SKP1A_ARATH
ID SKP1A_ARATH Reviewed; 160 AA.
AC Q39255; P92992;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 166.
DE RecName: Full=SKP1-like protein 1A {ECO:0000303|PubMed:10778750};
DE Short=SKP1-like 1 {ECO:0000303|PubMed:10778750};
DE AltName: Full=UFO-binding protein 1 {ECO:0000303|PubMed:10607296};
GN Name=SKP1A {ECO:0000303|PubMed:10778750};
GN Synonyms=ASK1 {ECO:0000303|PubMed:10528262},
GN SKP1 {ECO:0000303|PubMed:8706132}, UIP1 {ECO:0000303|PubMed:10607296};
GN OrderedLocusNames=At1g75950 {ECO:0000312|Araport:AT1G75950};
GN ORFNames=T4O12.17 {ECO:0000312|EMBL:AAF26761.1};
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 [MRNA].
RX PubMed=8706132; DOI=10.1016/s0092-8674(00)80099-9;
RA Connelly C., Hieter P.;
RT "Budding yeast SKP1 encodes an evolutionarily conserved kinetochore protein
RT required for cell cycle progression.";
RL Cell 86:275-285(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, 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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-160, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9530878; DOI=10.1007/s004250050265;
RA Porat R., Lu P., O'Neill S.D.;
RT "Arabidopsis SKP1, a homologue of a cell cycle regulator gene, is
RT predominantly expressed in meristematic cells.";
RL Planta 204:345-351(1998).
RN [8]
RP FUNCTION.
RX PubMed=10528262;
RX DOI=10.1002/(sici)1520-6408(1999)25:3<209::aid-dvg4>3.0.co;2-o;
RA Zhao D., Yang M., Solava J., Ma H.;
RT "The ASK1 gene regulates development and interacts with the UFO gene to
RT control floral organ identity in Arabidopsis.";
RL Dev. Genet. 25:209-223(1999).
RN [9]
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 [10]
RP FUNCTION.
RX PubMed=10500191; DOI=10.1073/pnas.96.20.11416;
RA Yang M., Hu Y., Lodhi M., McCombie W.R., Ma H.;
RT "The Arabidopsis SKP1-LIKE1 gene is essential for male meiosis and may
RT control homologue separation.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11416-11421(1999).
RN [11]
RP FUNCTION.
RX PubMed=11526079; DOI=10.1242/dev.128.14.2735;
RA Zhao D., Yu Q., Chen M., Ma H.;
RT "The ASK1 gene regulates B function gene expression in cooperation with UFO
RT and LEAFY in Arabidopsis.";
RL Development 128:2735-2746(2001).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SKIP1; SKIP2; SKIP3; SKIP4;
RP SKIP6; FIB1; CUL1; PAD1; KIN10 AND KIN11.
RX PubMed=11387208; DOI=10.1093/emboj/20.11.2742;
RA Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A.,
RA Salchert K., del Pozo C., Schell J., Koncz C.;
RT "SKP1-SnRK protein kinase interactions mediate proteasomal binding of a
RT plant SCF ubiquitin ligase.";
RL EMBO J. 20:2742-2756(2001).
RN [13]
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 [14]
RP INTERACTION WITH ORE9.
RX PubMed=11487692; DOI=10.2307/3871318;
RA Woo H.R., Chung K.M., Park J.-H., Oh S.A., Ahn T., Hong S.H., Jang S.K.,
RA Nam H.G.;
RT "ORE9, an F-box protein that regulates leaf senescence in Arabidopsis.";
RL Plant Cell 13:1779-1790(2001).
RN [15]
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 [16]
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 [17]
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 [18]
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 [19]
RP INTERACTION WITH EBF1 AND EBF2.
RX PubMed=14675532; DOI=10.1016/s0092-8674(03)00969-3;
RA Guo H., Ecker J.R.;
RT "Plant responses to ethylene gas are mediated by SCF(EBF1/EBF2)-dependent
RT proteolysis of EIN3 transcription factor.";
RL Cell 115:667-677(2003).
RN [20]
RP INTERACTION WITH AFR.
RX PubMed=14653999; DOI=10.1016/j.cub.2003.11.019;
RA Harmon F.G., Kay S.A.;
RT "The F box protein AFR is a positive regulator of phytochrome A-mediated
RT light signaling.";
RL Curr. Biol. 13:2091-2096(2003).
