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Database: UniProt
Entry: Q9UBT2
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Original site: Q9UBT2 
ID   SAE2_HUMAN              Reviewed;         640 AA.
AC   Q9UBT2; B3KWB9; O95605; Q59H87; Q6IBP6; Q9NTJ1; Q9UED2;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   29-SEP-2021, entry version 194.
DE   RecName: Full=SUMO-activating enzyme subunit 2;
DE            EC=2.3.2.-;
DE   AltName: Full=Anthracycline-associated resistance ARX;
DE   AltName: Full=Ubiquitin-like 1-activating enzyme E1B;
DE   AltName: Full=Ubiquitin-like modifier-activating enzyme 2;
GN   Name=UBA2; Synonyms=SAE2, UBLE1B; ORFNames=HRIHFB2115;
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), AND VARIANT ARG-307.
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), AND VARIANT ARG-307.
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).
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 [MRNA] (ISOFORM 1).
RA   Slapak C., Mizunuma N., Terashima M., Yamauchi T., Kufe D.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   [7]
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
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   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skin;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 346-640 (ISOFORM 1).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 536-640 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=9853615; DOI=10.1038/4315;
RA   Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT   "Selection system for genes encoding nuclear-targeted proteins.";
RL   Nat. Biotechnol. 16:1338-1342(1998).
RN   [13]
RP   SUBCELLULAR LOCATION, 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   [14]
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   [15]
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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [17]
RP   IDENTIFICATION BY MASS 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   [18]
RP   INTERACTION WITH UBE2I, FUNCTION, AND MUTAGENESIS OF ASP-484 AND GLY-485.
RX   PubMed=19443651; DOI=10.1074/jbc.m109.000257;
RA   Wang J., Lee B., Cai S., Fukui L., Hu W., Chen Y.;
RT   "Conformational transition associated with E1-E2 interaction in small
RT   ubiquitin-like modifications.";
RL   J. Biol. Chem. 284:20340-20348(2009).
RN   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-271, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [21]
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   [22]
RP   SUMOYLATION AT LYS-190; LYS-236; LYS-257; LYS-271 AND LYS-275.
RX   PubMed=22403398; DOI=10.1074/jbc.m112.353789;
RA   Truong K., Lee T.D., Chen Y.;
RT   "Small ubiquitin-like modifier (SUMO) modification of E1 Cys domain
RT   inhibits E1 Cys domain enzymatic activity.";
RL   J. Biol. Chem. 287:15154-15163(2012).
RN   [23]
RP   SUBCELLULAR LOCATION, AND SUMOYLATION AT LYS-611; LYS-613; LYS-617 AND
RP   LYS-623.
RX   PubMed=23095757; DOI=10.1074/jbc.m112.420877;
RA   Truong K., Lee T.D., Li B., Chen Y.;
RT   "Sumoylation of SAE2 C terminus regulates SAE nuclear localization.";
RL   J. Biol. Chem. 287:42611-42619(2012).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, 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   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY
RP   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   [26]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164 AND LYS-420, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [27]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-236, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [28]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-236; LYS-257; LYS-371; LYS-420
RP   AND LYS-540, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH SAE1; SUMO1; ZINC
RP   IONS AND ATP, FUNCTION, SUBUNIT, AND ACTIVE SITE.
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   [30]
RP   STRUCTURE BY NMR OF 166-382 IN COMPLEX WITH UBE2I, MUTAGENESIS OF ILE-235
RP   AND ILE-238, FUNCTION, AND INTERACTION WITH UBE2I.
RX   PubMed=17643372; DOI=10.1016/j.molcel.2007.05.023;
RA   Wang J., Hu W., Cai S., Lee B., Song J., Chen Y.;
RT   "The intrinsic affinity between E2 and the Cys domain of E1 in ubiquitin-
RT   like modifications.";
RL   Mol. Cell 27:228-237(2007).
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH SAE1; SUMO1 AND
RP   REACTION INTERMEDIATE, FUNCTION, ACTIVE SITE, SUBUNIT, AND MUTAGENESIS OF
RP   ASN-56; LEU-57; ARG-59; LYS-72; ASP-117; CYS-173; THR-174 AND HIS-184.
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:11451954, ECO:0000269|PubMed:11481243,
CC       ECO:0000269|PubMed:15660128, ECO:0000269|PubMed:17643372,
CC       ECO:0000269|PubMed:19443651, ECO:0000269|PubMed:20164921}.
