BAF_HUMAN
ID BAF_HUMAN Reviewed; 89 AA.
AC O75531; O60558; Q6FGG7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Barrier-to-autointegration factor {ECO:0000303|PubMed:9465049};
DE AltName: Full=Breakpoint cluster region protein 1 {ECO:0000303|PubMed:9740667};
DE Contains:
DE RecName: Full=Barrier-to-autointegration factor, N-terminally processed {ECO:0000305};
GN Name=BANF1 {ECO:0000303|PubMed:21549337, ECO:0000312|HGNC:HGNC:17397};
GN Synonyms=BAF {ECO:0000303|PubMed:9465049},
GN BCRG1 {ECO:0000303|PubMed:9740667};
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], FUNCTION (MICROBIAL INFECTION), AND FUNCTION.
RX PubMed=9465049; DOI=10.1073/pnas.95.4.1528;
RA Lee M.S., Craigie R.;
RT "A previously unidentified host protein protects retroviral DNA from
RT autointegration.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:1528-1533(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Uterus;
RX PubMed=9740667; DOI=10.1006/geno.1998.5406;
RA Lynch R.A., Piper M., Bankier A., Bhugra B., Surti U., Liu J., Buckler A.,
RA Dear P.H., Menon A.G.;
RT "Genomic and functional map of the chromosome 14 t(12;14) breakpoint
RT cluster region in uterine leiomyoma.";
RL Genomics 52:17-26(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang J., Liu T., Ye M., Zhang Q., Fu G., Zhou J., Wu J., Shen Y., Yu M.,
RA Chen S., Mao M., Chen Z.;
RT "Human BAF homolog gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [6]
RP FUNCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF LYS-6; PRO-14; LYS-18;
RP ILE-26; LYS-41; LEU-50; LYS-53; LYS-54; TRP-62 AND CYS-80.
RX PubMed=11005805; DOI=10.1074/jbc.m002626200;
RA Harris D., Engelman A.;
RT "Both the structure and DNA binding function of the barrier-to-
RT autointegration factor contribute to reconstitution of HIV type 1
RT integration in vitro.";
RL J. Biol. Chem. 275:39671-39677(2000).
RN [7]
RP MULTIMERIZATION, AND FUNCTION.
RX PubMed=10908652; DOI=10.1073/pnas.150240197;
RA Zheng R., Ghirlando R., Lee M.S., Mizuuchi K., Krause M., Craigie R.;
RT "Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-
RT order nucleoprotein complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8997-9002(2000).
RN [8]
RP FUNCTION, AND INTERACTION WITH EMD.
RX PubMed=11792822; DOI=10.1242/jcs.114.24.4575;
RA Haraguchi T., Koujin T., Segura-Totten M., Lee K.K., Matsuoka Y.,
RA Yoneda Y., Wilson K.L., Hiraoka Y.;
RT "BAF is required for emerin assembly into the reforming nuclear envelope.";
RL J. Cell Sci. 114:4575-4585(2001).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF LYS-6; ASP-9; GLY-25; GLY-27; LEU-46; GLY-47;
RP VAL-51; LYS-53; LYS-54 AND ARG-75.
RX PubMed=12163470; DOI=10.1083/jcb.200202019;
RA Segura-Totten M., Kowalski A.K., Craigie R., Wilson K.L.;
RT "Barrier-to-autointegration factor: major roles in chromatin decondensation
RT and nuclear assembly.";
RL J. Cell Biol. 158:475-485(2002).
RN [10]
RP INTERACTION WITH HIV-1 PRE-INTEGRATION COMPLEX (MICROBIAL INFECTION).
RX PubMed=12663813; DOI=10.1128/jvi.77.8.5030-5036.2003;
RA Lin C.W., Engelman A.;
RT "The barrier-to-autointegration factor is a component of functional human
RT immunodeficiency virus type 1 preintegration complexes.";
RL J. Virol. 77:5030-5036(2003).
RN [11]
RP INTERACTION WITH HIV-1 MATRIX PROTEIN (MICROBIAL INFECTION).
RX PubMed=14645565; DOI=10.1128/jvi.77.24.13084-13092.2003;
RA Mansharamani M., Graham D.R., Monie D., Lee K.K., Hildreth J.E.,
RA Siliciano R.F., Wilson K.L.;
RT "Barrier-to-autointegration factor BAF binds p55 Gag and matrix and is a
RT host component of human immunodeficiency virus type 1 virions.";
RL J. Virol. 77:13084-13092(2003).
RN [12]
RP INTERACTION WITH LEMD3/MAN1, MUTAGENESIS OF LYS-6; ARG-8; ASP-9; PRO-14;
RP GLY-25; ILE-26; ARG-37; LYS-41; LEU-46; GLY-47; LEU-50; VAL-51; LYS-53;
RP LYS-54; TRP-62 AND CYS-80, AND DOMAIN.
