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SKP1-like protein 1A (SKP1-like 1) (UFO-binding protein 1)

 SKP1A_ARATH             Reviewed;         160 AA.
Q39255; P92992;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-MAR-2018, entry version 144.
RecName: Full=SKP1-like protein 1A {ECO:0000303|PubMed:10778750};
Short=SKP1-like 1 {ECO:0000303|PubMed:10778750};
AltName: Full=UFO-binding protein 1 {ECO:0000303|PubMed:10607296};
Name=SKP1A {ECO:0000303|PubMed:10778750};
Synonyms=ASK1 {ECO:0000303|PubMed:10528262},
SKP1 {ECO:0000303|PubMed:8706132}, UIP1 {ECO:0000303|PubMed:10607296};
OrderedLocusNames=At1g75950 {ECO:0000312|Araport:AT1G75950};
ORFNames=T4O12.17 {ECO:0000312|EMBL:AAF26761.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8706132; DOI=10.1016/S0092-8674(00)80099-9;
Connelly C., Hieter P.;
"Budding yeast SKP1 encodes an evolutionarily conserved kinetochore
protein required for cell cycle progression.";
Cell 86:275-285(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
UFO.
STRAIN=cv. Columbia;
PubMed=10607296; DOI=10.1046/j.1365-313x.1999.00617.x;
Samach A., Klenz J.E., Kohalmi S.E., Risseeuw E., Haughn G.W.,
Crosby W.L.;
"The UNUSUAL FLORAL ORGANS gene of Arabidopsis thaliana is an F-box
protein required for normal patterning and growth in the floral
meristem.";
Plant J. 20:433-445(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Landsberg erecta;
PubMed=10778750; DOI=10.1007/s004380051173;
Schouten J., de Kam R.J., Fetter K., Hoge J.H.C.;
"Overexpression of Arabidopsis thaliana SKP1 homologues in yeast
inactivates the Mig1 repressor by destabilising the F-box protein
Grr1.";
Mol. Gen. Genet. 263:309-319(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 13-160, DEVELOPMENTAL STAGE, AND TISSUE
SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=9530878; DOI=10.1007/s004250050265;
Porat R., Lu P., O'Neill S.D.;
"Arabidopsis SKP1, a homologue of a cell cycle regulator gene, is
predominantly expressed in meristematic cells.";
Planta 204:345-351(1998).
[8]
FUNCTION.
PubMed=10528262;
DOI=10.1002/(SICI)1520-6408(1999)25:3<209::AID-DVG4>3.3.CO;2-F;
Zhao D., Yang M., Solava J., Ma H.;
"The ASK1 gene regulates development and interacts with the UFO gene
to control floral organ identity in Arabidopsis.";
Dev. Genet. 25:209-223(1999).
[9]
FUNCTION, AND INTERACTION WITH TIR1.
PubMed=10398681; DOI=10.1101/gad.13.13.1678;
Gray W.M., del Pozo J.C., Walker L., Hobbie L., Risseeuw E., Banks T.,
Crosby W.L., Yang M., Ma H., Estelle M.;
"Identification of an SCF ubiquitin-ligase complex required for auxin
response in Arabidopsis thaliana.";
Genes Dev. 13:1678-1691(1999).
[10]
FUNCTION.
PubMed=10500191; DOI=10.1073/pnas.96.20.11416;
Yang M., Hu Y., Lodhi M., McCombie W.R., Ma H.;
"The Arabidopsis SKP1-LIKE1 gene is essential for male meiosis and may
control homologue separation.";
Proc. Natl. Acad. Sci. U.S.A. 96:11416-11421(1999).
[11]
FUNCTION.
PubMed=11526079;
Zhao D., Yu Q., Chen M., Ma H.;
"The ASK1 gene regulates B function gene expression in cooperation
with UFO and LEAFY in Arabidopsis.";
Development 128:2735-2746(2001).
[12]
SUBCELLULAR LOCATION, AND INTERACTION WITH SKIP1; SKIP2; SKIP3; SKIP4;
SKIP6; FIB1; CUL1; PAD1; KIN10 AND KIN11.
PubMed=11387208; DOI=10.1093/emboj/20.11.2742;
Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A.,
Salchert K., del Pozo C., Schell J., Koncz C.;
"SKP1-SnRK protein kinase interactions mediate proteasomal binding of
a plant SCF ubiquitin ligase.";
EMBO J. 20:2742-2756(2001).
