MBD1_MOUSE
ID MBD1_MOUSE Reviewed; 636 AA.
AC Q9Z2E2; Q3TMA4; Q3U101; Q6NSW0; Q792D6; Q8CCL9; Q9DC19;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Methyl-CpG-binding domain protein 1 {ECO:0000305};
DE AltName: Full=Methyl-CpG-binding protein MBD1;
GN Name=Mbd1 {ECO:0000312|MGI:MGI:1333811};
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] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=9774669; DOI=10.1128/mcb.18.11.6538;
RA Hendrich B., Bird A.;
RT "Identification and characterization of a family of mammalian methyl-CpG
RT binding proteins.";
RL Mol. Cell. Biol. 18:6538-6547(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=10441743; DOI=10.1007/s003359901112;
RA Hendrich B., Abbott C., McQueen H., Chambers D., Cross S.H., Bird A.;
RT "Genomic structure and chromosomal mapping of the murine and human mbd1,
RT mbd2, mbd3, and mbd4 genes.";
RL Mamm. Genome 10:906-912(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung, Olfactory bulb, and Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 SUBCELLULAR LOCATION.
RX PubMed=12697822; DOI=10.1128/mcb.23.9.3226-3236.2003;
RA Reese B.E., Bachman K.E., Baylin S.B., Rountree M.R.;
RT "The methyl-CpG binding protein MBD1 interacts with the p150 subunit of
RT chromatin assembly factor 1.";
RL Mol. Cell. Biol. 23:3226-3236(2003).
RN [6]
RP FUNCTION, AND ALTERNATIVE SPLICING.
RX PubMed=15060159; DOI=10.1128/mcb.24.8.3387-3395.2004;
RA Joergensen H.F., Ben-Porath I., Bird A.P.;
RT "Mbd1 is recruited to both methylated and nonmethylated CpGs via distinct
RT DNA binding domains.";
RL Mol. Cell. Biol. 24:3387-3395(2004).
RN [7]
RP INTERACTION WITH TENM1, AND SUBCELLULAR LOCATION.
RX PubMed=15777793; DOI=10.1016/j.yexcr.2004.12.020;
RA Nunes S.M., Ferralli J., Choi K., Brown-Luedi M., Minet A.D.,
RA Chiquet-Ehrismann R.;
RT "The intracellular domain of teneurin-1 interacts with MBD1 and CAP/ponsin
RT resulting in subcellular codistribution and translocation to the nuclear
RT matrix.";
RL Exp. Cell Res. 305:122-132(2005).
CC -!- FUNCTION: Transcriptional repressor that binds CpG islands in promoters
CC where the DNA is methylated at position 5 of cytosine within CpG
CC dinucleotides. Binding is abolished by the presence of 7-mG that is
CC produced by DNA damage by methylmethanesulfonate (MMS). Acts as
CC transcriptional repressor and plays a role in gene silencing by
CC recruiting ATF7IP, which in turn recruits factors such as the histone
CC methyltransferase SETDB1. Probably forms a complex with SETDB1 and
CC ATF7IP that represses transcription and couples DNA methylation and
CC histone 'Lys-9' trimethylation. Isoform 1 can also repress
CC transcription from unmethylated promoters.
CC {ECO:0000269|PubMed:15060159, ECO:0000269|PubMed:9774669}.
CC -!- SUBUNIT: Interacts with OASL, ATF7IP, ATF7IP2 and BAHD1. Binds CHAF1A
CC and the SUV39H1-CBX5 complex via the MBD domain. Binds MGP via the TRD
CC domain. May be part of the MeCP1 complex. During DNA replication, it
CC recruits SETDB1 to form a S phase-specific complex that facilitates
CC methylation of H3 'Lys-9' during replication-coupled chromatin assembly
CC and is at least composed of the CAF-1 subunit CHAF1A, MBD1 and SETDB1
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with the Ten-1 ICD form of TENM1.
CC {ECO:0000269|PubMed:15777793}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus matrix. Nucleus speckle.
