ASK4_ARATH
ID ASK4_ARATH Reviewed; 163 AA.
AC Q9LNT9;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=SKP1-like protein 4;
DE Short=AtSK4;
GN Name=ASK4; OrderedLocusNames=At1g20140; ORFNames=T20H2.8;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=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 INTERACTION WITH AT1G56610; AT1G67340; AT3G62230; AT3G59000; AT4G27050;
RP AT1G55000; SKIP16 AND SKIP32.
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).
RN [5]
RP GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 (By
CC similarity). Interacts with At1g56610, At1g67340, At3g62230, At3g59000,
CC At4g27050, At1g55000, SKIP16 and SKIP32. {ECO:0000250,
CC ECO:0000269|PubMed:12169662}.
CC -!- INTERACTION:
CC Q9LNT9; Q8LEA8: EID1; NbExp=4; IntAct=EBI-604085, EBI-687388;
CC Q9LNT9; Q84JU4: IBR5; NbExp=3; IntAct=EBI-604085, EBI-604555;
CC Q9LNT9; Q9SZU7: KAI2; NbExp=3; IntAct=EBI-604085, EBI-25519488;
CC Q9LNT9; Q9SIM9: MAX2; NbExp=3; IntAct=EBI-604085, EBI-25529872;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in inflorescence and siliques,
CC and, to a lower extent, in seedlings, roots, and stems.
CC {ECO:0000269|PubMed:12970487}.
CC -!- DEVELOPMENTAL STAGE: Detected throughout the inflorescence at a higher
CC level in the inflorescence meristem (IM) than in the young flower. Very
CC strongly expressed in the valve, septum, and developing seed. Also
CC present in pollen grains. {ECO:0000269|PubMed:12970487}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR EMBL; AC022472; AAF79899.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29943.1; -; Genomic_DNA.
DR EMBL; AY058205; AAL25617.1; -; mRNA.
DR EMBL; AY098980; AAM19990.1; -; mRNA.
DR PIR; B86335; B86335.
DR RefSeq; NP_564105.1; NM_101868.5.
DR AlphaFoldDB; Q9LNT9; -.
DR SMR; Q9LNT9; -.
DR BioGRID; 23843; 68.
DR ComplexPortal; CPX-1431; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK4.
DR ComplexPortal; CPX-1452; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK4.
DR ComplexPortal; CPX-1474; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK4.
DR ComplexPortal; CPX-1495; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK4.
DR ComplexPortal; CPX-1517; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK4.
DR ComplexPortal; CPX-1538; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK4.
DR ComplexPortal; CPX-1560; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK4.
DR ComplexPortal; CPX-1581; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK4.
DR DIP; DIP-34007N; -.
DR IntAct; Q9LNT9; 32.
DR STRING; 3702.AT1G20140.1; -.
DR PaxDb; Q9LNT9; -.
DR PRIDE; Q9LNT9; -.
DR ProteomicsDB; 246795; -.
DR EnsemblPlants; AT1G20140.1; AT1G20140.1; AT1G20140.
DR GeneID; 838604; -.
DR Gramene; AT1G20140.1; AT1G20140.1; AT1G20140.
DR KEGG; ath:AT1G20140; -.
DR Araport; AT1G20140; -.
DR TAIR; locus:2198621; AT1G20140.
DR eggNOG; KOG1724; Eukaryota.
DR HOGENOM; CLU_059252_6_1_1; -.
DR OMA; ENCGMAN; -.
DR OrthoDB; 1412723at2759; -.
DR PhylomeDB; Q9LNT9; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LNT9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNT9; baseline and differential.
DR Genevisible; Q9LNT9; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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; IPR016072; Skp1_comp_dimer.
DR InterPro; IPR016073; Skp1_comp_POZ.
DR PANTHER; PTHR11165; PTHR11165; 1.
DR Pfam; PF01466; Skp1; 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 1: Evidence at protein level;
KW Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..163
FT /note="SKP1-like protein 4"
FT /id="PRO_0000375245"
FT REGION 105..163
FT /note="Interaction with the F-box domain of F-box proteins"
FT /evidence="ECO:0000250"
SQ SEQUENCE 163 AA; 18187 MW; 9B0AD6B569A5F932 CRC64;
MAETKKMIIL KSSDGESFEI EEAVAVKSQT IKHMIEDDCA DNGIPLPNVT GAILAKVIEY
CKKHVEAAAE AGGDKDFYGS AENDELKNWD SEFVKVDQPT LFDLILAANY LNIGGLLDLT
CKAVADQMRG KTPEQMRAHF NIKNDYTPEE EAEVRNENKW AFE
