ENY2_HUMAN
ID ENY2_HUMAN Reviewed; 101 AA.
AC Q9NPA8; B2RE52; G3V117;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Transcription and mRNA export factor ENY2 {ECO:0000255|HAMAP-Rule:MF_03046};
DE AltName: Full=Enhancer of yellow 2 transcription factor homolog {ECO:0000255|HAMAP-Rule:MF_03046};
GN Name=ENY2 {ECO:0000255|HAMAP-Rule:MF_03046}; ORFNames=DC6;
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).
RX PubMed=11438676; DOI=10.1128/mcb.21.15.5223-5231.2001;
RA Georgieva S., Nabirochkina E., Dilworth F.J., Eickhoff H., Becker P.,
RA Tora L., Georgiev P., Soldatov A.;
RT "The novel transcription factor e(y)2 interacts with TAF(II)40 and
RT potentiates transcription activation on chromatin templates.";
RL Mol. Cell. Biol. 21:5223-5231(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Gu J., Huang Q., Yu Y., Xu S., Han Z., Fu G., Chen Z.;
RT "Novel genes expressed in human dendritic cell.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SAGA COMPLEX.
RX PubMed=18206972; DOI=10.1016/j.molcel.2007.12.011;
RA Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S.,
RA Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G.,
RA Schuele R., Takeyama K., Kato S., Tora L., Devys D.;
RT "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
RT coactivates nuclear receptors, and counteracts heterochromatin silencing.";
RL Mol. Cell 29:92-101(2008).
RN [9]
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 [10]
RP FUNCTION, AND IDENTIFICATION IN THE SAGA COMPLEX.
RX PubMed=21746879; DOI=10.1128/mcb.05231-11;
RA Lang G., Bonnet J., Umlauf D., Karmodiya K., Koffler J., Stierle M.,
RA Devys D., Tora L.;
RT "The tightly controlled deubiquitination activity of the human SAGA complex
RT differentially modifies distinct gene regulatory elements.";
RL Mol. Cell. Biol. 31:3734-3744(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP IDENTIFICATION IN THE TREX-2 COMPLEX AND IN THE SAGA COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23591820; DOI=10.1242/jcs.118000;
RA Umlauf D., Bonnet J., Waharte F., Fournier M., Stierle M., Fischer B.,
RA Brino L., Devys D., Tora L.;
RT "The human TREX-2 complex is stably associated with the nuclear pore
RT basket.";
RL J. Cell Sci. 126:2656-2667(2013).
RN [13]
RP IDENTIFICATION IN THE SAGA COMPLEX, AND INTERACTION WITH ATXN7L3 AND
RP ATXN7L3B.
RX PubMed=27601583; DOI=10.1128/mcb.00193-16;
RA Li W., Atanassov B.S., Lan X., Mohan R.D., Swanson S.K., Farria A.T.,
RA Florens L., Washburn M.P., Workman J.L., Dent S.Y.;
RT "Cytoplasmic ATXN7L3B interferes with nuclear functions of the SAGA
RT deubiquitinase module.";
RL Mol. Cell. Biol. 36:2855-2866(2016).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-74, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH GANP, IDENTIFICATION
RP IN THE TREX-2 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=22307388; DOI=10.1093/nar/gks059;
RA Jani D., Lutz S., Hurt E., Laskey R.A., Stewart M., Wickramasinghe V.O.;
RT "Functional and structural characterization of the mammalian TREX-2 complex
RT that links transcription with nuclear messenger RNA export.";
RL Nucleic Acids Res. 40:4562-4573(2012).
CC -!- FUNCTION: Involved in mRNA export coupled transcription activation by
CC association with both the TREX-2 and the SAGA complexes. The
CC transcription regulatory histone acetylation (HAT) complex SAGA is a
CC multiprotein complex that activates transcription by remodeling
CC chromatin and mediating histone acetylation and deubiquitination.
CC Within the SAGA complex, participates in a subcomplex that specifically
CC deubiquitinates both histones H2A and H2B. The SAGA complex is
CC recruited to specific gene promoters by activators such as MYC, where
CC it is required for transcription. Required for nuclear receptor-
CC mediated transactivation (PubMed:18206972, PubMed:21746879). As a
CC component of the TREX-2 complex, involved in the export of mRNAs to the
CC cytoplasm through the nuclear pores (PubMed:23591820).
