ARI5B_MOUSE
ID ARI5B_MOUSE Reviewed; 1188 AA.
AC Q8BM75; E9Q523; Q8C0E0; Q8K4G8; Q8K4L9; Q9CU78; Q9JIX4;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=AT-rich interactive domain-containing protein 5B;
DE Short=ARID domain-containing protein 5B;
DE AltName: Full=Developmentally and sexually retarded with transient immune abnormalities protein;
DE Short=Desrt;
DE AltName: Full=MRF1-like;
DE AltName: Full=Modulator recognition factor protein 2;
DE Short=MRF-2;
GN Name=Arid5b; Synonyms=Desrt, Mrf2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=12215486; DOI=10.1161/01.res.0000033593.05545.7b;
RA Watanabe M., Layne M.D., Hsieh C.-M., Maemura K., Gray S., Lee M.-E.,
RA Jain M.K.;
RT "Regulation of smooth muscle cell differentiation by AT-rich interaction
RT domain transcription factors Mrf2alpha and Mrf2beta.";
RL Circ. Res. 91:382-389(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-253 AND 528-1188.
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-819 (ISOFORM 1), DNA-BINDING, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6 X CBA; TISSUE=Lung, and Placenta;
RX PubMed=11483573; DOI=10.1101/gr.168801;
RA Lahoud M.H., Ristevski S., Venter D.J., Jermiin L.S., Bertoncello I.,
RA Zavarsek S., Hasthorpe S., Drago J., de Kretser D., Hertzog P.J., Kola I.;
RT "Gene targeting of Desrt, a novel ARID class DNA-binding protein, causes
RT growth retardation and abnormal development of reproductive organs.";
RL Genome Res. 11:1327-1334(2001).
RN [5]
RP PROTEIN SEQUENCE OF 374-397, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=11404092; DOI=10.1016/s0925-4773(01)00370-7;
RA Ristevski S., Tam P.P.L., Kola I., Hertzog P.;
RT "Desrt, an AT-rich interaction domain family transcription factor gene, is
RT an early marker for nephrogenic mesoderm and is expressed dynamically
RT during mouse limb development.";
RL Mech. Dev. 104:139-142(2001).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14651970; DOI=10.1016/j.bbrc.2003.11.026;
RA Whitson R.H., Tsark W., Huang T.H., Itakura K.;
RT "Neonatal mortality and leanness in mice lacking the ARID transcription
RT factor Mrf-2.";
RL Biochem. Biophys. Res. Commun. 312:997-1004(2003).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=18070594; DOI=10.1016/j.bbrc.2007.12.002;
RA Dong J., Ishimori N., Paigen B., Tsutsui H., Fujii S.;
RT "Role of modulator recognition factor 2 in adipogenesis and leptin
RT expression in 3T3-L1 cells.";
RL Biochem. Biophys. Res. Commun. 366:551-555(2008).
RN [9]
RP FUNCTION.
RX PubMed=17962384; DOI=10.1210/me.2007-0271;
RA Yamakawa T., Whitson R.H., Li S.L., Itakura K.;
RT "Modulator recognition factor-2 is required for adipogenesis in mouse
RT embryo fibroblasts and 3T3-L1 cells.";
RL Mol. Endocrinol. 22:441-453(2008).
RN [10]
RP FUNCTION.
RX PubMed=19913508; DOI=10.1016/j.bbrc.2009.11.049;
RA Yamakawa T., Sugimoto K., Whitson R.H., Itakura K.;
RT "Modulator recognition factor-2 regulates triglyceride metabolism in
RT adipocytes.";
RL Biochem. Biophys. Res. Commun. 391:277-281(2010).
CC -!- FUNCTION: Transcription coactivator that binds to the 5'-AATA[CT]-3'
CC core sequence and plays a key role in adipogenesis and liver
CC development. Acts by forming a complex with phosphorylated PHF2, which
CC mediates demethylation at Lys-337, leading to target the PHF2-ARID5B
CC complex to target promoters, where PHF2 mediates demethylation of
CC dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription
CC activation of target genes. The PHF2-ARID5B complex acts as a
CC coactivator of HNF4A in liver (By similarity). Required for
CC adipogenesis: regulates triglyceride metabolism in adipocytes by
CC regulating expression of adipogenic genes. Overexpression leads to
CC induction of smooth muscle marker genes, suggesting that it may also
CC act as a regulator of smooth muscle cell differentiation and
CC proliferation. {ECO:0000250, ECO:0000269|PubMed:12215486,
CC ECO:0000269|PubMed:14651970, ECO:0000269|PubMed:17962384,
CC ECO:0000269|PubMed:18070594, ECO:0000269|PubMed:19913508}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000269|PubMed:12215486}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Mrf2alpha, Alpha;
CC IsoId=Q8BM75-1; Sequence=Displayed;
CC Name=2; Synonyms=Mrf2beta, Beta;
CC IsoId=Q8BM75-2; Sequence=VSP_009357, VSP_009358;
CC Name=3;
CC IsoId=Q8BM75-3; Sequence=VSP_009359, VSP_009360;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in lung, heart, small
CC intestine, kidney, muscle and brain. Also expressed in spleen, thymus,
CC endocrine organs and in uterus and testis.
