MSL1_MOUSE
ID MSL1_MOUSE Reviewed; 616 AA.
AC Q6PDM1; A3KFP2; A3KFP4; Q27QB3; Q3TTE5; Q80XS0; Q8BPN3; Q9CXF9; Q9D5C9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Male-specific lethal 1 homolog;
DE Short=MSL-1;
DE AltName: Full=Hampin;
DE AltName: Full=Male-specific lethal 1-like 1;
DE Short=MSL1-like 1;
DE AltName: Full=Male-specific lethal-1 homolog 1;
GN Name=Msl1; Synonyms=Msl1l1;
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 5), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=16119455; DOI=10.1007/s11171-005-0045-1;
RA Dmitriev R.I., Pestov N.B., Korneenko T.V., Gerasimova A.V., Zhao K.H.,
RA Modianov N.N., Kostina M.B., Shakhparonov M.I.;
RT "Tissue specificity of alternative splicing products of mouse mRNA encoding
RT new protein hampin homologous to the Drosophila MSL-1 protein.";
RL Bioorg. Khim. 31:363-371(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 6).
RC STRAIN=C57BL/6J; TISSUE=Eye, Head, 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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 INTERACTION WITH TTC4; PIH1D1; KAT8 AND ECM2, AND SUBCELLULAR LOCATION.
RX PubMed=17335777; DOI=10.1016/j.bbrc.2007.02.073;
RA Dmitriev R.I., Korneenko T.V., Bessonov A.A., Shakhparonov M.I.,
RA Modyanov N.N., Pestov N.B.;
RT "Characterization of hampin/MSL1 as a node in the nuclear interactome.";
RL Biochem. Biophys. Res. Commun. 355:1051-1057(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19390865; DOI=10.1007/s00441-009-0785-y;
RA Dmitriev R.I., Okkelman I.A., Abdulin R.A., Shakhparonov M.I., Pestov N.B.;
RT "Nuclear transport of protein TTC4 depends on the cell cycle.";
RL Cell Tissue Res. 336:521-527(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND BIPARTITE
RP NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=24913909; DOI=10.1002/jcb.24868;
RA Dmitriev R.I., Pestov N.B., Shakhparonov M.I., Okkelman I.A.;
RT "Two distinct nuclear localization signals in mammalian MSL1 regulate its
RT function.";
RL J. Cell. Biochem. 115:1967-1973(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 470-540 IN COMPLEXES WITH KAT8
RP AND MSL3, FUNCTION, INTERACTION WITH KAT8 AND MSL3, AND MUTAGENESIS OF
RP GLU-498; PHE-505; HIS-509; ALA-576; PHE-577 AND PHE-589.
RX PubMed=21217699; DOI=10.1038/nsmb.1960;
RA Kadlec J., Hallacli E., Lipp M., Holz H., Sanchez-Weatherby J., Cusack S.,
RA Akhtar A.;
RT "Structural basis for MOF and MSL3 recruitment into the dosage compensation
RT complex by MSL1.";
RL Nat. Struct. Mol. Biol. 18:142-149(2011).
CC -!- FUNCTION: Component of histone acetyltransferase complex responsible
CC for the majority of histone H4 acetylation at 'Lys-16' (H4K16ac) which
CC is implicated in the formation of higher-order chromatin structure
CC (PubMed:24913909). Greatly enhances MSL2 E3 ubiquitin ligase activity,
CC promoting monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub) (By
CC similarity). This modification in turn stimulates histone H3
CC methylation at 'Lys-5' (H3K4me) and 'Lys-80' (H3K79me) and leads to
CC gene activation, including that of HOXA9 and MEIS1 (By similarity). In
CC the MSL complex, acts as a scaffold to tether MSL3 and KAT8 together
CC for enzymatic activity regulation (PubMed:21217699). Isoform 2, isoform
CC 3, isoform 4 and isoform 5 can medite histone H4 acetylation at 'Lys-
CC 16' (H4K16ac) (PubMed:24913909). {ECO:0000250|UniProtKB:Q68DK7,
CC ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:24913909}.
CC -!- SUBUNIT: Component of a multisubunit histone acetyltransferase complex
CC (MSL) at least composed of the KAT8/MOF/MYST1, MSL1/hampin, MSL2 and
CC MSL3 (By similarity). Directly interacts with MSL2 via its coiled coil
CC domain (By similarity). Directly interacts with NUPR1 (By similarity).
