ID   ASH1L_HUMAN             Reviewed;        2969 AA.
AC   Q9NR48; Q59GP1; Q5T714; Q5T715; Q9P2C7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Histone-lysine N-methyltransferase ASH1L;
DE            EC=2.1.1.359 {ECO:0000269|PubMed:21239497};
DE            EC=2.1.1.367 {ECO:0000250|UniProtKB:Q99MY8};
DE   AltName: Full=ASH1-like protein;
DE            Short=huASH1;
DE   AltName: Full=Absent small and homeotic disks protein 1 homolog;
DE   AltName: Full=Lysine N-methyltransferase 2H;
GN   Name=ASH1L; Synonyms=KIAA1420, KMT2H;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND VARIANT ALA-1771.
RX   PubMed=10860993; DOI=10.1073/pnas.97.13.7284;
RA   Nakamura T., Blechman J., Tada S., Rozovskaia T., Itoyama T., Bullrich F.,
RA   Mazo A., Croce C.M., Geiger B., Canaani E.;
RT   "huASH1 protein, a putative transcription factor encoded by a human
RT   homologue of the Drosophila ash1 gene, localizes to both nuclei and cell-
RT   cell tight junctions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:7284-7289(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1345.
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI. The
RT   complete sequences of 150 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1345.
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2000-2183 (ISOFORM 2).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-375, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=22939622; DOI=10.1016/j.cell.2012.06.048;
RA   Pinheiro I., Margueron R., Shukeir N., Eisold M., Fritzsch C.,
RA   Richter F.M., Mittler G., Genoud C., Goyama S., Kurokawa M., Son J.,
RA   Reinberg D., Lachner M., Jenuwein T.;
RT   "Prdm3 and Prdm16 are H3K9me1 methyltransferases required for mammalian
RT   heterochromatin integrity.";
RL   Cell 150:948-960(2012).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25593309; DOI=10.1101/gad.252189.114;
RA   Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W.,
RA   Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.;
RT   "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of
RT   transcription-associated DNA damage that promotes homologous
RT   recombination.";
RL   Genes Dev. 29:197-211(2015).
RN   [12]
RP   METHYLATION AT GLN-1220, AND MUTAGENESIS OF GLN-1220.
RX   PubMed=26797129; DOI=10.1074/jbc.m115.711952;
RA   Kusevic D., Kudithipudi S., Jeltsch A.;
RT   "Substrate specificity of the HEMK2 protein glutamine methyltransferase and
RT   identification of novel substrates.";
RL   J. Biol. Chem. 291:6124-6133(2016).
RN   [13]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34 AND LYS-425, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 2074-2293 IN COMPLEX WITH
RP   S-ADENOSYL-L-METHIONINE, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=21239497; DOI=10.1074/jbc.m110.203380;
RA   An S., Yeo K.J., Jeon Y.H., Song J.J.;
RT   "Crystal structure of the human histone methyltransferase ASH1L catalytic
RT   domain and its implications for the regulatory mechanism.";
RL   J. Biol. Chem. 286:8369-8374(2011).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 2438-2561.
RX   PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA   Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA   Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA   Gingras A.C., Arrowsmith C.H., Knapp S.;
RT   "Histone recognition and large-scale structural analysis of the human
RT   bromodomain family.";
RL   Cell 149:214-231(2012).
RN   [16]
RP   INVOLVEMENT IN MRD52, VARIANTS MRD52 SER-724; ARG-972; HIS-1276; TRP-1775
RP   AND GLY-2853, AND VARIANT GLY-277.
RX   PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA   de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA   Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA   del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA   Veltman J.A., Vissers L.E.;
RT   "Diagnostic exome sequencing in persons with severe intellectual
RT   disability.";
RL   N. Engl. J. Med. 367:1921-1929(2012).
RN   [17]
RP   VARIANT MRD52 ILE-2085.
RX   PubMed=27824329; DOI=10.1038/ncomms13316;
RA   Wang T., Guo H., Xiong B., Stessman H.A., Wu H., Coe B.P., Turner T.N.,
RA   Liu Y., Zhao W., Hoekzema K., Vives L., Xia L., Tang M., Ou J., Chen B.,
RA   Shen Y., Xun G., Long M., Lin J., Kronenberg Z.N., Peng Y., Bai T., Li H.,
RA   Ke X., Hu Z., Zhao J., Zou X., Xia K., Eichler E.E.;
RT   "De novo genic mutations among a Chinese autism spectrum disorder cohort.";
RL   Nat. Commun. 7:13316-13316(2016).
