MGAP_MOUSE
ID MGAP_MOUSE Reviewed; 3003 AA.
AC A2AWL7; A2AWL6; Q3TS36; Q6A056; Q8BQX1; Q8CCL4; Q9QXJ5;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=MAX gene-associated protein;
GN Name=Mga; Synonyms=Kiaa4252;
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).
RX PubMed=10601024; DOI=10.1093/emboj/18.24.7019;
RA Hurlin P.J., Steingrimsson E., Copeland N.G., Jenkins N.A., Eisenman R.N.;
RT "Mga, a dual-specificity transcription factor that interacts with Max and
RT contains a T-domain DNA-binding motif.";
RL EMBO J. 18:7019-7028(1999).
RN [2]
RP ERRATUM OF PUBMED:10601024.
RA Hurlin P.J., Steingrimsson E., Copeland N.G., Jenkins N.A., Eisenman R.N.;
RL EMBO J. 19:3841-3841(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1129 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1-1129 (ISOFORM 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Colon, Corpora quadrigemina, Embryo, and Olfactory bulb;
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-2465 (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
CC -!- FUNCTION: Functions as a dual-specificity transcription factor,
CC regulating the expression of both MAX-network and T-box family target
CC genes. Functions as a repressor or an activator. Binds to 5'-
CC AATTTCACACCTAGGTGTGAAATT-3' core sequence and seems to regulate MYC-MAX
CC target genes. Suppresses transcriptional activation by MYC and inhibits
CC MYC-dependent cell transformation. Function activated by
CC heterodimerization with MAX. This heterodimerization serves the dual
CC function of both generating an E-box-binding heterodimer and
CC simultaneously blocking interaction of a corepressor.
CC -!- SUBUNIT: Component of some MLL1/MLL complex, at least composed of the
CC core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well
CC as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
CC LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10. Interacts with ZMYND11 (By similarity). Interacts with MAX.
CC Requires heterodimerization with MAX for E-box binding. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A2AWL7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AWL7-2; Sequence=VSP_034539, VSP_034540, VSP_034541,
CC VSP_034542;
CC Name=3;
CC IsoId=A2AWL7-3; Sequence=VSP_034538;
CC Name=4;
CC IsoId=A2AWL7-4; Sequence=VSP_034536, VSP_034537;
CC -!- DEVELOPMENTAL STAGE: Expressed at 9.5 dpc, 10 dpc and 10.5 dpc in the
CC limb buds, branchial arches and the tail region.
CC -!- DOMAIN: Transcription repression is enhanced or dependent on the
CC presence of the T-box DNA-binding domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32240.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF205935; AAF24761.1; -; mRNA.
DR EMBL; AK032570; BAC27930.1; -; mRNA.
DR EMBL; AK046252; BAC32658.1; -; mRNA.
DR EMBL; AK133775; BAE21832.1; -; mRNA.
DR EMBL; AK162302; BAE36840.1; -; mRNA.
DR EMBL; AL954662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK172962; BAD32240.1; ALT_INIT; mRNA.
DR RefSeq; NP_038748.2; NM_013720.2.
DR SMR; A2AWL7; -.
DR BioGRID; 205889; 23.
DR IntAct; A2AWL7; 6.
DR STRING; 10090.ENSMUSP00000106401; -.
DR iPTMnet; A2AWL7; -.
DR PhosphoSitePlus; A2AWL7; -.
DR EPD; A2AWL7; -.
DR jPOST; A2AWL7; -.
DR MaxQB; A2AWL7; -.
DR PaxDb; A2AWL7; -.
DR PeptideAtlas; A2AWL7; -.
DR PRIDE; A2AWL7; -.
DR ProteomicsDB; 295896; -. [A2AWL7-1]
DR ProteomicsDB; 295897; -. [A2AWL7-2]
DR ProteomicsDB; 295898; -. [A2AWL7-3]
DR ProteomicsDB; 295899; -. [A2AWL7-4]
DR Antibodypedia; 6067; 87 antibodies from 16 providers.
DR DNASU; 29808; -.