CC Interacts with TP53BP1; this interaction may be required for MSL1 DNA
CC repair activity, but not for histone acetyltransferase activity (By
CC similarity). Forms a MSL heterotetrameric core with MSL2 (By
CC similarity). Interacts with KAT8 and MSL3; both interactions are direct
CC (PubMed:21217699, PubMed:17335777). Isoform 1 and isoform 3 interact
CC with TTC4 (PubMed:17335777). Isoform 1 interacts with ECM2 and PIHD1
CC (PubMed:17335777). {ECO:0000250|UniProtKB:Q68DK7,
CC ECO:0000269|PubMed:17335777, ECO:0000269|PubMed:21217699}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17335777,
CC ECO:0000269|PubMed:24913909}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:24913909}. Nucleus speckle
CC {ECO:0000269|PubMed:24913909}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:19390865, ECO:0000269|PubMed:24913909}. Nucleus
CC speckle {ECO:0000269|PubMed:24913909}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
CC {ECO:0000269|PubMed:16119455}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:24913909}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:24913909}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:24913909}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Hampin A {ECO:0000303|PubMed:16119455};
CC IsoId=Q6PDM1-1; Sequence=Displayed;
CC Name=2; Synonyms=Hampin B {ECO:0000303|PubMed:16119455};
CC IsoId=Q6PDM1-2; Sequence=VSP_035241;
CC Name=3; Synonyms=Hampin C {ECO:0000303|PubMed:16119455};
CC IsoId=Q6PDM1-3; Sequence=VSP_035239, VSP_035240, VSP_035241;
CC Name=4; Synonyms=Hampin D {ECO:0000303|PubMed:16119455};
CC IsoId=Q6PDM1-4; Sequence=VSP_035242, VSP_035243;
CC Name=5; Synonyms=Hampin E {ECO:0000303|PubMed:16119455};
CC IsoId=Q6PDM1-5; Sequence=VSP_035239, VSP_035240, VSP_035242,
CC VSP_035243;
CC Name=6;
CC IsoId=Q6PDM1-6; Sequence=VSP_035238, VSP_035242, VSP_035243;
CC -!- TISSUE SPECIFICITY: Isoform 3 and isoform 5 are testis-specific
CC (PubMed:16119455). Isoform 1 and isoform 4 are ubiquitously expressed
CC (PubMed:16119455). Isoform 2 is expressed at low levels in the testis
CC and brain (PubMed:16119455). {ECO:0000269|PubMed:16119455}.
CC -!- DOMAIN: The coiled coil is formed by helices from two subunits in the
CC MSL1 homodimer. {ECO:0000250|UniProtKB:Q68DK7}.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000250|UniProtKB:Q68DK7}.
CC -!- SIMILARITY: Belongs to the msl-1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35489.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ387855; ABD46887.1; -; mRNA.
DR EMBL; AK014463; BAB29369.1; -; mRNA.
DR EMBL; AK015496; BAB29868.1; -; mRNA.
DR EMBL; AK161412; BAE36380.1; -; mRNA.
DR EMBL; AK053719; BAC35489.1; ALT_FRAME; mRNA.
DR EMBL; AL590963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043039; AAH43039.1; -; mRNA.
DR EMBL; BC055715; AAH55715.1; -; mRNA.
DR EMBL; BC058629; AAH58629.1; -; mRNA.
DR CCDS; CCDS25364.1; -. [Q6PDM1-1]
DR CCDS; CCDS88248.1; -. [Q6PDM1-2]
DR CCDS; CCDS88249.1; -. [Q6PDM1-4]
DR CCDS; CCDS88250.1; -. [Q6PDM1-3]
DR RefSeq; NP_082998.2; NM_028722.2. [Q6PDM1-1]
DR RefSeq; XP_006534414.1; XM_006534351.2.
DR RefSeq; XP_011247586.1; XM_011249284.2.
DR PDB; 2Y0M; X-ray; 2.70 A; B=470-540.
DR PDB; 2Y0N; X-ray; 3.00 A; E/F/G/H=545-597.
DR PDBsum; 2Y0M; -.
DR PDBsum; 2Y0N; -.
DR AlphaFoldDB; Q6PDM1; -.
DR SMR; Q6PDM1; -.
DR BioGRID; 216434; 5.