RN   [18]
RP   VARIANT MRD52 PRO-2791.
RX   PubMed=28394464; DOI=10.1002/ajmg.a.38193;
RA   Okamoto N., Miya F., Tsunoda T., Kato M., Saitoh S., Yamasaki M.,
RA   Kanemura Y., Kosaki K.;
RT   "Novel MCA/ID syndrome with ASH1L mutation.";
RL   Am. J. Med. Genet. A 173:1644-1648(2017).
RN   [19]
RP   VARIANTS MRD52 2148-GLU--LYS-2969 DEL AND HIS-2396.
RX   PubMed=28191889; DOI=10.1038/ng.3792;
RA   Stessman H.A., Xiong B., Coe B.P., Wang T., Hoekzema K., Fenckova M.,
RA   Kvarnung M., Gerdts J., Trinh S., Cosemans N., Vives L., Lin J.,
RA   Turner T.N., Santen G., Ruivenkamp C., Kriek M., van Haeringen A., Aten E.,
RA   Friend K., Liebelt J., Barnett C., Haan E., Shaw M., Gecz J.,
RA   Anderlid B.M., Nordgren A., Lindstrand A., Schwartz C., Kooy R.F.,
RA   Vandeweyer G., Helsmoortel C., Romano C., Alberti A., Vinci M., Avola E.,
RA   Giusto S., Courchesne E., Pramparo T., Pierce K., Nalabolu S., Amaral D.G.,
RA   Scheffer I.E., Delatycki M.B., Lockhart P.J., Hormozdiari F., Harich B.,
RA   Castells-Nobau A., Xia K., Peeters H., Nordenskjoeld M., Schenck A.,
RA   Bernier R.A., Eichler E.E.;
RT   "Targeted sequencing identifies 91 neurodevelopmental-disorder risk genes
RT   with autism and developmental-disability biases.";
RL   Nat. Genet. 49:515-526(2017).
CC   -!- FUNCTION: Histone methyltransferase specifically trimethylating 'Lys-
CC       36' of histone H3 forming H3K36me3 (PubMed:21239497). Also
CC       monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro (By
CC       similarity). The physiological significance of the H3K9me1 activity is
CC       unclear (By similarity). {ECO:0000250|UniProtKB:Q99MY8,
CC       ECO:0000269|PubMed:21239497}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC         + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC         COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC         Evidence={ECO:0000269|PubMed:21239497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367;
CC         Evidence={ECO:0000250|UniProtKB:Q99MY8};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10860993,
CC       ECO:0000269|PubMed:25593309}. Cell junction, tight junction
CC       {ECO:0000269|PubMed:10860993}. Chromosome
CC       {ECO:0000305|PubMed:10860993}. Note=The relevance of tight junction
CC       localization is however unclear. {ECO:0000269|PubMed:10860993}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NR48-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NR48-2; Sequence=VSP_039421;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest level in brain,
CC       heart and kidney. {ECO:0000269|PubMed:10860993}.
CC   -!- PTM: Methylated at Gln-1220 by N6AMT1. {ECO:0000269|PubMed:26797129}.
CC   -!- DISEASE: Intellectual developmental disorder, autosomal dominant 52
CC       (MRD52) [MIM:617796]: A disorder characterized by significantly below
CC       average general intellectual functioning associated with impairments in
CC       adaptive behavior and manifested during the developmental period.
CC       {ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:27824329,
CC       ECO:0000269|PubMed:28191889, ECO:0000269|PubMed:28394464}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA92658.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF257305; AAF68983.1; -; mRNA.
DR   EMBL; AL139410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL353807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB037841; BAA92658.1; ALT_INIT; mRNA.
DR   EMBL; AB209068; BAD92305.1; -; mRNA.
DR   EMBL; DB282357; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS1113.2; -. [Q9NR48-2]
DR   CCDS; CCDS91067.1; -. [Q9NR48-1]
DR   RefSeq; NP_060959.2; NM_018489.2. [Q9NR48-2]
DR   RefSeq; XP_006711513.1; XM_006711450.3. [Q9NR48-2]
DR   RefSeq; XP_006711514.1; XM_006711451.3. [Q9NR48-2]
DR   RefSeq; XP_016857273.1; XM_017001784.1.
