ID   RSBNL_HUMAN             Reviewed;         846 AA.
AC   Q6PCB5; C9K0P1; Q6ZS58; Q6ZVI9; Q86X48;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Lysine-specific demethylase RSBN1L {ECO:0000305};
DE            EC=1.14.11.- {ECO:0000250|UniProtKB:Q80T69};
DE   AltName: Full=Round spermatid basic protein 1-like protein;
GN   Name=RSBN1L;
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 2).
RC   TISSUE=Cerebellum;
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 GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye, and 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   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [6]
RP   IDENTIFICATION BY 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   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28, 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   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-32 AND SER-315, AND
RP   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   [10]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-763, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-763, AND IDENTIFICATION BY MASS
RP   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   [12]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-763 AND LYS-814, AND
RP   IDENTIFICATION BY MASS 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   [13]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-753, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [14]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-223; LYS-548; LYS-753; LYS-763
RP   AND LYS-814, 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).
CC   -!- FUNCTION: Lysine-specific demethylase that specifically demethylates
CC       methylated lysine residues of proteins. {ECO:0000250|UniProtKB:Q80T69}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q80T69};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9GRZ3};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9GRZ3}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PCB5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PCB5-2; Sequence=VSP_027658;
CC   -!- SIMILARITY: Belongs to the round spermatid basic protein 1 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH46353.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=BAC85872.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK124517; BAC85872.1; ALT_INIT; mRNA.
DR   EMBL; AK127713; BAC87096.1; -; mRNA.
DR   EMBL; AC004955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236949; EAL24197.1; -; Genomic_DNA.
DR   EMBL; BC046353; AAH46353.1; ALT_SEQ; mRNA.
DR   EMBL; BC059402; AAH59402.1; -; mRNA.
DR   CCDS; CCDS43607.1; -. [Q6PCB5-1]
DR   RefSeq; NP_940869.2; NM_198467.2. [Q6PCB5-1]
DR   AlphaFoldDB; Q6PCB5; -.
DR   SMR; Q6PCB5; -.
DR   BioGRID; 128788; 122.
DR   IntAct; Q6PCB5; 24.
DR   MINT; Q6PCB5; -.
DR   STRING; 9606.ENSP00000334040; -.
DR   GlyCosmos; Q6PCB5; 7 sites, 1 glycan.
DR   GlyGen; Q6PCB5; 9 sites, 1 O-linked glycan (9 sites).
DR   iPTMnet; Q6PCB5; -.
DR   PhosphoSitePlus; Q6PCB5; -.
DR   BioMuta; RSBN1L; -.
DR   DMDM; 313104176; -.
DR   EPD; Q6PCB5; -.
DR   jPOST; Q6PCB5; -.
DR   MassIVE; Q6PCB5; -.
DR   MaxQB; Q6PCB5; -.
DR   PaxDb; 9606-ENSP00000334040; -.
DR   PeptideAtlas; Q6PCB5; -.
DR   ProteomicsDB; 67056; -. [Q6PCB5-1]
DR   ProteomicsDB; 67057; -. [Q6PCB5-2]
DR   Pumba; Q6PCB5; -.
DR   Antibodypedia; 8364; 41 antibodies from 9 providers.
DR   DNASU; 222194; -.
DR   Ensembl; ENST00000334955.13; ENSP00000334040.7; ENSG00000187257.16. [Q6PCB5-1]
DR   Ensembl; ENST00000445288.5; ENSP00000393888.1; ENSG00000187257.16. [Q6PCB5-2]
DR   GeneID; 222194; -.
DR   KEGG; hsa:222194; -.
DR   MANE-Select; ENST00000334955.13; ENSP00000334040.7; NM_198467.3; NP_940869.2.
DR   UCSC; uc010ldt.2; human. [Q6PCB5-1]
DR   AGR; HGNC:24765; -.
DR   CTD; 222194; -.
DR   DisGeNET; 222194; -.
DR   GeneCards; RSBN1L; -.
DR   HGNC; HGNC:24765; RSBN1L.
DR   HPA; ENSG00000187257; Low tissue specificity.
DR   neXtProt; NX_Q6PCB5; -.
DR   OpenTargets; ENSG00000187257; -.
DR   PharmGKB; PA134948776; -.
DR   VEuPathDB; HostDB:ENSG00000187257; -.
DR   eggNOG; KOG4425; Eukaryota.