DR ComplexPortal; CPX-859; MSL histone acetyltransferase complex.
DR IntAct; Q6PDM1; 3.
DR STRING; 10090.ENSMUSP00000042792; -.
DR iPTMnet; Q6PDM1; -.
DR PhosphoSitePlus; Q6PDM1; -.
DR EPD; Q6PDM1; -.
DR jPOST; Q6PDM1; -.
DR MaxQB; Q6PDM1; -.
DR PaxDb; Q6PDM1; -.
DR PeptideAtlas; Q6PDM1; -.
DR PRIDE; Q6PDM1; -.
DR ProteomicsDB; 291515; -. [Q6PDM1-1]
DR ProteomicsDB; 291516; -. [Q6PDM1-2]
DR ProteomicsDB; 291517; -. [Q6PDM1-3]
DR ProteomicsDB; 291518; -. [Q6PDM1-4]
DR ProteomicsDB; 291519; -. [Q6PDM1-5]
DR ProteomicsDB; 291520; -. [Q6PDM1-6]
DR Antibodypedia; 7890; 93 antibodies from 20 providers.
DR Ensembl; ENSMUST00000037915; ENSMUSP00000042792; ENSMUSG00000052915. [Q6PDM1-1]
DR Ensembl; ENSMUST00000037930; ENSMUSP00000043328; ENSMUSG00000052915. [Q6PDM1-3]
DR Ensembl; ENSMUST00000107485; ENSMUSP00000103109; ENSMUSG00000052915. [Q6PDM1-4]
DR Ensembl; ENSMUST00000107487; ENSMUSP00000103111; ENSMUSG00000052915. [Q6PDM1-2]
DR GeneID; 74026; -.
DR KEGG; mmu:74026; -.
DR UCSC; uc007lhi.2; mouse. [Q6PDM1-4]
DR UCSC; uc007lhj.2; mouse. [Q6PDM1-1]
DR UCSC; uc007lhk.2; mouse. [Q6PDM1-2]
DR UCSC; uc007lhm.1; mouse. [Q6PDM1-5]
DR UCSC; uc007lhn.2; mouse. [Q6PDM1-3]
DR CTD; 339287; -.
DR MGI; MGI:1921276; Msl1.
DR VEuPathDB; HostDB:ENSMUSG00000052915; -.
DR eggNOG; ENOG502QQ0S; Eukaryota.
DR GeneTree; ENSGT00390000018292; -.
DR HOGENOM; CLU_030878_1_0_1; -.
DR InParanoid; Q6PDM1; -.
DR OMA; HAQANCL; -.
DR OrthoDB; 560559at2759; -.
DR PhylomeDB; Q6PDM1; -.
DR TreeFam; TF330735; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR BioGRID-ORCS; 74026; 14 hits in 71 CRISPR screens.
DR ChiTaRS; Msl1; mouse.
DR EvolutionaryTrace; Q6PDM1; -.
DR PRO; PR:Q6PDM1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6PDM1; protein.
DR Bgee; ENSMUSG00000052915; Expressed in granulocyte and 258 other tissues.
DR ExpressionAtlas; Q6PDM1; baseline and differential.
DR Genevisible; Q6PDM1; MM.
DR GO; GO:0072487; C:MSL complex; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IDA:ComplexPortal.
DR InterPro; IPR026711; Msl-1.
DR InterPro; IPR031840; MSL1_dimer.
DR InterPro; IPR029332; PEHE_dom.
DR PANTHER; PTHR21656; PTHR21656; 1.
DR Pfam; PF16801; MSL1_dimer; 1.
DR Pfam; PF15275; PEHE; 1.
