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Database: UniProt
Entry: Q96AY2
LinkDB: Q96AY2
Original site: Q96AY2 
ID   EME1_HUMAN              Reviewed;         570 AA.
AC   Q96AY2; Q96N62;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 2.
DT   02-JUN-2021, entry version 159.
DE   RecName: Full=Crossover junction endonuclease EME1;
DE            EC=3.1.22.-;
DE   AltName: Full=MMS4 homolog;
DE            Short=hMMS4;
GN   Name=EME1; Synonyms=MMS4;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-69.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ASP-69.
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH MUS81.
RX   PubMed=12686547; DOI=10.1074/jbc.m302484200;
RA   Oegruenc M., Sancar A.;
RT   "Identification and characterization of human MUS81-MMS4 structure-specific
RT   endonuclease.";
RL   J. Biol. Chem. 278:21715-21720(2003).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH MUS81.
RX   PubMed=12721304; DOI=10.1074/jbc.m302882200;
RA   Ciccia A., Constantinou A., West S.C.;
RT   "Identification and characterization of the human mus81-eme1
RT   endonuclease.";
RL   J. Biol. Chem. 278:25172-25178(2003).
RN   [5]
RP   FUNCTION, SELF-ASSOCIATION, INTERACTION WITH MUS81, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=14617801; DOI=10.1091/mbc.e03-08-0580;
RA   Blais V., Gao H., Elwell C.A., Boddy M.N., Gaillard P.-H.L., Russell P.,
RA   McGowan C.H.;
RT   "RNA interference inhibition of Mus81 reduces mitotic recombination in
RT   human cells.";
RL   Mol. Biol. Cell 15:552-562(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-85 AND SER-87, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH MUS81.
RX   PubMed=17289582; DOI=10.1016/j.molcel.2007.01.003;
RA   Ciccia A., Ling C., Coulthard R., Yan Z., Xue Y., Meetei A.R.,
RA   Laghmani el H., Joenje H., McDonald N., de Winter J.P., Wang W., West S.C.;
RT   "Identification of FAAP24, a Fanconi anemia core complex protein that
RT   interacts with FANCM.";
RL   Mol. Cell 25:331-343(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-150, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-15, AND
RP   IDENTIFICATION BY 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   [10]
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-85; SER-87; SER-111;
RP   SER-117 AND THR-150, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-85 AND SER-87, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-87; SER-111 AND
RP   THR-150, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [15]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-103; LYS-136 AND LYS-141, AND
RP   IDENTIFICATION BY MASS 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).
CC   -!- FUNCTION: Interacts with MUS81 to form a DNA structure-specific
CC       endonuclease with substrate preference for branched DNA structures with
CC       a 5'-end at the branch nick. Typical substrates include 3'-flap
CC       structures, replication forks and nicked Holliday junctions. May be
CC       required in mitosis for the processing of stalled or collapsed
CC       replication forks. {ECO:0000269|PubMed:12686547,
CC       ECO:0000269|PubMed:12721304, ECO:0000269|PubMed:14617801,
CC       ECO:0000269|PubMed:17289582}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBUNIT: May self-associate. Interacts with MUS81.
CC       {ECO:0000269|PubMed:12686547, ECO:0000269|PubMed:12721304,
CC       ECO:0000269|PubMed:14617801, ECO:0000269|PubMed:17289582}.
CC   -!- INTERACTION:
CC       Q96AY2; Q96NY9: MUS81; NbExp=9; IntAct=EBI-2370825, EBI-2370806;
CC       Q96AY2; Q8IY92: SLX4; NbExp=4; IntAct=EBI-2370825, EBI-2370740;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14617801}.
CC       Note=Recruited to regions of DNA damage in S-phase cells.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96AY2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96AY2-2; Sequence=VSP_017284;
CC   -!- SIMILARITY: Belongs to the EME1/MMS4 family. {ECO:0000305}.
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DR   EMBL; AK055926; BAB71047.1; -; mRNA.
DR   EMBL; BC016470; AAH16470.1; -; mRNA.
DR   CCDS; CCDS11565.1; -. [Q96AY2-1]
DR   CCDS; CCDS54141.1; -. [Q96AY2-2]
DR   RefSeq; NP_001159603.1; NM_001166131.1. [Q96AY2-2]
DR   RefSeq; NP_689676.2; NM_152463.2. [Q96AY2-1]
DR   PDB; 2ZIU; X-ray; 2.70 A; B=246-570.
DR   PDB; 2ZIV; X-ray; 2.70 A; B=246-367, B=403-570.
DR   PDB; 2ZIW; X-ray; 2.80 A; B=246-570.
DR   PDB; 2ZIX; X-ray; 3.50 A; B=246-570.