[13]
INTERACTION WITH EID1.
PubMed=11316788; DOI=10.1101/gad.197201;
Dieterle M., Zhou Y.-C., Schaefer E., Funk M., Kretsch T.;
"EID1, an F-box protein involved in phytochrome A-specific light
signaling.";
Genes Dev. 15:939-944(2001).
[14]
INTERACTION WITH ORE9.
PubMed=11487692; DOI=10.1105/tpc.13.8.1779;
Woo H.R., Chung K.M., Park J.-H., Oh S.A., Ahn T., Hong S.H.,
Jang S.K., Nam H.G.;
"ORE9, an F-box protein that regulates leaf senescence in
Arabidopsis.";
Plant Cell 13:1779-1790(2001).
[15]
IDENTIFICATION IN A SCF COMPLEX.
PubMed=12381738; DOI=10.1074/jbc.M204254200;
Lechner E., Xie D., Grava S., Pigaglio E., Planchais S.,
Murray J.A.H., Parmentier Y., Mutterer J., Dubreucq B., Shen W.-H.,
Genschik P.;
"The AtRbx1 protein is part of plant SCF complexes, and its down-
regulation causes severe growth and developmental defects.";
J. Biol. Chem. 277:50069-50080(2002).
[16]
INTERACTION WITH COI1, AND IDENTIFICATION IN A SCF(COI1) COMPLEX.
PubMed=12172031; DOI=10.1105/tpc.003368;
Xu L., Liu F., Lechner E., Genschik P., Crosby W.L., Ma H., Peng W.,
Huang D., Xie D.;
"The SCF(COI1) ubiquitin-ligase complexes are required for jasmonate
response in Arabidopsis.";
Plant Cell 14:1919-1935(2002).
[17]
INTERACTION WITH COI1, AND IDENTIFICATION IN A SCF(COI1) COMPLEX.
PubMed=12445118; DOI=10.1046/j.1365-313X.2002.01432.x;
Devoto A., Nieto-Rostro M., Xie D., Ellis C., Harmston R., Patrick E.,
Davis J., Sherratt L., Coleman M., Turner J.G.;
"COI1 links jasmonate signalling and fertility to the SCF ubiquitin-
ligase complex in Arabidopsis.";
Plant J. 32:457-466(2002).
[18]
INTERACTION WITH UFO; PP2A13; AT1G67340; AT4G38940; SKIP15; AT3G04660;
AT1G78100; AT1G55000; SKIP16; SKIP2; SKIP32 AND EBF1.
PubMed=12169662; DOI=10.1073/pnas.162339999;
Gagne J.M., Downes B.P., Shiu S.-H., Durski A.M., Vierstra R.D.;
"The F-box subunit of the SCF E3 complex is encoded by a diverse
superfamily of genes in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 99:11519-11524(2002).
[19]
INTERACTION WITH EBF1 AND EBF2.
PubMed=14675532; DOI=10.1016/S0092-8674(03)00969-3;
Guo H., Ecker J.R.;
"Plant responses to ethylene gas are mediated by SCF(EBF1/EBF2)-
dependent proteolysis of EIN3 transcription factor.";
Cell 115:667-677(2003).
[20]
INTERACTION WITH AFR.
PubMed=14653999; DOI=10.1016/j.cub.2003.11.019;
Harmon F.G., Kay S.A.;
"The F box protein AFR is a positive regulator of phytochrome A-
mediated light signaling.";
Curr. Biol. 13:2091-2096(2003).
[21]
INTERACTION WITH EID1; SKIP1; SKIP6; SKIP8; PP2A13/SKIP9;
PP2A11/SKIP10; SKIP11; PP2B11/SKIP12; PP2A14/SKIP13; SKIP14;
SKIP19/FBL20; SKIP20; PP2B1/SKIP21; SKIP22; SKIP23; SKIP24; SKIP25;
TULP10/SKIP26; SKIP27; SKIP28/MEE11; AFR/SKIP29; SKIP30; SKIP31;
SKIP32/FBP7; SKIP33 AND SKIP35.
PubMed=12795696; DOI=10.1046/j.1365-313X.2003.01768.x;
Risseeuw E.P., Daskalchuk T.E., Banks T.W., Liu E., Cotelesage J.,
Hellmann H., Estelle M., Somers D.E., Crosby W.L.;
"Protein interaction analysis of SCF ubiquitin E3 ligase subunits from
Arabidopsis.";
Plant J. 34:753-767(2003).
