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TLP10_ARATH
ID   TLP10_ARATH             Reviewed;         445 AA.
AC   Q9FRH7; B9DGL6; Q84JM8; Q84UG2; Q84UG3; Q8H0W5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 139.
DE   RecName: Full=Tubby-like F-box protein 10;
DE            Short=AtTLP10;
DE   AltName: Full=SKP1-interacting partner 26;
GN   Name=TULP10; Synonyms=SKIP26; OrderedLocusNames=At1g25280;
GN   ORFNames=F4F7.13;
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 [MRNA], TISSUE SPECIFICITY, GENE FAMILY, AND
RP   NOMENCLATURE.
RX   PubMed=15064372; DOI=10.1104/pp.103.037820;
RA   Lai C.-P., Lee C.-L., Chen P.-H., Wu S.-H., Yang C.-C., Shaw J.-F.;
RT   "Molecular analyses of the Arabidopsis TUBBY-like protein gene family.";
RL   Plant Physiol. 134:1586-1597(2004).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-432, AND VARIANTS ILE-114 AND
RP   PHE-244.
RC   STRAIN=cv. Bla-1, cv. Bretagny, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1,
RC   cv. Hau-0, cv. Jl-1, cv. Kas-1, cv. Kent, and cv. Lisse;
RX   PubMed=12618409; DOI=10.1093/genetics/163.2.723;
RA   Barrier M., Bustamante C.D., Yu J., Purugganan M.D.;
RT   "Selection on rapidly evolving proteins in the Arabidopsis genome.";
RL   Genetics 163:723-733(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-445.
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 179-445.
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   [7]
RP   INTERACTION WITH SKP1A/ASK1.
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. {ECO:0000250,
CC       ECO:0000269|PubMed:12795696}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9FRH7-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15064372}.
CC   -!- DOMAIN: The F-box is necessary for the interaction with ASK proteins.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TUB family. {ECO:0000305}.
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DR   EMBL; AF487271; AAQ06244.1; -; mRNA.
DR   EMBL; AC079374; AAG28805.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30599.1; -; Genomic_DNA.
DR   EMBL; AY140459; AAN46223.1; -; Genomic_DNA.
DR   EMBL; AY140460; AAN46224.1; -; Genomic_DNA.
DR   EMBL; AY140461; AAN46225.1; -; Genomic_DNA.
DR   EMBL; AY140462; AAN46226.1; -; Genomic_DNA.
DR   EMBL; AY140463; AAN46227.1; -; Genomic_DNA.
DR   EMBL; AY140464; AAN46228.1; -; Genomic_DNA.
DR   EMBL; AY140465; AAN46229.1; -; Genomic_DNA.
DR   EMBL; AY140466; AAN46230.1; -; Genomic_DNA.
DR   EMBL; AY140467; AAN46231.1; -; Genomic_DNA.
DR   EMBL; AY140468; AAN46232.1; -; Genomic_DNA.
DR   EMBL; AY140469; AAN46233.1; -; Genomic_DNA.
DR   EMBL; AK317199; BAH19883.1; -; mRNA.
DR   EMBL; BT001997; AAN72008.1; -; mRNA.
DR   EMBL; BT006290; AAP13398.1; -; mRNA.
DR   PIR; E86382; E86382.
DR   RefSeq; NP_001117353.1; NM_001123881.1.
DR   RefSeq; NP_173899.1; NM_102338.3. [Q9FRH7-1]
DR   RefSeq; NP_973909.1; NM_202180.1.
DR   AlphaFoldDB; Q9FRH7; -.
DR   SMR; Q9FRH7; -.
DR   BioGRID; 24349; 5.
DR   IntAct; Q9FRH7; 3.
DR   STRING; 3702.AT1G25280.1; -.
DR   iPTMnet; Q9FRH7; -.
DR   PaxDb; Q9FRH7; -.
DR   PRIDE; Q9FRH7; -.
DR   ProteomicsDB; 246410; -. [Q9FRH7-1]
DR   EnsemblPlants; AT1G25280.1; AT1G25280.1; AT1G25280. [Q9FRH7-1]
DR   GeneID; 839112; -.
DR   Gramene; AT1G25280.1; AT1G25280.1; AT1G25280. [Q9FRH7-1]
DR   KEGG; ath:AT1G25280; -.
DR   Araport; AT1G25280; -.
DR   TAIR; locus:2032950; AT1G25280.
DR   eggNOG; KOG2502; Eukaryota.
DR   HOGENOM; CLU_028236_3_0_1; -.
DR   InParanoid; Q9FRH7; -.
DR   OMA; QPPYTFA; -.
DR   PhylomeDB; Q9FRH7; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9FRH7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FRH7; baseline and differential.
DR   Genevisible; Q9FRH7; AT.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0009536; C:plastid; IDA:TAIR.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR   GO; GO:0009620; P:response to fungus; IMP:TAIR.
DR   Gene3D; 3.20.90.10; -; 1.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR025659; Tubby-like_C.
DR   InterPro; IPR000007; Tubby_C.
DR   InterPro; IPR018066; Tubby_C_CS.
DR   Pfam; PF00646; F-box; 1.
DR   Pfam; PF01167; Tub; 1.
DR   PRINTS; PR01573; SUPERTUBBY.
DR   SUPFAM; SSF54518; SSF54518; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   PROSITE; PS01200; TUB_1; 1.
DR   PROSITE; PS01201; TUB_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..445
FT                   /note="Tubby-like F-box protein 10"
FT                   /id="PRO_0000272238"
FT   DOMAIN          57..112
FT                   /note="F-box"
FT   REGION          382..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         114
FT                   /note="L -> I (in strain: cv. Lisse)"
FT                   /evidence="ECO:0000269|PubMed:12618409"
FT   VARIANT         244
FT                   /note="Y -> F (in strain: cv. Bretagny)"
FT                   /evidence="ECO:0000269|PubMed:12618409"
FT   CONFLICT        404
FT                   /note="K -> E (in Ref. 5; BAH19883)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   445 AA;  50010 MW;  C77BEA9ED18B9D21 CRC64;
     MSFRGIVQDL RDGFGSLSRR SFDFRLSSLH KGKAQGSSFR EYSSSRDLLS PVIVQTSRWA
     NLPPELLFDV IKRLEESESN WPARKHVVAC ASVCRSWRAM CQEIVLGPEI CGKLTFPVSL
     KQPGPRDAMI QCFIKRDKSK LTFHLFLCLS PALLVENGKF LLSAKRTRRT TRTEYIISMD
     ADNISRSSNS YLGKLRSNFL GTKFLVYDTQ PPPNTSSSAL ITDRTSRSRF HSRRVSPKVP
     SGSYNIAQIT YELNVLGTRG PRRMHCIMNS IPISSLEPGG SVPNQPEKLV PAPYSLDDSF
     RSNISFSKSS FDHRSLDFSS SRFSEMGISC DDNEEEASFR PLILKNKQPR WHEQLQCWCL
     NFRGRVTVAS VKNFQLVAAR QPQPQGTGAA AAPTSAPAHP EQDKVILQFG KVGKDMFTMD
     YRYPLSAFQA FAICLSSFDT KLACE
 
 
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