ASK20_ARATH
ID ASK20_ARATH Reviewed; 352 AA.
AC A8MQG7; B3H4L0; O80824; Q94K04;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=SKP1-like protein 20;
DE Short=AtSK20;
GN Name=ASK20; OrderedLocusNames=At2g45950; ORFNames=F4I18.7;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] (ISOFORM 3).
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 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A8MQG7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8MQG7-2; Sequence=VSP_037366, VSP_037367;
CC Name=3;
CC IsoId=A8MQG7-3; Sequence=VSP_037364, VSP_037365;
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings, roots, leaves, floral
CC stems, inflorescences, and siliques. {ECO:0000269|PubMed:12970487}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR EMBL; AC004665; AAC28530.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10620.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10621.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63251.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63252.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63253.1; -; Genomic_DNA.
DR EMBL; AF370493; AAK43870.1; -; mRNA.
DR EMBL; AY081697; AAM10259.1; -; mRNA.
DR PIR; T02452; T02452.
DR RefSeq; NP_001078065.1; NM_001084596.2. [A8MQG7-1]
DR RefSeq; NP_001325353.1; NM_001337164.1. [A8MQG7-2]
DR RefSeq; NP_001325354.1; NM_001337165.1. [A8MQG7-1]
DR RefSeq; NP_001325355.1; NM_001337163.1. [A8MQG7-2]
DR RefSeq; NP_566058.2; NM_130158.4. [A8MQG7-2]
DR AlphaFoldDB; A8MQG7; -.
DR SMR; A8MQG7; -.
DR BioGRID; 4539; 14.
DR ComplexPortal; CPX-1447; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK20.
DR ComplexPortal; CPX-1468; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK20.
DR ComplexPortal; CPX-1490; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK20.
DR ComplexPortal; CPX-1513; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK20.
DR ComplexPortal; CPX-1533; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK20.
DR ComplexPortal; CPX-1554; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK20.
DR ComplexPortal; CPX-1576; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK20.
DR ComplexPortal; CPX-1597; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK20.
DR IntAct; A8MQG7; 7.
DR STRING; 3702.AT2G45950.2; -.
DR PaxDb; A8MQG7; -.
DR PRIDE; A8MQG7; -.
DR ProteomicsDB; 246858; -. [A8MQG7-1]
DR EnsemblPlants; AT2G45950.1; AT2G45950.1; AT2G45950. [A8MQG7-2]
DR EnsemblPlants; AT2G45950.2; AT2G45950.2; AT2G45950. [A8MQG7-1]
DR EnsemblPlants; AT2G45950.3; AT2G45950.3; AT2G45950. [A8MQG7-2]
DR EnsemblPlants; AT2G45950.4; AT2G45950.4; AT2G45950. [A8MQG7-2]
DR EnsemblPlants; AT2G45950.5; AT2G45950.5; AT2G45950. [A8MQG7-1]
DR GeneID; 819203; -.
DR Gramene; AT2G45950.1; AT2G45950.1; AT2G45950. [A8MQG7-2]
DR Gramene; AT2G45950.2; AT2G45950.2; AT2G45950. [A8MQG7-1]
DR Gramene; AT2G45950.3; AT2G45950.3; AT2G45950. [A8MQG7-2]
DR Gramene; AT2G45950.4; AT2G45950.4; AT2G45950. [A8MQG7-2]
DR Gramene; AT2G45950.5; AT2G45950.5; AT2G45950. [A8MQG7-1]
DR KEGG; ath:AT2G45950; -.
DR Araport; AT2G45950; -.
DR TAIR; locus:2050709; AT2G45950.
DR eggNOG; KOG1724; Eukaryota.
DR InParanoid; A8MQG7; -.
DR OMA; LICHEIH; -.
DR OrthoDB; 987444at2759; -.
DR PhylomeDB; A8MQG7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:A8MQG7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; A8MQG7; baseline and differential.
DR Genevisible; A8MQG7; 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 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; IPR016072; Skp1_comp_dimer.
DR PANTHER; PTHR11165; PTHR11165; 1.
DR Pfam; PF01466; Skp1; 1.
DR SMART; SM00512; Skp1; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF81382; SSF81382; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..352
FT /note="SKP1-like protein 20"
FT /id="PRO_0000375261"
FT REGION 108..167
FT /note="Interaction with the F-box domain of F-box proteins"
FT /evidence="ECO:0000250"
FT REGION 214..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..231
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 212..260
FT /note="DHKAVKMSKGKKKKKKKKDQKIVSSNNIHDKESHDLRSKQQCVEEIGSS ->
FT GLFGSKENSVSQITRL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_037364"
FT VAR_SEQ 261..352
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_037365"
FT VAR_SEQ 340..342
FT /note="MVS -> QSP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037366"
FT VAR_SEQ 343..352
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037367"
SQ SEQUENCE 352 AA; 40734 MW; 4C4AA4AE60386258 CRC64;
MSEGDLAVMK PETMKSYIWL QTADGSIQQV EQEVAMFCPM ICQEVIQKGV GSSKNHAISL
PQRVNPAMFS LILDYCRFHQ LPGRSNKERK TYDERFIRMD TKRLCELTSA ADSLQLKPLV
DLTSRALARI IEGKNPEEIR EIFHLPDDLT EEEKLEPLKN SMDDPRIRLL NRLYAKKRKE
LKERERLKNV EVEEHVDERS VDDLLSFING RDHKAVKMSK GKKKKKKKKD QKIVSSNNIH
DKESHDLRSK QQCVEEIGSS MREVPNLLSA EDDISTPNAG SEDEDIDDEI DPAMRELLDR
EVEDFAQRLN SNWVRSLGKE RRPVHFSING NGTTRRHTGM VSIWRPCMFT LF