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:17643372,
CC       ECO:0000269|PubMed:19443651, ECO:0000269|PubMed:20164921}.
CC   -!- INTERACTION:
CC       Q9UBT2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-718569, EBI-16439278;
CC       Q9UBT2; Q9UBE0: SAE1; NbExp=9; IntAct=EBI-718569, EBI-743154;
CC       Q9UBT2; P63165: SUMO1; NbExp=9; IntAct=EBI-718569, EBI-80140;
CC       Q9UBT2; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-718569, EBI-10175576;
CC       Q9UBT2; P63279: UBE2I; NbExp=6; IntAct=EBI-718569, EBI-80168;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the
CC       cytoplasm and the nucleus, sumoylation is required either for nuclear
CC       translocation or nuclear retention.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UBT2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UBT2-2; Sequence=VSP_056164;
CC   -!- PTM: Sumoylated with SUMO1 and SUMO2/3 and by UBC9. Sumoylation at Lys-
CC       236 inhibits enzymatic activity. Sumoylation at the C-terminal lysine
CC       cluster plays an essential role in nuclear trafficking.
CC       {ECO:0000269|PubMed:22403398, ECO:0000269|PubMed:23095757}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000305}.
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DR   EMBL; AF090384; AAD12784.1; -; mRNA.
DR   EMBL; AF079566; AAD23914.1; -; mRNA.
DR   EMBL; AF110957; AAD24434.1; -; mRNA.
DR   EMBL; U35832; AAC99992.1; -; mRNA.
DR   EMBL; AL136905; CAB66839.1; -; mRNA.
DR   EMBL; AK124730; BAG54081.1; -; mRNA.
DR   EMBL; BT009781; AAP88783.1; -; mRNA.
DR   EMBL; CR456756; CAG33037.1; -; mRNA.
DR   EMBL; AC008747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC003153; AAH03153.1; -; mRNA.
DR   EMBL; AB208872; BAD92109.1; -; mRNA.
DR   EMBL; AB015337; BAA34795.1; -; mRNA.
DR   CCDS; CCDS12439.1; -. [Q9UBT2-1]
DR   PIR; T46936; T46936.
DR   RefSeq; NP_005490.1; NM_005499.2. [Q9UBT2-1]
DR   PDB; 1Y8Q; X-ray; 2.25 A; B/D=1-640.
DR   PDB; 1Y8R; X-ray; 2.75 A; B/E=1-640.
DR   PDB; 2PX9; NMR; -; A=166-382.
DR   PDB; 3KYC; X-ray; 2.45 A; B=1-640.
DR   PDB; 3KYD; X-ray; 2.61 A; B=1-549.
DR   PDB; 4W5V; X-ray; 2.50 A; B=445-561.
DR   PDB; 5FQ2; X-ray; 2.20 A; B=446-547.
DR   PDB; 6CWY; X-ray; 2.46 A; D=1-640.
DR   PDB; 6CWZ; X-ray; 3.10 A; D=1-640.
DR   PDB; 6XOG; X-ray; 1.98 A; B=1-640.
DR   PDB; 6XOH; X-ray; 2.23 A; B=1-640.
DR   PDB; 6XOI; X-ray; 2.00 A; B=1-640.
DR   PDBsum; 1Y8Q; -.
DR   PDBsum; 1Y8R; -.
DR   PDBsum; 2PX9; -.
DR   PDBsum; 3KYC; -.
DR   PDBsum; 3KYD; -.
DR   PDBsum; 4W5V; -.
DR   PDBsum; 5FQ2; -.
DR   PDBsum; 6CWY; -.
DR   PDBsum; 6CWZ; -.
DR   PDBsum; 6XOG; -.
DR   PDBsum; 6XOH; -.
DR   PDBsum; 6XOI; -.
DR   SMR; Q9UBT2; -.
DR   BioGRID; 115365; 186.
DR   ComplexPortal; CPX-2161; SUMO activating enzyme complex.
DR   CORUM; Q9UBT2; -.
DR   DIP; DIP-35136N; -.
DR   IntAct; Q9UBT2; 23.
DR   MINT; Q9UBT2; -.
DR   STRING; 9606.ENSP00000246548; -.
DR   BindingDB; Q9UBT2; -.
DR   ChEMBL; CHEMBL2095174; -.
