SKP1B_ARATH
ID SKP1B_ARATH Reviewed; 171 AA.
AC Q9FHW7; O65283; Q0WSZ3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=SKP1-like protein 1B;
DE AltName: Full=SKP1-like 2;
DE AltName: Full=UFO-binding protein 2;
GN Name=SKP1B; Synonyms=ASK2, UIP2; OrderedLocusNames=At5g42190;
GN ORFNames=MJC20.30;
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 [MRNA], AND INTERACTION WITH UFO.
RC STRAIN=cv. Columbia;
RX PubMed=10607296; DOI=10.1046/j.1365-313x.1999.00617.x;
RA Samach A., Klenz J.E., Kohalmi S.E., Risseeuw E., Haughn G.W., Crosby W.L.;
RT "The UNUSUAL FLORAL ORGANS gene of Arabidopsis thaliana is an F-box protein
RT required for normal patterning and growth in the floral meristem.";
RL Plant J. 20:433-445(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10778750; DOI=10.1007/pl00008682;
RA Schouten J., de Kam R.J., Fetter K., Hoge J.H.C.;
RT "Overexpression of Arabidopsis thaliana SKP1 homologues in yeast
RT inactivates the Mig1 repressor by destabilising the F-box protein Grr1.";
RL Mol. Gen. Genet. 263:309-319(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND INTERACTION WITH TIR1.
RX PubMed=10398681; DOI=10.1101/gad.13.13.1678;
RA Gray W.M., del Pozo J.C., Walker L., Hobbie L., Risseeuw E., Banks T.,
RA Crosby W.L., Yang M., Ma H., Estelle M.;
RT "Identification of an SCF ubiquitin-ligase complex required for auxin
RT response in Arabidopsis thaliana.";
RL Genes Dev. 13:1678-1691(1999).
RN [8]
RP INTERACTION WITH EID1.
RX PubMed=11316788; DOI=10.1101/gad.197201;
RA Dieterle M., Zhou Y.-C., Schaefer E., Funk M., Kretsch T.;
RT "EID1, an F-box protein involved in phytochrome A-specific light
RT signaling.";
RL Genes Dev. 15:939-944(2001).
RN [9]
RP IDENTIFICATION IN A SCF COMPLEX.
RX PubMed=12381738; DOI=10.1074/jbc.m204254200;
RA Lechner E., Xie D., Grava S., Pigaglio E., Planchais S., Murray J.A.H.,
RA Parmentier Y., Mutterer J., Dubreucq B., Shen W.-H., Genschik P.;
RT "The AtRbx1 protein is part of plant SCF complexes, and its down-regulation
RT causes severe growth and developmental defects.";
RL J. Biol. Chem. 277:50069-50080(2002).
RN [10]
RP INTERACTION WITH COI1, AND IDENTIFICATION IN A SCF(COI1) COMPLEX.
RX PubMed=12172031; DOI=10.1105/tpc.003368;
RA Xu L., Liu F., Lechner E., Genschik P., Crosby W.L., Ma H., Peng W.,
RA Huang D., Xie D.;
RT "The SCF(COI1) ubiquitin-ligase complexes are required for jasmonate
RT response in Arabidopsis.";
RL Plant Cell 14:1919-1935(2002).
RN [11]
RP INTERACTION WITH COI1, AND IDENTIFICATION IN A SCF(COI1) COMPLEX.
RX PubMed=12445118; DOI=10.1046/j.1365-313x.2002.01432.x;
RA Devoto A., Nieto-Rostro M., Xie D., Ellis C., Harmston R., Patrick E.,
RA Davis J., Sherratt L., Coleman M., Turner J.G.;
RT "COI1 links jasmonate signalling and fertility to the SCF ubiquitin-ligase
RT complex in Arabidopsis.";
RL Plant J. 32:457-466(2002).
RN [12]
RP INTERACTION WITH UFO; PP2A13; AT1G67340; AT4G38940; SKIP15; AT3G04660;
RP 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 [13]
RP INTERACTION WITH EID1; SKIP1; PP2A13/SKIP9; SKIP11; PP2B11/SKIP12;
RP PP2A14/SKIP13; SKIP14; SKIP15/FBX3; SKIP16; SKIP17; FBW2/SKIP18;
RP SKIP19/FBL20; SKIP20; PP2B1/SKIP21; SKIP22; SKIP24; SKIP27; SKIP31 AND
RP SKIP34.