DR Ensembl; ENSMUST00000046717; ENSMUSP00000043795; ENSMUSG00000033943. [A2AWL7-1]
DR Ensembl; ENSMUST00000110773; ENSMUSP00000106400; ENSMUSG00000033943. [A2AWL7-3]
DR Ensembl; ENSMUST00000156510; ENSMUSP00000119044; ENSMUSG00000033943. [A2AWL7-2]
DR GeneID; 29808; -.
DR KEGG; mmu:29808; -.
DR UCSC; uc008lur.1; mouse. [A2AWL7-4]
DR CTD; 23269; -.
DR MGI; MGI:1352483; Mga.
DR VEuPathDB; HostDB:ENSMUSG00000033943; -.
DR eggNOG; KOG3585; Eukaryota.
DR GeneTree; ENSGT00940000156269; -.
DR HOGENOM; CLU_000469_1_0_1; -.
DR InParanoid; A2AWL7; -.
DR PhylomeDB; A2AWL7; -.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 29808; 9 hits in 76 CRISPR screens.
DR ChiTaRS; Mga; mouse.
DR PRO; PR:A2AWL7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AWL7; protein.
DR Bgee; ENSMUSG00000033943; Expressed in undifferentiated genital tubercle and 247 other tissues.
DR ExpressionAtlas; A2AWL7; baseline and differential.
DR Genevisible; A2AWL7; MM.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00182; TBOX; 1.
DR Gene3D; 2.60.40.820; -; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR037935; MAX_gene-associated_protein.
DR InterPro; IPR032060; MGA_dom.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR046360; T-box_DNA-bd.
DR InterPro; IPR036960; T-box_sf.
DR InterPro; IPR001699; TF_T-box.
DR InterPro; IPR018186; TF_T-box_CS.
DR PANTHER; PTHR11267; PTHR11267; 1.
DR PANTHER; PTHR11267:SF32; PTHR11267:SF32; 1.
DR Pfam; PF16059; DUF4801; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF00907; T-box; 1.
DR PRINTS; PR00937; TBOX.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00425; TBOX; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS01264; TBOX_2; 1.
DR PROSITE; PS50252; TBOX_3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; DNA-binding; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..3003
FT /note="MAX gene-associated protein"
FT /id="PRO_0000342693"
FT DOMAIN 2362..2413
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DNA_BIND 84..260
FT /note="T-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT REGION 259..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1476..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1722..1746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1856..1885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1920..1954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1964..1983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1988..2038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2087..2110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2207..2255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2515..2534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2629..2654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2877..2917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1924..1954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1964..1979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2003..2021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2240..2255
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2517..2534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2629..2650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2882..2897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT MOD_RES 848
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT MOD_RES 921
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT MOD_RES 1423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT MOD_RES 1450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT MOD_RES 2206
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT MOD_RES 2480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT MOD_RES 2849
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT MOD_RES 2860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 329
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 348
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 431
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 463
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 567
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 610
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 651
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 782
