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UBA1A_ARATH
ID   UBA1A_ARATH             Reviewed;         343 AA.
AC   Q9SHZ6; Q680T3; Q8L990; Q8RYD4; Q8VZW7;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=UBP1-associated proteins 1A;
DE   AltName: Full=UBP1-interacting protein 1a;
GN   Name=UBA1A; OrderedLocusNames=At2g22090; ORFNames=T16B14.6;
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], FUNCTION, INTERACTION WITH UBA1A; UBA2A; UBP1A;
RP   UBP1B AND UBP1C, AND SUBCELLULAR LOCATION.
RX   PubMed=12024044; DOI=10.1128/mcb.22.12.4346-4357.2002;
RA   Lambermon M.H., Fu Y., Wieczorek Kirk D.A., Dupasquier M., Filipowicz W.,
RA   Lorkovic Z.J.;
RT   "UBA1 and UBA2, two proteins that interact with UBP1, a multifunctional
RT   effector of pre-mRNA maturation in plants.";
RL   Mol. Cell. Biol. 22:4346-4357(2002).
RN   [2]
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   [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 [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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as component of a complex regulating the turnover of
CC       mRNAs in the nucleus. Binds with high affinity to RNA molecules that
CC       contain U-rich sequences in 3'-UTRs. May function in complex with UBP1
CC       and contribute to the stabilization of mRNAs in the nucleus. However,
CC       unlike UBP1, UBA1A does not stimulate pre-mRNA splicing.
CC       {ECO:0000269|PubMed:12024044}.
CC   -!- SUBUNIT: Interacts with UBA1A, UBA2A, UBP1A, UBP1B and UBP1C.
CC       {ECO:0000269|PubMed:12024044}.
CC   -!- INTERACTION:
CC       Q9SHZ6; Q8L9Y3: ARR14; NbExp=5; IntAct=EBI-346271, EBI-1100737;
CC       Q9SHZ6; Q9LP80: At1g48450; NbExp=3; IntAct=EBI-346271, EBI-4442510;
CC       Q9SHZ6; Q9ZVI3: At2g38610; NbExp=3; IntAct=EBI-346271, EBI-4440478;
CC       Q9SHZ6; Q9FG30: At5g06770; NbExp=3; IntAct=EBI-346271, EBI-4440997;
CC       Q9SHZ6; Q8GZ26: BRN2; NbExp=3; IntAct=EBI-346271, EBI-4425532;
CC       Q9SHZ6; Q0WW84: RBP47B; NbExp=3; IntAct=EBI-346271, EBI-25522105;
CC       Q9SHZ6; O64647: TCP9; NbExp=3; IntAct=EBI-346271, EBI-9838721;
CC       Q9SHZ6; Q9SHZ6: UBA1A; NbExp=8; IntAct=EBI-346271, EBI-346271;
CC       Q9SHZ6; Q9LES2: UBA2A; NbExp=3; IntAct=EBI-346271, EBI-346288;
CC       Q9SHZ6; Q9SYG4: UBP1A; NbExp=4; IntAct=EBI-346271, EBI-346310;
CC       Q9SHZ6; Q9LQI9: UBP1B; NbExp=2; IntAct=EBI-346271, EBI-346277;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12024044}.
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=Q9SHZ6-1; Sequence=Displayed;
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DR   EMBL; AJ439403; CAD28134.1; -; mRNA.
DR   EMBL; AC007232; AAD25815.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07262.1; -; Genomic_DNA.
DR   EMBL; AY063782; AAL36089.1; -; mRNA.
DR   EMBL; AY117273; AAM51348.1; -; mRNA.
DR   EMBL; AK175749; BAD43512.1; -; mRNA.
DR   EMBL; AK175784; BAD43547.1; -; mRNA.
DR   EMBL; AK176364; BAD44127.1; -; mRNA.
DR   EMBL; AY088576; AAM66107.1; -; mRNA.
DR   PIR; H84608; H84608.
DR   RefSeq; NP_565525.1; NM_127778.5. [Q9SHZ6-1]
DR   AlphaFoldDB; Q9SHZ6; -.
DR   SMR; Q9SHZ6; -.
DR   BioGRID; 2097; 12.
DR   IntAct; Q9SHZ6; 11.
DR   STRING; 3702.AT2G22090.2; -.
DR   iPTMnet; Q9SHZ6; -.
DR   PaxDb; Q9SHZ6; -.
DR   ProteomicsDB; 228592; -. [Q9SHZ6-1]
DR   EnsemblPlants; AT2G22090.1; AT2G22090.1; AT2G22090. [Q9SHZ6-1]
DR   GeneID; 816744; -.
DR   Gramene; AT2G22090.1; AT2G22090.1; AT2G22090. [Q9SHZ6-1]
DR   KEGG; ath:AT2G22090; -.
DR   Araport; AT2G22090; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_012062_1_6_1; -.
DR   OMA; GNQYHPV; -.
DR   PRO; PR:Q9SHZ6; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SHZ6; baseline and differential.
DR   Genevisible; Q9SHZ6; AT.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..343
FT                   /note="UBP1-associated proteins 1A"
FT                   /id="PRO_0000425437"
FT   DOMAIN          104..181
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        7
FT                   /note="K -> KS (in Ref. 1; CAD28134)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        136
FT                   /note="V -> L (in Ref. 1; CAD28134)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209
FT                   /note="P -> S (in Ref. 6; AAM66107)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        304
FT                   /note="Y -> C (in Ref. 5; BAD43512/BAD43547)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   343 AA;  36150 MW;  C93E1BDFF1CFC690 CRC64;
     MAKTLDKSKK RKLVKSKSTN FDKKQKINKQ QQQPESSTPY SSSSSSSDSS DSESDNEFDP
     EELRELLQPY SKDQLVDLVC SASRIGSSIY SAVVEAADRD VTHRKIFVYG LPWETTRETL
     VGVFEGYGEI EECTVVIDKA TGKAKGFGFV MFKTRKGAKE ALKEPKKRIL NRTATCQLAS
     MGPAASGKGH DQPGPVKISM GSMANHGQPQ QQQVQGQHVF NGGGMAASPF MLGNQYHPLY
     GAGMLGNPAL AAAAAAGGGY MYPMLAGALA HGGLGSDMVQ SSQMGGIGVD PSVGAAGLSA
     LGSYFRGQSL PSTYPDSDAG GKRGTGKDSD AGGSSFHGYS NYS
 
 
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