CC {ECO:0000269|PubMed:11483573, ECO:0000269|PubMed:12215486}.
CC -!- DEVELOPMENTAL STAGE: First detected in the intermediate plate mesoderm,
CC and subsequently in the nephrogenic cords of the urogenital ridges.
CC Expressed in the developing limb. Also expressed in the myotome of the
CC somites from 9.5 dpc, the oro-nasopharyngeal ectoderm and underlying
CC mesenchyme, otic vesicles, the gut and its derivatives, and transiently
CC in the liver at 11.5 dpc. {ECO:0000269|PubMed:11404092}.
CC -!- INDUCTION: During smooth muscle cell differentiation in vitro. Upon
CC adipogenesis. {ECO:0000269|PubMed:12215486,
CC ECO:0000269|PubMed:18070594}.
CC -!- DOMAIN: The ARID domain mediates the interaction with DNA.
CC -!- PTM: Methylation at Lys-337 prevents DNA-binding. Demethylation by PHF2
CC promotes recruitment of the PHF2-ARID5B complex to promoters (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: High rate of neonatal mortality. Embryonic growth
CC or birth weight are not effected, while lipid accumulation is severely
CC reduced in brown adipose neonates at 24 hours of age. Mice weigh
CC significantly less than controls from postnatal day 5 onward. Adult
CC mice are lean, with significant reductions in brown and white adipose
CC tissues, and in the percentage of body fat. Mice are also resistant to
CC weight gains and obesity when maintained on high-fat diets.
CC {ECO:0000269|PubMed:14651970}.
CC -!- SIMILARITY: Belongs to the ARID5B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF89682.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF89682.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC28778.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF280065; AAM93269.1; -; mRNA.
DR EMBL; AF401550; AAM93282.1; -; mRNA.
DR EMBL; AK017396; BAB30727.1; -; mRNA.
DR EMBL; AK031596; BAC27467.1; -; mRNA.
DR EMBL; AK034633; BAC28778.1; ALT_INIT; mRNA.
DR EMBL; AC122293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF169968; AAF89682.1; ALT_SEQ; mRNA.
DR CCDS; CCDS35929.1; -. [Q8BM75-1]
DR RefSeq; NP_076087.2; NM_023598.2. [Q8BM75-1]
DR AlphaFoldDB; Q8BM75; -.
DR BMRB; Q8BM75; -.
DR SMR; Q8BM75; -.
DR BioGRID; 214670; 3.
DR IntAct; Q8BM75; 1.
DR MINT; Q8BM75; -.
DR STRING; 10090.ENSMUSP00000020106; -.
DR iPTMnet; Q8BM75; -.
DR PhosphoSitePlus; Q8BM75; -.
DR EPD; Q8BM75; -.
DR jPOST; Q8BM75; -.
DR MaxQB; Q8BM75; -.
DR PaxDb; Q8BM75; -.
DR PeptideAtlas; Q8BM75; -.
DR PRIDE; Q8BM75; -.
DR ProteomicsDB; 265096; -. [Q8BM75-1]
DR ProteomicsDB; 265097; -. [Q8BM75-2]
DR ProteomicsDB; 265098; -. [Q8BM75-3]
DR Antibodypedia; 2974; 123 antibodies from 24 providers.
DR DNASU; 71371; -.
DR Ensembl; ENSMUST00000218532; ENSMUSP00000151665; ENSMUSG00000019947. [Q8BM75-2]
DR Ensembl; ENSMUST00000219238; ENSMUSP00000151227; ENSMUSG00000019947. [Q8BM75-1]
DR GeneID; 71371; -.
DR KEGG; mmu:71371; -.
DR UCSC; uc007fmf.1; mouse. [Q8BM75-2]
DR UCSC; uc007fmg.1; mouse. [Q8BM75-1]
DR UCSC; uc007fmj.1; mouse. [Q8BM75-3]
DR CTD; 84159; -.
DR MGI; MGI:2175912; Arid5b.
DR VEuPathDB; HostDB:ENSMUSG00000019947; -.
DR eggNOG; KOG2744; Eukaryota.
DR GeneTree; ENSGT00940000161078; -.
DR HOGENOM; CLU_007985_0_0_1; -.
DR InParanoid; Q8BM75; -.
DR OMA; YRQTEHH; -.
DR OrthoDB; 368297at2759; -.
DR TreeFam; TF324725; -.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR BioGRID-ORCS; 71371; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Arid5b; mouse.
DR PRO; PR:Q8BM75; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BM75; protein.
DR Bgee; ENSMUSG00000019947; Expressed in animal zygote and 262 other tissues.
DR ExpressionAtlas; Q8BM75; baseline and differential.
DR Genevisible; Q8BM75; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0060612; P:adipose tissue development; IMP:UniProtKB.