DR   ChEMBL; CHEMBL3137290; -.
DR   DrugCentral; Q9UBT2; -.
DR   GlyGen; Q9UBT2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UBT2; -.
DR   MetOSite; Q9UBT2; -.
DR   PhosphoSitePlus; Q9UBT2; -.
DR   SwissPalm; Q9UBT2; -.
DR   BioMuta; UBA2; -.
DR   DMDM; 42559898; -.
DR   EPD; Q9UBT2; -.
DR   jPOST; Q9UBT2; -.
DR   MassIVE; Q9UBT2; -.
DR   PaxDb; Q9UBT2; -.
DR   PeptideAtlas; Q9UBT2; -.
DR   PRIDE; Q9UBT2; -.
DR   ProteomicsDB; 3787; -.
DR   ProteomicsDB; 84055; -. [Q9UBT2-1]
DR   Antibodypedia; 29159; 364 antibodies.
DR   DNASU; 10054; -.
DR   Ensembl; ENST00000246548; ENSP00000246548; ENSG00000126261. [Q9UBT2-1]
DR   Ensembl; ENST00000439527; ENSP00000437484; ENSG00000126261. [Q9UBT2-2]
DR   GeneID; 10054; -.
DR   KEGG; hsa:10054; -.
DR   UCSC; uc002nvk.4; human. [Q9UBT2-1]
DR   CTD; 10054; -.
DR   DisGeNET; 10054; -.
DR   GeneCards; UBA2; -.
DR   HGNC; HGNC:30661; UBA2.
DR   HPA; ENSG00000126261; Low tissue specificity.
DR   MIM; 613295; gene.
DR   neXtProt; NX_Q9UBT2; -.
DR   OpenTargets; ENSG00000126261; -.
DR   PharmGKB; PA162407583; -.
DR   VEuPathDB; HostDB:ENSG00000126261; -.
DR   eggNOG; KOG2013; Eukaryota.
DR   GeneTree; ENSGT00550000074924; -.
DR   HOGENOM; CLU_013325_7_4_1; -.
DR   InParanoid; Q9UBT2; -.
DR   OMA; RTECYDC; -.
DR   OrthoDB; 686413at2759; -.
DR   PhylomeDB; Q9UBT2; -.
DR   TreeFam; TF300765; -.
DR   PathwayCommons; Q9UBT2; -.
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   SIGNOR; Q9UBT2; -.
DR   UniPathway; UPA00886; -.
DR   BioGRID-ORCS; 10054; 712 hits in 1024 CRISPR screens.
DR   ChiTaRS; UBA2; human.
DR   EvolutionaryTrace; Q9UBT2; -.
DR   GeneWiki; UBA2; -.
DR   GenomeRNAi; 10054; -.
DR   Pharos; Q9UBT2; Tbio.
DR   PRO; PR:Q9UBT2; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9UBT2; protein.
DR   Bgee; ENSG00000126261; Expressed in testis and 172 other tissues.
DR   ExpressionAtlas; Q9UBT2; baseline and differential.
DR   Genevisible; Q9UBT2; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0031510; C:SUMO activating enzyme complex; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IMP:CAFA.
DR   GO; GO:0000287; F:magnesium ion binding; IMP:CAFA.
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:0019948; F:SUMO activating enzyme activity; IDA:UniProtKB.
DR   GO; GO:0032183; F:SUMO binding; IPI:CAFA.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IPI:CAFA.
DR   GO; GO:0033235; P:positive regulation of protein sumoylation; IDA:UniProtKB.
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; DP00486; -.
DR   Gene3D; 1.10.10.520; -; 1.
DR   Gene3D; 3.50.50.80; -; 1.
DR   IDEAL; IID00104; -.
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; IPR018074; UBQ-activ_enz_E1_CS.
DR   InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
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; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR   PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW   Isopeptide bond; Metal-binding; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc.