DR   RefSeq; XP_016857274.1; XM_017001785.1. [Q9NR48-2]
DR   PDB; 3MQM; X-ray; 2.54 A; A/B=2438-2561.
DR   PDB; 3OPE; X-ray; 2.90 A; A/B=2074-2293.
DR   PDB; 4YNM; X-ray; 2.19 A; A/B=2074-2293.
DR   PDB; 4YNP; X-ray; 2.90 A; A/B=2074-2293.
DR   PDB; 4YPA; X-ray; 2.30 A; A/B/C/D=2074-2293.
DR   PDB; 4YPE; X-ray; 2.20 A; A/B=2074-2293.
DR   PDB; 4YPU; X-ray; 2.60 A; A/B=2074-2293.
DR   PDB; 6AGO; X-ray; 3.10 A; A/B=2039-2293.
DR   PDB; 6INE; X-ray; 2.60 A; A=2026-2293.
DR   PDB; 6WZW; X-ray; 1.69 A; A=2074-2293.
DR   PDB; 6X0P; X-ray; 1.69 A; A/B/C/D=2074-2293.
DR   PDB; 7Y0I; NMR; -; A=2584-2635.
DR   PDBsum; 3MQM; -.
DR   PDBsum; 3OPE; -.
DR   PDBsum; 4YNM; -.
DR   PDBsum; 4YNP; -.
DR   PDBsum; 4YPA; -.
DR   PDBsum; 4YPE; -.
DR   PDBsum; 4YPU; -.
DR   PDBsum; 6AGO; -.
DR   PDBsum; 6INE; -.
DR   PDBsum; 6WZW; -.
DR   PDBsum; 6X0P; -.
DR   PDBsum; 7Y0I; -.
DR   SMR; Q9NR48; -.
DR   BioGRID; 120969; 47.
DR   IntAct; Q9NR48; 21.
DR   MINT; Q9NR48; -.
DR   STRING; 9606.ENSP00000376204; -.
DR   BindingDB; Q9NR48; -.
DR   ChEMBL; CHEMBL3588739; -.
DR   CarbonylDB; Q9NR48; -.
DR   GlyGen; Q9NR48; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NR48; -.
DR   PhosphoSitePlus; Q9NR48; -.
DR   BioMuta; ASH1L; -.
DR   DMDM; 117949323; -.
DR   EPD; Q9NR48; -.
DR   jPOST; Q9NR48; -.
DR   MassIVE; Q9NR48; -.
DR   MaxQB; Q9NR48; -.
DR   PaxDb; 9606-ENSP00000376204; -.
DR   PeptideAtlas; Q9NR48; -.
DR   ProteomicsDB; 82273; -. [Q9NR48-1]
DR   ProteomicsDB; 82274; -. [Q9NR48-2]
DR   Pumba; Q9NR48; -.
DR   Antibodypedia; 1436; 212 antibodies from 19 providers.
DR   DNASU; 55870; -.
DR   Ensembl; ENST00000368346.7; ENSP00000357330.3; ENSG00000116539.14. [Q9NR48-1]
DR   Ensembl; ENST00000392403.8; ENSP00000376204.3; ENSG00000116539.14. [Q9NR48-2]
DR   Ensembl; ENST00000677213.1; ENSP00000503315.1; ENSG00000116539.14. [Q9NR48-2]
DR   Ensembl; ENST00000678117.1; ENSP00000504629.1; ENSG00000116539.14. [Q9NR48-2]
DR   Ensembl; ENST00000679097.1; ENSP00000503265.1; ENSG00000116539.14. [Q9NR48-2]
DR   GeneID; 55870; -.
DR   KEGG; hsa:55870; -.
DR   MANE-Select; ENST00000392403.8; ENSP00000376204.3; NM_018489.3; NP_060959.2. [Q9NR48-2]
DR   UCSC; uc001fkt.4; human. [Q9NR48-1]
DR   AGR; HGNC:19088; -.
DR   CTD; 55870; -.
DR   DisGeNET; 55870; -.
DR   GeneCards; ASH1L; -.
DR   HGNC; HGNC:19088; ASH1L.
