ID   SAE1_MOUSE              Reviewed;         350 AA.
AC   Q9R1T2; Q3TRG9; Q3TWJ0; Q9CSW9;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=SUMO-activating enzyme subunit 1;
DE   AltName: Full=Ubiquitin-like 1-activating enzyme E1A;
DE   Contains:
DE     RecName: Full=SUMO-activating enzyme subunit 1, N-terminally processed;
GN   Name=Sae1; Synonyms=Aos1, Sua1, Ubl1a1, Uble1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Kaneta Y., Takada S., Itoh M., Takagi N.;
RT   "Mus musculus cDNA similar to human Sua1 complete cds, complete cds.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC   TISSUE=Embryo, Embryonic stem cell, Eye, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RX   PubMed=11481243; DOI=10.1096/fj.00-0818fje;
RA   Azuma Y., Tan S.-H., Cavenagh M.M., Ainsztein A.M., Saitoh H., Dasso M.;
RT   "Expression and regulation of the mammalian SUMO-1 E1 enzyme.";
RL   FASEB J. 15:1825-1827(2001).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3,
CC       and probably SUMO4. It mediates ATP-dependent activation of SUMO
CC       proteins followed by formation of a thioester bond between a SUMO
CC       protein and a conserved active site cysteine residue on UBA2/SAE2 (By
CC       similarity). {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: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9R1T2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9R1T2-2; Sequence=VSP_022004;
CC   -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in testis.
CC       {ECO:0000269|PubMed:11481243}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000305}.
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DR   EMBL; AB024303; BAA82876.1; -; mRNA.
DR   EMBL; AK010313; BAB26845.1; -; mRNA.
DR   EMBL; AK011783; BAB27838.1; -; mRNA.
DR   EMBL; AK087556; BAC39925.1; -; mRNA.
DR   EMBL; AK090012; BAC41044.1; -; mRNA.
DR   EMBL; AK154139; BAE32401.1; -; mRNA.
DR   EMBL; AK159672; BAE35276.1; -; mRNA.
DR   EMBL; AK162789; BAE37060.1; -; mRNA.
DR   EMBL; BC068164; AAH68164.1; -; mRNA.
DR   CCDS; CCDS20848.1; -. [Q9R1T2-1]
DR   CCDS; CCDS85221.1; -. [Q9R1T2-2]
DR   RefSeq; NP_001272820.1; NM_001285891.1. [Q9R1T2-1]
DR   RefSeq; NP_001272821.1; NM_001285892.1. [Q9R1T2-2]
DR   RefSeq; NP_062722.1; NM_019748.3. [Q9R1T2-1]
DR   AlphaFoldDB; Q9R1T2; -.
DR   SMR; Q9R1T2; -.
DR   BioGRID; 207998; 36.
DR   ComplexPortal; CPX-3041; SUMO activating enzyme complex, SAE1-UBA2.
DR   IntAct; Q9R1T2; 1.
DR   MINT; Q9R1T2; -.
DR   STRING; 10090.ENSMUSP00000092409; -.
DR   GlyGen; Q9R1T2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9R1T2; -.
DR   PhosphoSitePlus; Q9R1T2; -.
DR   SwissPalm; Q9R1T2; -.
DR   REPRODUCTION-2DPAGE; Q9R1T2; -.
DR   EPD; Q9R1T2; -.
DR   jPOST; Q9R1T2; -.
DR   MaxQB; Q9R1T2; -.
DR   PaxDb; 10090-ENSMUSP00000092409; -.
DR   PeptideAtlas; Q9R1T2; -.
DR   ProteomicsDB; 256688; -. [Q9R1T2-1]
DR   ProteomicsDB; 256689; -. [Q9R1T2-2]
DR   Pumba; Q9R1T2; -.
DR   Antibodypedia; 18168; 637 antibodies from 46 providers.
DR   DNASU; 56459; -.