DR GO; GO:0030325; P:adrenal gland development; IMP:MGI.
DR GO; GO:0048468; P:cell development; IMP:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
DR GO; GO:0060613; P:fat pad development; IMP:MGI.
DR GO; GO:0008585; P:female gonad development; IMP:MGI.
DR GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0048644; P:muscle organ morphogenesis; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IMP:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR030408; ARID5B.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR PANTHER; PTHR13964:SF37; PTHR13964:SF37; 1.
DR Pfam; PF01388; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1188
FT /note="AT-rich interactive domain-containing protein 5B"
FT /id="PRO_0000200582"
FT DOMAIN 319..411
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT REGION 251..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT MOD_RES 337
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT MOD_RES 1032
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 446
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 494
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 496
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 767
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 774
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 803
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 810
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 893
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 916
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 920
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 935
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 988
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 1000
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 1013
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 1055
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 1070
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT VAR_SEQ 1..243
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12215486"
FT /id="VSP_009357"
FT VAR_SEQ 244
FT /note="F -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12215486"
FT /id="VSP_009358"
FT VAR_SEQ 245..276
FT /note="APNLKGRPRKKKTCPQRRDSFSGSKDPNNNCD -> GECFSFTLFETRPNES
FT LFSIHGVSSAGEQGLV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009359"
FT VAR_SEQ 277..1188
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009360"
FT CONFLICT 111
FT /note="K -> T (in Ref. 3; AAF89682)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="A -> G (in Ref. 3; AAF89682)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="K -> E (in Ref. 1; AAM93282/AAM93269 and 3;
FT AAF89682)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="N -> S (in Ref. 1; AAM93282/AAM93269 and 3;
FT AAF89682)"
FT /evidence="ECO:0000305"
FT CONFLICT 928
FT /note="T -> A (in Ref. 1; AAM93282/AAM93269)"
FT /evidence="ECO:0000305"
FT CONFLICT 1056
FT /note="G -> S (in Ref. 1; AAM93282/AAM93269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1188 AA; 131837 MW; F0B1A99D3E88D71F CRC64;
MEPNSLQWVG SPCGLHGPYI FYKAFQFHLE GKPRILSLGD FFFVRCTPKD PICIAELQLL
WEERTSRQLL SSSKLYFLPE DTPQGRNSDH GEDEVIAVSE KVIVKLEDLV KWAHSDFSKW
RCGLRATPVK TEAFGRNGQK EALLRYRQST LNSGLNFKDV LKEKADLGED EEETNVIVLS
YPQYCRYRSM LKRIQDKPSS ILTDQFALAL GGIAVVSRNP QILYCRDTFD HPTLIENESV
CDEFAPNLKG RPRKKKTCPQ RRDSFSGSKD PNNNCDGKVI SKVKGEARSA LTKPKNNHNN
CKKTSNEEKP KLSIGEECRA DEQAFLVALY KYMKERKTPI ERIPYLGFKQ INLWTMFQAA
QKLGGYETIT ARRQWKHIYD ELGGNPGSTS AATCTRRHYE RLILPYERFI KGEEDKPLPP
IKPRKQENNT QENENKTKVS GNKRIKQEMA KNKKEKENTP KPQDTSEVSS EQRKEEETLN
HKSAPEPLPA PEVKGKPEGH KDLGARAPVS RADPEKANET DQGSNSEKEA EEMGDKGLAP
LLPSPPLPPE KDSAPTPGAG KQPLASPSTQ MDSKQEAKPC CFTESPEKDL QGAPFSSFSA
TKPPLTSQNE AEEEQLPATA NYIANCTVKV DQLGSDDIHT ALKQTPKVLV VQSFDMFKDK
DLTGPMNENH GLNYTPLLYS RGNPGIMSPL AKKKLLSQVS GASLSSSYPY GSPPPLISKK
KLIAREDLCS GLSQGHHSQS SDHTAVSRPS VIQHVQSFKN KASEDRKSIN DIFKHDKLSR
SDAHRCGFSK HQLGSLADSY ILKQETQEGK DKLLEKRAVS HAHVPSFLAD FYSSPHLHSL
YRHTEHHLHN EQSSKYAARD AYQESENGAF LSHKHPEKIH VNYLASLHLQ DKKVAAAEAS
TDDQPTDLSL PKNPHKLTSK VLGLAHSTSG SQEIKGASQF QVVSNQSRDC HPKACRVSPM
TMSGPKKYPE SLARSGKPHQ VRLENFRKME GMVHPILHRK MSPQNIGAAR PIKRSLEDLD
LVIAGKKARA VSPLDPAKEA SGKEKASEQE SEGNKGAYGG HSGAASEGHK LPLSTPIFPG
LYSGSLCNSG LNSRLPAGYS HSLQYLKNQT VLSPLMQPLA FHSLVMQRGI FTSPTNSQQL
YRHLAAATPV GSSYGDLLHN SIYPLAGINP QAAFPSSQLS SVHPSTKL
