SAE1_HUMAN
ID SAE1_HUMAN Reviewed; 346 AA.
AC Q9UBE0; B2RDP5; B3KMQ2; F5GXX7; G3XAK6; O95717; Q9P020;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 192.
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, UBLE1A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DIMERIZATION, AND FUNCTION.
RC TISSUE=Cervix carcinoma;
RX PubMed=9920803; DOI=10.1006/bbrc.1998.9995;
RA Okuma T., Honda R., Ichikawa G., Tsumagari N., Yasuda H.;
RT "In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2.";
RL Biochem. Biophys. Res. Commun. 254:693-698(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DIMERIZATION, AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=10217437; DOI=10.1016/s0014-5793(99)00367-1;
RA Gong L., Li B., Millas S., Yeh E.T.H.;
RT "Molecular cloning and characterization of human AOS1 and UBA2, components
RT of the sentrin-activating enzyme complex.";
RL FEBS Lett. 448:185-189(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 1-11; 109-117
RP AND 186-193, DIMERIZATION, AND FUNCTION.
RC TISSUE=Cervix carcinoma;
RX PubMed=10187858; DOI=10.1074/jbc.274.15.10618;
RA Desterro J.M.P., Rodriguez M.S., Kemp G.D., Hay R.T.;
RT "Identification of the enzyme required for activation of the small
RT ubiquitin-like protein SUMO-1.";
RL J. Biol. Chem. 274:10618-10624(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=B-cell;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, Lung, and Placenta;
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 [11]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DIMERIZATION, AND FUNCTION.
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 [12]
RP FUNCTION.
RX PubMed=11451954; DOI=10.1074/jbc.m104214200;
RA Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H.,
RA Naismith J.H., Hay R.T.;
RT "Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates
RT by SAE1/SAE2 and Ubc9.";
RL J. Biol. Chem. 276:35368-35374(2001).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16620772; DOI=10.1016/j.abb.2006.03.002;
RA Li T., Santockyte R., Shen R.-F., Tekle E., Wang G., Yang D.C.H.,
RA Chock P.B.;
RT "A general approach for investigating enzymatic pathways and substrates for
RT ubiquitin-like modifiers.";
RL Arch. Biochem. Biophys. 453:70-74(2006).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP ACETYLATION AT VAL-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH UBA2; SUMO1 AND ATP,
RP AND FUNCTION.
RX PubMed=15660128; DOI=10.1038/sj.emboj.7600552;
RA Lois L.M., Lima C.D.;
RT "Structures of the SUMO E1 provide mechanistic insights into SUMO
RT activation and E2 recruitment to E1.";
RL EMBO J. 24:439-451(2005).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH UBA2 AND SUMO1,
RP FUNCTION, AND MUTAGENESIS OF ARG-21 AND 24-ARG--TRP-26.
RX PubMed=20164921; DOI=10.1038/nature08765;
RA Olsen S.K., Capili A.D., Lu X., Tan D.S., Lima C.D.;
RT "Active site remodelling accompanies thioester bond formation in the SUMO
RT E1.";
RL Nature 463:906-912(2010).
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.
CC {ECO:0000269|PubMed:10187858, ECO:0000269|PubMed:10217437,
CC ECO:0000269|PubMed:11451954, ECO:0000269|PubMed:11481243,
CC ECO:0000269|PubMed:15660128, ECO:0000269|PubMed:20164921,
CC ECO:0000269|PubMed:9920803}.
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.
CC {ECO:0000269|PubMed:15660128, ECO:0000269|PubMed:20164921}.
CC -!- INTERACTION:
CC Q9UBE0; O43186: CRX; NbExp=3; IntAct=EBI-743154, EBI-748171;
CC Q9UBE0; Q6FHY5: MEOX2; NbExp=5; IntAct=EBI-743154, EBI-16439278;
CC Q9UBE0; Q13952-2: NFYC; NbExp=3; IntAct=EBI-743154, EBI-11956831;
CC Q9UBE0; Q02548: PAX5; NbExp=3; IntAct=EBI-743154, EBI-296331;
CC Q9UBE0; P26367: PAX6; NbExp=3; IntAct=EBI-743154, EBI-747278;
CC Q9UBE0; Q06710: PAX8; NbExp=3; IntAct=EBI-743154, EBI-2683132;
CC Q9UBE0; Q9UBT2: UBA2; NbExp=9; IntAct=EBI-743154, EBI-718569;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11481243}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UBE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBE0-2; Sequence=VSP_045373, VSP_045374;
CC Name=3;
CC IsoId=Q9UBE0-3; Sequence=VSP_045372, VSP_045375;
CC -!- TISSUE SPECIFICITY: Expression level increases during S phase and drops
CC in G2 phase (at protein level). {ECO:0000269|PubMed:11481243}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; AF090385; AAD12785.2; -; mRNA.