RN [21]
RP INTERACTION WITH EID1; SKIP1; SKIP6; SKIP8; PP2A13/SKIP9; PP2A11/SKIP10;
RP SKIP11; PP2B11/SKIP12; PP2A14/SKIP13; SKIP14; SKIP19/FBL20; SKIP20;
RP PP2B1/SKIP21; SKIP22; SKIP23; SKIP24; SKIP25; TULP10/SKIP26; SKIP27;
RP SKIP28/MEE11; AFR/SKIP29; SKIP30; SKIP31; SKIP32/FBP7; SKIP33 AND SKIP35.
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 [22]
RP INTERACTION WITH UFO.
RX PubMed=12826617; DOI=10.1073/pnas.1033043100;
RA Durfee T., Roe J.L., Sessions R.A., Inouye C., Serikawa K., Feldmann K.A.,
RA Weigel D., Zambryski P.C.;
RT "The F-box-containing protein UFO and AGAMOUS participate in antagonistic
RT pathways governing early petal development in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8571-8576(2003).
RN [23]
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 [24]
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 [25]
RP INTERACTION WITH AGROBACTERIUM VIRF.
RX PubMed=15343337; DOI=10.1038/nature02857;
RA Tzfira T., Vaidya M., Citovsky V.;
RT "Involvement of targeted proteolysis in plant genetic transformation by
RT Agrobacterium.";
RL Nature 431:87-92(2004).
RN [26]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [27]
RP TISSUE SPECIFICITY, AND INTERACTION WITH EBF1/FBL6; COI1/FBL2; ADO3/FKF1;
RP 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 [28]
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 [29]
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 [30]
RP INTERACTION WITH FBL17.
RX PubMed=18948957; DOI=10.1038/nature07289;
RA Kim H.J., Oh S.A., Brownfield L., Hong S.H., Ryu H., Hwang I., Twell D.,
RA Nam H.G.;
RT "Control of plant germline proliferation by SCF(FBL17) degradation of cell
RT cycle inhibitors.";
RL Nature 455:1134-1137(2008).
RN [31]
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 [32]
RP INTERACTION WITH DOR.
RX PubMed=18835996; DOI=10.1104/pp.108.126912;
RA Zhang Y., Xu W., Li Z., Deng X.W., Wu W., Xue Y.;
RT "F-box protein DOR functions as a novel inhibitory factor for abscisic
RT acid-induced stomatal closure under drought stress in Arabidopsis.";
RL Plant Physiol. 148:2121-2133(2008).
RN [33]
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 [34]
RP INTERACTION WITH VBF.
RX PubMed=20227663; DOI=10.1016/j.chom.2010.02.009;
RA Zaltsman A., Krichevsky A., Loyter A., Citovsky V.;
RT "Agrobacterium induces expression of a host F-box protein required for
RT tumorigenicity.";
RL Cell Host Microbe 7:197-209(2010).
RN [35]
RP INTERACTION WITH KIB1.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=28575660; DOI=10.1016/j.molcel.2017.05.012;
RA Zhu J.-Y., Li Y., Cao D.-M., Yang H., Oh E., Bi Y., Zhu S., Wang Z.-Y.;
RT "The F-box protein KIB1 mediates brassinosteroid-induced inactivation and
RT degradation of GSK3-like kinases in Arabidopsis.";
RL Mol. Cell 66:648-657(2017).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH TIR1; AUXIN; AUX/IAA
RP POLYPEPTIDE SUBSTRATE; AUXIN ANALOGS AND MYO-INOSITOL HEXAKISPHOSPHATE.
RX PubMed=17410169; DOI=10.1038/nature05731;
RA Tan X., Calderon-Villalobos L.I.A., Sharon M., Zheng C., Robinson C.V.,
RA Estelle M., Zheng N.;
RT "Mechanism of auxin perception by the TIR1 ubiquitin ligase.";
RL Nature 446:640-645(2007).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SKP1A; AUX/IAA
RP POLYPEPTIDE SUBSTRATE; AUXIN; AUXIN AGONISTS; AUXIN ANTAGONISTS AND
RP MYO-INOSITOL HEXAKISPHOSPHATE.
RX PubMed=18391211; DOI=10.1073/pnas.0711146105;
RA Hayashi K., Tan X., Zheng N., Hatate T., Kimura Y., Kepinski S., Nozaki H.;
RT "Small-molecule agonists and antagonists of F-box protein-substrate
RT interactions in auxin perception and signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5632-5637(2008).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-160, AND INTERACTION WITH COI1.