[22]
INTERACTION WITH UFO.
PubMed=12826617; DOI=10.1073/pnas.1033043100;
Durfee T., Roe J.L., Sessions R.A., Inouye C., Serikawa K.,
Feldmann K.A., Weigel D., Zambryski P.C.;
"The F-box-containing protein UFO and AGAMOUS participate in
antagonistic pathways governing early petal development in
Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 100:8571-8576(2003).
[23]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12970487; DOI=10.1104/pp.103.024703;
Zhao D., Ni W., Feng B., Han T., Petrasek M.G., Ma H.;
"Members of the Arabidopsis-SKP1-like gene family exhibit a variety of
expression patterns and may play diverse roles in Arabidopsis.";
Plant Physiol. 133:203-217(2003).
[24]
INTERACTION WITH ADO1; ADO2 AND ADO3.
PubMed=15310821; DOI=10.1093/jxb/erh226;
Yasuhara M., Mitsui S., Hirano H., Takanabe R., Tokioka Y., Ihara N.,
Komatsu A., Seki M., Shinozaki K., Kiyosue T.;
"Identification of ASK and clock-associated proteins as molecular
partners of LKP2 (LOV kelch protein 2) in Arabidopsis.";
J. Exp. Bot. 55:2015-2027(2004).
[25]
INTERACTION WITH AGROBACTERIUM VIRF.
PubMed=15343337; DOI=10.1038/nature02857;
Tzfira T., Vaidya M., Citovsky V.;
"Involvement of targeted proteolysis in plant genetic transformation
by Agrobacterium.";
Nature 431:87-92(2004).
[26]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14688296; DOI=10.1105/tpc.017772;
Liu F., Ni W., Griffith M.E., Huang Z., Chang C., Peng W., Ma H.,
Xie D.;
"The ASK1 and ASK2 genes are essential for Arabidopsis early
development.";
Plant Cell 16:5-20(2004).
[27]
TISSUE SPECIFICITY, AND INTERACTION WITH EBF1/FBL6; COI1/FBL2;
ADO3/FKF1; AT3G61590 AND AT5G49610.
PubMed=14749489; DOI=10.1093/pcp/pch009;
Takahashi N., Kuroda H., Kuromori T., Hirayama T., Seki M.,
Shinozaki K., Shimada H., Matsui M.;
"Expression and interaction analysis of Arabidopsis Skp1-related
genes.";
Plant Cell Physiol. 45:83-91(2004).
[28]
INTERACTION WITH ADO1.
PubMed=15447654; DOI=10.1111/j.1365-313X.2004.02207.x;
Han L., Mason M., Risseeuw E.P., Crosby W.L., Somers D.E.;
"Formation of an SCF(ZTL) complex is required for proper regulation of
circadian timing.";
Plant J. 40:291-301(2004).
[29]
INTERACTION WITH TURNIP YELLOWS VIRUS PROTEIN P0, AND IDENTIFICATION
IN A SCF P0 COMPLEX.
PubMed=16446454; DOI=10.1073/pnas.0510784103;
Pazhouhandeh M., Dieterle M., Marrocco K., Lechner E., Berry B.,
Brault V., Hemmer O., Kretsch T., Richards K.E., Genschik P.,
Ziegler-Graff V.;
"F-box-like domain in the polerovirus protein P0 is required for
silencing suppressor function.";
Proc. Natl. Acad. Sci. U.S.A. 103:1994-1999(2006).
[30]
INTERACTION WITH FBL17.
PubMed=18948957; DOI=10.1038/nature07289;
Kim H.J., Oh S.A., Brownfield L., Hong S.H., Ryu H., Hwang I.,
Twell D., Nam H.G.;
"Control of plant germline proliferation by SCF(FBL17) degradation of
cell cycle inhibitors.";
Nature 455:1134-1137(2008).
[31]
INTERACTION WITH SKP2A.
PubMed=18036202; DOI=10.1111/j.1365-313X.2007.03378.x;
Jurado S., Diaz-Trivino S., Abraham Z., Manzano C., Gutierrez C.,
del Pozo C.;
"SKP2A, an F-box protein that regulates cell division, is degraded via
the ubiquitin pathway.";
Plant J. 53:828-841(2008).
