SPT2_HUMAN
ID SPT2_HUMAN Reviewed; 685 AA.
AC Q68D10; Q6AWA5; Q6MZI5; Q7Z390; Q7Z470; Q86VG8; Q8N3E7; Q8N417; Q8N8I3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein SPT2 homolog;
DE AltName: Full=Protein KU002155;
DE AltName: Full=SPT2 domain-containing protein 1;
GN Name=SPTY2D1;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-617.
RC TISSUE=Amygdala, Colon endothelium, Salivary gland, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 389-685 (ISOFORM 1), AND VARIANT ARG-617.
RC TISSUE=Pancreas, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-627.
RC TISSUE=Prostate;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 131-685 (ISOFORM 2).
RA Kim N.-S., Shon H.-Y., Oh J.-H., Lee J.-Y., Kim J.-M., Hahn Y., Park H.-S.,
RA Kim S., Kim Y.S.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599, 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-582, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND DOMAIN.
RX PubMed=23378026; DOI=10.1242/jcs.112623;
RA Osakabe A., Tachiwana H., Takaku M., Hori T., Obuse C., Kimura H.,
RA Fukagawa T., Kurumizaka H.;
RT "Vertebrate Spt2 is a novel nucleolar histone chaperone that assists in
RT ribosomal DNA transcription.";
RL J. Cell Sci. 126:1323-1332(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-37 AND LYS-187, 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 [12]
RP INTERACTION WITH HISTONE H3.3.
RX PubMed=33857403; DOI=10.1016/j.molcel.2021.03.041;
RA Hammond C.M., Bao H., Hendriks I.A., Carraro M., Garcia-Nieto A., Liu Y.,
RA Reveron-Gomez N., Spanos C., Chen L., Rappsilber J., Nielsen M.L.,
RA Patel D.J., Huang H., Groth A.;
RT "DNAJC9 integrates heat shock molecular chaperones into the histone
RT chaperone network.";
RL Mol. Cell 0:0-0(2021).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 571-685 IN COMPLEX WITH HISTONE H3
RP AND H4, FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF MET-641;
RP 651-GLU-GLU-652; 658-LEU-GLY-659 AND 662-GLU-ASP-663.
RX PubMed=26109053; DOI=10.1101/gad.261115.115;
RA Chen S., Rufiange A., Huang H., Rajashankar K.R., Nourani A., Patel D.J.;
RT "Structure-function studies of histone H3/H4 tetramer maintenance during
RT transcription by chaperone Spt2.";
RL Genes Dev. 29:1326-1340(2015).
CC -!- FUNCTION: Histone chaperone that stabilizes pre-existing histone
CC tetramers and regulates replication-independent histone exchange on
CC chromatin (PubMed:26109053). Required for normal chromatin refolding in
CC the coding region of transcribed genes, and for the suppression of
CC spurious transcription (PubMed:26109053). Binds DNA and histones and
CC promotes nucleosome assembly (in vitro) (PubMed:23378026,
CC PubMed:26109053). Facilitates formation of tetrameric histone complexes
CC containing histone H3 and H4 (PubMed:26109053). Modulates RNA
CC polymerase 1-mediated transcription (By similarity). Binds DNA, with a
CC preference for branched DNA species, such as Y-form DNA and Holliday
CC junction DNA (PubMed:23378026). {ECO:0000250|UniProtKB:E1BUG7,
CC ECO:0000269|PubMed:23378026}.
CC -!- SUBUNIT: Interacts with histones (PubMed:23378026). Interacts with a
CC heterotetrameric complex formed by histone H3 and H4, especially when
CC the histone tetramer is not bound to DNA (PubMed:26109053). Interacts
CC with histone H3.3 (PubMed:33857403). {ECO:0000269|PubMed:23378026,
CC ECO:0000269|PubMed:26109053, ECO:0000269|PubMed:33857403}.
CC -!- INTERACTION:
CC Q68D10-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12018536, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:E1BUG7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q68D10-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68D10-2; Sequence=VSP_030690;
CC Name=3;
CC IsoId=Q68D10-3; Sequence=VSP_030688, VSP_030689;
CC -!- DOMAIN: The acidic C-terminal domain mediates interaction with histone
CC H3/H4 complexes. {ECO:0000269|PubMed:23378026,
CC ECO:0000269|PubMed:26109053}.
CC -!- MISCELLANEOUS: The histone binding domain can functionally complement
CC the yeast ortholog in regulating histone exchange and suppression of
CC spurious transcription. {ECO:0000269|PubMed:26109053}.
CC -!- SIMILARITY: Belongs to the SPT2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP13351.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL834393; CAD39055.1; -; mRNA.
