GenomeNet

Database: UniProt
Entry: Q6PDM1
LinkDB: Q6PDM1
Original site: Q6PDM1 
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   29-SEP-2021, entry version 124.
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   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   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; 91 antibodies.
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; CFGDAKV; -.
DR   OrthoDB; 560559at2759; -.
DR   PhylomeDB; Q6PDM1; -.
DR   TreeFam; TF330735; -.
DR   Reactome; R-MMU-3214847; HATs acetylate histones.
DR   BioGRID-ORCS; 74026; 13 hits in 62 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 cochlea and 313 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:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
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
//
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