MBIP1_HUMAN
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 03-AUG-2022, entry version 169.
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; 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; 159.
DR ComplexPortal; CPX-1004; PCAF-containing ATAC complex.
DR ComplexPortal; CPX-997; GCN5-containing ATAC complex.
DR CORUM; Q9NS73; -.
DR IntAct; Q9NS73; 112.
DR MINT; Q9NS73; -.
DR STRING; 9606.ENSP00000399718; -.
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; Q9NS73; -.
DR PeptideAtlas; Q9NS73; -.
DR PRIDE; Q9NS73; -.
DR ProteomicsDB; 82502; -. [Q9NS73-1]
DR ProteomicsDB; 82503; -. [Q9NS73-2]
DR ProteomicsDB; 82504; -. [Q9NS73-3]
DR ProteomicsDB; 82505; -. [Q9NS73-5]
DR Antibodypedia; 166; 146 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 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 PhylomeDB; Q9NS73; -.
DR TreeFam; TF331763; -.
DR PathwayCommons; Q9NS73; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q9NS73; -.
DR BioGRID-ORCS; 51562; 14 hits in 1074 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 193 other tissues.
DR ExpressionAtlas; Q9NS73; baseline and differential.
DR Genevisible; Q9NS73; HS.
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; IC: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:0043966; P:histone H3 acetylation; IDA:BHF-UCL.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:ComplexPortal.
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:0045995; P:regulation of embryonic development; IC:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; IMP:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IMP:ComplexPortal.
DR InterPro; IPR026062; MBIP.
DR PANTHER; PTHR23404:SF3; PTHR23404:SF3; 1.
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