DR EMBL; BX538046; CAD97985.1; -; mRNA.
DR EMBL; BX641102; CAE46047.1; -; mRNA.
DR EMBL; BX648114; CAH10772.1; -; mRNA.
DR EMBL; CR749626; CAH18420.1; -; mRNA.
DR EMBL; AC112694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036844; AAH36844.1; -; mRNA.
DR EMBL; BC056261; AAH56261.1; -; mRNA.
DR EMBL; AK096760; BAC04858.1; -; mRNA.
DR EMBL; AF452716; AAP13351.1; ALT_INIT; mRNA.
DR CCDS; CCDS31441.1; -. [Q68D10-1]
DR RefSeq; NP_919261.2; NM_194285.2. [Q68D10-1]
DR PDB; 5BS7; X-ray; 3.30 A; E/F=571-685.
DR PDB; 5BSA; X-ray; 4.61 A; E/F=571-685.
DR PDBsum; 5BS7; -.
DR PDBsum; 5BSA; -.
DR AlphaFoldDB; Q68D10; -.
DR SMR; Q68D10; -.
DR BioGRID; 126830; 109.
DR IntAct; Q68D10; 23.
DR STRING; 9606.ENSP00000337991; -.
DR iPTMnet; Q68D10; -.
DR MetOSite; Q68D10; -.
DR PhosphoSitePlus; Q68D10; -.
DR BioMuta; SPTY2D1; -.
DR DMDM; 296452945; -.
DR EPD; Q68D10; -.
DR jPOST; Q68D10; -.
DR MassIVE; Q68D10; -.
DR MaxQB; Q68D10; -.
DR PaxDb; Q68D10; -.
DR PeptideAtlas; Q68D10; -.
DR PRIDE; Q68D10; -.
DR ProteomicsDB; 66043; -. [Q68D10-1]
DR ProteomicsDB; 66044; -. [Q68D10-2]
DR ProteomicsDB; 66045; -. [Q68D10-3]
DR Antibodypedia; 64057; 16 antibodies from 8 providers.
DR DNASU; 144108; -.
DR Ensembl; ENST00000336349.6; ENSP00000337991.5; ENSG00000179119.15. [Q68D10-1]
DR GeneID; 144108; -.
DR KEGG; hsa:144108; -.
DR MANE-Select; ENST00000336349.6; ENSP00000337991.5; NM_194285.3; NP_919261.2.
DR UCSC; uc001moy.4; human. [Q68D10-1]
DR CTD; 144108; -.
DR DisGeNET; 144108; -.
DR GeneCards; SPTY2D1; -.
DR HGNC; HGNC:26818; SPTY2D1.
DR HPA; ENSG00000179119; Tissue enhanced (bone).
DR neXtProt; NX_Q68D10; -.
DR OpenTargets; ENSG00000179119; -.
DR PharmGKB; PA142670875; -.
DR VEuPathDB; HostDB:ENSG00000179119; -.
DR eggNOG; ENOG502QWHS; Eukaryota.
DR GeneTree; ENSGT00940000154133; -.
DR HOGENOM; CLU_025934_0_0_1; -.
DR InParanoid; Q68D10; -.
DR OMA; MMDFDNI; -.
DR OrthoDB; 1092455at2759; -.
DR PhylomeDB; Q68D10; -.
DR TreeFam; TF350176; -.
DR PathwayCommons; Q68D10; -.
DR SignaLink; Q68D10; -.
DR BioGRID-ORCS; 144108; 12 hits in 1084 CRISPR screens.
DR ChiTaRS; SPTY2D1; human.
DR GenomeRNAi; 144108; -.
DR Pharos; Q68D10; Tdark.
DR PRO; PR:Q68D10; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q68D10; protein.
DR Bgee; ENSG00000179119; Expressed in amniotic fluid and 187 other tissues.
DR Genevisible; Q68D10; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0140713; F:histone chaperone activity; IMP:GO_Central.
DR GO; GO:0001042; F:RNA polymerase I core binding; ISS:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:GO_Central.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IMP:UniProtKB.
DR GO; GO:0010847; P:regulation of chromatin assembly; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR InterPro; IPR013256; Chromatin_SPT2.
DR Pfam; PF08243; SPT2; 1.
