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 27-MAR-2024, entry version 206.
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 INVOLVEMENT IN ACCES, AND VARIANT ACCES VAL-24.
RX PubMed=28110515; DOI=10.1002/ajmg.a.38078;
RA Marble M., Guillen Sacoto M.J., Chikarmane R., Gargiulo D., Juusola J.;
RT "Missense variant in UBA2 associated with aplasia cutis congenita, duane
RT anomaly, hip dysplasia and other anomalies: A possible new disorder
RT involving the SUMOylation pathway.";
RL Am. J. Med. Genet. A 173:758-761(2017).
RN [29]
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 [30]
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 [31]
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 [32]
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).
RN [33]
RP VARIANTS ACCES VAL-24; THR-56; 122-ARG--ASP-640 DEL; GLY-122;
RP 267-LEU--ASP-640 DEL AND LYS-483, AND CHARACTERIZATION OF VARIANTS ACCES
RP VAL-24; GLY-122 AND LYS-483.
RX PubMed=34040189; DOI=10.1038/s41436-021-01182-1;
RA Schnur R.E., Yousaf S., Liu J., Chung W.K., Rhodes L., Marble M.,
RA Zambrano R.M., Sobreira N., Jayakar P., Pierpont M.E., Schultz M.J.,
RA Pichurin P.N., Olson R.J., Graham G.E., Osmond M., Contreras-Garcia G.A.,
RA Campo-Neira K.A., Penaloza-Mantilla C.A., Flage M., Kuppa S., Navarro K.,
RA Sacoto M.J.G., Wentzensen I.M., Scarano M.I., Juusola J., Prada C.E.,
RA Hufnagel R.B.;
RT "UBA2 variants underlie a recognizable syndrome with variable aplasia cutis
RT congenita and ectrodactyly.";
RL Genet. Med. 23:1624-1635(2021).
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 -!- DISEASE: ACCES syndrome (ACCES) [MIM:619959]: An autosomal dominant
CC syndrome characterized by a highly variable phenotypic spectrum.
CC Clinical features include aplasia cutis congenita, thin scalp hair, dry
CC skin, dental anomalies, ectrodactyly, and skeletal and
CC neurodevelopmental abnormalities. Craniofacial, cardiac, renal and
CC genital anomalies have also been reported. Affected individuals have
CC early growth deficiencies that improve with age.
CC {ECO:0000269|PubMed:28110515, ECO:0000269|PubMed:34040189}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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 CCDS; CCDS92583.1; -. [Q9UBT2-2]
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 AlphaFoldDB; Q9UBT2; -.
DR SMR; Q9UBT2; -.
DR BioGRID; 115365; 240.
DR ComplexPortal; CPX-2161; SUMO activating enzyme complex, SAE1-UBA2.
DR CORUM; Q9UBT2; -.
DR DIP; DIP-35136N; -.
DR IntAct; Q9UBT2; 27.
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 MaxQB; Q9UBT2; -.
DR PaxDb; 9606-ENSP00000246548; -.
DR PeptideAtlas; Q9UBT2; -.
DR ProteomicsDB; 3787; -.
DR ProteomicsDB; 84055; -. [Q9UBT2-1]
DR Pumba; Q9UBT2; -.
DR Antibodypedia; 29159; 416 antibodies from 42 providers.
DR DNASU; 10054; -.
DR Ensembl; ENST00000246548.9; ENSP00000246548.3; ENSG00000126261.13. [Q9UBT2-1]
DR Ensembl; ENST00000439527.6; ENSP00000437484.1; ENSG00000126261.13. [Q9UBT2-2]
DR GeneID; 10054; -.
DR KEGG; hsa:10054; -.
DR MANE-Select; ENST00000246548.9; ENSP00000246548.3; NM_005499.3; NP_005490.1.
DR UCSC; uc002nvk.4; human. [Q9UBT2-1]
DR AGR; HGNC:30661; -.
DR CTD; 10054; -.
DR DisGeNET; 10054; -.
DR GeneCards; UBA2; -.
DR HGNC; HGNC:30661; UBA2.
DR HPA; ENSG00000126261; Low tissue specificity.
DR MalaCards; UBA2; -.
DR MIM; 613295; gene.
DR MIM; 619959; phenotype.
DR neXtProt; NX_Q9UBT2; -.
DR OpenTargets; ENSG00000126261; -.
DR Orphanet; 1114; Aplasia cutis congenita.
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; RFDIKQM; -.
DR OrthoDB; 20494at2759; -.
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 SignaLink; Q9UBT2; -.
DR SIGNOR; Q9UBT2; -.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 10054; 756 hits in 1172 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 ventricular zone and 135 other cell types or 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:0016925; P:protein sumoylation; IDA:UniProtKB.
DR CDD; cd01489; Uba2_SUMO; 1.
DR DisProt; DP00486; -.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 2.
DR IDEAL; IID00104; -.
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; IPR018074; UBQ-activ_enz_E1_CS.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953:SF5; SUMO-ACTIVATING ENZYME SUBUNIT 2; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 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; Activating enzymes of the ubiquitin-like proteins; 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 Disease variant; Ectodermal dysplasia; Isopeptide bond; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc.
FT CHAIN 1..640
FT /note="SUMO-activating enzyme subunit 2"
FT /id="PRO_0000194968"
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 BINDING 24..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15660128"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15660128"
FT BINDING 56..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15660128"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15660128"
FT BINDING 95..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15660128"
FT BINDING 117..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15660128"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 24
FT /note="G -> V (in ACCES; loss of function; does not rescue
FT the abnormal phenotype in a zebrafish disease model;
FT dbSNP:rs2075211884)"
FT /evidence="ECO:0000269|PubMed:28110515,
FT ECO:0000269|PubMed:34040189"
FT /id="VAR_087611"
FT VARIANT 56
FT /note="N -> T (in ACCES; dbSNP:rs2075242496)"
FT /evidence="ECO:0000269|PubMed:34040189"
FT /id="VAR_087612"
FT VARIANT 122..640
FT /note="Missing (in ACCES)"
FT /evidence="ECO:0000269|PubMed:34040189"
FT /id="VAR_087613"
FT VARIANT 122
FT /note="R -> G (in ACCES; loss of function; does not rescue
FT the abnormal phenotype in a zebrafish disease model)"
FT /evidence="ECO:0000269|PubMed:34040189"
FT /id="VAR_087614"
FT VARIANT 267..640
FT /note="Missing (in ACCES)"
FT /evidence="ECO:0000269|PubMed:34040189"
FT /id="VAR_087615"
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 VARIANT 483
FT /note="E -> K (in ACCES; loss of function; does not rescue
FT the abnormal phenotype in a zebrafish disease model;
FT dbSNP:rs2075619600)"
FT /evidence="ECO:0000269|PubMed:34040189"
FT /id="VAR_087616"
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:6XOG"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 27..39
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:6XOG"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6CWY"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 182..197
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6XOG"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:2PX9"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2PX9"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:6XOG"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:1Y8Q"
FT HELIX 284..288
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 315..335
FT /evidence="ECO:0007829|PDB:6XOG"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:1Y8R"
FT HELIX 349..365
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 373..381
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 388..405
FT /evidence="ECO:0007829|PDB:6XOG"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:6XOG"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:6XOG"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 461..466
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 467..472
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:6XOG"
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:6XOG"
FT STRAND 516..521
FT /evidence="ECO:0007829|PDB:6XOG"
FT TURN 522..525
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 526..534
FT /evidence="ECO:0007829|PDB:6XOG"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:6XOG"
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
//