FT   CHAIN           1..640
FT                   /note="SUMO-activating enzyme subunit 2"
FT                   /id="PRO_0000194968"
FT   NP_BIND         24..29
FT                   /note="ATP"
FT                   /evidence="ECO:0000269|PubMed:15660128"
FT   NP_BIND         56..59
FT                   /note="ATP"
FT                   /evidence="ECO:0000269|PubMed:15660128"
FT   NP_BIND         95..96
FT                   /note="ATP"
FT                   /evidence="ECO:0000269|PubMed:15660128"
FT   NP_BIND         117..122
FT                   /note="ATP"
FT                   /evidence="ECO:0000269|PubMed:15660128"
FT   REGION          202..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..601
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        173
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10132,
FT                   ECO:0000269|PubMed:15660128, ECO:0000269|PubMed:20164921"
FT   METAL           158
FT                   /note="Zinc"
FT   METAL           161
FT                   /note="Zinc"
FT   METAL           441
FT                   /note="Zinc"
FT   METAL           444
FT                   /note="Zinc"
FT   BINDING         48
FT                   /note="ATP"
FT                   /evidence="ECO:0000269|PubMed:15660128"
FT   BINDING         72
FT                   /note="ATP"
FT                   /evidence="ECO:0000269|PubMed:15660128"
FT   MOD_RES         207
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         271
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         507
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         592
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         613
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1F9"
FT   CROSSLNK        164
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        190
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT   CROSSLNK        236
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT   CROSSLNK        236
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        257
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT   CROSSLNK        257
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        271
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT   CROSSLNK        275
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT   CROSSLNK        371
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        420
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        420
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        540
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        611
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT   CROSSLNK        613
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT   CROSSLNK        617
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT   CROSSLNK        623
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT   VAR_SEQ         1..96
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056164"
FT   VARIANT         307
FT                   /note="L -> R (in dbSNP:rs1043062)"
FT                   /evidence="ECO:0000269|PubMed:10217437,
FT                   ECO:0000269|PubMed:9920803"
FT                   /id="VAR_017689"
FT   MUTAGEN         56
FT                   /note="N->A: Abolishes ATP-dependent activation of SUMO
FT                   proteins."
FT                   /evidence="ECO:0000269|PubMed:20164921"
FT   MUTAGEN         57
FT                   /note="L->A: Strongly reduces ATP-dependent activation of
FT                   SUMO proteins."
FT                   /evidence="ECO:0000269|PubMed:20164921"
FT   MUTAGEN         59
FT                   /note="R->A: Strongly reduces ATP-dependent activation of
FT                   SUMO proteins."
FT                   /evidence="ECO:0000269|PubMed:20164921"
FT   MUTAGEN         72
FT                   /note="K->A: Abolishes ATP-dependent activation of SUMO
FT                   proteins."
FT                   /evidence="ECO:0000269|PubMed:20164921"
FT   MUTAGEN         117
FT                   /note="D->A: Abolishes ATP-dependent activation of SUMO
FT                   proteins."
FT                   /evidence="ECO:0000269|PubMed:20164921"
FT   MUTAGEN         173
FT                   /note="C->A: Loss of enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:20164921"
FT   MUTAGEN         174
FT                   /note="T->A: Slightly reduced enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:20164921"
FT   MUTAGEN         184
FT                   /note="H->Q: No effect on enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:20164921"
FT   MUTAGEN         235
FT                   /note="I->A: Strongly reduced interaction with UBE2I; when
FT                   associated with A-238."
FT                   /evidence="ECO:0000269|PubMed:17643372"
FT   MUTAGEN         238
FT                   /note="I->A: Strongly reduced interaction with UBE2I; when
FT                   associated with A-235."
FT                   /evidence="ECO:0000269|PubMed:17643372"
FT   MUTAGEN         484
FT                   /note="Missing: Strongly reduced interaction with UBE2I."
FT                   /evidence="ECO:0000269|PubMed:19443651"
FT   MUTAGEN         485
FT                   /note="G->GGGG: Strongly reduced interaction with UBE2I."