[32]
INTERACTION WITH DOR.
PubMed=18835996; DOI=10.1104/pp.108.126912;
Zhang Y., Xu W., Li Z., Deng X.W., Wu W., Xue Y.;
"F-box protein DOR functions as a novel inhibitory factor for abscisic
acid-induced stomatal closure under drought stress in Arabidopsis.";
Plant Physiol. 148:2121-2133(2008).
[33]
INTERACTION WITH CPR1/CPR30.
PubMed=19682297; DOI=10.1111/j.1365-313X.2009.03995.x;
Gou M., Su N., Zheng J., Huai J., Wu G., Zhao J., He J., Tang D.,
Yang S., Wang G.;
"An F-box gene, CPR30, functions as a negative regulator of the
defense response in Arabidopsis.";
Plant J. 60:757-770(2009).
[34]
INTERACTION WITH VBF.
PubMed=20227663; DOI=10.1016/j.chom.2010.02.009;
Zaltsman A., Krichevsky A., Loyter A., Citovsky V.;
"Agrobacterium induces expression of a host F-box protein required for
tumorigenicity.";
Cell Host Microbe 7:197-209(2010).
[35]
INTERACTION WITH KIB1.
STRAIN=cv. Columbia, and cv. Wassilewskija;
PubMed=28575660; DOI=10.1016/j.molcel.2017.05.012;
Zhu J.-Y., Li Y., Cao D.-M., Yang H., Oh E., Bi Y., Zhu S.,
Wang Z.-Y.;
"The F-box protein KIB1 mediates brassinosteroid-induced inactivation
and degradation of GSK3-like kinases in Arabidopsis.";
Mol. Cell 66:648-657(2017).
[36]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH TIR1; AUXIN;
AUX/IAA POLYPEPTIDE SUBSTRATE; AUXIN ANALOGS AND MYO-INOSITOL
HEXAKISPHOSPHATE.
PubMed=17410169; DOI=10.1038/nature05731;
Tan X., Calderon-Villalobos L.I.A., Sharon M., Zheng C.,
Robinson C.V., Estelle M., Zheng N.;
"Mechanism of auxin perception by the TIR1 ubiquitin ligase.";
Nature 446:640-645(2007).
[37]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SKP1A; AUX/IAA
POLYPEPTIDE SUBSTRATE; AUXIN; AUXIN AGONISTS; AUXIN ANTAGONISTS AND
MYO-INOSITOL HEXAKISPHOSPHATE.
PubMed=18391211; DOI=10.1073/pnas.0711146105;
Hayashi K., Tan X., Zheng N., Hatate T., Kimura Y., Kepinski S.,
Nozaki H.;
"Small-molecule agonists and antagonists of F-box protein-substrate
interactions in auxin perception and signaling.";
Proc. Natl. Acad. Sci. U.S.A. 105:5632-5637(2008).
[38]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-160, AND INTERACTION WITH
COI1.
PubMed=20927106; DOI=10.1038/nature09430;
Sheard L.B., Tan X., Mao H., Withers J., Ben-Nissan G., Hinds T.R.,
Kobayashi Y., Hsu F.F., Sharon M., Browse J., He S.Y., Rizo J.,
Howe G.A., Zheng N.;
"Jasmonate perception by inositol-phosphate-potentiated COI1-JAZ co-
receptor.";
Nature 468:400-405(2010).
[39]
INTERACTION WITH NUP58.
PubMed=23840761; DOI=10.1371/journal.pone.0067661;
Ferrandez-Ayela A., Alonso-Peral M.M., Sanchez-Garcia A.B.,
Micol-Ponce R., Perez-Perez J.M., Micol J.L., Ponce M.R.;
"Arabidopsis TRANSCURVATA1 encodes NUP58, a component of the
nucleopore central channel.";
PLoS ONE 8:E67661-E67661(2013).
-!- FUNCTION: Involved in ubiquitination and subsequent proteasomal
degradation of target proteins. Together with CUL1, RBX1 and a F-
box protein, it forms a SCF E3 ubiquitin ligase complex. The
functional specificity of this complex depends on the type of F-
box protein. In the SCF complex, it serves as an adapter that
links the F-box protein to CUL1. SCF(UFO) is required for
vegetative and floral organ development as well as for male
gametogenesis. SCF(TIR1) is involved in auxin signaling pathway.
