SA1B2_ARATH
ID SA1B2_ARATH Reviewed; 320 AA.
AC P0DI13; Q8LCB9; Q8LKN3; Q9LUF3;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=SUMO-activating enzyme subunit 1B-2;
DE AltName: Full=SUMO-activating enzyme subunit 1-2;
DE AltName: Full=Ubiquitin-like 1-activating enzyme E1A;
GN Name=SAE1B-2; Synonyms=SAE1-2; OrderedLocusNames=At5g50680;
GN ORFNames=MFB16.15;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 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 (By similarity). {ECO:0000250}.
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=P0DI13-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DI13-2; Sequence=VSP_042660;
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; AB023037; BAA96981.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95978.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95979.1; -; Genomic_DNA.
DR RefSeq; NP_001032050.1; NM_001036973.2. [P0DI13-2]
DR RefSeq; NP_568732.2; NM_124436.4. [P0DI13-1]
DR RefSeq; NP_568741.1; NM_124446.3. [P0DI13-1]
DR RefSeq; NP_851162.1; NM_180831.2. [P0DI13-2]
DR AlphaFoldDB; P0DI13; -.
DR SMR; P0DI13; -.
DR BioGRID; 20373; 4.
DR BioGRID; 20385; 4.
DR iPTMnet; P0DI13; -.
DR EnsemblPlants; AT5G50580.1; AT5G50580.1; AT5G50580.
DR EnsemblPlants; AT5G50580.2; AT5G50580.2; AT5G50580.
DR EnsemblPlants; AT5G50680.1; AT5G50680.1; AT5G50680.
DR EnsemblPlants; AT5G50680.2; AT5G50680.2; AT5G50680.
DR GeneID; 835127; -.
DR GeneID; 835139; -.
DR Gramene; AT5G50580.1; AT5G50580.1; AT5G50580.
DR Gramene; AT5G50580.2; AT5G50580.2; AT5G50580.
DR Gramene; AT5G50680.1; AT5G50680.1; AT5G50680.
DR Gramene; AT5G50680.2; AT5G50680.2; AT5G50680.
DR KEGG; ath:AT5G50580; -.
DR KEGG; ath:AT5G50680; -.
DR Araport; AT5G50680; -.
DR TAIR; locus:2832477; AT5G50680.
DR InParanoid; P0DI13; -.
DR OMA; FFSEMAP; -.
DR OrthoDB; 1180926at2759; -.
DR PhylomeDB; P0DI13; -.
DR UniPathway; UPA00886; -.
DR PRO; PR:P0DI13; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P0DI13; baseline and differential.
DR Genevisible; P0DI13; 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-2"
FT /id="PRO_0000416588"
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:0000305"
FT /id="VSP_042660"
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