FT                   /evidence="ECO:0000269|PubMed:19443651"
FT   CONFLICT        229
FT                   /note="S -> C (in Ref. 1; AAD12784 and 2; AAD23914)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        341
FT                   /note="E -> G (in Ref. 5; CAB66839)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        456
FT                   /note="V -> L (in Ref. 11; BAD92109)"
FT                   /evidence="ECO:0000305"
FT   HELIX           9..17
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   STRAND          19..23
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           27..39
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   STRAND          43..48
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           54..58
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           72..81
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   STRAND          88..94
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           103..106
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   STRAND          110..114
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           119..132
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   STRAND          136..142
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   STRAND          145..151
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   TURN            153..155
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   STRAND          168..170
FT                   /evidence="ECO:0007829|PDB:6CWY"
FT   TURN            172..176
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           182..197
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           202..204
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           213..215
FT                   /evidence="ECO:0007829|PDB:3KYC"
FT   STRAND          225..227
FT                   /evidence="ECO:0007829|PDB:2PX9"
FT   STRAND          234..236
FT                   /evidence="ECO:0007829|PDB:2PX9"
FT   HELIX           241..246
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           251..259
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           261..266
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           270..272
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   STRAND          274..276
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           284..289
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           308..310
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           315..335
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   TURN            337..339
FT                   /evidence="ECO:0007829|PDB:1Y8R"
FT   HELIX           349..365
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           373..381
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           388..406
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           410..412
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   STRAND          414..418
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   STRAND          426..433
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   TURN            442..444
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   STRAND          445..447
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   STRAND          449..454
FT                   /evidence="ECO:0007829|PDB:5FQ2"
FT   TURN            456..458
FT                   /evidence="ECO:0007829|PDB:5FQ2"
FT   HELIX           461..466
FT                   /evidence="ECO:0007829|PDB:5FQ2"
FT   HELIX           467..472
FT                   /evidence="ECO:0007829|PDB:5FQ2"
FT   STRAND          476..482
FT                   /evidence="ECO:0007829|PDB:5FQ2"
FT   STRAND          484..486
FT                   /evidence="ECO:0007829|PDB:5FQ2"
FT   STRAND          488..491
FT                   /evidence="ECO:0007829|PDB:5FQ2"
FT   STRAND          493..498
FT                   /evidence="ECO:0007829|PDB:1Y8Q"
FT   HELIX           499..501
FT                   /evidence="ECO:0007829|PDB:5FQ2"
FT   STRAND          503..505
FT                   /evidence="ECO:0007829|PDB:6CWZ"
FT   HELIX           506..509
FT                   /evidence="ECO:0007829|PDB:5FQ2"
FT   STRAND          516..525
FT                   /evidence="ECO:0007829|PDB:5FQ2"
FT   STRAND          527..534
FT                   /evidence="ECO:0007829|PDB:5FQ2"
FT   STRAND          543..546
FT                   /evidence="ECO:0007829|PDB:5FQ2"
FT   TURN            609..611
FT                   /evidence="ECO:0007829|PDB:3KYC"
FT   TURN            614..619
FT                   /evidence="ECO:0007829|PDB:3KYC"
FT   HELIX           620..626
FT                   /evidence="ECO:0007829|PDB:3KYC"
FT   HELIX           627..629
FT                   /evidence="ECO:0007829|PDB:3KYC"
FT   STRAND          636..638
FT                   /evidence="ECO:0007829|PDB:3KYC"
SQ   SEQUENCE   640 AA;  71224 MW;  C12D15293BBF90EB CRC64;
     MALSRGLPRE LAEAVAGGRV LVVGAGGIGC ELLKNLVLTG FSHIDLIDLD TIDVSNLNRQ
     FLFQKKHVGR SKAQVAKESV LQFYPKANIV AYHDSIMNPD YNVEFFRQFI LVMNALDNRA
     ARNHVNRMCL AADVPLIESG TAGYLGQVTT IKKGVTECYE CHPKPTQRTF PGCTIRNTPS
     EPIHCIVWAK YLFNQLFGEE DADQEVSPDR ADPEAAWEPT EAEARARASN EDGDIKRIST
     KEWAKSTGYD PVKLFTKLFK DDIRYLLTMD KLWRKRKPPV PLDWAEVQSQ GEETNASDQQ
     NEPQLGLKDQ QVLDVKSYAR LFSKSIETLR VHLAEKGDGA ELIWDKDDPS AMDFVTSAAN
     LRMHIFSMNM KSRFDIKSMA GNIIPAIATT NAVIAGLIVL EGLKILSGKI DQCRTIFLNK
     QPNPRKKLLV PCALDPPNPN CYVCASKPEV TVRLNVHKVT VLTLQDKIVK EKFAMVAPDV
     QIEDGKGTIL ISSEEGETEA NNHKKLSEFG IRNGSRLQAD DFLQDYTLLI NILHSEDLGK
     DVEFEVVGDA PEKVGPKQAE DAAKSITNGS DDGAQPSTST AQEQDDVLIV DSDEEDSSNN
     ADVSEEERSR KRKLDEKENL SAKRSRIEQK EELDDVIALD
//
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