SAE2_DANRE
ID SAE2_DANRE Reviewed; 650 AA.
AC Q7SXG4; A7MCK7; B0S543; B0S544;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=SUMO-activating enzyme subunit 2;
DE EC=2.3.2.-;
DE AltName: Full=Ubiquitin-like 1-activating enzyme E1B;
DE AltName: Full=Ubiquitin-like modifier-activating enzyme 2;
GN Name=uba2; Synonyms=sae2, sae2b, uble1b;
GN ORFNames=si:ch211-149o7.1, zgc:66354;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=SJD; TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
CC -!- FUNCTION: The heterodimer acts as an E1 ligase for sumo1, sumo2, and
CC sumo3. It mediates ATP-dependent activation of sumo proteins followed
CC by formation of a thioester bond between a sumo protein and a conserved
CC active site cysteine residue on uba2/sae2 (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Heterodimer of sae1 and uba2/sae2. The heterodimer corresponds
CC to the two domains that are encoded on a single polypeptide chain in
CC ubiquitin-activating enzyme E1. Interacts with ube2i (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Shuttles between the cytoplasm and the nucleus, sumoylation is
CC required either for nuclear translocation or nuclear retention.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7SXG4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7SXG4-2; Sequence=VSP_034008;
CC -!- PTM: Sumoylated with SUMO1 and SUMO2/3 and by UBC9. Sumoylation at Lys-
CC 237 inhibits enzymatic activity. Sumoylation at the C-terminal lysine
CC cluster plays an essential role in nuclear trafficking (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; BX005103; CAQ13480.1; -; Genomic_DNA.
DR EMBL; BX005103; CAQ13481.1; -; Genomic_DNA.
DR EMBL; BC055614; AAH55614.1; -; mRNA.
DR EMBL; BC152218; AAI52219.1; -; mRNA.
DR RefSeq; NP_998528.1; NM_213363.1.
DR AlphaFoldDB; Q7SXG4; -.
DR SMR; Q7SXG4; -.
DR STRING; 7955.ENSDARP00000102182; -.
DR iPTMnet; Q7SXG4; -.
DR PaxDb; Q7SXG4; -.
DR PeptideAtlas; Q7SXG4; -.
DR PRIDE; Q7SXG4; -.
DR Ensembl; ENSDART00000169126; ENSDARP00000130924; ENSDARG00000101332. [Q7SXG4-2]
DR Ensembl; ENSDART00000171801; ENSDARP00000139796; ENSDARG00000101332. [Q7SXG4-1]
DR GeneID; 406672; -.
DR KEGG; dre:406672; -.
DR CTD; 10054; -.
DR ZFIN; ZDB-GENE-040426-2681; uba2.
DR eggNOG; KOG2013; Eukaryota.
DR GeneTree; ENSGT00550000074924; -.
DR InParanoid; Q7SXG4; -.
DR OMA; VQWDTLL; -.
DR OrthoDB; 686413at2759; -.
DR PhylomeDB; Q7SXG4; -.
DR Reactome; R-DRE-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-DRE-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR UniPathway; UPA00886; -.
DR PRO; PR:Q7SXG4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 25.
DR Bgee; ENSDARG00000101332; Expressed in gastrula and 29 other tissues.
DR ExpressionAtlas; Q7SXG4; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031510; C:SUMO activating enzyme complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019948; F:SUMO activating enzyme activity; ISS:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR Gene3D; 1.10.10.520; -; 1.
DR Gene3D; 3.50.50.80; -; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR028077; UAE_UbL_dom.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR030661; Uba2.
DR InterPro; IPR032426; UBA2_C.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR PANTHER; PTHR10953:SF5; PTHR10953:SF5; 1.
DR Pfam; PF00899; ThiF; 1.
DR Pfam; PF14732; UAE_UbL; 1.
DR Pfam; PF16195; UBA2_C; 1.
DR PIRSF; PIRSF039133; SUMO_E1B; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Isopeptide bond;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc.
FT CHAIN 1..650
FT /note="SUMO-activating enzyme subunit 2"
FT /id="PRO_0000268872"
FT REGION 554..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 25..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 57..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 96..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 118..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250"
FT CROSSLNK 258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 618
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 630
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 259..268
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_034008"
FT CONFLICT 301
FT /note="L -> LA (in Ref. 1; CAQ13481)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="R -> H (in Ref. 2; AAH55614)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="A -> P (in Ref. 2; AAI52219)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="A -> ADD (in Ref. 2; AAI52219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 71794 MW; D637AF3C64FBB770 CRC64;
MAELVGPLRK QLADSLSSCR VLVVGAGGIG CELLKNLVLT GFKNIEVIDL DTIDVSNLNR
QFLFQKKHVG KSKAQVAKES VLRFCPSANI TAYHDSIMNP DYNVEFFRNF QLVMNALDNR
AARNHVNRMC LAADIPLIES GTAGYLGQVT VIKKGQTECY ECQPKPTQKT FPGCTIRNTP
SEPIHCIVWA KYLFNQLFGE EDADQEVSPD TADPEAAWNP ADAAARATAS DQDGDIKRVS
TKEWARSTGY DPIKLFNKVS ALSQTSPYLF KDDIMYLLTM DKLWKKRKAP LPLEWEEINQ
LGSQEQVIGS GLKDQQVLGV QGYAQLFQHS VETLRSQLKE KGDGAELVWD KDDPPAMDFV
TAASNLRMNV FSMNMKSRFD VKSMAGNIIP AIATTNAVIA GLIVLEALKI LNSDFEQCRT
IFLNKQPNPR KKLLVPCALD PPNASCYVCA SKPEVTVKLN VHKTMVQALQ DKILKEKFGM
VAPDVQIEDG KGTILISSEE GETEANNNKF LSDFGIRNGS RLQADDFLQD YTLLVNVIHS
EELEKDVEFE VVGDAPDKAP APSAPEEGKN IANGNKDSAQ PSTSSKAAVE DDDVLLVDSD
EEPSSSTMDT ESSNRKRKHH DAETDDASSK RKRLDQQPAD DDDEDIIALD
