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ASK7_ARATH
ID   ASK7_ARATH              Reviewed;         125 AA.
AC   Q9LSY0;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=SKP1-like protein 7;
DE            Short=AtSK7;
GN   Name=ASK7; OrderedLocusNames=At3g21840; ORFNames=MSD21.21;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
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].
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [4]
RP   GENE FAMILY, NOMENCLATURE, 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).
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 (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Restricted to siliques.
CC       {ECO:0000269|PubMed:12970487}.
CC   -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR   EMBL; AB025634; BAB02846.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76557.1; -; Genomic_DNA.
DR   EMBL; BX841469; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_566693.1; NM_113079.2.
DR   AlphaFoldDB; Q9LSY0; -.
DR   SMR; Q9LSY0; -.
DR   BioGRID; 7070; 12.
DR   ComplexPortal; CPX-1434; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK7.
DR   ComplexPortal; CPX-1455; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK7.
DR   ComplexPortal; CPX-1477; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK7.
DR   ComplexPortal; CPX-1498; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK7.
DR   ComplexPortal; CPX-1520; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK7.
DR   ComplexPortal; CPX-1541; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK7.
DR   ComplexPortal; CPX-1563; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK7.
DR   ComplexPortal; CPX-1584; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK7.
DR   IntAct; Q9LSY0; 1.
DR   STRING; 3702.AT3G21840.1; -.
DR   PaxDb; Q9LSY0; -.
DR   PRIDE; Q9LSY0; -.
DR   ProteomicsDB; 246511; -.
DR   EnsemblPlants; AT3G21840.1; AT3G21840.1; AT3G21840.
DR   GeneID; 821738; -.
DR   Gramene; AT3G21840.1; AT3G21840.1; AT3G21840.
DR   KEGG; ath:AT3G21840; -.
DR   Araport; AT3G21840; -.
DR   TAIR; locus:2093074; AT3G21840.
DR   eggNOG; KOG1724; Eukaryota.
DR   HOGENOM; CLU_059252_5_0_1; -.
DR   OMA; CKENEWA; -.
DR   OrthoDB; 1412723at2759; -.
DR   PhylomeDB; Q9LSY0; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9LSY0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LSY0; baseline and differential.
DR   Genevisible; Q9LSY0; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS: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:0009867; P:jasmonic acid mediated signaling pathway; IMP:ComplexPortal.
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   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:TAIR.
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; IPR016073; Skp1_comp_POZ.
DR   PANTHER; PTHR11165; PTHR11165; 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   2: Evidence at transcript level;
KW   Nucleus; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..125
FT                   /note="SKP1-like protein 7"
FT                   /id="PRO_0000375248"
FT   REGION          94..125
FT                   /note="Interaction with the F-box domain of F-box proteins"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        51
FT                   /note="I -> N (in Ref. 3; BX841469)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="D -> E (in Ref. 3; BX841469)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="W -> R (in Ref. 3; BX841469)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   125 AA;  14454 MW;  92FBD538A99CB3A8 CRC64;
     MSTKKIMLKS SDGKMFEIEE ETARQCQTIA HMIEAECTDN VIPVSNVTSE ILEMVIEYCN
     KHHVDAANPC SDEDLKKWDK EFMEKDQYTI FHLMNAAYDL HIKSLLALAY QTVADMVNDN
     KWAFE
 
 
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