CC {ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:21746879,
CC ECO:0000269|PubMed:23591820}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC)-associated TREX-2
CC complex (transcription and export complex 2), composed of at least
CC ENY2, the isoform GANP of the MCM3AP gene, PCID2, SEM1, and either
CC centrin CETN2 or CETN3. TREX-2 contains 2 ENY2 chains. The TREX-2
CC complex also associates with ALYREF/ALY and with the nucleoporin NUP153
CC (PubMed:23591820, PubMed:22307388). Component of some SAGA
CC transcription coactivator-HAT complexes, at least composed of ATXN7,
CC ATXN7L3, ENY2, GCN5L2, SUPT3H/SPT3, TAF10, TRRAP and USP22
CC (PubMed:18206972, PubMed:21746879, PubMed:23591820, PubMed:27601583).
CC Within the SAGA complex, ENY2, ATXN7, ATXN7L3, and USP22 form an
CC additional subcomplex of SAGA called the DUB module (deubiquitination
CC module) (PubMed:18206972, PubMed:21746879, PubMed:27601583). Interacts
CC with RNA polymerase II subunit POLR2A (PubMed:22307388). Interacts with
CC ATXN7L3B (PubMed:27601583). {ECO:0000255|HAMAP-Rule:MF_03046,
CC ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:21746879,
CC ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820,
CC ECO:0000269|PubMed:27601583}.
CC -!- INTERACTION:
CC Q9NPA8; Q14CW9: ATXN7L3; NbExp=6; IntAct=EBI-719226, EBI-949215;
CC Q9NPA8; Q9H6J7-2: C11orf49; NbExp=3; IntAct=EBI-719226, EBI-13328871;
CC Q9NPA8; I6L957: HNRNPA2B1; NbExp=3; IntAct=EBI-719226, EBI-1642515;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC Rule:MF_03046, ECO:0000269|PubMed:22307388}. Note=Localization at the
CC nuclear pore complex requires NUP153 and TPR.
CC {ECO:0000269|PubMed:23591820}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NPA8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPA8-2; Sequence=VSP_046891;
CC -!- SIMILARITY: Belongs to the ENY2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03046}.
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DR EMBL; AF173296; AAF89829.1; -; mRNA.
DR EMBL; AF201940; AAF86876.1; -; mRNA.
DR EMBL; AK290752; BAF83441.1; -; mRNA.
DR EMBL; AK316560; BAG38149.1; -; mRNA.
DR EMBL; CR457183; CAG33464.1; -; mRNA.
DR EMBL; AC021237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW91927.1; -; Genomic_DNA.
DR EMBL; CH471060; EAW91930.1; -; Genomic_DNA.
DR EMBL; BC007870; AAH07870.1; -; mRNA.
DR CCDS; CCDS43762.1; -. [Q9NPA8-1]
DR CCDS; CCDS55270.1; -. [Q9NPA8-2]
DR RefSeq; NP_001180486.1; NM_001193557.1. [Q9NPA8-2]
DR RefSeq; NP_064574.1; NM_020189.5. [Q9NPA8-1]
DR PDB; 4DHX; X-ray; 2.10 A; B/C/E/F=1-101.
DR PDBsum; 4DHX; -.
DR AlphaFoldDB; Q9NPA8; -.
DR SMR; Q9NPA8; -.
DR BioGRID; 121267; 55.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR ComplexPortal; CPX-903; TFTC histone acetylation complex.
DR CORUM; Q9NPA8; -.
DR IntAct; Q9NPA8; 27.
DR MINT; Q9NPA8; -.
DR STRING; 9606.ENSP00000429986; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR iPTMnet; Q9NPA8; -.
DR PhosphoSitePlus; Q9NPA8; -.
DR BioMuta; ENY2; -.
DR DMDM; 74752879; -.
DR CPTAC; CPTAC-1607; -.
DR EPD; Q9NPA8; -.
DR jPOST; Q9NPA8; -.