RX PubMed=12795696; DOI=10.1046/j.1365-313x.2003.01768.x;
RA Risseeuw E.P., Daskalchuk T.E., Banks T.W., Liu E., Cotelesage J.,
RA Hellmann H., Estelle M., Somers D.E., Crosby W.L.;
RT "Protein interaction analysis of SCF ubiquitin E3 ligase subunits from
RT Arabidopsis.";
RL Plant J. 34:753-767(2003).
RN [14]
RP FUNCTION, 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 [15]
RP INTERACTION WITH ADO1; ADO2 AND ADO3.
RX PubMed=15310821; DOI=10.1093/jxb/erh226;
RA Yasuhara M., Mitsui S., Hirano H., Takanabe R., Tokioka Y., Ihara N.,
RA Komatsu A., Seki M., Shinozaki K., Kiyosue T.;
RT "Identification of ASK and clock-associated proteins as molecular partners
RT of LKP2 (LOV kelch protein 2) in Arabidopsis.";
RL J. Exp. Bot. 55:2015-2027(2004).
RN [16]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14688296; DOI=10.1105/tpc.017772;
RA Liu F., Ni W., Griffith M.E., Huang Z., Chang C., Peng W., Ma H., Xie D.;
RT "The ASK1 and ASK2 genes are essential for Arabidopsis early development.";
RL Plant Cell 16:5-20(2004).
RN [17]
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 [18]
RP INTERACTION WITH ADO1.
RX PubMed=15447654; DOI=10.1111/j.1365-313x.2004.02207.x;
RA Han L., Mason M., Risseeuw E.P., Crosby W.L., Somers D.E.;
RT "Formation of an SCF(ZTL) complex is required for proper regulation of
RT circadian timing.";
RL Plant J. 40:291-301(2004).
RN [19]
RP INTERACTION WITH TURNIP YELLOWS VIRUS PROTEIN P0, AND IDENTIFICATION IN A
RP SCF P0 COMPLEX.
RX PubMed=16446454; DOI=10.1073/pnas.0510784103;
RA Pazhouhandeh M., Dieterle M., Marrocco K., Lechner E., Berry B., Brault V.,
RA Hemmer O., Kretsch T., Richards K.E., Genschik P., Ziegler-Graff V.;
RT "F-box-like domain in the polerovirus protein P0 is required for silencing
RT suppressor function.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:1994-1999(2006).
RN [20]
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 [21]
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).
RN [22]
RP INTERACTION WITH SNL1.
RX PubMed=19962994; DOI=10.1016/j.jmb.2009.11.065;
RA Bowen A.J., Gonzalez D., Mullins J.G., Bhatt A.M., Martinez A.,
RA Conlan R.S.;
RT "PAH-domain-specific interactions of the Arabidopsis transcription
RT coregulator SIN3-LIKE1 (SNL1) with telomere-binding protein 1 and ALWAYS
RT EARLY2 Myb-DNA binding factors.";
RL J. Mol. Biol. 395:937-949(2010).
RN [23]
RP INTERACTION WITH NUP58.
RX PubMed=23840761; DOI=10.1371/journal.pone.0067661;
RA Ferrandez-Ayela A., Alonso-Peral M.M., Sanchez-Garcia A.B., Micol-Ponce R.,
RA Perez-Perez J.M., Micol J.L., Ponce M.R.;
RT "Arabidopsis TRANSCURVATA1 encodes NUP58, a component of the nucleopore
RT central channel.";
RL PLoS ONE 8:E67661-E67661(2013).
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. SCF(UFO) is required for vegetative and floral organ
CC development as well as for male gametogenesis. SCF(TIR1) is involved in
CC auxin signaling pathway. SCF(COI1) regulates responses to jasmonates.
CC SCF(EID1) and SCF(AFR) are implicated in phytochrome A light signaling.
CC SCF(ADO1), SCF(ADO2), SCF(ADO3) are related to the circadian clock.
