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SKP1-like protein 1B (SKP1-like 2) (UFO-binding protein 2)

 SKP1B_ARATH             Reviewed;         171 AA.
Q9FHW7; O65283; Q0WSZ3;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
20-DEC-2017, entry version 126.
RecName: Full=SKP1-like protein 1B;
AltName: Full=SKP1-like 2;
AltName: Full=UFO-binding protein 2;
Name=SKP1B; Synonyms=ASK2, UIP2; OrderedLocusNames=At5g42190;
ORFNames=MJC20.30;
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], 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).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10470850; DOI=10.1093/dnares/6.3.183;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IX.
Sequence features of the regions of 1,011,550 bp covered by seventeen
P1 and TAC clones.";
DNA Res. 6:183-195(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[7]
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).
[8]
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).
[9]
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).
[10]
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).
[11]
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).
[12]
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).
[13]
INTERACTION WITH EID1; SKIP1; PP2A13/SKIP9; SKIP11; PP2B11/SKIP12;
PP2A14/SKIP13; SKIP14; SKIP15/FBX3; SKIP16; SKIP17; FBW2/SKIP18;
SKIP19/FBL20; SKIP20; PP2B1/SKIP21; SKIP22; SKIP24; SKIP27; SKIP31 AND
SKIP34.
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).
[14]
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).
[15]
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).
[16]
FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
[17]
TISSUE SPECIFICITY, AND INTERACTION WITH EBF1/FBL6; COI1/FBL2;
ADO3/FKF1; PP2B10; 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).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
INTERACTION WITH SNL1.
PubMed=19962994; DOI=10.1016/j.jmb.2009.11.065;
Bowen A.J., Gonzalez D., Mullins J.G., Bhatt A.M., Martinez A.,
Conlan R.S.;
"PAH-domain-specific interactions of the Arabidopsis transcription
coregulator SIN3-LIKE1 (SNL1) with telomere-binding protein 1 and
ALWAYS EARLY2 Myb-DNA binding factors.";
J. Mol. Biol. 395:937-949(2010).
[23]
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: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, PP2A13/SKIP9,
SKIP11, PP2B11/SKIP12, PP2A14/SKIP13, SKIP14, SKIP15/FBX3, SKIP16,
SKIP17, FBW2/SKIP18, SKIP19/FBL20, SKIP20, PP2B1/SKIP21, SKIP22,
SKIP24, SKIP27, SKIP31, SKIP32, SKIP34, ADO1/ZTL, ADO2/LKP2,
ADO3/FKF1, AFR, COI1, EBF1, EBF2, EID1, ORE9, PP2A13, PP2B10,
TIR1, UFO, SKP2A, CPR1/CPR30, NUP58, At1g55000, At1g67340,
At1g78100, At3g04660, At3g61590, At4g38940 and At5g49610. The
SKP1B subunit of the SCF E3 ubiquitin ligase complex can probably
interact directly with KIN10, KIN11 and the proteasome subunit
PAD1. Interacts with SNL1. 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.
{ECO:0000269|PubMed:10398681, ECO:0000269|PubMed:10607296,
ECO:0000269|PubMed:11316788, ECO:0000269|PubMed:12169662,
ECO:0000269|PubMed:12172031, ECO:0000269|PubMed:12381738,
ECO:0000269|PubMed:12445118, ECO:0000269|PubMed:12795696,
ECO:0000269|PubMed:14749489, ECO:0000269|PubMed:15310821,
ECO:0000269|PubMed:15447654, ECO:0000269|PubMed:16446454,
ECO:0000269|PubMed:18036202, ECO:0000269|PubMed:19682297,
ECO:0000269|PubMed:19962994, ECO:0000269|PubMed:23840761}.