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 788
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 814
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 823
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 925
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 987
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 1088
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 1136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 1158
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 1194
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 1202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 1454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 1495
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 1937
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 1944
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2060
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2084
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2152
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2352
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2471
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2568
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2618
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2724
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT CROSSLNK 2979
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWI9"
FT VAR_SEQ 669..671
FT /note="EAL -> VWL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034536"
FT VAR_SEQ 672..3003
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034537"
FT VAR_SEQ 727..805
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034538"
FT VAR_SEQ 1214
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_034539"
FT VAR_SEQ 1521..1728
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_034540"
FT VAR_SEQ 1754
FT /note="L -> LLIPVQQGSPTLRPIQNPQLQGQRMVLQPVRGPSGMNLFR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_034541"
FT VAR_SEQ 2466..3003
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_034542"
FT CONFLICT 11
FT /note="N -> T (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="H -> Y (in Ref. 3; BAC27930)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="Q -> P (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="H -> P (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="Q -> P (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="H -> P (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="S -> R (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="Q -> P (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="K -> R (in Ref. 3; BAC32658)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="T -> P (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="E -> D (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="A -> G (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="F -> L (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="N -> D (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="S -> C (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 903
FT /note="T -> A (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 1061
FT /note="E -> D (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 1136
FT /note="K -> E (in Ref. 5; BAD32240)"
FT /evidence="ECO:0000305"
FT CONFLICT 1191
FT /note="S -> ST (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 1593
FT /note="P -> L (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 1753..1755
FT /note="LLH -> FDVG (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 1763
FT /note="L -> F (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 1826
FT /note="S -> P (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 1845
FT /note="F -> L (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2033
FT /note="V -> A (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2043
FT /note="M -> I (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2478
FT /note="C -> G (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2800..2802
FT /note="RAF -> ARLI (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2809
FT /note="G -> V (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2814