DR EMBL; AF046025; AAD23902.2; -; mRNA.
DR EMBL; AF110956; AAD24433.1; -; mRNA.
DR EMBL; AF161489; AAF29104.1; -; mRNA.
DR EMBL; AL560234; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT007290; AAP35954.1; -; mRNA.
DR EMBL; AK021978; BAG51064.1; -; mRNA.
DR EMBL; AK315624; BAG37992.1; -; mRNA.
DR EMBL; AC008532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW57461.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57463.1; -; Genomic_DNA.
DR EMBL; BC000344; AAH00344.1; -; mRNA.
DR EMBL; BC003611; AAH03611.1; -; mRNA.
DR EMBL; BC018271; AAH18271.1; -; mRNA.
DR CCDS; CCDS12696.1; -. [Q9UBE0-1]
DR CCDS; CCDS54284.1; -. [Q9UBE0-2]
DR CCDS; CCDS54285.1; -. [Q9UBE0-3]
DR RefSeq; NP_001139185.1; NM_001145713.1. [Q9UBE0-3]
DR RefSeq; NP_001139186.1; NM_001145714.1. [Q9UBE0-2]
DR RefSeq; NP_005491.1; NM_005500.2. [Q9UBE0-1]
DR PDB; 1Y8Q; X-ray; 2.25 A; A/C=1-346.
DR PDB; 1Y8R; X-ray; 2.75 A; A/D=1-346.
DR PDB; 3KYC; X-ray; 2.45 A; A=1-346.
DR PDB; 3KYD; X-ray; 2.61 A; A=1-346.
DR PDB; 6CWY; X-ray; 2.46 A; C=1-346.
DR PDB; 6CWZ; X-ray; 3.10 A; C=1-346.
DR PDB; 6XOG; X-ray; 1.98 A; A=1-346.
DR PDB; 6XOH; X-ray; 2.23 A; A=1-346.
DR PDB; 6XOI; X-ray; 2.00 A; A=1-346.
DR PDBsum; 1Y8Q; -.
DR PDBsum; 1Y8R; -.
DR PDBsum; 3KYC; -.
DR PDBsum; 3KYD; -.
DR PDBsum; 6CWY; -.
DR PDBsum; 6CWZ; -.
DR PDBsum; 6XOG; -.
DR PDBsum; 6XOH; -.
DR PDBsum; 6XOI; -.
DR AlphaFoldDB; Q9UBE0; -.
DR SMR; Q9UBE0; -.
DR BioGRID; 115366; 105.
DR ComplexPortal; CPX-2161; SUMO activating enzyme complex.
DR CORUM; Q9UBE0; -.
DR DIP; DIP-34587N; -.
DR IntAct; Q9UBE0; 38.
DR MINT; Q9UBE0; -.
DR STRING; 9606.ENSP00000270225; -.
DR BindingDB; Q9UBE0; -.
DR ChEMBL; CHEMBL1615388; -.
DR DrugCentral; Q9UBE0; -.
DR GlyGen; Q9UBE0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UBE0; -.
DR MetOSite; Q9UBE0; -.
DR PhosphoSitePlus; Q9UBE0; -.
DR SwissPalm; Q9UBE0; -.
DR BioMuta; SAE1; -.
DR DMDM; 42559897; -.
DR EPD; Q9UBE0; -.
DR jPOST; Q9UBE0; -.
DR MassIVE; Q9UBE0; -.
DR MaxQB; Q9UBE0; -.
DR PaxDb; Q9UBE0; -.
DR PeptideAtlas; Q9UBE0; -.
DR PRIDE; Q9UBE0; -.
DR ProteomicsDB; 24559; -.
DR ProteomicsDB; 33772; -.
DR ProteomicsDB; 83952; -. [Q9UBE0-1]
DR Antibodypedia; 18168; 560 antibodies from 46 providers.
DR DNASU; 10055; -.
DR Ensembl; ENST00000270225.12; ENSP00000270225.6; ENSG00000142230.13. [Q9UBE0-1]
DR Ensembl; ENST00000392776.3; ENSP00000440818.1; ENSG00000142230.13. [Q9UBE0-2]
DR Ensembl; ENST00000413379.7; ENSP00000416557.2; ENSG00000142230.13. [Q9UBE0-3]
DR GeneID; 10055; -.
DR KEGG; hsa:10055; -.
DR MANE-Select; ENST00000270225.12; ENSP00000270225.6; NM_005500.3; NP_005491.1.
DR UCSC; uc002pgc.4; human. [Q9UBE0-1]
DR CTD; 10055; -.
DR DisGeNET; 10055; -.
DR GeneCards; SAE1; -.
DR HGNC; HGNC:30660; SAE1.