RX PubMed=20927106; DOI=10.1038/nature09430;
RA Sheard L.B., Tan X., Mao H., Withers J., Ben-Nissan G., Hinds T.R.,
RA Kobayashi Y., Hsu F.F., Sharon M., Browse J., He S.Y., Rizo J., Howe G.A.,
RA Zheng N.;
RT "Jasmonate perception by inositol-phosphate-potentiated COI1-JAZ co-
RT receptor.";
RL Nature 468:400-405(2010).
RN [39]
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:10500191, ECO:0000269|PubMed:10528262,
CC ECO:0000269|PubMed:11526079, ECO:0000269|PubMed:12970487,
CC 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, SKIP8, PP2A11/SKIP10, SKIP11,
CC PP2B11/SKIP12, PP2A14/SKIP13, SKIP14, SKIP15, SKIP16, SKIP19/FBL20,
CC SKIP20, PP2B1/SKIP21, SKIP22, SKIP23, SKIP24, SKIP25, TULP10/SKIP26,
CC SKIP27, SKIP28/MEE11, AFR/SKIP29, SKIP30, SKIP31, SKIP32/FBP7, SKIP33,
CC SKIP35, ADO1/ZTL, ADO2/LKP2, ADO3/FKF1, AFR, COI1, DOR, EBF1, EBF2,
CC EID1, ORE9, PP2A13/SKIP9, TIR1, UFO, SKP2A, CPR1/CPR30, FBL17, NUP58,
CC At1g55000, At1g67340, At1g78100, At3g04660, At3g61590, At4g38940 and
CC At5g49610. The SKP1A subunit of the SCF E3 ubiquitin ligase complex can
CC interact directly with KIN10, KIN11 and the proteasome subunit PAD1.
CC This interaction can be disrupted by PRL1. In case of polerovirus
CC infection, part of a SCF P0 complex composed of the viral silencing
CC suppressor P0, SKP1 and CUL1. Interacts with turnip yellows virus P0.
CC Interacts with VBF and Agrobacterium virF. Binds to KIB1
CC (PubMed:28575660). {ECO:0000269|PubMed:10398681,
CC ECO:0000269|PubMed:10607296, ECO:0000269|PubMed:11316788,
CC ECO:0000269|PubMed:11387208, ECO:0000269|PubMed:11487692,
CC ECO:0000269|PubMed:12169662, ECO:0000269|PubMed:12172031,
CC ECO:0000269|PubMed:12381738, ECO:0000269|PubMed:12445118,
CC ECO:0000269|PubMed:12795696, ECO:0000269|PubMed:12826617,
CC ECO:0000269|PubMed:14653999, ECO:0000269|PubMed:14675532,
CC ECO:0000269|PubMed:14749489, ECO:0000269|PubMed:15310821,
CC ECO:0000269|PubMed:15343337, ECO:0000269|PubMed:15447654,
CC ECO:0000269|PubMed:16446454, ECO:0000269|PubMed:17410169,
CC ECO:0000269|PubMed:18036202, ECO:0000269|PubMed:18391211,
CC ECO:0000269|PubMed:18835996, ECO:0000269|PubMed:18948957,
CC ECO:0000269|PubMed:19682297, ECO:0000269|PubMed:20227663,
CC ECO:0000269|PubMed:20927106, ECO:0000269|PubMed:23840761,
CC ECO:0000269|PubMed:28575660}.