CC Chromosome. Note=Nuclear, in a punctate pattern. Associated with
CC euchromatic regions of the chromosomes. Colocalizes with the Ten-1 ICD
CC form of TENM1 in foci associated with the nuclear matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=MBD1a;
CC IsoId=Q9Z2E2-1; Sequence=Displayed;
CC Name=2; Synonyms=MBD1b;
CC IsoId=Q9Z2E2-2; Sequence=VSP_011072, VSP_011073;
CC Name=3; Synonyms=MBD1d;
CC IsoId=Q9Z2E2-3; Sequence=VSP_011072, VSP_011073, VSP_011074,
CC VSP_011075;
CC Name=4;
CC IsoId=Q9Z2E2-4; Sequence=VSP_011073;
CC Name=5;
CC IsoId=Q9Z2E2-5; Sequence=VSP_011073, VSP_011074, VSP_011075;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, liver and brain.
CC Detected at lower levels in heart, lung, skeletal muscle, spleen and
CC testis. {ECO:0000269|PubMed:9774669}.
CC -!- DOMAIN: The methyl-CpG-binding domain (MBD) functions both in binding
CC to methylated DNA and in protein interactions.
CC {ECO:0000250|UniProtKB:Q9UIS9}.
CC -!- DOMAIN: The third CXXC-type zinc finger mediates binding to DNA
CC containing unmethylated CpG dinucleotides.
CC {ECO:0000250|UniProtKB:Q9UIS9}.
CC -!- DOMAIN: The transcriptional repression domain (TRD) is involved in
CC transcription repression and in protein interactions.
CC {ECO:0000250|UniProtKB:Q9UIS9}.
CC -!- PTM: Sumoylated, sumoylation may increase interaction with ATF7IP.
CC {ECO:0000250|UniProtKB:Q9UIS9}.
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DR EMBL; AF072240; AAC68869.1; -; mRNA.
DR EMBL; AF120978; AAD48908.1; -; Genomic_DNA.
DR EMBL; AK004624; BAB23419.1; -; mRNA.
DR EMBL; AK032535; BAC27914.1; -; mRNA.
DR EMBL; AK156401; BAE33700.1; -; mRNA.
DR EMBL; AK166042; BAE38538.1; -; mRNA.
DR EMBL; BC069837; AAH69837.1; -; mRNA.
DR CCDS; CCDS50321.1; -. [Q9Z2E2-2]
DR RefSeq; NP_038622.2; NM_013594.2.
DR AlphaFoldDB; Q9Z2E2; -.
DR SMR; Q9Z2E2; -.
DR BioGRID; 201330; 1.
DR IntAct; Q9Z2E2; 1.
DR MINT; Q9Z2E2; -.
DR iPTMnet; Q9Z2E2; -.
DR PhosphoSitePlus; Q9Z2E2; -.
DR EPD; Q9Z2E2; -.
DR jPOST; Q9Z2E2; -.
DR MaxQB; Q9Z2E2; -.
DR PeptideAtlas; Q9Z2E2; -.
DR PRIDE; Q9Z2E2; -.
DR ProteomicsDB; 295963; -. [Q9Z2E2-1]
DR ProteomicsDB; 295964; -. [Q9Z2E2-2]
DR ProteomicsDB; 295965; -. [Q9Z2E2-3]
DR ProteomicsDB; 295966; -. [Q9Z2E2-4]
DR ProteomicsDB; 295967; -. [Q9Z2E2-5]
DR DNASU; 17190; -.
DR GeneID; 17190; -.
DR KEGG; mmu:17190; -.
DR UCSC; uc008fpj.2; mouse. [Q9Z2E2-2]
DR UCSC; uc008fpk.1; mouse. [Q9Z2E2-5]
DR UCSC; uc012bex.1; mouse. [Q9Z2E2-1]
DR CTD; 4152; -.
DR MGI; MGI:1333811; Mbd1.
DR InParanoid; Q9Z2E2; -.
DR OrthoDB; 1431783at2759; -.
DR PhylomeDB; Q9Z2E2; -.