DR   GeneTree; ENSGT00390000001969; -.
DR   HOGENOM; CLU_009952_0_1_1; -.
DR   InParanoid; Q6PCB5; -.
DR   OMA; WPAQPRI; -.
DR   OrthoDB; 5404645at2759; -.
DR   PhylomeDB; Q6PCB5; -.
DR   TreeFam; TF323256; -.
DR   PathwayCommons; Q6PCB5; -.
DR   SignaLink; Q6PCB5; -.
DR   BioGRID-ORCS; 222194; 43 hits in 1165 CRISPR screens.
DR   ChiTaRS; RSBN1L; human.
DR   GenomeRNAi; 222194; -.
DR   Pharos; Q6PCB5; Tdark.
DR   PRO; PR:Q6PCB5; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q6PCB5; Protein.
DR   Bgee; ENSG00000187257; Expressed in tendon of biceps brachii and 195 other cell types or tissues.
DR   ExpressionAtlas; Q6PCB5; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR026306; RSBN1/Dpy-21.
DR   PANTHER; PTHR13354:SF9; LYSINE-SPECIFIC DEMETHYLASE RSBN1L; 1.
DR   PANTHER; PTHR13354; ROUND SPERMATID BASIC PROTEIN 1; 1.
DR   Genevisible; Q6PCB5; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Dioxygenase; Iron; Isopeptide bond;
KW   Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   CHAIN           2..846
FT                   /note="Lysine-specific demethylase RSBN1L"
FT                   /id="PRO_0000299414"
FT   REGION          15..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          827..846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..267
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..846
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         568
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT   BINDING         571
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT   BINDING         573
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT   BINDING         665
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT   BINDING         673
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         28
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        223
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        548
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        753
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        763
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25114211,
FT                   ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        814
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..270
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_027658"
FT   CONFLICT        38
FT                   /note="G -> V (in Ref. 4; AAH46353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="H -> K (in Ref. 4; AAH46353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        375
FT                   /note="M -> V (in Ref. 1; BAC87096)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        428..431
FT                   /note="Missing (in Ref. 3; EAL24197 and 4; AAH59402)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        808
FT                   /note="N -> S (in Ref. 1; BAC85872)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   846 AA;  94870 MW;  591E3AC544227B27 CRC64;
     MAEPPSPVHC VAAAAPTATV SEKEPFGKLQ LSSRDPPGSL SAKKVRTEEK KAPRRVNGEG
     GSGGNSRQLQ PPAAPSPQSY GSPASWSFAP LSAAPSPSSS RSSFSFSAGT AVPSSASASL
     SQPVPRKLLV PPTLLHAQPH HLLLPAAAAA ASANAKSRRP KEKREKERRR HGLGGAREAG
     GASREENGEV KPLPRDKIKD KIKERDKEKE REKKKHKVMN EIKKENGEVK ILLKSGKEKP
     KTNIEDLQIK KVKKKKKKKH KENEKRKRPK MYSKSIQTIC SGLLTDVEDQ AAKGILNDNI
     KDYVGKNLDT KNYDSKIPEN SEFPFVSLKE PRVQNNLKRL DTLEFKQLIH IEHQPNGGAS
     VIHAYSNELS HLSPMEMERF AEEFVGLVFS ENENSAAFYV MGIVHGAATY LPDFLDYFSF
     NFPNSPVKME ILGKKDIETT TMSNFHAQVK RTYSHGTYRA GPMRQISLVG AVDEEVGDYF
     PEFLDMLEES PFLKCTLPWG TLSSLKLQSR KDSDDGPIMW VRPGEQMIPV ADMPKSPFKR
     KRTTNEIKNL QYLPRTSEPR EMLFEDRTRA HADHIGQGFE RQTTAAVGVL KAVHCGEWPD
     QPRITKDVIC FHAEDFLEVV QRMQLDLHEP PLSQCVQWVD DAKLNQLRRE GIRYARIQLY
     DNDIYFIPRN VVHQFKTVSA VCSLAWHIRL KLYHSEEDTS QNTATHETGT SSDSTSSVLG
     PHTDNMICAV SKASLDSVFS DKLHSKYELQ QIKHEPIASV RIKEEPVNVN IPEKTTALNN
     MDGKNVKAKL DHVQFAEFKI DMDSKFENSN KDLKEELCPG NLSLVDTRQH SSAHSNQDKK
     DDDILC
//