DR HPA; ENSG00000142230; Low tissue specificity.
DR MIM; 613294; gene.
DR neXtProt; NX_Q9UBE0; -.
DR OpenTargets; ENSG00000142230; -.
DR PharmGKB; PA162402387; -.
DR VEuPathDB; HostDB:ENSG00000142230; -.
DR eggNOG; KOG2014; Eukaryota.
DR GeneTree; ENSGT00550000075007; -.
DR InParanoid; Q9UBE0; -.
DR OMA; TDVWGTF; -.
DR PhylomeDB; Q9UBE0; -.
DR TreeFam; TF315037; -.
DR PathwayCommons; Q9UBE0; -.
DR Reactome; R-HSA-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-HSA-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR SignaLink; Q9UBE0; -.
DR SIGNOR; Q9UBE0; -.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 10055; 723 hits in 1101 CRISPR screens.
DR ChiTaRS; SAE1; human.
DR EvolutionaryTrace; Q9UBE0; -.
DR GeneWiki; SAE1; -.
DR GenomeRNAi; 10055; -.
DR Pharos; Q9UBE0; Tbio.
DR PRO; PR:Q9UBE0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UBE0; protein.
DR Bgee; ENSG00000142230; Expressed in ventricular zone and 209 other tissues.
DR ExpressionAtlas; Q9UBE0; baseline and differential.
DR Genevisible; Q9UBE0; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0031510; C:SUMO activating enzyme complex; IDA:UniProtKB.
DR GO; GO:0043008; F:ATP-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0008022; F:protein C-terminus binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0044388; F:small protein activating enzyme binding; IPI:CAFA.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; TAS:UniProtKB.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; IDA:UniProtKB.
DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR DisProt; DP00485; -.
DR IDEAL; IID00397; -.
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 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Ligase; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..346
FT /note="SUMO-activating enzyme subunit 1"
FT /id="PRO_0000194966"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..346
FT /note="SUMO-activating enzyme subunit 1, N-terminally
FT processed"
FT /id="PRO_0000423290"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="N-acetylvaline; in SUMO-activating enzyme subunit 1,
FT N-terminally processed"
FT /evidence="ECO:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:19413330"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1T2"
FT VAR_SEQ 245..299
FT /note="VLLKFRTDKGRDPSSDTYEEDSELLLQIRNDVLDSLGISPDLLPEDFVRYCF
FT SEM -> GPVSAGPSSQQLLLLRWHEGEWDCGVPWPQVNSRFGSPRDANCSMPTCIPCP
FT LPS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045372"
FT VAR_SEQ 245..266
FT /note="VLLKFRTDKGRDPSSDTYEEDS -> GTASPRWPQCVRWLEGFWHRKL (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_045373"
FT VAR_SEQ 267..346
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_045374"
FT VAR_SEQ 300..346
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045375"
FT MUTAGEN 21
FT /note="R->A: Abolishes ATP-dependent activation of SUMO
FT proteins."
FT /evidence="ECO:0000269|PubMed:20164921"
FT MUTAGEN 24..26
FT /note="RLW->AAA: Abolishes ATP-dependent activation of SUMO
FT proteins."
FT /evidence="ECO:0000269|PubMed:20164921"
FT CONFLICT 115
FT /note="I -> M (in Ref. 6; BAG51064)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="V -> A (in Ref. 4; AAF29104)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..180
FT /note="KTK -> ETD (in Ref. 4; AAF29104)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="Q -> H (in Ref. 4; AAF29104)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="R -> G (in Ref. 1; AAD12785)"
FT /evidence="ECO:0000305"
FT HELIX 13..18
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3KYC"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1Y8Q"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6CWY"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 262..278
FT /evidence="ECO:0007829|PDB:6XOG"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:3KYC"
FT HELIX 300..319
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:6XOG"
FT TURN 333..336
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:6XOG"
SQ SEQUENCE 346 AA; 38450 MW; E2B10A69FF2ED746 CRC64;
MVEKEEAGGG ISEEEAAQYD RQIRLWGLEA QKRLRASRVL LVGLKGLGAE IAKNLILAGV
KGLTMLDHEQ VTPEDPGAQF LIRTGSVGRN RAEASLERAQ NLNPMVDVKV DTEDIEKKPE
SFFTQFDAVC LTCCSRDVIV KVDQICHKNS IKFFTGDVFG YHGYTFANLG EHEFVEEKTK
VAKVSQGVED GPDTKRAKLD SSETTMVKKK VVFCPVKEAL EVDWSSEKAK AALKRTTSDY
FLLQVLLKFR TDKGRDPSSD TYEEDSELLL QIRNDVLDSL GISPDLLPED FVRYCFSEMA
PVCAVVGGIL AQEIVKALSQ RDPPHNNFFF FDGMKGNGIV ECLGPK
