ID   MBIP1_HUMAN             Reviewed;         344 AA.
AC   Q9NS73; Q86TZ2; Q96AS5; Q9BS93; Q9NZE1;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=MAP3K12-binding inhibitory protein 1;
DE   AltName: Full=MAPK upstream kinase-binding inhibitory protein;
DE            Short=MUK-binding inhibitory protein;
GN   Name=MBIP; ORFNames=BM-015;
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 VARIANTS HIS-7 AND SER-22.
RC   TISSUE=Kidney;
RX   PubMed=10801814; DOI=10.1074/jbc.m001488200;
RA   Fukuyama K., Yoshida M., Yamashita A., Deyama T., Baba M., Suzuki A.,
RA   Mohri H., Ikezawa Z., Nakajima H., Hirai S., Ohno S.;
RT   "MAPK upstream kinase (MUK)-binding inhibitory protein, a negative
RT   regulator of MUK/Dual leucine zipper-bearing kinase/leucine zipper protein
RT   kinase.";
RL   J. Biol. Chem. 275:21247-21254(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS HIS-7 AND
RP   SER-22.
RC   TISSUE=Bone marrow;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for 300
RT   previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT   cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Placenta;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANTS
RP   HIS-7 AND SER-22.
RC   TISSUE=Bone marrow, and Urinary bladder;
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, 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   [8]
RP   FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX.
RX   PubMed=19103755; DOI=10.1128/mcb.01599-08;
RA   Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J.,
RA   Lill J.R., Zha J.;
RT   "The double-histone-acetyltransferase complex ATAC is essential for
RT   mammalian development.";
RL   Mol. Cell. Biol. 29:1176-1188(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY
RP   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   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-94, 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   [12]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-94 AND LYS-129, AND
RP   IDENTIFICATION BY MASS 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   [13]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-94; LYS-118; LYS-129; LYS-139;
RP   LYS-153; LYS-235; LYS-301; LYS-304 AND LYS-325, 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).
CC   -!- FUNCTION: Inhibits the MAP3K12 activity to induce the activation of the
CC       JNK/SAPK pathway. Component of the ATAC complex, a complex with histone
CC       acetyltransferase activity on histones H3 and H4.
CC       {ECO:0000269|PubMed:19103755}.
CC   -!- SUBUNIT: Component of the ADA2A-containing complex (ATAC), composed of
CC       KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1.
CC       In the complex, it probably interacts directly with KAT2A, KAT14 and
CC       WDR5. {ECO:0000269|PubMed:19103755}.
CC   -!- INTERACTION:
CC       Q9NS73; P00533: EGFR; NbExp=2; IntAct=EBI-741953, EBI-297353;
CC       Q9NS73; Q96HL7: EPB41L3; NbExp=3; IntAct=EBI-741953, EBI-749393;
CC       Q9NS73; P51116: FXR2; NbExp=3; IntAct=EBI-741953, EBI-740459;
CC       Q9NS73; Q9H8E8: KAT14; NbExp=6; IntAct=EBI-741953, EBI-750907;
CC       Q9NS73; Q9NS73: MBIP; NbExp=3; IntAct=EBI-741953, EBI-741953;
CC       Q9NS73; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-741953, EBI-742388;
CC       Q9NS73; Q13136: PPFIA1; NbExp=3; IntAct=EBI-741953, EBI-745426;