SCF(COI1) regulates responses to jasmonates. SCF(EID1) and
SCF(AFR) are implicated in phytochrome A light signaling.
SCF(ADO1), SCF(ADO2), SCF(ADO3) are related to the circadian
clock. SCF(ORE9) seems to be involved in senescence.
SCF(EBF1/EBF2) may regulate ethylene signaling. Plays a role
during embryogenesis and early postembryonic development,
especially during cell elongation and division. Contributes to the
correct chromosome segregation during tetrad formation.
{ECO:0000269|PubMed:10398681, ECO:0000269|PubMed:10500191,
ECO:0000269|PubMed:10528262, ECO:0000269|PubMed:11526079,
ECO:0000269|PubMed:12970487, ECO:0000269|PubMed:14688296}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Part of a SCF E3 ubiquitin ligase complex composed of
SKP1, CUL1, RBX1 (RBX1A or RBX1B) and F-box proteins. Interacts
with SKIP1, SKIP2, SKIP3, SKIP4, SKIP6, FIB1/SKIP7, SKIP8,
PP2A11/SKIP10, SKIP11, PP2B11/SKIP12, PP2A14/SKIP13, SKIP14,
SKIP15, SKIP16, SKIP19/FBL20, SKIP20, PP2B1/SKIP21, SKIP22,
SKIP23, SKIP24, SKIP25, TULP10/SKIP26, SKIP27, SKIP28/MEE11,
AFR/SKIP29, SKIP30, SKIP31, SKIP32/FBP7, SKIP33, SKIP35, ADO1/ZTL,
ADO2/LKP2, ADO3/FKF1, AFR, COI1, DOR, EBF1, EBF2, EID1, ORE9,
PP2A13/SKIP9, TIR1, UFO, SKP2A, CPR1/CPR30, FBL17, NUP58,
At1g55000, At1g67340, At1g78100, At3g04660, At3g61590, At4g38940
and At5g49610. The SKP1A subunit of the SCF E3 ubiquitin ligase
complex can interact directly with KIN10, KIN11 and the proteasome
subunit PAD1. This interaction can be disrupted by PRL1. In case
of polerovirus infection, part of a SCF P0 complex composed of the
viral silencing suppressor P0, SKP1 and CUL1. Interacts with
turnip yellows virus P0. Interacts with VBF and Agrobacterium
virF. Binds to KIB1 (PubMed:28575660).
{ECO:0000269|PubMed:10398681, ECO:0000269|PubMed:10607296,
ECO:0000269|PubMed:11316788, ECO:0000269|PubMed:11387208,
ECO:0000269|PubMed:11487692, ECO:0000269|PubMed:12169662,
ECO:0000269|PubMed:12172031, ECO:0000269|PubMed:12381738,
ECO:0000269|PubMed:12445118, ECO:0000269|PubMed:12795696,
ECO:0000269|PubMed:12826617, ECO:0000269|PubMed:14653999,
ECO:0000269|PubMed:14675532, ECO:0000269|PubMed:14749489,
ECO:0000269|PubMed:15310821, ECO:0000269|PubMed:15343337,
ECO:0000269|PubMed:15447654, ECO:0000269|PubMed:16446454,
ECO:0000269|PubMed:17410169, ECO:0000269|PubMed:18036202,
ECO:0000269|PubMed:18391211, ECO:0000269|PubMed:18835996,
ECO:0000269|PubMed:18948957, ECO:0000269|PubMed:19682297,
ECO:0000269|PubMed:20227663, ECO:0000269|PubMed:20927106,
ECO:0000269|PubMed:23840761, ECO:0000269|PubMed:28575660}.