DR   Ensembl; ENSMUST00000094815.5; ENSMUSP00000092409.4; ENSMUSG00000052833.10. [Q9R1T2-1]
DR   Ensembl; ENSMUST00000210999.2; ENSMUSP00000147409.2; ENSMUSG00000052833.10. [Q9R1T2-1]
DR   Ensembl; ENSMUST00000211741.2; ENSMUSP00000147771.2; ENSMUSG00000052833.10. [Q9R1T2-2]
DR   GeneID; 56459; -.
DR   KEGG; mmu:56459; -.
DR   UCSC; uc009fhp.2; mouse. [Q9R1T2-1]
DR   UCSC; uc009fhq.2; mouse. [Q9R1T2-2]
DR   AGR; MGI:1929264; -.
DR   CTD; 10055; -.
DR   MGI; MGI:1929264; Sae1.
DR   VEuPathDB; HostDB:ENSMUSG00000052833; -.
DR   eggNOG; KOG2014; Eukaryota.
DR   GeneTree; ENSGT00550000075007; -.
DR   HOGENOM; CLU_002556_4_0_1; -.
DR   InParanoid; Q9R1T2; -.
DR   OMA; EFFGQFD; -.
DR   OrthoDB; 5483037at2759; -.
DR   PhylomeDB; Q9R1T2; -.
DR   TreeFam; TF315037; -.
DR   Reactome; R-MMU-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR   Reactome; R-MMU-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR   UniPathway; UPA00886; -.
DR   BioGRID-ORCS; 56459; 26 hits in 76 CRISPR screens.
DR   ChiTaRS; Sae1; mouse.
DR   PRO; PR:Q9R1T2; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9R1T2; Protein.
DR   Bgee; ENSMUSG00000052833; Expressed in ventricular zone and 275 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0031510; C:SUMO activating enzyme complex; ISS:UniProtKB.
DR   GO; GO:0043008; F:ATP-dependent protein binding; ISO:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0044388; F:small protein activating enzyme binding; ISO:MGI.
DR   GO; GO:0019948; F:SUMO activating enzyme activity; IBA:GO_Central.
DR   GO; GO:0033235; P:positive regulation of protein sumoylation; ISO:MGI.
DR   GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProt.
DR   CDD; cd01492; Aos1_SUMO; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR   Genevisible; Q9R1T2; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Ligase; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..350
FT                   /note="SUMO-activating enzyme subunit 1"
FT                   /id="PRO_0000423291"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBE0"
FT   CHAIN           2..350
FT                   /note="SUMO-activating enzyme subunit 1, N-terminally
FT                   processed"
FT                   /id="PRO_0000194967"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBE0"
FT   MOD_RES         2
FT                   /note="N-acetylvaline; in SUMO-activating enzyme subunit 1,
FT                   N-terminally processed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBE0"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBE0"
FT   MOD_RES         202
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   VAR_SEQ         321..350
FT                   /note="ALSQRDPPHNNFFFFDGMKGSGIVECLGPQ -> VCLGTMCV (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_022004"
SQ   SEQUENCE   350 AA;  38620 MW;  333108F6E98BABAA CRC64;
     MVEKEEAGGG GGGGISEEEA AQYDRQIRLW GLEAQKRLRA SRVLIVGMKG LGAEIAKNLI
     LAGVKGLTML DHEQVSPEDP GAQFLIQTGS VGRNRAEASL ERAQNLNPMV DVKVDTEDVE
     KKPESFFTKF DAVCLTCCSR DVIIKVDQIC HRNSIKFFTG DVFGYHGYTF ANLGEHEFVE
     EKTKVAKVSQ GVEDGPEAKR AKLDSSETTM VKKKVLFCPV KEALEVDWSG EKAKAALKRT
     APDYFLLQVL LKFRTDKGRD PTSESYKEDA ELLLQIRNDV FDSLGISPDL LPDDFVRYCF
     SEMAPVCAVV GGILAQEIVK ALSQRDPPHN NFFFFDGMKG SGIVECLGPQ
//