CC SCF(ORE9) seems to be involved in senescence. SCF(EBF1/EBF2) may
CC regulate ethylene signaling. Plays a role during embryogenesis and
CC early postembryonic development, especially during cell elongation and
CC division. Contributes to the correct chromosome segregation during
CC tetrad formation. {ECO:0000269|PubMed:10398681,
CC ECO:0000269|PubMed:12970487, ECO:0000269|PubMed:14688296}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF E3 ubiquitin ligase complex composed of SKP1,
CC CUL1, RBX1 (RBX1A or RBX1B) and F-box proteins. Interacts with SKIP1,
CC SKIP2, SKIP3, SKIP4, SKIP6, FIB1/SKIP7, PP2A13/SKIP9, SKIP11,
CC PP2B11/SKIP12, PP2A14/SKIP13, SKIP14, SKIP15/FBX3, SKIP16, SKIP17,
CC FBW2/SKIP18, SKIP19/FBL20, SKIP20, PP2B1/SKIP21, SKIP22, SKIP24,
CC SKIP27, SKIP31, SKIP32, SKIP34, ADO1/ZTL, ADO2/LKP2, ADO3/FKF1, AFR,
CC COI1, EBF1, EBF2, EID1, ORE9, PP2A13, PP2B10, TIR1, UFO, SKP2A,
CC CPR1/CPR30, NUP58, At1g55000, At1g67340, At1g78100, At3g04660,
CC At3g61590, At4g38940 and At5g49610. The SKP1B subunit of the SCF E3
CC ubiquitin ligase complex can probably interact directly with KIN10,
CC KIN11 and the proteasome subunit PAD1. Interacts with SNL1. In case of
CC polerovirus infection, part of a SCF P0 complex composed of the viral
CC silencing suppressor P0, SKP1, and CUL1. Interacts with turnip yellows
CC virus P0. {ECO:0000269|PubMed:10398681, ECO:0000269|PubMed:10607296,
CC ECO:0000269|PubMed:11316788, ECO:0000269|PubMed:12169662,
CC ECO:0000269|PubMed:12172031, ECO:0000269|PubMed:12381738,
CC ECO:0000269|PubMed:12445118, ECO:0000269|PubMed:12795696,
CC ECO:0000269|PubMed:14749489, ECO:0000269|PubMed:15310821,
CC ECO:0000269|PubMed:15447654, ECO:0000269|PubMed:16446454,
CC ECO:0000269|PubMed:18036202, ECO:0000269|PubMed:19682297,
CC ECO:0000269|PubMed:19962994, ECO:0000269|PubMed:23840761}.
CC -!- INTERACTION:
CC Q9FHW7; Q94BT6: ADO1; NbExp=5; IntAct=EBI-604076, EBI-300691;
CC Q9FHW7; Q9C9W9: ADO3; NbExp=5; IntAct=EBI-604076, EBI-401228;
CC Q9FHW7; O04197: COI1; NbExp=6; IntAct=EBI-604076, EBI-401159;
CC Q9FHW7; Q9SKK0: EBF1; NbExp=5; IntAct=EBI-604076, EBI-401198;
CC Q9FHW7; Q8LEA8: EID1; NbExp=4; IntAct=EBI-604076, EBI-687388;
CC Q9FHW7; Q9ZPE4: FBW2; NbExp=3; IntAct=EBI-604076, EBI-604740;
CC Q9FHW7; Q9STX3: GID2; NbExp=3; IntAct=EBI-604076, EBI-619033;
CC Q9FHW7; Q9SZU7: KAI2; NbExp=3; IntAct=EBI-604076, EBI-25519488;
CC Q9FHW7; Q9SIM9: MAX2; NbExp=3; IntAct=EBI-604076, EBI-25529872;
CC Q9FHW7; Q9LEX0: PP2A13; NbExp=6; IntAct=EBI-604076, EBI-604261;
CC Q9FHW7; Q9FJ80: PP2A14; NbExp=3; IntAct=EBI-604076, EBI-604303;
CC Q9FHW7; O49279: SKIP15; NbExp=6; IntAct=EBI-604076, EBI-591174;
CC Q9FHW7; Q9LND7: SKIP16; NbExp=3; IntAct=EBI-604076, EBI-591078;
CC Q9FHW7; Q0WRC9: SKIP17; NbExp=3; IntAct=EBI-604076, EBI-604757;
CC Q9FHW7; Q8GX29: SKIP25; NbExp=3; IntAct=EBI-604076, EBI-604376;
CC Q9FHW7; Q570C0: TIR1; NbExp=7; IntAct=EBI-604076, EBI-307183;
CC Q9FHW7; Q39090: UFO; NbExp=5; IntAct=EBI-604076, EBI-590758;
CC Q9FHW7; Q8XZN9: ripG; Xeno; NbExp=2; IntAct=EBI-604076, EBI-15602092;
CC Q9FHW7; P15597: virF; Xeno; NbExp=5; IntAct=EBI-604076, EBI-605118;
CC Q9FHW7; Q65967; Xeno; NbExp=3; IntAct=EBI-604076, EBI-848577;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in tips, cortical layer and epidermis of
CC roots. Detected in whole seedling, vascular tissues, pith and vascular
CC bundle of young stem, leaves, inflorescence meristem, young floral buds
CC and organ primordia, flowers, developing seeds and through the valve of
CC siliques. Expressed in male meiocytes, pollen, embryo and endosperm.