-!- INTERACTION:
Q65967:- (xeno); NbExp=3; IntAct=EBI-532357, EBI-848577;
Q94BT6:ADO1; NbExp=9; IntAct=EBI-532357, EBI-300691;
Q8LAW2:AFR; NbExp=4; IntAct=EBI-532357, EBI-604438;
Q9SHY1:At1g65740; NbExp=2; IntAct=EBI-532357, EBI-15923123;
O04197:COI1; NbExp=11; IntAct=EBI-532357, EBI-401159;
Q94AH6:CUL1; NbExp=7; IntAct=EBI-532357, EBI-532411;
Q9SKK0:EBF1; NbExp=4; IntAct=EBI-532357, EBI-401198;
Q8LEA8:EID1; NbExp=4; IntAct=EBI-532357, EBI-687388;
Q9ZR12:GRH1; NbExp=3; IntAct=EBI-532357, EBI-617479;
Q38825:IAA7; NbExp=4; IntAct=EBI-532357, EBI-602959;
Q9LEX0:PP2A13; NbExp=4; IntAct=EBI-532357, EBI-604261;
Q9FDX1:SKIP1; NbExp=5; IntAct=EBI-532357, EBI-604228;
O49279:SKIP15; NbExp=4; IntAct=EBI-532357, EBI-591174;
Q9FE83:SKIP2; NbExp=3; IntAct=EBI-532357, EBI-591107;
Q9ZU90:SKIP28; NbExp=3; IntAct=EBI-532357, EBI-604427;
Q570C0:TIR1; NbExp=8; IntAct=EBI-532357, EBI-307183;
Q39090:UFO; NbExp=6; IntAct=EBI-532357, EBI-590758;
P15597:virF (xeno); NbExp=6; IntAct=EBI-532357, EBI-605118;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11387208}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11387208}.
Cytoplasm, cytoskeleton, phragmoplast
{ECO:0000269|PubMed:11387208}. Note=Associated to mitotic spindle
and phragmoplasts during cell division.
-!- TISSUE SPECIFICITY: Accumulates only in meristematic cells.
Expressed in inflorescence, shoot and root apical meristems, as
well as in developing organs such as gametocytes and seeds. Also
detected in cortical layer and epidermis of roots, leaves, pith
and vascular bundle of young stem, young floral buds and organ
primordia, pollen and through the valve of siliques. Not
detectable in mature root tissues. {ECO:0000269|PubMed:10607296,
ECO:0000269|PubMed:12970487, ECO:0000269|PubMed:14688296,
ECO:0000269|PubMed:14749489, ECO:0000269|PubMed:9530878}.
-!- DEVELOPMENTAL STAGE: During flower development, expressed in the
tapetal layer surrounding the male microsporocytes, and in the
endothelium layer surrounding the embryo sac within the ovule.
During embryogenesis, expressed in all cells of the embryo and in
developing endosperm surrounding the embryo, at the time of free
nuclei proliferation. {ECO:0000269|PubMed:9530878}.
-!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB38862.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; U60981; AAB17535.1; -; mRNA.
EMBL; U97020; AAC63109.1; -; mRNA.
EMBL; AF059294; AAC14444.1; -; mRNA.
EMBL; AC007396; AAF26761.1; -; Genomic_DNA.
EMBL; CP002684; AEE35780.1; -; Genomic_DNA.
EMBL; AY080884; AAL87354.1; -; mRNA.
EMBL; AY113971; AAM45019.1; -; mRNA.
EMBL; U70034; AAB38862.1; ALT_INIT; mRNA.
PIR; T51309; T51309.
RefSeq; NP_565123.1; NM_106245.5.
UniGene; At.23531; -.
PDB; 2P1M; X-ray; 1.80 A; A=1-160.
PDB; 2P1N; X-ray; 2.50 A; A/D=1-160.
PDB; 2P1O; X-ray; 1.90 A; A=1-160.
PDB; 2P1P; X-ray; 2.21 A; A=1-160.
PDB; 2P1Q; X-ray; 1.91 A; A=1-160.
PDB; 3C6N; X-ray; 2.60 A; A=1-160.
PDB; 3C6O; X-ray; 2.70 A; A=1-160.
PDB; 3C6P; X-ray; 2.70 A; A=1-160.
PDB; 3OGK; X-ray; 2.80 A; A/C/E/G/I/K/M/O=1-160.
PDB; 3OGL; X-ray; 3.18 A; A/C/E/G/I/K/M/O=1-160.
PDB; 3OGM; X-ray; 3.34 A; A/C/E/G/I/K/M/O=1-160.
PDB; 5HYW; X-ray; 3.01 A; B/D=1-160.
PDB; 5HZG; X-ray; 3.30 A; C/G=1-160.
PDBsum; 2P1M; -.
PDBsum; 2P1N; -.
PDBsum; 2P1O; -.
PDBsum; 2P1P; -.
PDBsum; 2P1Q; -.
PDBsum; 3C6N; -.
PDBsum; 3C6O; -.
PDBsum; 3C6P; -.
PDBsum; 3OGK; -.
