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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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. DR Genevisible; Q9UBT2; HS. 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 //