DR   HPA; ENSG00000116539; Low tissue specificity.
DR   MalaCards; ASH1L; -.
DR   MIM; 607999; gene.
DR   MIM; 617796; phenotype.
DR   neXtProt; NX_Q9NR48; -.
DR   OpenTargets; ENSG00000116539; -.
DR   Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR   PharmGKB; PA134891064; -.
DR   VEuPathDB; HostDB:ENSG00000116539; -.
DR   eggNOG; KOG1083; Eukaryota.
DR   GeneTree; ENSGT00940000156698; -.
DR   HOGENOM; CLU_000657_0_0_1; -.
DR   InParanoid; Q9NR48; -.
DR   OMA; DKDNGHE; -.
DR   OrthoDB; 2882778at2759; -.
DR   PhylomeDB; Q9NR48; -.
DR   TreeFam; TF106416; -.
DR   BioCyc; MetaCyc:HS04019-MONOMER; -.
DR   BRENDA; 2.1.1.357; 2681.
DR   PathwayCommons; Q9NR48; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   SignaLink; Q9NR48; -.
DR   SIGNOR; Q9NR48; -.
DR   BioGRID-ORCS; 55870; 44 hits in 1182 CRISPR screens.
DR   ChiTaRS; ASH1L; human.
DR   EvolutionaryTrace; Q9NR48; -.
DR   GeneWiki; ASH1L; -.
DR   GenomeRNAi; 55870; -.
DR   Pharos; Q9NR48; Tbio.
DR   PRO; PR:Q9NR48; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9NR48; Protein.
DR   Bgee; ENSG00000116539; Expressed in Brodmann (1909) area 23 and 188 other cell types or tissues.
DR   ExpressionAtlas; Q9NR48; baseline and differential.
DR   GO; GO:0005923; C:bicellular tight junction; TAS:ProtInc.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0140938; F:histone H3 methyltransferase activity; TAS:Reactome.
DR   GO; GO:0046975; F:histone H3K36 methyltransferase activity; IDA:HGNC.
DR   GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0046974; F:histone H3K9 methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0140948; F:histone H3K9 monomethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0140947; F:histone H3K9me2 methyltransferase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR   GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0007338; P:single fertilization; IEA:Ensembl.
DR   GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR   GO; GO:1903699; P:tarsal gland development; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:1903709; P:uterine gland development; IEA:Ensembl.
DR   GO; GO:0061038; P:uterus morphogenesis; IEA:Ensembl.
DR   CDD; cd04717; BAH_polybromo; 1.
DR   CDD; cd05525; Bromo_ASH1; 1.
DR   CDD; cd15548; PHD_ASH1L; 1.
DR   CDD; cd19174; SET_ASH1L; 1.
DR   Gene3D; 2.30.30.490; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR043320; Bromo_ASH1L.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR043319; PHD_ASH1L.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46147; HISTONE-LYSINE N-METHYLTRANSFERASE ASH1; 1.
DR   PANTHER; PTHR46147:SF2; SET-BINDING PROTEIN; 1.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF20826; PHD_5; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00384; AT_hook; 4.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   Genevisible; Q9NR48; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative splicing; Bromodomain;
KW   Cell junction; Chromatin regulator; Chromosome; Disease variant;
KW   Intellectual disability; Isopeptide bond; Metal-binding; Methylation;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Tight junction; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..2969
FT                   /note="Histone-lysine N-methyltransferase ASH1L"
FT                   /id="PRO_0000259516"
FT   DOMAIN          2091..2142
FT                   /note="AWS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT   DOMAIN          2145..2261
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          2269..2285
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   DOMAIN          2463..2533
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DOMAIN          2661..2798
FT                   /note="BAH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   DNA_BIND        887..899
FT                   /note="A.T hook 1"
FT   DNA_BIND        1347..1359
FT                   /note="A.T hook 2"
FT   DNA_BIND        1847..1859
FT                   /note="A.T hook 3"
FT   ZN_FING         2585..2631
FT                   /note="PHD-type"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          878..966
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1100..1128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1151..1231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1243..1281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1489..1508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1580..1711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1741..1761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1911..1991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2069..2288