CC -!- INTERACTION:
CC Q39255; Q94BT6: ADO1; NbExp=9; IntAct=EBI-532357, EBI-300691;
CC Q39255; Q8LAW2: AFR; NbExp=4; IntAct=EBI-532357, EBI-604438;
CC Q39255; Q9SHY1: At1g65740; NbExp=2; IntAct=EBI-532357, EBI-15923123;
CC Q39255; O04197: COI1; NbExp=11; IntAct=EBI-532357, EBI-401159;
CC Q39255; Q94AH6: CUL1; NbExp=7; IntAct=EBI-532357, EBI-532411;
CC Q39255; Q9SKK0: EBF1; NbExp=7; IntAct=EBI-532357, EBI-401198;
CC Q39255; Q8LEA8: EID1; NbExp=4; IntAct=EBI-532357, EBI-687388;
CC Q39255; Q8RWQ8: FBX14; NbExp=3; IntAct=EBI-532357, EBI-1235922;
CC Q39255; Q9ZR12: GRH1; NbExp=3; IntAct=EBI-532357, EBI-617479;
CC Q39255; Q38825: IAA7; NbExp=4; IntAct=EBI-532357, EBI-602959;
CC Q39255; Q9SZU7: KAI2; NbExp=3; IntAct=EBI-532357, EBI-25519488;
CC Q39255; Q9SIM9: MAX2; NbExp=3; IntAct=EBI-532357, EBI-25529872;
CC Q39255; Q9LEX0: PP2A13; NbExp=4; IntAct=EBI-532357, EBI-604261;
CC Q39255; Q9FDX1: SKIP1; NbExp=5; IntAct=EBI-532357, EBI-604228;
CC Q39255; O49279: SKIP15; NbExp=4; IntAct=EBI-532357, EBI-591174;
CC Q39255; Q9FE83: SKIP2; NbExp=3; IntAct=EBI-532357, EBI-591107;
CC Q39255; Q9ZU90: SKIP28; NbExp=3; IntAct=EBI-532357, EBI-604427;
CC Q39255; Q570C0: TIR1; NbExp=11; IntAct=EBI-532357, EBI-307183;
CC Q39255; Q39090: UFO; NbExp=6; IntAct=EBI-532357, EBI-590758;
CC Q39255; P15597: virF; Xeno; NbExp=6; IntAct=EBI-532357, EBI-605118;
CC Q39255; Q65967; Xeno; NbExp=3; IntAct=EBI-532357, EBI-848577;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11387208}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:11387208}. Cytoplasm,
CC cytoskeleton, phragmoplast {ECO:0000269|PubMed:11387208}.
CC Note=Associated to mitotic spindle and phragmoplasts during cell
CC division.
CC -!- TISSUE SPECIFICITY: Accumulates only in meristematic cells. Expressed
CC in inflorescence, shoot and root apical meristems, as well as in
CC developing organs such as gametocytes and seeds. Also detected in
CC cortical layer and epidermis of roots, leaves, pith and vascular bundle
CC of young stem, young floral buds and organ primordia, pollen and
CC through the valve of siliques. Not detectable in mature root tissues.
CC {ECO:0000269|PubMed:10607296, ECO:0000269|PubMed:12970487,
CC ECO:0000269|PubMed:14688296, ECO:0000269|PubMed:14749489,
CC ECO:0000269|PubMed:9530878}.
CC -!- DEVELOPMENTAL STAGE: During flower development, expressed in the
CC tapetal layer surrounding the male microsporocytes, and in the
CC endothelium layer surrounding the embryo sac within the ovule. During
CC embryogenesis, expressed in all cells of the embryo and in developing
CC endosperm surrounding the embryo, at the time of free nuclei
CC proliferation. {ECO:0000269|PubMed:9530878}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB38862.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U60981; AAB17535.1; -; mRNA.
DR EMBL; U97020; AAC63109.1; -; mRNA.
DR EMBL; AF059294; AAC14444.1; -; mRNA.
DR EMBL; AC007396; AAF26761.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35780.1; -; Genomic_DNA.
DR EMBL; AY080884; AAL87354.1; -; mRNA.
DR EMBL; AY113971; AAM45019.1; -; mRNA.
DR EMBL; U70034; AAB38862.1; ALT_INIT; mRNA.
DR PIR; T51309; T51309.
DR RefSeq; NP_565123.1; NM_106245.5.
DR PDB; 2P1M; X-ray; 1.80 A; A=1-160.
DR PDB; 2P1N; X-ray; 2.50 A; A/D=1-160.
DR PDB; 2P1O; X-ray; 1.90 A; A=1-160.
DR PDB; 2P1P; X-ray; 2.21 A; A=1-160.
DR PDB; 2P1Q; X-ray; 1.91 A; A=1-160.
DR PDB; 3C6N; X-ray; 2.60 A; A=1-160.
DR PDB; 3C6O; X-ray; 2.70 A; A=1-160.
DR PDB; 3C6P; X-ray; 2.70 A; A=1-160.
DR PDB; 3OGK; X-ray; 2.80 A; A/C/E/G/I/K/M/O=1-160.
