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SKI31_ARATH
ID   SKI31_ARATH             Reviewed;         316 AA.
AC   Q9FHK0; Q84TE4;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=F-box protein SKIP31;
DE   AltName: Full=SKP1-interacting partner 31;
GN   Name=SKIP31; OrderedLocusNames=At5g45360; ORFNames=MFC19.2;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INTERACTION WITH SKP1A/ASK1 AND SPK1B/ASK2.
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).
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 and SPK1B/ASK2. {ECO:0000250,
CC       ECO:0000269|PubMed:12795696}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9FHK0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FHK0-2; Sequence=VSP_024323;
CC   -!- DOMAIN: The F-box is necessary for the interaction with ASK proteins.
CC       {ECO:0000250}.
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DR   EMBL; AB018113; BAB09164.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95238.1; -; Genomic_DNA.
DR   EMBL; BT002873; AAO22690.1; -; mRNA.
DR   EMBL; BT004395; AAO42389.1; -; mRNA.
DR   EMBL; BT005876; AAO64811.1; -; mRNA.
DR   EMBL; AK227481; BAE99482.1; -; mRNA.
DR   EMBL; AY087595; AAM65137.1; -; mRNA.
DR   RefSeq; NP_568643.1; NM_123904.4. [Q9FHK0-1]
DR   AlphaFoldDB; Q9FHK0; -.
DR   BioGRID; 19821; 14.
DR   IntAct; Q9FHK0; 2.
DR   STRING; 3702.AT5G45360.1; -.
DR   PaxDb; Q9FHK0; -.
DR   PRIDE; Q9FHK0; -.
DR   ProteomicsDB; 232507; -. [Q9FHK0-1]
DR   EnsemblPlants; AT5G45360.1; AT5G45360.1; AT5G45360. [Q9FHK0-1]
DR   GeneID; 834572; -.
DR   Gramene; AT5G45360.1; AT5G45360.1; AT5G45360. [Q9FHK0-1]
DR   KEGG; ath:AT5G45360; -.
DR   Araport; AT5G45360; -.
DR   TAIR; locus:2163503; AT5G45360.
DR   eggNOG; ENOG502QT73; Eukaryota.
DR   HOGENOM; CLU_054288_0_0_1; -.
DR   InParanoid; Q9FHK0; -.
DR   OMA; YNCADEE; -.
DR   PhylomeDB; Q9FHK0; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9FHK0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FHK0; baseline and differential.
DR   Genevisible; Q9FHK0; AT.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
DR   GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   Pfam; PF12937; F-box-like; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..316
FT                   /note="F-box protein SKIP31"
FT                   /id="PRO_0000283550"
FT   DOMAIN          68..114
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REGION          15..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         225..316
FT                   /note="FICKETGNVHVCDDNCKEVILSPEGDLMVCTISGVCSDTLLVQTEPDADGCY
FT                   EEEAELEAEVFTDKSRLARAFELGYNCDDEQELERTLRFC -> SLSLLLNVCGKKVPS
FT                   GFVCA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.4"
FT                   /id="VSP_024323"
SQ   SEQUENCE   316 AA;  36238 MW;  EDE10BCF073E8CF8 CRC64;
     MSVSDEEDEC FARFLESEVS SVEDKEETKE PEAKRQRIEK GETKALEKDE DQKENGNKDK
     TDAKRIESGV FTNVPTELFR HILKFLSSED LVSCSLVCKF LNFAAADESL WRRLYCIRWG
     LTLPSRKLRE SAWKKLYIDR DEQDMIELVR TCPSDFKEYY VHMQAAKRSQ APLPSQMVDD
     RIILDNTVLE QVSLWKKSKG LTDKAVTGHI CLGTKCSYHQ IDDVFICKET GNVHVCDDNC
     KEVILSPEGD LMVCTISGVC SDTLLVQTEP DADGCYEEEA ELEAEVFTDK SRLARAFELG
     YNCDDEQELE RTLRFC
 
 
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