FT                   /note="Catalytic domain"
FT   REGION          2288..2346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2825..2856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2876..2919
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        824..841
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        922..937
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        946..966
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1100..1126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1165..1214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1215..1230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1580..1640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1653..1702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1911..1943
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2289..2306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2309..2326
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2838..2856
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2879..2904
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         375
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         1162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MY8"
FT   MOD_RES         1170
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MY8"
FT   MOD_RES         1220
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000269|PubMed:26797129"
FT   MOD_RES         2317
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MY8"
FT   MOD_RES         2319
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MY8"
FT   MOD_RES         2323
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MY8"
FT   CROSSLNK        34
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        425
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         2035..2039
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_039421"
FT   VARIANT         277
FT                   /note="S -> G (in dbSNP:rs186255422)"
FT                   /evidence="ECO:0000269|PubMed:23033978"
FT                   /id="VAR_069405"
FT   VARIANT         724
FT                   /note="A -> S (in MRD52; uncertain significance;
FT                   dbSNP:rs1293246328)"
FT                   /evidence="ECO:0000269|PubMed:23033978"
FT                   /id="VAR_069406"
FT   VARIANT         972
FT                   /note="K -> R (in MRD52; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:23033978"
FT                   /id="VAR_069407"
FT   VARIANT         1276
FT                   /note="Y -> H (in MRD52; uncertain significance;
FT                   dbSNP:rs539982914)"
FT                   /evidence="ECO:0000269|PubMed:23033978"
FT                   /id="VAR_069408"
FT   VARIANT         1416
FT                   /note="S -> P (in dbSNP:rs13373934)"
FT                   /id="VAR_055905"
FT   VARIANT         1771
FT                   /note="T -> A (in dbSNP:rs4971053)"
FT                   /evidence="ECO:0000269|PubMed:10860993"
FT                   /id="VAR_028949"
FT   VARIANT         1775
FT                   /note="C -> W (in MRD52; uncertain significance;
FT                   dbSNP:rs753734834)"
FT                   /evidence="ECO:0000269|PubMed:23033978"
FT                   /id="VAR_069409"
FT   VARIANT         2085
FT                   /note="V -> I (in MRD52; uncertain significance;
FT                   dbSNP:rs749494995)"
FT                   /evidence="ECO:0000269|PubMed:27824329"
FT                   /id="VAR_080559"
FT   VARIANT         2148..2969
FT                   /note="Missing (in MRD52)"
FT                   /evidence="ECO:0000269|PubMed:28191889"
FT                   /id="VAR_080560"
FT   VARIANT         2396
FT                   /note="R -> H (in MRD52; uncertain significance;
FT                   dbSNP:rs753029013)"
FT                   /evidence="ECO:0000269|PubMed:28191889"
FT                   /id="VAR_080561"
FT   VARIANT         2791
FT                   /note="A -> P (in MRD52; dbSNP:rs1553241570)"
FT                   /evidence="ECO:0000269|PubMed:28394464"
FT                   /id="VAR_080562"
FT   VARIANT         2853
FT                   /note="D -> G (in MRD52; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:23033978"
FT                   /id="VAR_069410"
FT   MUTAGEN         1220
FT                   /note="Q->R: Abolishes methylation by N6AMT1."
