SA1B1_ARATH
ID SA1B1_ARATH Reviewed; 320 AA.
AC P0DI12; Q8LCB9; Q8LKN3; Q9LUF3;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=SUMO-activating enzyme subunit 1B-1;
DE AltName: Full=SUMO-activating enzyme subunit 1-2;
DE AltName: Full=Ubiquitin-like 1-activating enzyme E1A;
GN Name=SAE1B-1; Synonyms=SAE1-2; OrderedLocusNames=At5g50580;
GN ORFNames=MBA10.22;
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=12482876; DOI=10.1074/jbc.m209694200;
RA Kurepa J., Walker J.M., Smalle J., Gosink M.M., Davis S.J., Durham T.L.,
RA Sung D.Y., Vierstra R.D.;
RT "The small ubiquitin-like modifier (SUMO) protein modification system in
RT Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by
RT stress.";
RL J. Biol. Chem. 278:6862-6872(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 1).
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] (ISOFORM 1).
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.
RN [7]
RP FUNCTION.
RX PubMed=17644626; DOI=10.1104/pp.107.102285;
RA Saracco S.A., Miller M.J., Kurepa J., Vierstra R.D.;
RT "Genetic analysis of SUMOylation in Arabidopsis: conjugation of SUMO1 and
RT SUMO2 to nuclear proteins is essential.";
RL Plant Physiol. 145:119-134(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: The dimeric enzyme acts as an E1 ligase for SUMO1 and SUMO2.
CC It mediates ATP-dependent activation of SUMO proteins and formation of
CC a thioester with a conserved cysteine residue on SAE2. Functionally
CC redundant with its paralog SAE1A. {ECO:0000269|PubMed:17644626}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Heterodimer of SAE1A or SAE1B and SAE2. The complex binds SUMO
CC proteins via SAE2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0DI12-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DI12-2; Sequence=VSP_039564;
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; AF510524; AAN03850.1; -; mRNA.
DR EMBL; AB025619; BAB09143.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95964.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95965.1; -; Genomic_DNA.
DR EMBL; AY091012; AAM14034.1; -; mRNA.
DR EMBL; AY117230; AAM51305.1; -; mRNA.
DR EMBL; AK227039; BAE99099.1; -; mRNA.
DR EMBL; AY086686; AAM63741.1; -; mRNA.
DR RefSeq; NP_001032050.1; NM_001036973.2. [P0DI12-2]
DR RefSeq; NP_568732.2; NM_124436.4. [P0DI12-1]
DR RefSeq; NP_568741.1; NM_124446.3. [P0DI12-1]
DR RefSeq; NP_851162.1; NM_180831.2. [P0DI12-2]
DR AlphaFoldDB; P0DI12; -.
DR SMR; P0DI12; -.
DR BioGRID; 20373; 4.
DR BioGRID; 20385; 4.
DR STRING; 3702.AT5G50580.2; -.
DR iPTMnet; P0DI12; -.
DR PaxDb; P0DI12; -.
DR PRIDE; P0DI12; -.
DR EnsemblPlants; AT5G50580.1; AT5G50580.1; AT5G50580. [P0DI12-2]
DR EnsemblPlants; AT5G50580.2; AT5G50580.2; AT5G50580. [P0DI12-1]
DR EnsemblPlants; AT5G50680.1; AT5G50680.1; AT5G50680. [P0DI12-1]
DR EnsemblPlants; AT5G50680.2; AT5G50680.2; AT5G50680. [P0DI12-2]
DR GeneID; 835127; -.
DR GeneID; 835139; -.
DR Gramene; AT5G50580.1; AT5G50580.1; AT5G50580. [P0DI12-2]
DR Gramene; AT5G50580.2; AT5G50580.2; AT5G50580. [P0DI12-1]
DR Gramene; AT5G50680.1; AT5G50680.1; AT5G50680. [P0DI12-1]
DR Gramene; AT5G50680.2; AT5G50680.2; AT5G50680. [P0DI12-2]
DR KEGG; ath:AT5G50580; -.
DR KEGG; ath:AT5G50680; -.
DR Araport; AT5G50580; -.
DR TAIR; locus:2159727; AT5G50580.
DR eggNOG; KOG2014; Eukaryota.
DR InParanoid; P0DI12; -.
DR OMA; FFSEMAP; -.
DR OrthoDB; 1180926at2759; -.
DR PhylomeDB; P0DI12; -.
DR UniPathway; UPA00886; -.
DR PRO; PR:P0DI12; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P0DI12; baseline and differential.
DR Genevisible; P0DI12; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0031510; C:SUMO activating enzyme complex; IBA:GO_Central.
DR GO; GO:0019948; F:SUMO activating enzyme activity; IDA:TAIR.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IDA:TAIR.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Ligase; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..320
FT /note="SUMO-activating enzyme subunit 1B-1"
FT /id="PRO_0000396011"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 176..177
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_039564"
FT CONFLICT 15
FT /note="D -> Y (in Ref. 6; AAM63741)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="D -> R (in Ref. 6; AAM63741)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="E -> Q (in Ref. 1; AAN03850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 35655 MW; 881F95354DB89BEA CRC64;
MDGDELTEQE TALYDRQIRV WGAGAQRRLS KSHVLVSGIK GTVAEFCKNI VLAGVGSVTL
LDDRLVTTEV FNANFLILPD ENAYVGKTVA EICCDSLKDF NPMVHVSIEK GDLSTLGVDF
FEKFDVVVIG YSSRATKKAV NEKCRNLAKD VAFYTVDCRG SCGEIFVDLQ NYKYTKKKLD
ETVECELTFP SFEEAVSVPW KPMPRRTAKL YFAMRVIELF EETEGRKPGE CSLSDLPRVL
KLKKELCEGN SVSENHIPDI LLERLVSNNT EFPPACAIIG GILGQEVIKV ISGKGEPLKN
FFYFDAEDGK GVIEDLSHKL
