AC O49484; A0MFB7;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=SKP1-like protein 11;
DE Short=AtSK11;
GN Name=ASK11; OrderedLocusNames=At4g34210; ORFNames=F10M10.2;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP INTERACTION WITH UFO; PP2A13; AT1G67340; AT4G38940; SKIP15; AT3G16740;
RP AT3G04660; AT1G78100; AT1G55000; SKIP16; SKIP2; SKIP32 AND EBF1.
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 FUNCTION, GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP 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 [6]
RP TISSUE SPECIFICITY, AND INTERACTION WITH EBF1/FBL6; COI1/FBL2; ADO3/FKF1;
RP PP2B10; 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 [7]
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). Plays a role during early flowers reproductive
CC development. {ECO:0000250, ECO:0000269|PubMed:12970487}.
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, COI1/FBL2, EBF1/FBL6, PP2A13,
CC PP2B10, UFO, SKIP2, SKIP15, SKIP16, SKIP32, CPR1/CPR30, At1g55000,
CC At1g67340, At1g78100, At3g04660, At3g16740, At3g61590, At4g38940 and
CC At5g49610. {ECO:0000250, ECO:0000269|PubMed:12169662,
CC ECO:0000269|PubMed:14749489, ECO:0000269|PubMed:19682297}.
CC -!- INTERACTION:
CC O49484; Q94BT6: ADO1; NbExp=3; IntAct=EBI-401185, EBI-300691;
CC O49484; Q9SKK0: EBF1; NbExp=3; IntAct=EBI-401185, EBI-401198;
CC O49484; Q8LEA8: EID1; NbExp=3; IntAct=EBI-401185, EBI-687388;
CC O49484; O49279: SKIP15; NbExp=3; IntAct=EBI-401185, EBI-591174;
CC O49484; Q39090: UFO; NbExp=3; IntAct=EBI-401185, EBI-590758;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings, cotyledons, roots,
CC leaves, floral stems, inflorescences, pollen, and siliques, with a
CC slightly higher level in inflorescence than in other tissues.
CC {ECO:0000269|PubMed:12970487, ECO:0000269|PubMed:14749489}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the inflorescence meristem (IM) and
CC young buds, particularly in stamen. Also detected in pollen grains.
CC {ECO:0000269|PubMed:12970487}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28664.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL021961; CAA17551.1; -; Genomic_DNA.
DR EMBL; AL161585; CAB80138.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86340.1; -; Genomic_DNA.
DR EMBL; DQ446893; ABE66110.1; -; mRNA.
DR EMBL; DQ653243; ABK28664.1; ALT_SEQ; mRNA.
DR PIR; T05415; T05415.
DR RefSeq; NP_567959.1; NM_119584.2.
DR AlphaFoldDB; O49484; -.
DR SMR; O49484; -.
DR BioGRID; 14851; 92.
DR ComplexPortal; CPX-1438; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK11.
DR ComplexPortal; CPX-1459; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK11.
DR ComplexPortal; CPX-1481; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK11.
DR ComplexPortal; CPX-1504; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK11.
DR ComplexPortal; CPX-1524; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK11.
DR ComplexPortal; CPX-1545; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK11.
DR ComplexPortal; CPX-1567; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK11.
DR ComplexPortal; CPX-1588; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK11.
DR DIP; DIP-31327N; -.
DR IntAct; O49484; 38.
DR STRING; 3702.AT4G34210.1; -.
DR PaxDb; O49484; -.
DR PRIDE; O49484; -.
DR ProteomicsDB; 246503; -.
DR EnsemblPlants; AT4G34210.1; AT4G34210.1; AT4G34210.
DR GeneID; 829569; -.
DR Gramene; AT4G34210.1; AT4G34210.1; AT4G34210.
DR KEGG; ath:AT4G34210; -.
DR Araport; AT4G34210; -.
DR TAIR; locus:2124281; AT4G34210.
DR eggNOG; KOG1724; Eukaryota.
DR HOGENOM; CLU_059252_6_1_1; -.
DR InParanoid; O49484; -.
DR OMA; HNCADNG; -.
DR OrthoDB; 1412723at2759; -.
DR PhylomeDB; O49484; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O49484; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49484; baseline and differential.
DR Genevisible; O49484; 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..152
FT /note="SKP1-like protein 11"
FT /id="PRO_0000375252"
FT REGION 94..152
FT /note="Interaction with the F-box domain of F-box proteins"
FT /evidence="ECO:0000250"
SQ SEQUENCE 152 AA; 17288 MW; 95D23CC17C1523B0 CRC64;
MSSKMIVLMS SDGQSFEVEE AVAIQSQTIA HMVEDDCVAD GIPLANVESK ILVKVIEYCK
KHHVDEANPI SEEDLNNWDE KFMDLEQSTI FELILAANYL NIKSLLDLTC QTVADMIKGK
TPEEIRSTFN IENDFTPEEE EAVRKENQWA FE
