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ASK13_ARATH
ID   ASK13_ARATH             Reviewed;         154 AA.
AC   Q9M1X5;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=SKP1-like protein 13;
DE            Short=AtSK13;
GN   Name=ASK13; OrderedLocusNames=At3g60010; ORFNames=F24G16.280, T2O9.1;
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   INTERACTION WITH AT3G04660; PP2A13; AT1G67340; AT4G38940; SKIP15;
RP   AT1G78100; AT1G55000; SKIP16 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   [4]
RP   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   [5]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH ADO3/FKF1; AT4G39550; AT3G61590
RP   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   [6]
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 ADO3/FKF1, EBF1, PP2A13, SKIP15, SKIP16,
CC       CPR1/CPR30, At1g55000, At3g61590, At1g67340, At1g78100, At3g04660,
CC       At4g38940, At4g39550 and At5g49610. {ECO:0000250,
CC       ECO:0000269|PubMed:12169662, ECO:0000269|PubMed:14749489,
CC       ECO:0000269|PubMed:19682297}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in inflorescences, and, to a lower
CC       extent, in seedlings and siliques. Also detected in cotyledons, leaves,
CC       pollen and seeds. {ECO:0000269|PubMed:12970487,
CC       ECO:0000269|PubMed:14749489}.
CC   -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR   EMBL; AL138647; CAB75820.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE80002.1; -; Genomic_DNA.
DR   PIR; T47825; T47825.
DR   RefSeq; NP_567090.1; NM_115864.2.
DR   AlphaFoldDB; Q9M1X5; -.
DR   SMR; Q9M1X5; -.
DR   BioGRID; 10485; 82.
DR   ComplexPortal; CPX-1440; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK13.
DR   ComplexPortal; CPX-1461; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK13.
DR   ComplexPortal; CPX-1483; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK13.
DR   ComplexPortal; CPX-1506; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK13.
DR   ComplexPortal; CPX-1526; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK13.
DR   ComplexPortal; CPX-1547; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK13.
DR   ComplexPortal; CPX-1569; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK13.
DR   ComplexPortal; CPX-1590; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK13.
DR   DIP; DIP-31331N; -.
DR   IntAct; Q9M1X5; 26.
DR   STRING; 3702.AT3G60010.1; -.
DR   PaxDb; Q9M1X5; -.
DR   PRIDE; Q9M1X5; -.
DR   ProteomicsDB; 246504; -.
DR   EnsemblPlants; AT3G60010.1; AT3G60010.1; AT3G60010.
DR   GeneID; 825171; -.
DR   Gramene; AT3G60010.1; AT3G60010.1; AT3G60010.
DR   KEGG; ath:AT3G60010; -.
DR   Araport; AT3G60010; -.
DR   TAIR; locus:2080532; AT3G60010.
DR   eggNOG; KOG1724; Eukaryota.
DR   HOGENOM; CLU_059252_6_1_1; -.
DR   InParanoid; Q9M1X5; -.
DR   OMA; EDDCVAN; -.
DR   OrthoDB; 1412723at2759; -.
DR   PhylomeDB; Q9M1X5; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9M1X5; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M1X5; baseline and differential.
DR   Genevisible; Q9M1X5; 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..154
FT                   /note="SKP1-like protein 13"
FT                   /id="PRO_0000375254"
FT   REGION          96..154
FT                   /note="Interaction with the F-box domain of F-box proteins"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   154 AA;  17234 MW;  FF771FCF3B9844A5 CRC64;
     MSKMVMLLSS DGESFQVEEA VAVQSQTIAH MIEDDCVANG VPIANVTGVI LSKVIEYCKK
     HVVSDSPTEE SKDELKKWDA EFMKALEQSS TLFDVMLAAN YLNIKDLLDL GCQTVADMIT
     GKKPDEIRAL LGIENDFTPE EEEEIRKENQ WAFE
 
 
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