DR   PDB; 4P0P; X-ray; 2.80 A; B=178-570.
DR   PDB; 4P0Q; X-ray; 2.85 A; B=178-570.
DR   PDB; 4P0R; X-ray; 6.50 A; B/D=178-570.
DR   PDB; 4P0S; X-ray; 6.00 A; B/D/F/H=178-570.
DR   PDBsum; 2ZIU; -.
DR   PDBsum; 2ZIV; -.
DR   PDBsum; 2ZIW; -.
DR   PDBsum; 2ZIX; -.
DR   PDBsum; 4P0P; -.
DR   PDBsum; 4P0Q; -.
DR   PDBsum; 4P0R; -.
DR   PDBsum; 4P0S; -.
DR   SMR; Q96AY2; -.
DR   BioGRID; 127026; 46.
DR   ComplexPortal; CPX-511; Deoxyribonuclease complex MUS81-EME1.
DR   DIP; DIP-48629N; -.
DR   IntAct; Q96AY2; 41.
DR   MINT; Q96AY2; -.
DR   STRING; 9606.ENSP00000376952; -.
DR   iPTMnet; Q96AY2; -.
DR   PhosphoSitePlus; Q96AY2; -.
DR   BioMuta; EME1; -.
DR   DMDM; 88909612; -.
DR   EPD; Q96AY2; -.
DR   jPOST; Q96AY2; -.
DR   MassIVE; Q96AY2; -.
DR   MaxQB; Q96AY2; -.
DR   PaxDb; Q96AY2; -.
DR   PeptideAtlas; Q96AY2; -.
DR   PRIDE; Q96AY2; -.
DR   ProteomicsDB; 76018; -. [Q96AY2-1]
DR   ProteomicsDB; 76019; -. [Q96AY2-2]
DR   Antibodypedia; 4245; 218 antibodies.
DR   DNASU; 146956; -.
DR   Ensembl; ENST00000338165; ENSP00000339897; ENSG00000154920. [Q96AY2-1]
DR   Ensembl; ENST00000393271; ENSP00000376952; ENSG00000154920. [Q96AY2-2]
DR   Ensembl; ENST00000511648; ENSP00000421700; ENSG00000154920. [Q96AY2-2]
DR   GeneID; 146956; -.
DR   KEGG; hsa:146956; -.
DR   UCSC; uc002iqs.3; human. [Q96AY2-1]
DR   CTD; 146956; -.
DR   DisGeNET; 146956; -.
DR   GeneCards; EME1; -.
DR   HGNC; HGNC:24965; EME1.
DR   HPA; ENSG00000154920; Tissue enhanced (blood, epididymis, testis).
DR   MIM; 610885; gene.
DR   neXtProt; NX_Q96AY2; -.
DR   OpenTargets; ENSG00000154920; -.
DR   PharmGKB; PA134904115; -.
DR   VEuPathDB; HostDB:ENSG00000154920.14; -.
DR   eggNOG; ENOG502R8ER; Eukaryota.
DR   GeneTree; ENSGT00530000063937; -.
DR   HOGENOM; CLU_034099_2_0_1; -.
DR   InParanoid; Q96AY2; -.
DR   OMA; DHQNNEG; -.
DR   OrthoDB; 1595761at2759; -.
DR   PhylomeDB; Q96AY2; -.
DR   TreeFam; TF325310; -.
DR   PathwayCommons; Q96AY2; -.
DR   Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR   Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR   BioGRID-ORCS; 146956; 22 hits in 998 CRISPR screens.
DR   EvolutionaryTrace; Q96AY2; -.
DR   GeneWiki; EME1; -.
DR   GenomeRNAi; 146956; -.
DR   Pharos; Q96AY2; Tbio.
DR   PRO; PR:Q96AY2; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q96AY2; protein.
DR   Bgee; ENSG00000154920; Expressed in amniotic fluid and 208 other tissues.
DR   ExpressionAtlas; Q96AY2; baseline and differential.
DR   Genevisible; Q96AY2; HS.
DR   GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR   GO; GO:0048476; C:Holliday junction resolvase complex; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR   GO; GO:0036297; P:interstrand cross-link repair; TAS:Reactome.
DR   GO; GO:0031573; P:intra-S DNA damage checkpoint; IBA:GO_Central.
DR   GO; GO:0031297; P:replication fork processing; IBA:GO_Central.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR   GO; GO:0072429; P:response to intra-S DNA damage checkpoint signaling; IMP:MGI.
DR   DisProt; DP01877; -.
DR   Gene3D; 1.10.150.670; -; 1.
DR   Gene3D; 3.40.1620.30; -; 1.
DR   Gene3D; 3.40.50.11760; -; 2.