FT                   /evidence="ECO:0000269|PubMed:26797129"
FT   CONFLICT        2594
FT                   /note="K -> N (in Ref. 1; AAF68983)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2697
FT                   /note="D -> H (in Ref. 1; AAF68983)"
FT                   /evidence="ECO:0000305"
FT   HELIX           2040..2044
FT                   /evidence="ECO:0007829|PDB:6INE"
FT   HELIX           2054..2065
FT                   /evidence="ECO:0007829|PDB:6INE"
FT   STRAND          2081..2084
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   STRAND          2104..2106
FT                   /evidence="ECO:0007829|PDB:3OPE"
FT   STRAND          2108..2111
FT                   /evidence="ECO:0007829|PDB:6AGO"
FT   HELIX           2116..2118
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   TURN            2124..2126
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   HELIX           2130..2132
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   STRAND          2133..2135
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   TURN            2137..2141
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   STRAND          2147..2151
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   STRAND          2155..2163
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   STRAND          2170..2173
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   STRAND          2177..2180
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   HELIX           2181..2190
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   HELIX           2192..2194
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   HELIX           2195..2197
FT                   /evidence="ECO:0007829|PDB:6AGO"
FT   STRAND          2200..2204
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   STRAND          2207..2210
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   STRAND          2212..2215
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   HELIX           2217..2220
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   STRAND          2228..2236
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   STRAND          2239..2248
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   HELIX           2260..2263
FT                   /evidence="ECO:0007829|PDB:6WZW"
FT   STRAND          2282..2284
FT                   /evidence="ECO:0007829|PDB:4YNM"
FT   HELIX           2438..2458
FT                   /evidence="ECO:0007829|PDB:3MQM"
FT   HELIX           2469..2471
FT                   /evidence="ECO:0007829|PDB:3MQM"
FT   HELIX           2477..2479
FT                   /evidence="ECO:0007829|PDB:3MQM"
FT   HELIX           2483..2486
FT                   /evidence="ECO:0007829|PDB:3MQM"
FT   HELIX           2493..2501
FT                   /evidence="ECO:0007829|PDB:3MQM"
FT   HELIX           2508..2526
FT                   /evidence="ECO:0007829|PDB:3MQM"
FT   HELIX           2531..2558
FT                   /evidence="ECO:0007829|PDB:3MQM"
SQ   SEQUENCE   2969 AA;  332790 MW;  DA0135C72A2E2065 CRC64;
     MDPRNTAMLG LGSDSEGFSR KSPSAISTGT LVSKREVELE KNTKEEEDLR KRNRERNIEA
     GKDDGLTDAQ QQFSVKETNF SEGNLKLKIG LQAKRTKKPP KNLENYVCRP AIKTTIKHPR
     KALKSGKMTD EKNEHCPSKR DPSKLYKKAD DVAAIECQSE EVIRLHSQGE NNPLSKKLSP