DR SMART; SM01300; PEHE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..616
FT /note="Male-specific lethal 1 homolog"
FT /id="PRO_0000349237"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..239
FT /note="Interaction with MSL2"
FT /evidence="ECO:0000250"
FT REGION 306..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..520
FT /note="Interaction with KAT8"
FT /evidence="ECO:0000269|PubMed:21217699"
FT REGION 552..593
FT /note="Interaction with MSL3 MRG domain"
FT COILED 215..284
FT /evidence="ECO:0000250"
FT MOTIF 319..348
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:24913909"
FT MOTIF 507..521
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:24913909"
FT COMPBIAS 41..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK7"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK7"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 355
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK7"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK7"
FT MOD_RES 398
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK7"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK7"
FT CROSSLNK 303
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q68DK7"
FT CROSSLNK 367
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q68DK7"
FT CROSSLNK 380
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q68DK7"
FT VAR_SEQ 1..265
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035238"
FT VAR_SEQ 1..230
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16119455,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_035239"
FT VAR_SEQ 231..258
FT /note="QLDLIEQQQQQLQAKEKEIEELKSERDT -> MLRVFARHGQEALIPSLAAQ
FT TTTTNRNK (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16119455,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_035240"
FT VAR_SEQ 461..477
FT /note="RCLMPSSVAGETSVLAV -> I (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035241"
FT VAR_SEQ 461..463
FT /note="RCL -> SKA (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16119455, ECO:0000303|PubMed:16141072"
FT /id="VSP_035242"
FT VAR_SEQ 464..616
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16119455, ECO:0000303|PubMed:16141072"
FT /id="VSP_035243"
FT MUTAGEN 498
FT /note="E->R: Abolishes interaction with KAT8."
FT /evidence="ECO:0000269|PubMed:21217699"
FT MUTAGEN 505
FT /note="F->R: Abolishes interaction with KAT8."
FT /evidence="ECO:0000269|PubMed:21217699"
FT MUTAGEN 509
FT /note="H->R: Abolishes interaction with KAT8."
FT /evidence="ECO:0000269|PubMed:21217699"
FT MUTAGEN 556
FT /note="F->E: Strongly reduces interaction with MSL3; when
FT associated with E-576 and E-589 or E-577 and E-589."
FT MUTAGEN 576
FT /note="A->E: No effect on interaction with MSL3. Reduces
FT interaction; when associated with E-589. Strongly reduces
FT interaction with MSL3; when associated with E-556 and E-
FT 589."
FT /evidence="ECO:0000269|PubMed:21217699"
FT MUTAGEN 577
FT /note="F->E: No effect on interaction with MSL3. Reduces
FT interaction; when associated with E-589. Strongly reduces
FT interaction with MSL3; when associated with E-556 and E-
FT 589."
FT /evidence="ECO:0000269|PubMed:21217699"
FT MUTAGEN 589
FT /note="F->E: Strongly reduces interaction with MSL3; when
FT associated with E-556 and E-576 or E-556 and E-577."
FT /evidence="ECO:0000269|PubMed:21217699"
FT CONFLICT 344
FT /note="T -> N (in Ref. 2; BAB29369)"
FT /evidence="ECO:0000305"
FT CONFLICT 388..389
FT /note="TP -> PQ (in Ref. 2; BAB29868)"
FT /evidence="ECO:0000305"
FT HELIX 502..534
FT /evidence="ECO:0007829|PDB:2Y0M"
SQ SEQUENCE 616 AA; 67320 MW; 2679AF230DBC0A7D CRC64;
MTMRSAVFKA AAAPAGGNPE QRLDYERAAA LGGPEDESGA AEAHFLPRHR KLKEPGPPLA
SSQGGSPSPS PAGCGGGKGR GLLLPAGAAP GQQEESWGGS VPLPCPPPAT KQAGIGGEPV
AAGAGCSPRP KYQAVLPIQT GSIVVAAAKE PTPWAGDKGG AAPPAATASD PAGPPPLPLP
GPPPLAPTAT AGTLAASEGR WKSIRKSPLG GGGGSGASSQ AACLKQILLL QLDLIEQQQQ
QLQAKEKEIE ELKSERDTLL ARIERMERRM QLVKRDNEKE RHKLLQGYEP EEREEAELSE
KIKLERQPEL CETSQALPSK PFSCGRSGKG HKRKTPFGNT ERKTPVKKLA PEFSKVKTKT
PKHSPIKEEP CGSISETVCK RELRSQETPE KPRSSVDTPP RLSTPQKGPS THPKEKAFSS
EMEDLPYLST TEMYLCRWHQ PPPSPLPLRE SSPKKEETVA RCLMPSSVAG ETSVLAVPSW
RDHSVEPLRD PNPSDILENL DDSVFSKRHA KLELDEKRRK RWDIQRIREQ RILQRLQLRM
YKKKGIQESE PEVTSFFPEP DDVESLLITP FLPVVAFGRP LPKLAPQNFE LPWLDERSRC
RLEIQKKHTP HRTCRK