DR SMART; SM00784; SPT2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..685
FT /note="Protein SPT2 homolog"
FT /id="PRO_0000315736"
FT REGION 1..570
FT /note="Important for interaction with DNA"
FT /evidence="ECO:0000269|PubMed:23378026"
FT REGION 79..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..685
FT /note="Important for interaction with histones"
FT /evidence="ECO:0000269|PubMed:23378026"
FT REGION 644..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 45..81
FT /evidence="ECO:0000255"
FT COILED 123..148
FT /evidence="ECO:0000255"
FT COILED 645..685
FT /evidence="ECO:0000255"
FT COMPBIAS 100..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..610
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 582
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 187
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 106
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030688"
FT VAR_SEQ 323..685
FT /note="SVPKTSASRTQKSAVEHKAKKSLSHPSHSRPGPMVTPHNKAKSPGVRQPGSS
FT SSSAPGQPSTGVARPTVSSGPVPRRQNGSSSSGPERSISGSKKPTNDSNPSRRTVSGTC
FT GPGQPASSSGGPGRPISGSVSSARPLGSSRGPGRPVSSPHELRRPVSGLGPPGRSVSGP
FT GRSISGSIPAGRTVSNSVPGRPVSSLGPGQTVSSSGPTIKPKCTVVSETISSKNIISRS
FT SNGQMNGMKPPLSGYRAAQGPQRLPFPTGYKRQREYEEEDDDDDEYDSEMEDFIEDEGE
FT PQEEISKHIREIFGYDRKKYKDESDYALRYMESSWKEQQKEEAKSLRLGMQEDLEEMRR
FT EEEEMQRRRAKKLKRR -> KHVWKENKYMKRDWLFYFQCIEYIRLLFIF (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030689"
FT VAR_SEQ 648..659
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_030690"
FT VARIANT 317
FT /note="S -> F (in dbSNP:rs12795406)"
FT /id="VAR_038298"
FT VARIANT 447
FT /note="R -> Q (in dbSNP:rs16935599)"
FT /id="VAR_038299"
FT VARIANT 617
FT /note="K -> R (in dbSNP:rs35411689)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_038300"
FT MUTAGEN 641
FT /note="M->A: Strongly reduces affinity for histones."
FT /evidence="ECO:0000269|PubMed:26109053"
FT MUTAGEN 651..652
FT /note="EE->AA: Strongly reduces affinity for histones."
FT /evidence="ECO:0000269|PubMed:26109053"
FT MUTAGEN 658..659
FT /note="LG->AN: Strongly reduces affinity for histones."
FT /evidence="ECO:0000269|PubMed:26109053"
FT MUTAGEN 662..663
FT /note="ED->AA: Strongly reduces affinity for histones."
FT /evidence="ECO:0000269|PubMed:26109053"
FT CONFLICT 29
FT /note="P -> L (in Ref. 1; CAE46047)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="P -> Q (in Ref. 1; CAE46047)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="R -> Q (in Ref. 1; CAE46047)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="E -> G (in Ref. 1; CAE46047)"
FT /evidence="ECO:0000305"
FT HELIX 614..623
FT /evidence="ECO:0007829|PDB:5BS7"
FT HELIX 636..639
FT /evidence="ECO:0007829|PDB:5BS7"
FT HELIX 645..674
FT /evidence="ECO:0007829|PDB:5BS7"
SQ SEQUENCE 685 AA; 75599 MW; D3A324C9598DD2D1 CRC64;
MDFREILMIA SKGQGVNNVP KRYSLAVGPP KKDPKVKGVQ SAAVQAFLKR KEEELRRKAL
EEKRRKEELV KKRIELKHDK KARAMAKRTK DNFHGYNGIP IEEKSKKRQA TESHTSQGTD
REYEMEEENE FLEYNHAESE QEYEEEQEPP KVESKPKVPL KSAPPPMNFT DLLRLAEKKQ
FEPVEIKVVK KSEERPMTAE ELREREFLER KHRRKKLETD GKLPPTVSKK APSQKESVGT
KLSKGSGDRH PSSKGMPLPH AEKKSRPSMA NEKHLALSSS KSMPGERIKA GSGNSSQPSL
REGHDKPVFN GAGKPHSSTS SPSVPKTSAS RTQKSAVEHK AKKSLSHPSH SRPGPMVTPH
NKAKSPGVRQ PGSSSSSAPG QPSTGVARPT VSSGPVPRRQ NGSSSSGPER SISGSKKPTN
DSNPSRRTVS GTCGPGQPAS SSGGPGRPIS GSVSSARPLG SSRGPGRPVS SPHELRRPVS
GLGPPGRSVS GPGRSISGSI PAGRTVSNSV PGRPVSSLGP GQTVSSSGPT IKPKCTVVSE
TISSKNIISR SSNGQMNGMK PPLSGYRAAQ GPQRLPFPTG YKRQREYEEE DDDDDEYDSE
MEDFIEDEGE PQEEISKHIR EIFGYDRKKY KDESDYALRY MESSWKEQQK EEAKSLRLGM
QEDLEEMRRE EEEMQRRRAK KLKRR