PDBsum; 3OGL; -.
PDBsum; 3OGM; -.
PDBsum; 5HYW; -.
PDBsum; 5HZG; -.
ProteinModelPortal; Q39255; -.
SMR; Q39255; -.
BioGrid; 29147; 128.
DIP; DIP-31325N; -.
IntAct; Q39255; 73.
STRING; 3702.AT1G75950.1; -.
iPTMnet; Q39255; -.
SwissPalm; Q39255; -.
PaxDb; Q39255; -.
PRIDE; Q39255; -.
EnsemblPlants; AT1G75950.1; AT1G75950.1; AT1G75950.
GeneID; 843928; -.
Gramene; AT1G75950.1; AT1G75950.1; AT1G75950.
KEGG; ath:AT1G75950; -.
Araport; AT1G75950; -.
TAIR; locus:2204435; AT1G75950.
eggNOG; KOG1724; Eukaryota.
eggNOG; COG5201; LUCA.
HOGENOM; HOG000172184; -.
InParanoid; Q39255; -.
KO; K03094; -.
OMA; TMFARGE; -.
OrthoDB; EOG09360RN0; -.
PhylomeDB; Q39255; -.
Reactome; R-ATH-8951664; Neddylation.
Reactome; R-ATH-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q39255; -.
PRO; PR:Q39255; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q39255; baseline and differential.
Genevisible; Q39255; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0009524; C:phragmoplast; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005819; C:spindle; IDA:TAIR.
GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:TAIR.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0045910; P:negative regulation of DNA recombination; IMP:TAIR.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR016897; SKP1.
InterPro; IPR001232; SKP1-like.
InterPro; IPR036296; SKP1-like_dim_sf.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
InterPro; IPR016072; Skp1_comp_dimer.
InterPro; IPR016073; Skp1_comp_POZ.
Pfam; PF01466; Skp1; 1.
Pfam; PF03931; Skp1_POZ; 1.
PIRSF; PIRSF028729; E3_ubiquit_lig_SCF_Skp; 1.
SMART; SM00512; Skp1; 1.
SUPFAM; SSF54695; SSF54695; 1.
SUPFAM; SSF81382; SSF81382; 1.
1: Evidence at protein level;
3D-structure; Auxin signaling pathway; Chromosome partition;
Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
Ethylene signaling pathway; Host-virus interaction; Nucleus;
Reference proteome; Ubl conjugation pathway.
CHAIN 1 160 SKP1-like protein 1A.
/FTId=PRO_0000187255.
REGION 102 160 Interaction with the F-box domain of F-
box proteins.
{ECO:0000269|PubMed:17410169}.
CONFLICT 43 43 P -> L (in Ref. 7; AAB38862).
{ECO:0000305}.
STRAND 6 9 {ECO:0000244|PDB:2P1O}.
STRAND 11 13 {ECO:0000244|PDB:2P1N}.
STRAND 15 18 {ECO:0000244|PDB:2P1O}.
HELIX 21 24 {ECO:0000244|PDB:2P1M}.
TURN 27 29 {ECO:0000244|PDB:2P1M}.
TURN 31 36 {ECO:0000244|PDB:3OGK}.
HELIX 37 40 {ECO:0000244|PDB:3OGK}.
HELIX 49 57 {ECO:0000244|PDB:2P1M}.
TURN 80 85 {ECO:0000244|PDB:5HZG}.
STRAND 89 91 {ECO:0000244|PDB:2P1N}.
STRAND 94 96 {ECO:0000244|PDB:5HZG}.
HELIX 102 107 {ECO:0000244|PDB:2P1M}.
HELIX 111 123 {ECO:0000244|PDB:2P1M}.
TURN 124 127 {ECO:0000244|PDB:2P1M}.
HELIX 130 136 {ECO:0000244|PDB:2P1M}.
HELIX 145 159 {ECO:0000244|PDB:2P1M}.
SEQUENCE 160 AA; 17857 MW; 56B84C19FD5ABF17 CRC64;
MSAKKIVLKS SDGESFEVEE AVALESQTIA HMVEDDCVDN GVPLPNVTSK ILAKVIEYCK
RHVEAAASKA EAVEGAATSD DDLKAWDADF MKIDQATLFE LILAANYLNI KNLLDLTCQT
VADMIKGKTP EEIRTTFNIK NDFTPEEEEE VRRENQWAFE


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