CC       Q9NS73; Q8N3L3: TXLNB; NbExp=4; IntAct=EBI-741953, EBI-6116822;
CC       Q9NS73; P61964: WDR5; NbExp=6; IntAct=EBI-741953, EBI-540834;
CC       Q9NS73-5; Q13515: BFSP2; NbExp=6; IntAct=EBI-10182361, EBI-10229433;
CC       Q9NS73-5; P24863: CCNC; NbExp=3; IntAct=EBI-10182361, EBI-395261;
CC       Q9NS73-5; Q14689-6: DIP2A; NbExp=3; IntAct=EBI-10182361, EBI-10233719;
CC       Q9NS73-5; Q8IY82: DRC7; NbExp=3; IntAct=EBI-10182361, EBI-10262896;
CC       Q9NS73-5; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-10182361, EBI-742102;
CC       Q9NS73-5; P22607: FGFR3; NbExp=3; IntAct=EBI-10182361, EBI-348399;
CC       Q9NS73-5; Q8WYH8: ING5; NbExp=3; IntAct=EBI-10182361, EBI-488533;
CC       Q9NS73-5; Q9H8E8: KAT14; NbExp=3; IntAct=EBI-10182361, EBI-750907;
CC       Q9NS73-5; O60333-2: KIF1B; NbExp=3; IntAct=EBI-10182361, EBI-10975473;
CC       Q9NS73-5; Q6P597: KLC3; NbExp=3; IntAct=EBI-10182361, EBI-1643885;
CC       Q9NS73-5; P25791: LMO2; NbExp=3; IntAct=EBI-10182361, EBI-739696;
CC       Q9NS73-5; P33993: MCM7; NbExp=3; IntAct=EBI-10182361, EBI-355924;
CC       Q9NS73-5; Q9NYP9: MIS18A; NbExp=3; IntAct=EBI-10182361, EBI-1104552;
CC       Q9NS73-5; Q96BY2: MOAP1; NbExp=3; IntAct=EBI-10182361, EBI-739825;
CC       Q9NS73-5; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-10182361, EBI-928842;
CC       Q9NS73-5; P07196: NEFL; NbExp=3; IntAct=EBI-10182361, EBI-475646;
CC       Q9NS73-5; P16284: PECAM1; NbExp=3; IntAct=EBI-10182361, EBI-716404;
CC       Q9NS73-5; O43933: PEX1; NbExp=3; IntAct=EBI-10182361, EBI-988601;
CC       Q9NS73-5; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-10182361, EBI-742388;
CC       Q9NS73-5; O15160: POLR1C; NbExp=3; IntAct=EBI-10182361, EBI-1055079;
CC       Q9NS73-5; P20339: RAB5A; NbExp=3; IntAct=EBI-10182361, EBI-399437;
CC       Q9NS73-5; P52306: RAP1GDS1; NbExp=3; IntAct=EBI-10182361, EBI-746389;
CC       Q9NS73-5; O75558: STX11; NbExp=3; IntAct=EBI-10182361, EBI-714135;
CC       Q9NS73-5; Q8IUE0: TGIF2LY; NbExp=3; IntAct=EBI-10182361, EBI-8063723;
CC       Q9NS73-5; P40222: TXLNA; NbExp=3; IntAct=EBI-10182361, EBI-359793;
CC       Q9NS73-5; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-10182361, EBI-6116822;
CC       Q9NS73-5; P08670: VIM; NbExp=3; IntAct=EBI-10182361, EBI-353844;
CC       Q9NS73-5; Q548N1: VPS28; NbExp=3; IntAct=EBI-10182361, EBI-10243107;
CC       Q9NS73-5; Q9UK41: VPS28; NbExp=3; IntAct=EBI-10182361, EBI-727424;
CC       Q9NS73-5; P61964: WDR5; NbExp=4; IntAct=EBI-10182361, EBI-540834;
CC       Q9NS73-5; O76024: WFS1; NbExp=3; IntAct=EBI-10182361, EBI-720609;
CC       Q9NS73-5; Q9Y649; NbExp=3; IntAct=EBI-10182361, EBI-25900580;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shows a cytoplasmic
CC       localization when coexpressed with MAP3K12.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9NS73-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NS73-2; Sequence=VSP_010266;
CC       Name=3;
CC         IsoId=Q9NS73-3; Sequence=VSP_010265;
CC       Name=4;
CC         IsoId=Q9NS73-5; Sequence=VSP_040134;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. High expression seen in the heart and
CC       lung.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD62615.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB038523; BAA94083.1; -; mRNA.