DR MassIVE; Q9NPA8; -.
DR MaxQB; Q9NPA8; -.
DR PaxDb; Q9NPA8; -.
DR PeptideAtlas; Q9NPA8; -.
DR PRIDE; Q9NPA8; -.
DR ProteomicsDB; 32228; -.
DR ProteomicsDB; 81953; -. [Q9NPA8-1]
DR TopDownProteomics; Q9NPA8-1; -. [Q9NPA8-1]
DR Antibodypedia; 7042; 120 antibodies from 19 providers.
DR DNASU; 56943; -.
DR Ensembl; ENST00000521662.5; ENSP00000429713.1; ENSG00000120533.13. [Q9NPA8-2]
DR Ensembl; ENST00000521688.6; ENSP00000429986.1; ENSG00000120533.13. [Q9NPA8-1]
DR GeneID; 56943; -.
DR KEGG; hsa:56943; -.
DR MANE-Select; ENST00000521688.6; ENSP00000429986.1; NM_020189.6; NP_064574.1.
DR UCSC; uc003ync.4; human. [Q9NPA8-1]
DR CTD; 56943; -.
DR DisGeNET; 56943; -.
DR GeneCards; ENY2; -.
DR HGNC; HGNC:24449; ENY2.
DR HPA; ENSG00000120533; Low tissue specificity.
DR MIM; 619015; gene.
DR neXtProt; NX_Q9NPA8; -.
DR OpenTargets; ENSG00000120533; -.
DR PharmGKB; PA142671907; -.
DR VEuPathDB; HostDB:ENSG00000120533; -.
DR eggNOG; KOG4479; Eukaryota.
DR GeneTree; ENSGT00390000011748; -.
DR HOGENOM; CLU_134052_1_1_1; -.
DR InParanoid; Q9NPA8; -.
DR OMA; RLMCRNI; -.
DR PhylomeDB; Q9NPA8; -.
DR TreeFam; TF326556; -.
DR PathwayCommons; Q9NPA8; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q9NPA8; -.
DR BioGRID-ORCS; 56943; 327 hits in 1063 CRISPR screens.
DR ChiTaRS; ENY2; human.
DR GenomeRNAi; 56943; -.
DR Pharos; Q9NPA8; Tbio.
DR PRO; PR:Q9NPA8; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NPA8; protein.
DR Bgee; ENSG00000120533; Expressed in tendon of biceps brachii and 200 other tissues.
DR ExpressionAtlas; Q9NPA8; baseline and differential.
DR Genevisible; Q9NPA8; HS.
DR GO; GO:0071819; C:DUBm complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB.
DR GO; GO:0070390; C:transcription export complex 2; IDA:UniProtKB.
DR GO; GO:0033276; C:transcription factor TFTC complex; IC:ComplexPortal.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:ComplexPortal.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.246.140; -; 1.
DR HAMAP; MF_03046; ENY2_Sus1; 1.
DR InterPro; IPR018783; TF_ENY2.
DR InterPro; IPR038212; TF_EnY2_sf.
DR PANTHER; PTHR12514; PTHR12514; 1.
DR Pfam; PF10163; EnY2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Chromatin regulator; Isopeptide bond; mRNA transport; Nucleus;
KW Protein transport; Reference proteome; Transcription;
KW Transcription regulation; Translocation; Transport; Ubl conjugation.
FT CHAIN 1..101
FT /note="Transcription and mRNA export factor ENY2"
FT /id="PRO_0000314130"
FT CROSSLNK 74
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..5
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046891"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:4DHX"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:4DHX"
FT HELIX 42..57
FT /evidence="ECO:0007829|PDB:4DHX"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:4DHX"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:4DHX"
FT HELIX 81..98
FT /evidence="ECO:0007829|PDB:4DHX"
FT MOD_RES Q9NPA8-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 101 AA; 11529 MW; A0617024C59AABFB CRC64;
MVVSKMNKDA QMRAAINQKL IETGERERLK ELLRAKLIEC GWKDQLKAHC KEVIKEKGLE
HVTVDDLVAE ITPKGRALVP DSVKKELLQR IRTFLAQHAS L