FT /note="F -> Y (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2819..2821
FT /note="LGA -> MGT (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2830
FT /note="Q -> L (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2835
FT /note="S -> T (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2852..2853
FT /note="EK -> VR (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2865
FT /note="L -> H (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2877
FT /note="L -> R (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2928
FT /note="A -> T (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2969
FT /note="A -> T (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2971
FT /note="I -> S (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
FT CONFLICT 2998
FT /note="S -> L (in Ref. 1; AAF24761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3003 AA; 328802 MW; C0963FF86506A75C CRC64;
MEEKQQIILA NQDGGTVTGG APTFFVILKQ PGNGKTDQGI LVTNRDARAL LSRESSPGKS
KEKICLPADC TVGKITVTLD NNSMWNEFHN RSTEMILTKQ GRRMFPYCRY WITGLDSNLK
YILVMDISPV DSHRYKWNGR WWEPSGKAEP HILGRVFIHP ESPSTGHYWM HQPVSFYKLK
LTNNTLDQEG HIILHSMHRY LPRLHLVPAE KATEVIQLNG PGVHTFTFPQ TEFFAVTAYQ
NIQITQLKID YNPFAKGFRD DGLSSKPQRE GKQRNSSDQE GNSVSSSPAH RVRLTEGEGS
EIHSGDFDPV LRGHEASSLS LEKAPHNVKQ DFLGFMNTDS THEVPQLKHE ISESRIVNSF
EDDSQISSPS NPNGNFNVVI KEEPLDDYDY ELGECPEGIT VKQEETDEET DVYSNSDDDP
ILEKQLKRHN KVDNLEADHP SYKWLPNSPG VAKAKMFKLD AGKMPVVYLE PCAVTKSTVK
ISELPDNMLS TSRKDKSMLA ELEYLPAYIE NSDGTDFCLS KDSENSLRKH SPDLRIVQKY
TLLKEPNWKY PDILDNSSTE RIHDSSKGST AESFSGKEDL GKKRTTMLKM AIPSKTVTAS
HSASPNTPGK RGRPRKLRLS KAGRPPKNTG KSLTAAKNIP VGPGSTFPDV KPDLEDVDGV
LFVSFESKEA LDIHAVDGTT EEPSSLQTTT TNDSGCRTRI SQLEKELIED LKSLRHKQVI
HPALQEVGLK LNSVDPTVSI DLKYLGVQLP LAPATSFPLW NVTGTNPASP DAGFPFVSRT
GKTNDFTKIK GWRGKFQNAS ASRNEGGNSE ASLKNRSAFC SDKLDEYLEN EGKLMETNIG
FSSNAPTSPV VYQLPTKSTS YVRTLDSVLK KQSTISPSTS HSVKPQSVTT ASRKTKAQNK
QTTLSGRTKS SYKSILPYPV SPKQKNSHVS QGDKITKNSL SSTSDNQVTN LVVPSVDENA
FPKQISLRQA QQQHLQQQGT RPPGLSKSQV KLMDLEDCAL WEGKPRTYIT EERADVSLTT
LLTAQASLKT KPIHTIIRKR APPCNNDFCR LGCVCSSLAL EKRQPAHCRR PDCMFGCTCL
KRKVVLVKGG SKTKHFHKKA ANRDPLFYDT LGEEGREGGG VREDEEQLKE KKKRKKLEYT
VCEAEPEQPV RHYPLWVKVE GEVDPEPVYI PTPSVIEPIK PLVLPQPDLS STTKGKLTPG
IKPARTYTPK PNPVIREEDK DPVYLYFESM MTCARVRVYE RKKEEQRQLS PPLSPSSSFQ
QQSSCYSSPE NRVTKELDSE QTLKQLICDL EDDSDKSQEK SWKSSCNEGE SSSTSYVHQR
SPGGPTKLIE IISDCNWEED RNKILSILSQ HINSNMPQSL KVGSFIIELA SQRKCRGEKT
PPVYSSRVKI SMPSSQDQDD MAEKSGSETP DGPLSPGKMD DISPVQTDAL DSVRERLHGG
KGLPFYAGLS PSGKLVAYKR KPSSTTSGLI QVASNAKVAA SRKPRTLLPS TSNSKMASSG
PATNRSGKNL KAFVPAKRPI AARPSPGGVF TQFVMSKVGA LQQKIPGVRT PQPLTGPQKF
SIRPSPVMVV TPVVSSEQVQ VCSTVAAAVT TSPQVFLENV TAVPSLTANS DMGAKEATYS
SSASTAGVVE ISETNNTTLV TSTQSTATVN LTKTTGITTS PVASVSFAKP LVASPTITLP
VASTASTSIV MVTTAASSSV VTTPTSSLSS VPIILSGING SPPVSQRPEN APQIPVTTPQ
ISSNNVKRTG PRLLHPNGQI VQLLPLHQIR GSNAQPSLQP VVFRNPGSMV GIRLPAPCKS
SETPSSSASS SAFSVMSPVI QAVGSSPTVN VISQAPSLLS SGSSFVSQAG TLTLRISPPE
TQNLASKTGS ESKITPSTGG QPVGTASLIP LQSGSFALLQ LPGQKPIPSS VLQHVASLQI
KKESQSTDQK DETNSIKREE ETKKALPSKD KALDSEANIM KQNSGIIASE NTSNNSLDDG
GDLLDEETLR EDARPYEYSY STGSHTDEDK DGDEDSGNKN QNSPKEKQTV PEVRAGSKNI
DIMALQSIRS IRPQKCVKVK VEPQEGSDNP ENPDDFLVLS KDSKFELSGN QVKEQQSNSQ
AEAKKDCEDS LGKDSLRERW RKHLKGPLTQ KYIGISQNFN KEANVQFFTE MKPCQENSEQ
DISELLGKSG TIESGGVLKT EDGSWSGISS SAAFSIIPRR ATKGRRGSRH FQGHLLLPRE
QMKPKQQTKD GRSSAADFTV LDLEDEDEED EKTDDSLDEI VDVVSGYQSE EVDVEKNNYV
DYLEDDEQVD VETIEELSEE INFPYKKTTA THTQSFKQQC HSHISADEKA SEKSRKVSLI
SSKLKDDCWG DKPHKETEAF AYYRRTHTAN ERRRRGEMRD LFEKLKITLG LLHSSKVSKS
LILNRAFSEI QGLTDQADKL IGQKNLLSRK RSILIRKVSS LSGKTEEVVL KKLEYIYAKQ
QALEAQKRKK KLGSDEFCVS PRIGTQLEGS SASSVDLGQM LMNNRRGKPL ILSRKRDQAT
ENASPSDTPH SSANLVMTPQ GQLLTLKGPL FSGPVVAVSP ALLEGGLKPQ VASSTMSQSE
NDDLFMMPRI VNVTSLAAEE DLGGMSGNKY RHEVPDGKPL DHLRDIAGSE ASSLKDTERI
SSRGNHRDSR KALGPTQVLL ANKDSGFPHV ADVSTMQAAQ EFIPKNMSGD VRGHRYKWKE
CELRGERLKS KESQFHKLKM KDLKDSSIEM ELRKVASAIE EAALHPSELL TNMEDEDDTD
ETLTSLLNEI AFLNQQLNDD SGLAELSGSM DTEFSGDAQR AFISKLAPGN RSAFQVGHLG
AGVKELPDVQ EESESISPLL LHLEDDDFSE NEKQLGDTAS EPDVLKIVID PEIKDSLVSH
RKSSDGGQST SGLPAEPESV SSPPILHMKT GPENSNTDTL WRPMPKLAPL GLKVANPPSD
ADGQSLKVMP ALAPIAAKVG SIGHKMNLAG IDQEGRGSKV MPTLAPVVPK LGNSGAPSSS
SGK
