ID   ASK11_ARATH             Reviewed;         152 AA.
AC   O49484; A0MFB7;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=SKP1-like protein 11;
DE            Short=AtSK11;
GN   Name=ASK11; OrderedLocusNames=At4g34210; ORFNames=F10M10.2;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [3]
RP   INTERACTION WITH UFO; PP2A13; AT1G67340; AT4G38940; SKIP15; AT3G16740;
RP   AT3G04660; AT1G78100; AT1G55000; SKIP16; SKIP2; SKIP32 AND EBF1.
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   [4]
RP   FUNCTION, GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=22851094; 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).
RN   [5]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH EBF1/FBL6; COI1/FBL2;
RP   ADO3/FKF1; PP2B10; AT3G61590 AND AT5G49610.
RX   PubMed=14749489; DOI=10.1093/pcp/pch009;
RA   Takahashi N., Kuroda H., Kuromori T., Hirayama T., Seki M.,
RA   Shinozaki K., Shimada H., Matsui M.;
RT   "Expression and interaction analysis of Arabidopsis Skp1-related
RT   genes.";
RL   Plant Cell Physiol. 45:83-91(2004).
CC   -!- FUNCTION: Involved in ubiquitination and subsequent proteasomal
CC       degradation of target proteins. Together with CUL1, RBX1 and a F-
CC       box protein, it forms a SCF E3 ubiquitin ligase complex. The
CC       functional specificity of this complex depends of the type of F-
CC       box protein. In the SCF complex, it serves as an adapter that
CC       links the F-box protein to CUL1 (By similarity). Plays a role
CC       during early flowers reproductive development.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex
CC       (By similarity). Interacts with ADO3/FKF1, COI1/FBL2, EBF1/FBL6,
CC       PP2A13, PP2B10, UFO, SKIP2, SKIP15, SKIP16, SKIP32, At1g55000,
CC       At1g67340, At1g78100, At3g04660, At3g16740, At3g61590, At4g38940
CC       and At5g49610.
CC   -!- INTERACTION:
CC       Q94BT6:ADO1; NbExp=2; IntAct=EBI-401185, EBI-300691;
CC       Q9C9W9:ADO3; NbExp=2; IntAct=EBI-401185, EBI-401228;
CC       Q9SKK0:EBF1; NbExp=2; IntAct=EBI-401185, EBI-401198;
CC       O49279:FBX3; NbExp=2; IntAct=EBI-401185, EBI-591174;
CC       Q9LEX0:PP2A13; NbExp=2; IntAct=EBI-401185, EBI-604261;
CC       Q39090:UFO; NbExp=2; IntAct=EBI-401185, EBI-590758;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in young seedlings, cotyledons,
CC       roots, leaves, floral stems, inflorescences, pollen, and siliques,
CC       with a slightly higher level in inflorescence than in other
CC       tissues.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the inflorescence meristem (IM)
CC       and young buds, particularly in stamen. Also detected in pollen
CC       grains.
CC   -!- SIMILARITY: Belongs to the SKP1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK28664.1; Type=Erroneous termination; Positions=153; Note=Translated as stop;
CC   -!- WEB RESOURCE: Name=PlantsUBQ; Note=A functional genomics database
CC       for the ubiquitin/26S proteasome proteolytic pathway in plants;
CC       URL="http://plantsubq.genomics.purdue.edu/";
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DR   EMBL; AL021961; CAA17551.1; -; Genomic_DNA.
DR   EMBL; AL161585; CAB80138.1; -; Genomic_DNA.
DR   EMBL; DQ446893; ABE66110.1; -; mRNA.
DR   EMBL; DQ653243; ABK28664.1; -; mRNA.
DR   IPI; IPI00541308; -.
DR   PIR; T05415; T05415.
DR   RefSeq; NP_567959.1; -.
DR   UniGene; At.54598; -.
DR   HSSP; P34991; 1FQV.
DR   SMR; O49484; 6-152.
DR   IntAct; O49484; 34.
DR   GeneID; 829569; -.
DR   KEGG; ath:AT4G34210; -.
DR   NMPDR; fig|3702.1.peg.21481; -.
DR   TAIR; At4g34210; -.
DR   OMA; O49484; IRRAFNI.
DR   ArrayExpress; O49484; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR016897; E3_ubiquit_lig_SCF_Skp.
DR   InterPro; IPR001232; Skp1_comp.
DR   InterPro; IPR016072; Skp1_comp_dimer.
DR   InterPro; IPR016073; Skp1_comp_POZ.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   PANTHER; PTHR11165; Skp1; 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.
PE   1: Evidence at protein level;
KW   Complete proteome; Nucleus; Ubl conjugation pathway.
FT   CHAIN         1    152       SKP1-like protein 11.
FT                                /FTId=PRO_0000375252.
FT   REGION       94    152       Interaction with the F-box domain of F-
FT                                box proteins (By similarity).
SQ   SEQUENCE   152 AA;  17288 MW;  95D23CC17C1523B0 CRC64;
     MSSKMIVLMS SDGQSFEVEE AVAIQSQTIA HMVEDDCVAD GIPLANVESK ILVKVIEYCK
     KHHVDEANPI SEEDLNNWDE KFMDLEQSTI FELILAANYL NIKSLLDLTC QTVADMIKGK
     TPEEIRSTFN IENDFTPEEE EAVRKENQWA FE
//