DR   EMBL; AF208857; AAF64271.1; -; mRNA.
DR   EMBL; BX248287; CAD62615.1; ALT_INIT; mRNA.
DR   EMBL; AL137226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005197; AAH05197.1; -; mRNA.
DR   EMBL; BC016821; AAH16821.1; -; mRNA.
DR   CCDS; CCDS45096.1; -. [Q9NS73-5]
DR   CCDS; CCDS76672.1; -. [Q9NS73-3]
DR   CCDS; CCDS9658.1; -. [Q9NS73-1]
DR   RefSeq; NP_001138363.1; NM_001144891.1. [Q9NS73-5]
DR   RefSeq; NP_001295039.1; NM_001308110.1. [Q9NS73-3]
DR   RefSeq; NP_057670.2; NM_016586.2. [Q9NS73-1]
DR   AlphaFoldDB; Q9NS73; -.
DR   SMR; Q9NS73; -.
DR   BioGRID; 119612; 170.
DR   ComplexPortal; CPX-1004; PCAF-containing ATAC complex.
DR   ComplexPortal; CPX-997; GCN5-containing ATAC complex.
DR   CORUM; Q9NS73; -.
DR   IntAct; Q9NS73; 114.
DR   MINT; Q9NS73; -.
DR   STRING; 9606.ENSP00000399718; -.
DR   GlyGen; Q9NS73; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NS73; -.
DR   PhosphoSitePlus; Q9NS73; -.
DR   BioMuta; MBIP; -.
DR   DMDM; 160112798; -.
DR   EPD; Q9NS73; -.
DR   jPOST; Q9NS73; -.
DR   MassIVE; Q9NS73; -.
DR   MaxQB; Q9NS73; -.
DR   PaxDb; 9606-ENSP00000399718; -.
DR   PeptideAtlas; Q9NS73; -.
DR   ProteomicsDB; 82502; -. [Q9NS73-1]
DR   ProteomicsDB; 82503; -. [Q9NS73-2]
DR   ProteomicsDB; 82504; -. [Q9NS73-3]
DR   ProteomicsDB; 82505; -. [Q9NS73-5]
DR   Pumba; Q9NS73; -.
DR   Antibodypedia; 166; 168 antibodies from 26 providers.
DR   DNASU; 51562; -.
DR   Ensembl; ENST00000318473.11; ENSP00000324444.5; ENSG00000151332.20. [Q9NS73-5]
DR   Ensembl; ENST00000359527.11; ENSP00000352517.5; ENSG00000151332.20. [Q9NS73-3]
DR   Ensembl; ENST00000416007.9; ENSP00000399718.2; ENSG00000151332.20. [Q9NS73-1]
DR   GeneID; 51562; -.
DR   KEGG; hsa:51562; -.
DR   MANE-Select; ENST00000416007.9; ENSP00000399718.2; NM_016586.3; NP_057670.2.
DR   UCSC; uc001wtm.2; human. [Q9NS73-1]
DR   AGR; HGNC:20427; -.
DR   CTD; 51562; -.
DR   DisGeNET; 51562; -.
DR   GeneCards; MBIP; -.
DR   HGNC; HGNC:20427; MBIP.
DR   HPA; ENSG00000151332; Low tissue specificity.
DR   MIM; 609431; gene.
DR   neXtProt; NX_Q9NS73; -.
DR   OpenTargets; ENSG00000151332; -.
DR   PharmGKB; PA134929415; -.
DR   VEuPathDB; HostDB:ENSG00000151332; -.
DR   eggNOG; ENOG502R8QG; Eukaryota.
DR   GeneTree; ENSGT00510000047831; -.
DR   HOGENOM; CLU_069631_0_0_1; -.
DR   InParanoid; Q9NS73; -.
DR   OMA; HKSNSML; -.
DR   OrthoDB; 5395458at2759; -.