DR TreeFam; TF350557; -.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR BioGRID-ORCS; 17190; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Mbd1; mouse.
DR PRO; PR:Q9Z2E2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z2E2; protein.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; ISO:MGI.
DR GO; GO:0008327; F:methyl-CpG binding; ISO:MGI.
DR GO; GO:0045322; F:unmethylated CpG binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR002857; Znf_CXXC.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF02008; zf-CXXC; 3.
DR SMART; SM00391; MBD; 1.
DR SUPFAM; SSF54171; SSF54171; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS51058; ZF_CXXC; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..636
FT /note="Methyl-CpG-binding domain protein 1"
FT /id="PRO_0000096259"
FT DOMAIN 1..69
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT ZN_FING 187..234
FT /note="CXXC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT ZN_FING 235..281
FT /note="CXXC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT ZN_FING 348..396
FT /note="CXXC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT REGION 75..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..612
FT /note="Transcriptional repression domain (TRD)"
FT /evidence="ECO:0000250|UniProtKB:Q9UIS9"
FT MOTIF 84..88
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 80..94
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UIS9"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UIS9"
FT CROSSLNK 293
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UIS9"
FT CROSSLNK 443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UIS9"
FT CROSSLNK 461
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UIS9"
FT CROSSLNK 520
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UIS9"
FT CROSSLNK 559
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UIS9"
FT VAR_SEQ 142
FT /note="S -> SSSASASAS (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011072"
FT VAR_SEQ 345..400
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011073"
FT VAR_SEQ 614..625
FT /note="LHKLLAVNEKEY -> SKDLKNPEAKMQ (in isoform 3 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011074"
FT VAR_SEQ 626..636
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011075"
FT CONFLICT 109
FT /note="I -> R (in Ref. 3; BAB23419 and 4; AAH69837)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="H -> R (in Ref. 4; AAH69837)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="R -> Q (in Ref. 1; AAC68869, 2; AAD48908 and 3;
FT BAE33700)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="T -> A (in Ref. 1; AAC68869, 2; AAD48908 and 3;
FT BAE33700)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="S -> C (in Ref. 1; AAC68869, 2; AAD48908 and 3;
FT BAE33700)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="S -> P (in Ref. 1; AAC68869, 2; AAD48908 and 3;
FT BAE33700)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="L -> F (in Ref. 4; AAH69837)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9Z2E2-2:144
FT /note="S -> F (in Ref. 4; AAH69837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 70023 MW; 02D8B94EBD522F65 CRC64;
MAESWQDCPA LGPGWKRRES FRKSGASFGR SDIYYQSPTG EKIRSKVELT RYLGPACDLT
LFDFRQGTLC HPIPKTHPLA VPSKKKKKPS KPAKTKKQQV GLQRSEVRIE TPQGEYKAPT
ATALASLSVS ASASSSASAS ASASSHAPVC CENCGIHFSW DGVKRQRLKT LCKDCRAQRI
AFNREQRMFK RVGCGDCAAC LVKEDCGVCS TCRLQLPSDV ASGLYCKCER RRCLRIMEKS
RGCGVCRGCQ TQEDCGHCCI CLRSPRPGLK RQWRCLQRRC FWGKRDSSKR GSKVASQRHS
QAPPLPPHPA SQYTEPTELH ISDIAPTSPA EFIYYCVDED EDELQPYTNQ RQNRKCGACA
ACLRRMDCGR CDFCCDKPKF GGGNQKRQKC RWRQCLQFAM KRLLPSAGSG SGEGAGLRPY
QTHQTHQKRP ASARQLQLSS PLKAPWAVVT APPGPVRDSR KQQAGRGSVL PQPDTDFVFL
QEGTSSAMQM PGTAAASTEV PVQAAQCSAP SWVVALPQVK QETADAPEEW TAVTTFLTSS
TLQSGFPSKA ADPDLSPVKQ EPPGPEEDGE EKKDDVSETT PAEEIGGVGT PVITEIFSLG
GTRLRDAEAW LPRLHKLLAV NEKEYFTELQ LKEEVL
