ASK12_ARATH
ID ASK12_ARATH Reviewed; 152 AA.
AC O65674;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=SKP1-like protein 12;
DE Short=AtSK12;
GN Name=ASK12; OrderedLocusNames=At4g34470; ORFNames=T4L20.50;
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 FUNCTION, GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
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 [4]
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).
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, PP2B10,
CC At3g61590 and At5g49610. {ECO:0000250, ECO:0000269|PubMed:14749489}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings, roots, leaves, floral
CC stems, inflorescences, and siliques, with a slightly higher level in
CC inflorescence than in other tissues. {ECO:0000269|PubMed:12970487,
CC ECO:0000269|PubMed:14749489}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR EMBL; AL023094; CAA18826.1; -; Genomic_DNA.
DR EMBL; AL161585; CAB80164.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86383.1; -; Genomic_DNA.
DR PIR; T05267; T05267.
DR RefSeq; NP_567967.1; NM_119612.2.
DR AlphaFoldDB; O65674; -.
DR SMR; O65674; -.
DR BioGRID; 14880; 78.
DR ComplexPortal; CPX-1439; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK12.
DR ComplexPortal; CPX-1460; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK12.
DR ComplexPortal; CPX-1482; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK12.
DR ComplexPortal; CPX-1505; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK12.
DR ComplexPortal; CPX-1525; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK12.
DR ComplexPortal; CPX-1546; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK12.
DR ComplexPortal; CPX-1568; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK12.
DR ComplexPortal; CPX-1589; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK12.
DR IntAct; O65674; 12.
DR STRING; 3702.AT4G34470.1; -.
DR PaxDb; O65674; -.
DR PRIDE; O65674; -.
DR EnsemblPlants; AT4G34470.1; AT4G34470.1; AT4G34470.
DR GeneID; 829598; -.
DR Gramene; AT4G34470.1; AT4G34470.1; AT4G34470.
DR KEGG; ath:AT4G34470; -.
DR Araport; AT4G34470; -.
DR TAIR; locus:2139504; AT4G34470.
DR eggNOG; KOG1724; Eukaryota.
DR HOGENOM; CLU_059252_6_1_1; -.
DR InParanoid; O65674; -.
DR OMA; SWEIAIS; -.
DR OrthoDB; 1412723at2759; -.
DR PhylomeDB; O65674; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O65674; -.
DR Proteomes; UP000006548; Chromosome 4.
DR Genevisible; O65674; 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 GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:TAIR.
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 12"
FT /id="PRO_0000375253"
FT REGION 94..152
FT /note="Interaction with the F-box domain of F-box proteins"
FT /evidence="ECO:0000250"
SQ SEQUENCE 152 AA; 17363 MW; 0F694CC439552EDD CRC64;
MSSKMIVLMS SDGQSFEVEE AVAIQSQTIA HMVEDDCVAD GIPLANVESK ILVKVIEYCK
KYHVDEANPI SEEDLNKWDE KFMDLEQSTI FELILAANYL NIKSLFDLTC QTVADMIKGK
TPEEIRSTFN IENDFTPEEE EAVRKENQWA FE