-!- INTERACTION:
Q65967:- (xeno); NbExp=3; IntAct=EBI-604076, EBI-848577;
Q94BT6:ADO1; NbExp=5; IntAct=EBI-604076, EBI-300691;
Q9C9W9:ADO3; NbExp=5; IntAct=EBI-604076, EBI-401228;
O04197:COI1; NbExp=6; IntAct=EBI-604076, EBI-401159;
Q9SKK0:EBF1; NbExp=5; IntAct=EBI-604076, EBI-401198;
Q8LEA8:EID1; NbExp=4; IntAct=EBI-604076, EBI-687388;
Q9ZPE4:FBW2; NbExp=3; IntAct=EBI-604076, EBI-604740;
Q9STX3:GID2; NbExp=3; IntAct=EBI-604076, EBI-619033;
Q9LEX0:PP2A13; NbExp=6; IntAct=EBI-604076, EBI-604261;
Q9FJ80:PP2A14; NbExp=3; IntAct=EBI-604076, EBI-604303;
Q8XZN9:ripG (xeno); NbExp=2; IntAct=EBI-604076, EBI-15602092;
O49279:SKIP15; NbExp=6; IntAct=EBI-604076, EBI-591174;
Q9LND7:SKIP16; NbExp=3; IntAct=EBI-604076, EBI-591078;
Q0WRC9:SKIP17; NbExp=3; IntAct=EBI-604076, EBI-604757;
Q8GX29:SKIP25; NbExp=3; IntAct=EBI-604076, EBI-604376;
Q570C0:TIR1; NbExp=4; IntAct=EBI-604076, EBI-307183;
Q39090:UFO; NbExp=5; IntAct=EBI-604076, EBI-590758;
P15597:virF (xeno); NbExp=5; IntAct=EBI-604076, EBI-605118;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in tips, cortical layer and
epidermis of roots. Detected in whole seedling, vascular tissues,
pith and vascular bundle of young stem, leaves, inflorescence
meristem, young floral buds and organ primordia, flowers,
developing seeds and through the valve of siliques. Expressed in
male meiocytes, pollen, embryo and endosperm.
{ECO:0000269|PubMed:12970487, ECO:0000269|PubMed:14688296,
ECO:0000269|PubMed:14749489}.
-!- DEVELOPMENTAL STAGE: Expressed during all stages of embryogenesis.
{ECO:0000269|PubMed:14688296}.
-!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC63110.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U97021; AAC63110.1; ALT_INIT; mRNA.
EMBL; AF059295; AAC14445.1; -; mRNA.
EMBL; AB017067; BAB08452.1; -; Genomic_DNA.
EMBL; CP002688; AED94777.1; -; Genomic_DNA.
EMBL; BT004798; AAO44064.1; -; mRNA.
EMBL; AK227773; BAE99755.1; -; mRNA.
RefSeq; NP_568603.1; NM_123584.5.
UniGene; At.23304; -.
UniGene; At.71056; -.
ProteinModelPortal; Q9FHW7; -.
SMR; Q9FHW7; -.
BioGrid; 19474; 131.
DIP; DIP-31326N; -.
IntAct; Q9FHW7; 93.
STRING; 3702.AT5G42190.1; -.
iPTMnet; Q9FHW7; -.
PaxDb; Q9FHW7; -.
PRIDE; Q9FHW7; -.
EnsemblPlants; AT5G42190.1; AT5G42190.1; AT5G42190.
GeneID; 834224; -.
Gramene; AT5G42190.1; AT5G42190.1; AT5G42190.
KEGG; ath:AT5G42190; -.
Araport; AT5G42190; -.
TAIR; locus:2165825; AT5G42190.
eggNOG; KOG1724; Eukaryota.
eggNOG; COG5201; LUCA.
HOGENOM; HOG000172184; -.
InParanoid; Q9FHW7; -.
KO; K03094; -.
OMA; NDFLPQE; -.
OrthoDB; EOG09360RN0; -.
PhylomeDB; Q9FHW7; -.
Reactome; R-ATH-8951664; Neddylation.
Reactome; R-ATH-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
PRO; PR:Q9FHW7; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FHW7; baseline and differential.
Genevisible; Q9FHW7; AT.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:TAIR.
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;
Auxin signaling pathway; Chromosome partition; Complete proteome;
Developmental protein; Ethylene signaling pathway;
Host-virus interaction; Nucleus; Reference proteome;
Ubl conjugation pathway.
CHAIN 1 171 SKP1-like protein 1B.
/FTId=PRO_0000187256.
REGION 113 171 Interaction with the F-box domain of F-
box proteins.
{ECO:0000250|UniProtKB:Q39255}.
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


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