RX PubMed=15681850; DOI=10.1074/jbc.m413020200;
RA Mansharamani M., Wilson K.L.;
RT "Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two
RT modes of binding to barrier-to-autointegration factor.";
RL J. Biol. Chem. 280:13863-13870(2005).
RN [13]
RP INTERACTION WITH HISTONE H1/H3, AND MUTAGENESIS OF LYS-6; ARG-8; ASP-9;
RP PRO-14; LYS-18; GLY-25; ILE-26; VAL-29; LYS-32; LYS-33; ARG-37; LYS-41;
RP LEU-46; GLY-47; LEU-50; VAL-51; LYS-53; LYS-54; ARG-60; TRP-62; LYS-64;
RP ARG-75; CYS-80 AND ARG-82.
RX PubMed=16203725; DOI=10.1074/jbc.m509917200;
RA de Oca R.M., Lee K.K., Wilson K.L.;
RT "Binding of barrier to autointegration factor (BAF) to histone H3 and
RT selected linker histones including H1.1.";
RL J. Biol. Chem. 280:42252-42262(2005).
RN [14]
RP PHOSPHORYLATION AT SER-4, AND MUTAGENESIS OF SER-4.
RX PubMed=16371512; DOI=10.1091/mbc.e05-04-0356;
RA Bengtsson L., Wilson K.L.;
RT "Barrier-to-autointegration factor phosphorylation on Ser-4 regulates
RT emerin binding to lamin A in vitro and emerin localization in vivo.";
RL Mol. Biol. Cell 17:1154-1163(2006).
RN [15]
RP INTERACTION WITH BANF2.
RX PubMed=16337940; DOI=10.1016/j.yexcr.2005.11.013;
RA Tifft K.E., Segura-Totten M., Lee K.K., Wilson K.L.;
RT "Barrier-to-autointegration factor-like (BAF-L): a proposed regulator of
RT BAF.";
RL Exp. Cell Res. 312:478-487(2006).
RN [16]
RP PHOSPHORYLATION AT THR-2; THR-3 AND SER-4, SUBCELLULAR LOCATION,
RP DNA-BINDING, AND MUTAGENESIS OF 2-THR--SER-4.
RX PubMed=16495336; DOI=10.1091/mbc.e05-12-1179;
RA Nichols R.J., Wiebe M.S., Traktman P.;
RT "The vaccinia-related kinases phosphorylate the N' terminus of BAF,
RT regulating its interaction with DNA and its retention in the nucleus.";
RL Mol. Biol. Cell 17:2451-2464(2006).
RN [17]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=16680152; DOI=10.1038/nature04682;
RA Jacque J.-M., Stevenson M.;
RT "The inner-nuclear-envelope protein emerin regulates HIV-1 infectivity.";
RL Nature 441:641-645(2006).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION (MICROBIAL INFECTION).
RX PubMed=18005698; DOI=10.1016/j.chom.2007.03.007;
RA Wiebe M.S., Traktman P.;
RT "Poxviral B1 kinase overcomes barrier to autointegration factor, a host
RT defense against virus replication.";
RL Cell Host Microbe 1:187-197(2007).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [20]
RP IDENTIFICATION BY MASS 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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION, DEPHOSPHORYLATION, AND INTERACTION WITH ANKLE2.
RX PubMed=22770216; DOI=10.1016/j.cell.2012.04.043;
RA Asencio C., Davidson I.F., Santarella-Mellwig R., Ly-Hartig T.B., Mall M.,
RA Wallenfang M.R., Mattaj I.W., Gorjanacz M.;
RT "Coordination of kinase and phosphatase activities by Lem4 enables nuclear
RT envelope reassembly during mitosis.";
RL Cell 150:122-135(2012).
RN [24]
RP REVIEW.
RX PubMed=15130582; DOI=10.1016/j.tcb.2004.03.004;
RA Segura-Totten M., Wilson K.L.;
RT "BAF: roles in chromatin, nuclear structure and retrovirus integration.";
RL Trends Cell Biol. 14:261-266(2004).
RN [25]
RP INTERACTION WITH ANKLE1, SUBUNIT, AND DIMERIZATION.
RX PubMed=22399800; DOI=10.1242/jcs.098392;
RA Brachner A., Braun J., Ghodgaonkar M., Castor D., Zlopasa L., Ehrlich V.,
RA Jiricny J., Gotzmann J., Knasmueller S., Foisner R.;
RT "The endonuclease Ankle1 requires its LEM and GIY-YIG motifs for DNA
RT cleavage in vivo.";
RL J. Cell Sci. 125:1048-1057(2012).
RN [26]
RP PHOSPHORYLATION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 2-THR--SER-4.