DR   IDEAL; IID00096; -.
DR   InterPro; IPR042530; EME1/EME2_C.
DR   InterPro; IPR006166; ERCC4_domain.
DR   InterPro; IPR043086; ERCC4_Mus81-Eme1_nucdom_sub1.
DR   InterPro; IPR043087; ERCC4_Mus81-Eme1_nucdom_sub2.
DR   InterPro; IPR033310; Mms4/EME1/EME2.
DR   PANTHER; PTHR21077; PTHR21077; 1.
DR   Pfam; PF02732; ERCC4; 1.
DR   SMART; SM00891; ERCC4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA damage; DNA recombination;
KW   DNA repair; Endonuclease; Hydrolase; Isopeptide bond; Magnesium;
KW   Metal-binding; Nuclease; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..570
FT                   /note="Crossover junction endonuclease EME1"
FT                   /id="PRO_0000223630"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         111
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         150
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   CROSSLNK        103
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        136
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        141
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         370
FT                   /note="F -> FSLELLFFDFLPCT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017284"
FT   VARIANT         5
FT                   /note="K -> N (in dbSNP:rs35248609)"
FT                   /id="VAR_055708"
FT   VARIANT         49
FT                   /note="I -> V (in dbSNP:rs9896405)"
FT                   /id="VAR_025337"
FT   VARIANT         63
FT                   /note="F -> L (in dbSNP:rs17714854)"
FT                   /id="VAR_055709"
FT   VARIANT         69
FT                   /note="E -> D (in dbSNP:rs3760413)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_025338"
FT   VARIANT         347
FT                   /note="V -> I (in dbSNP:rs7222520)"
FT                   /id="VAR_055710"
FT   VARIANT         350
FT                   /note="I -> T (in dbSNP:rs12450550)"
FT                   /id="VAR_025339"
FT   CONFLICT        214
FT                   /note="R -> Q (in Ref. 1; BAB71047)"
FT                   /evidence="ECO:0000305"
FT   STRAND          242..244
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   TURN            245..247
FT                   /evidence="ECO:0007829|PDB:4P0Q"
FT   HELIX           249..251
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   STRAND          253..256
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   HELIX           258..261
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   HELIX           266..275
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   STRAND          279..282
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   STRAND          290..294
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   STRAND          301..303
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   STRAND          312..317
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   HELIX           318..326
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   HELIX           345..354
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   STRAND          359..364
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   HELIX           405..418
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   STRAND          425..428
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   HELIX           429..444
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   HELIX           456..460
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   STRAND          462..464
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   STRAND          473..475
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   HELIX           478..486
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   STRAND          487..491
FT                   /evidence="ECO:0007829|PDB:2ZIX"
FT   HELIX           494..503
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   STRAND          504..506
FT                   /evidence="ECO:0007829|PDB:4P0Q"
FT   HELIX           507..515
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   STRAND          517..519
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   HELIX           520..523
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   TURN            524..529
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   TURN            532..535
FT                   /evidence="ECO:0007829|PDB:2ZIU"
FT   HELIX           547..558
FT                   /evidence="ECO:0007829|PDB:2ZIU"
SQ   SEQUENCE   570 AA;  63252 MW;  BA08F5655761AF85 CRC64;
     MALKKSSPSL DSGDSDSEEL PTFAFLKKEP SSTKRRQPER EEKIVVVDIS DCEASCPPAP
     ELFSPPVPEI AETVTQTQPV RLLSSESEDE EEFIPLAQRL TCKFLTHKQL SPEDSSSPVK
     SVLDHQNNEG ASCDWKKPFP KIPEVPLHDT PERSAADNKD LILDPCCQLP AYLSTCPGQS
     SSLAVTKTNS DILPPQKKTK PSQKVQGRGS HGCRQQRQAR QKESTLRRQE RKNAALVTRM
     KAQRPEECLK HIIVVLDPVL LQMEGGGQLL GALQTMECRC VIEAQAVPCS VTWRRRAGPS
     EDREDWVEEP TVLVLLRAEA FVSMIDNGKQ GSLDSTMKGK ETLQGFVTDI TAKTAGKALS
     LVIVDQEKCF SAQNPPRRGK QGANKQTKKQ QQRQPEASIG SMVSRVDAEE ALVDLQLHTE
     AQAQIVQSWK ELADFTCAFT KAVAEAPFKK LRDETTFSFC LESDWAGGVK VDLAGRGLAL
     VWRRQIQQLN RVSLEMASAV VNAYPSPQLL VQAYQQCFSD KERQNLLADI QVRRGEGVTS
     TSRRIGPELS RRIYLQMTTL QPHLSLDSAD
//
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