DR   PhylomeDB; Q9NS73; -.
DR   TreeFam; TF331763; -.
DR   PathwayCommons; Q9NS73; -.
DR   Reactome; R-HSA-3214847; HATs acetylate histones.
DR   Reactome; R-HSA-9772755; Formation of WDR5-containing histone-modifying complexes.
DR   SignaLink; Q9NS73; -.
DR   BioGRID-ORCS; 51562; 17 hits in 1154 CRISPR screens.
DR   ChiTaRS; MBIP; human.
DR   GenomeRNAi; 51562; -.
DR   Pharos; Q9NS73; Tbio.
DR   PRO; PR:Q9NS73; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9NS73; Protein.
DR   Bgee; ENSG00000151332; Expressed in left lobe of thyroid gland and 194 other cell types or tissues.
DR   ExpressionAtlas; Q9NS73; baseline and differential.
DR   GO; GO:0140672; C:ATAC complex; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0072686; C:mitotic spindle; NAS:ComplexPortal.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004860; F:protein kinase inhibitor activity; IDA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:GO_Central.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IDA:GO_Central.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR   GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:ComplexPortal.
DR   GO; GO:0045995; P:regulation of embryonic development; ISO:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0090043; P:regulation of tubulin deacetylation; IMP:ComplexPortal.
DR   Genevisible; Q9NS73; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT   CHAIN           1..344
FT                   /note="MAP3K12-binding inhibitory protein 1"
FT                   /id="PRO_0000096269"
FT   REGION          172..344
FT                   /note="Interaction with MAP3K12"
FT   REGION          271..285
FT                   /note="Leucine-zipper 1"
FT                   /evidence="ECO:0000255"
FT   REGION          314..329
FT                   /note="Leucine-zipper 2"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         301
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LQ1"
FT   CROSSLNK        94
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        118
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        129
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        139
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        153
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        235
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        301
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        304
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        325
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         264..344
FT                   /note="GGPVPRDIYQRIKKLEDKILELEGISPEYFQSVSFSGKRRKVQPPQQNYSLA
FT                   ELDEKISALKQALLRKSREAESMATHHLP -> ELFWKKKKSSTTSTELFTG (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_010265"
FT   VAR_SEQ         298..344
FT                   /note="FSGKRRKVQPPQQNYSLAELDEKISALKQALLRKSREAESMATHHLP -> L
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11042152"
FT                   /id="VSP_010266"
FT   VAR_SEQ         309
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040134"
FT   VARIANT         7
FT                   /note="L -> H (in dbSNP:rs2899849)"
FT                   /evidence="ECO:0000269|PubMed:10801814,
FT                   ECO:0000269|PubMed:11042152, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_018449"
FT   VARIANT         22
FT                   /note="R -> S (in dbSNP:rs3168891)"
FT                   /evidence="ECO:0000269|PubMed:10801814,
FT                   ECO:0000269|PubMed:11042152, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_034093"
FT   CONFLICT        218
FT                   /note="N -> Y (in Ref. 5; AAH05197)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   344 AA;  39281 MW;  9DABB35CA8695C02 CRC64;
     MAAATELNRP SSGDRNLERR CRPNLSREVL YEIFRSLHTL VGQLDLRDDV VKITIDWNKL
     QSLSAFQPAL LFSALEQHIL YLQPFLAKLQ SPIKEENTTA VEEIGRTEMG NKNEVNDKFS
     IGDLQEEEKH KESDLRDVKK TQIHFDPEVV QIKAGKAEID RRISAFIERK QAEINENNVR
     EFCNVIDCNQ ENSCARTDAI FTPYPGFKSH VKVSRVVNTY GPQTRPEGIP GSGHKPNSML
     RDCGNQAVEE RLQNIEAHLR LQTGGPVPRD IYQRIKKLED KILELEGISP EYFQSVSFSG
     KRRKVQPPQQ NYSLAELDEK ISALKQALLR KSREAESMAT HHLP
//