DR PDB; 3OGL; X-ray; 3.18 A; A/C/E/G/I/K/M/O=1-160.
DR PDB; 3OGM; X-ray; 3.34 A; A/C/E/G/I/K/M/O=1-160.
DR PDB; 5HYW; X-ray; 3.01 A; B/D=1-160.
DR PDB; 5HZG; X-ray; 3.30 A; C/G=1-160.
DR PDB; 6BRO; X-ray; 2.50 A; A/C=1-160.
DR PDB; 6BRP; X-ray; 2.39 A; A/C=1-160.
DR PDB; 6BRQ; X-ray; 2.99 A; A/C=1-160.
DR PDBsum; 2P1M; -.
DR PDBsum; 2P1N; -.
DR PDBsum; 2P1O; -.
DR PDBsum; 2P1P; -.
DR PDBsum; 2P1Q; -.
DR PDBsum; 3C6N; -.
DR PDBsum; 3C6O; -.
DR PDBsum; 3C6P; -.
DR PDBsum; 3OGK; -.
DR PDBsum; 3OGL; -.
DR PDBsum; 3OGM; -.
DR PDBsum; 5HYW; -.
DR PDBsum; 5HZG; -.
DR PDBsum; 6BRO; -.
DR PDBsum; 6BRP; -.
DR PDBsum; 6BRQ; -.
DR AlphaFoldDB; Q39255; -.
DR SMR; Q39255; -.
DR BioGRID; 29147; 140.
DR ComplexPortal; CPX-1339; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1A.
DR ComplexPortal; CPX-1343; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1A.
DR ComplexPortal; CPX-1449; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1A.
DR ComplexPortal; CPX-1471; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1A.
DR ComplexPortal; CPX-1492; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1A.
DR ComplexPortal; CPX-1535; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1A.
DR ComplexPortal; CPX-1557; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1A.
DR ComplexPortal; CPX-1578; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1A.
DR DIP; DIP-31325N; -.
DR IntAct; Q39255; 76.
DR STRING; 3702.AT1G75950.1; -.
DR iPTMnet; Q39255; -.
DR SwissPalm; Q39255; -.
DR PaxDb; Q39255; -.
DR PRIDE; Q39255; -.
DR ProteomicsDB; 234585; -.
DR EnsemblPlants; AT1G75950.1; AT1G75950.1; AT1G75950.
DR GeneID; 843928; -.
DR Gramene; AT1G75950.1; AT1G75950.1; AT1G75950.
DR KEGG; ath:AT1G75950; -.
DR Araport; AT1G75950; -.
DR TAIR; locus:2204435; AT1G75950.
DR eggNOG; KOG1724; Eukaryota.
DR HOGENOM; CLU_059252_6_1_1; -.
DR InParanoid; Q39255; -.
DR OMA; TSRKIML; -.
DR OrthoDB; 1412723at2759; -.
DR PhylomeDB; Q39255; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q39255; -.
DR PRO; PR:Q39255; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39255; baseline and differential.
DR Genevisible; Q39255; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:ComplexPortal.
DR GO; GO:0005819; C:spindle; IDA:TAIR.
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:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:ComplexPortal.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:TAIR.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IMP:TAIR.
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 3D-structure; Auxin signaling pathway; Chromosome partition; Cytoplasm;
KW Cytoskeleton; Developmental protein; Ethylene signaling pathway;
KW Host-virus interaction; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..160
FT /note="SKP1-like protein 1A"
FT /id="PRO_0000187255"
FT REGION 102..160
FT /note="Interaction with the F-box domain of F-box proteins"
FT /evidence="ECO:0000269|PubMed:17410169"
FT CONFLICT 43
FT /note="P -> L (in Ref. 7; AAB38862)"
FT /evidence="ECO:0000305"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:2P1O"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2P1N"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:2P1O"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:2P1M"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2P1M"
FT TURN 31..36
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:2P1M"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:2P1M"
SQ SEQUENCE 160 AA; 17857 MW; 56B84C19FD5ABF17 CRC64;
MSAKKIVLKS SDGESFEVEE AVALESQTIA HMVEDDCVDN GVPLPNVTSK ILAKVIEYCK
RHVEAAASKA EAVEGAATSD DDLKAWDADF MKIDQATLFE LILAANYLNI KNLLDLTCQT
VADMIKGKTP EEIRTTFNIK NDFTPEEEEE VRRENQWAFE