CC {ECO:0000269|PubMed:12970487, ECO:0000269|PubMed:14688296,
CC ECO:0000269|PubMed:14749489}.
CC -!- DEVELOPMENTAL STAGE: Expressed during all stages of embryogenesis.
CC {ECO:0000269|PubMed:14688296}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC63110.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U97021; AAC63110.1; ALT_INIT; mRNA.
DR EMBL; AF059295; AAC14445.1; -; mRNA.
DR EMBL; AB017067; BAB08452.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94777.1; -; Genomic_DNA.
DR EMBL; BT004798; AAO44064.1; -; mRNA.
DR EMBL; AK227773; BAE99755.1; -; mRNA.
DR RefSeq; NP_568603.1; NM_123584.5.
DR AlphaFoldDB; Q9FHW7; -.
DR SMR; Q9FHW7; -.
DR BioGRID; 19474; 140.
DR ComplexPortal; CPX-1429; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1B.
DR ComplexPortal; CPX-1450; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1B.
DR ComplexPortal; CPX-1472; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1B.
DR ComplexPortal; CPX-1493; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1B.
DR ComplexPortal; CPX-1515; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1B.
DR ComplexPortal; CPX-1536; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1B.
DR ComplexPortal; CPX-1558; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1B.
DR ComplexPortal; CPX-1579; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1B.
DR DIP; DIP-31326N; -.
DR IntAct; Q9FHW7; 95.
DR STRING; 3702.AT5G42190.1; -.
DR iPTMnet; Q9FHW7; -.
DR PaxDb; Q9FHW7; -.
DR PRIDE; Q9FHW7; -.
DR ProteomicsDB; 234514; -.
DR EnsemblPlants; AT5G42190.1; AT5G42190.1; AT5G42190.
DR GeneID; 834224; -.
DR Gramene; AT5G42190.1; AT5G42190.1; AT5G42190.
DR KEGG; ath:AT5G42190; -.
DR Araport; AT5G42190; -.
DR TAIR; locus:2165825; AT5G42190.
DR eggNOG; KOG1724; Eukaryota.
DR HOGENOM; CLU_059252_6_1_1; -.
DR InParanoid; Q9FHW7; -.
DR OMA; LYMIEKG; -.
DR OrthoDB; 1412723at2759; -.
DR PhylomeDB; Q9FHW7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FHW7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHW7; baseline and differential.
DR Genevisible; Q9FHW7; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA: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:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
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; TAS: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 Auxin signaling pathway; Chromosome partition; Developmental protein;
KW Ethylene signaling pathway; Host-virus interaction; Nucleus;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..171
FT /note="SKP1-like protein 1B"
FT /id="PRO_0000187256"
FT REGION 113..171
FT /note="Interaction with the F-box domain of F-box proteins"
FT /evidence="ECO:0000250|UniProtKB:Q39255"
SQ SEQUENCE 171 AA; 19097 MW; 9695CC9F57FC935F CRC64;
MSTVRKITLK SSDGENFEID EAVALESQTI KHMIEDDCTD NGIPLPNVTS KILSKVIEYC
KRHVEAAEKS ETTADAAAAT TTTTVASGSS DEDLKTWDSE FIKVDQGTLF DLILAANYLN
IKGLLDLTCQ TVADMIKGKT PEEIRKTFNI KNDFTPEEEE EVRRENQWAF E