     VHSEMADYIN ATPSTLLGSR DPDLKDRALL NGGTSVTEKL AQLIATCPPS KSSKTKPKKL
     GTGTTAGLVS KDLIRKAGVG SVAGIIHKDL IKKPTISTAV GLVTKDPGKK PVFNAAVGLV
     NKDSVKKLGT GTTAVFINKN LGKKPGTITT VGLLSKDSGK KLGIGIVPGL VHKESGKKLG
     LGTVVGLVNK DLGKKLGSTV GLVAKDCAKK IVASSAMGLV NKDIGKKLMS CPLAGLISKD
     AINLKAEALL PTQEPLKASC STNINNQESQ ELSESLKDSA TSKTFEKNVV RQNKESILEK
     FSVRKEIINL EKEMFNEGTC IQQDSFSSSE KGSYETSKHE KQPPVYCTSP DFKMGGASDV
     STAKSPFSAV GESNLPSPSP TVSVNPLTRS PPETSSQLAP NPLLLSSTTE LIEEISESVG
     KNQFTSESTH LNVGHRSVGH SISIECKGID KEVNDSKTTH IDIPRISSSL GKKPSLTSES
     SIHTITPSVV NFTSLFSNKP FLKLGAVSAS DKHCQVAESL STSLQSKPLK KRKGRKPRWT
     KVVARSTCRS PKGLELERSE LFKNVSCSSL SNSNSEPAKF MKNIGPPSFV DHDFLKRRLP
     KLSKSTAPSL ALLADSEKPS HKSFATHKLS SSMCVSSDLL SDIYKPKRGR PKSKEMPQLE
     GPPKRTLKIP ASKVFSLQSK EEQEPPILQP EIEIPSFKQG LSVSPFPKKR GRPKRQMRSP
     VKMKPPVLSV APFVATESPS KLESESDNHR SSSDFFESED QLQDPDDLDD SHRPSVCSMS
     DLEMEPDKKI TKRNNGQLMK TIIRKINKMK TLKRKKLLNQ ILSSSVESSN KGKVQSKLHN
     TVSSLAATFG SKLGQQINVS KKGTIYIGKR RGRKPKTVLN GILSGSPTSL AVLEQTAQQA
     AGSALGQILP PLLPSSASSS EILPSPICSQ SSGTSGGQSP VSSDAGFVEP SSVPYLHLHS
     RQGSMIQTLA MKKASKGRRR LSPPTLLPNS PSHLSELTSL KEATPSPISE SHSDETIPSD
     SGIGTDNNST SDRAEKFCGQ KKRRHSFEHV SLIPPETSTV LSSLKEKHKH KCKRRNHDYL
     SYDKMKRQKR KRKKKYPQLR NRQDPDFIAE LEELISRLSE IRITHRSHHF IPRDLLPTIF
     RINFNSFYTH PSFPLDPLHY IRKPDLKKKR GRPPKMREAM AEMPFMHSLS FPLSSTGFYP
     SYGMPYSPSP LTAAPIGLGY YGRYPPTLYP PPPSPSFTTP LPPPSYMHAG HLLLNPAKYH
     KKKHKLLRQE AFLTTSRTPL LSMSTYPSVP PEMAYGWMVE HKHRHRHKHR EHRSSEQPQV
     SMDTGSSRSV LESLKRYRFG KDAVGERYKH KEKHRCHMSC PHLSPSKSLI NREEQWVHRE
     PSESSPLALG LQTPLQIDCS ESSPSLSLGG FTPNSEPASS DEHTNLFTSA IGSCRVSNPN
     SSGRKKLTDS PGLFSAQDTS LNRLHRKESL PSNERAVQTL AGSQPTSDKP SQRPSESTNC
     SPTRKRSSSE STSSTVNGVP SRSPRLVASG DDSVDSLLQR MVQNEDQEPM EKSIDAVIAT
     ASAPPSSSPG RSHSKDRTLG KPDSLLVPAV TSDSCNNSIS LLSEKLTSSC SPHHIKRSVV
     EAMQRQARKM CNYDKILATK KNLDHVNKIL KAKKLQRQAR TGNNFVKRRP GRPRKCPLQA
     VVSMQAFQAA QFVNPELNRD EEGAALHLSP DTVTDVIEAV VQSVNLNPEH KKGLKRKGWL
     LEEQTRKKQK PLPEEEEQEN NKSFNEAPVE IPSPSETPAK PSEPESTLQP VLSLIPREKK
     PPRPPKKKYQ KAGLYSDVYK TTDPKSRLIQ LKKEKLEYTP GEHEYGLFPA PIHVVFFVSG
     KYLRQKRIDF QLPYDILWQW KHNQLYKKPD VPLYKKIRSN VYVDVKPLSG YEATTCNCKK
     PDDDTRKGCV DDCLNRMIFA ECSPNTCPCG EQCCNQRIQR HEWVQCLERF RAEEKGWGIR
     TKEPLKAGQF IIEYLGEVVS EQEFRNRMIE QYHNHSDHYC LNLDSGMVID SYRMGNEARF
     INHSCDPNCE MQKWSVNGVY RIGLYALKDM PAGTELTYDY NFHSFNVEKQ QLCKCGFEKC
     RGIIGGKSQR VNGLTSSKNS QPMATHKKSG RSKEKRKSKH KLKKRRGHLS EEPSENINTP
     TRLTPQLQMK PMSNRERNFV LKHHVFLVRN WEKIRQKQEE VKHTSDNIHS ASLYTRWNGI
     CRDDGNIKSD VFMTQFSALQ TARSVRTRRL AAAEENIEVA RAARLAQIFK EICDGIISYK
     DSSRQALAAP LLNLPPKKKN ADYYEKISDP LDLITIEKQI LTGYYKTVEA FDADMLKVFR
     NAEKYYGRKS PVGRDVCRLR KAYYNARHEA SAQIDEIVGE TASEADSSET SVSEKENGHE
     KDDDVIRCIC GLYKDEGLMI QCDKCMVWQH CDCMGVNSDV EHYLCEQCDP RPVDREVPMI
     PRPHYAQPGC VYFICLLRDD LLLRQGDCVY LMRDSRRTPD GHPVRQSYRL LSHINRDKLD
     IFRIEKLWKN EKEERFAFGH HYFRPHETHH SPSRRFYHNE LFRVPLYEII PLEAVVGTCC
     VLDLYTYCKG RPKGVKEQDV YICDYRLDKS AHLFYKIHRN RYPVCTKPYA FDHFPKKLTP
     KKDFSPHYVP DNYKRNGGRS SWKSERSKPP LKDLGQEDDA LPLIEEVLAS QEQAANEIPS
     LEEPEREGAT ANVSEGEKKT EESSQEPQST CTPEERRHNQ RERLNQILLN LLEKIPGKNA
     IDVTYLLEEG SGRKLRRRTL FIPENSFRK
//