SKIP2_ARATH
ID SKIP2_ARATH Reviewed; 527 AA.
AC Q9FE83; Q0WWL1; Q940A1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=F-box protein SKIP2;
DE AltName: Full=SKP1-interacting partner 2;
GN Name=SKIP2; OrderedLocusNames=At5g67250; ORFNames=K21H1.21;
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 SKP1A/ASK1.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 INTERACTION WITH SKP1A/ASK1; SKP1B/ASK2 AND ASK11.
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).
CC -!- FUNCTION: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase
CC complexes, which may mediate the ubiquitination and subsequent
CC proteasomal degradation of target proteins. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (ASK-cullin-F-box) protein ligase complex (By
CC similarity). Interacts with SKP1A/ASK1, SKP1B/ASK2 and ASK11.
CC {ECO:0000250, ECO:0000269|PubMed:11387208,
CC ECO:0000269|PubMed:12169662}.
CC -!- INTERACTION:
CC Q9FE83; Q39255: SKP1A; NbExp=3; IntAct=EBI-591107, EBI-532357;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The F-box is necessary for the interaction with ASK proteins.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL07231.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF263378; AAG21977.1; -; mRNA.
DR EMBL; AB020742; BAB10959.1; -; Genomic_DNA.
DR EMBL; AB025614; BAB10959.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED98320.1; -; Genomic_DNA.
DR EMBL; AY056152; AAL07231.1; ALT_FRAME; mRNA.
DR EMBL; BT002473; AAO00833.1; -; mRNA.
DR EMBL; BT008886; AAP68325.1; -; mRNA.
DR EMBL; AK226338; BAE98487.1; -; mRNA.
DR RefSeq; NP_569047.1; NM_126125.3.
DR AlphaFoldDB; Q9FE83; -.
DR SMR; Q9FE83; -.
DR BioGRID; 22102; 5.
DR IntAct; Q9FE83; 3.
DR STRING; 3702.AT5G67250.1; -.
DR PaxDb; Q9FE83; -.
DR PRIDE; Q9FE83; -.
DR ProteomicsDB; 234586; -.
DR EnsemblPlants; AT5G67250.1; AT5G67250.1; AT5G67250.
DR GeneID; 836860; -.
DR Gramene; AT5G67250.1; AT5G67250.1; AT5G67250.
DR KEGG; ath:AT5G67250; -.
DR Araport; AT5G67250; -.
DR TAIR; locus:2155578; AT5G67250.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_016072_4_0_1; -.
DR InParanoid; Q9FE83; -.
DR OMA; LWEIAWH; -.
DR OrthoDB; 1046098at2759; -.
DR PhylomeDB; Q9FE83; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FE83; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FE83; baseline and differential.
DR Genevisible; Q9FE83; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:TAIR.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF13516; LRR_6; 2.
DR SMART; SM00367; LRR_CC; 7.
DR SUPFAM; SSF81383; SSF81383; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..527
FT /note="F-box protein SKIP2"
FT /id="PRO_0000272224"
FT DOMAIN 39..85
FT /note="F-box"
FT CONFLICT 467
FT /note="V -> I (in Ref. 6; BAE98487)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 57393 MW; 736E4AA792ADE1FA CRC64;
MGQAPSSTAE SNGRELDLRL WSPVIVAGGE SMAVGNVVDR DFTGDLPDEC LAHVFQFLGA
GDRKRCSLVC KRWLLVDGQS RHRLSLDAKD EISSFLTSMF NRFDSVTKLA LRCDRKSVSL
SDEALAMISV RCLNLTRVKL RGCREITDLG MEDFAKNCKN LKKLSVGSCN FGAKGVNAML
EHCKLLEELS VKRLRGIHEA AELIHLPDDA SSSSLRSICL KELVNGQVFE PLLATTRTLK
TLKIIRCLGD WDKVLQMIAN GKSSLSEIHL ERLQVSDIGL SAISKCSNVE TLHIVKTPEC
SNFGLIYVAE RCKLLRKLHI DGWRTNRIGD EGLLSVAKHC LNLQELVLIG VNATHMSLAA
IASNCEKLER LALCGSGTIG DTEIACIARK CGALRKFCIK GCPVSDRGIE ALAVGCPNLV
KLKVKKCKVV TGEIGDWLRE QRRTLVVSMD GDETEAVVVV DGEVETVVEE PRVAQAGGIV
AEIGSSNGGG GSRLAMIRSK LGFLAGRNLV TCTFRRWSHN DNASSST