RX PubMed=24600006; DOI=10.1128/jvi.00427-14;
RA Jamin A., Wicklund A., Wiebe M.S.;
RT "Cell- and virus-mediated regulation of the barrier-to-autointegration
RT factor's phosphorylation state controls its DNA binding, dimerization,
RT subcellular localization, and antipoxviral activity.";
RL J. Virol. 88:5342-5355(2014).
RN [27]
RP FUNCTION.
RX PubMed=25991860; DOI=10.1073/pnas.1501235112;
RA Kobayashi S., Koujin T., Kojidani T., Osakada H., Mori C., Hiraoka Y.,
RA Haraguchi T.;
RT "BAF is a cytosolic DNA sensor that leads to exogenous DNA avoiding
RT autophagy.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:7027-7032(2015).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [29]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DNA-BINDING, AND MUTAGENESIS OF
RP GLY-47 AND LEU-58.
RX PubMed=28841419; DOI=10.1016/j.cell.2017.07.038;
RA Samwer M., Schneider M.W.G., Hoefler R., Schmalhorst P.S., Jude J.G.,
RA Zuber J., Gerlich D.W.;
RT "DNA cross-bridging shapes a single nucleus from a set of mitotic
RT chromosomes.";
RL Cell 170:956-972(2017).
RN [30]
RP INTERACTION WITH LEMD2.
RX PubMed=32494070; DOI=10.1038/s41586-020-2232-x;
RA von Appen A., LaJoie D., Johnson I.E., Trnka M.J., Pick S.M.,
RA Burlingame A.L., Ullman K.S., Frost A.;
RT "LEM2 phase separation promotes ESCRT-mediated nuclear envelope
RT reformation.";
RL Nature 582:115-118(2020).
RN [31]
RP FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, AND MUTAGENESIS OF GLY-47 AND
RP LEU-58.
RX PubMed=32792394; DOI=10.1126/science.aaw6421;
RA Guey B., Wischnewski M., Decout A., Makasheva K., Kaynak M., Sakar M.S.,
RA Fierz B., Ablasser A.;
RT "BAF restricts cGAS on nuclear DNA to prevent innate immune activation.";
RL Science 369:823-828(2020).
RN [32]
RP STRUCTURE BY NMR.
RX PubMed=9783751; DOI=10.1038/2345;
RA Cai M., Huang Y., Zheng R., Wei S.Q., Ghirlando R., Lee M.S., Craigie R.,
RA Gronenborn A.M., Clore G.M.;
RT "Solution structure of the cellular factor BAF responsible for protecting
RT retroviral DNA from autointegration.";
RL Nat. Struct. Biol. 5:903-909(1998).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF HOMODIMER, AND DOMAIN.
RX PubMed=10924106; DOI=10.1021/bi000572w;
RA Umland T.C., Wei S.-Q., Craigie R., Davies D.R.;
RT "Structural basis of DNA bridging by barrier-to-autointegration factor.";
RL Biochemistry 39:9130-9138(2000).
RN [34]
RP VARIANT NGPS THR-12.
RX PubMed=21549337; DOI=10.1016/j.ajhg.2011.04.010;
RA Puente X.S., Quesada V., Osorio F.G., Cabanillas R., Cadinanos J.,
RA Fraile J.M., Ordonez G.R., Puente D.A., Gutierrez-Fernandez A.,
RA Fanjul-Fernandez M., Levy N., Freije J.M., Lopez-Otin C.;
RT "Exome sequencing and functional analysis identifies BANF1 mutation as the
RT cause of a hereditary progeroid syndrome.";
RL Am. J. Hum. Genet. 88:650-656(2011).
CC -!- FUNCTION: Non-specific DNA-binding protein that plays key roles in
CC mitotic nuclear reassembly, chromatin organization, DNA damage
CC response, gene expression and intrinsic immunity against foreign DNA
CC (PubMed:10908652, PubMed:11792822, PubMed:12163470, PubMed:18005698,
CC PubMed:25991860, PubMed:28841419, PubMed:32792394). Contains two non-
CC specific double-stranded DNA (dsDNA)-binding sites which promote DNA
CC cross-bridging (PubMed:9465049). Plays a key role in nuclear membrane
CC reformation at the end of mitosis by driving formation of a single
CC nucleus in a spindle-independent manner (PubMed:28841419). Transiently
CC cross-bridges anaphase chromosomes via its ability to bridge distant
CC DNA sites, leading to the formation of a dense chromatin network at the
CC chromosome ensemble surface that limits membranes to the surface
CC (PubMed:28841419). Also acts as a negative regulator of innate immune
CC activation by restricting CGAS activity toward self-DNA upon acute loss
CC of nuclear membrane integrity (PubMed:32792394). Outcompetes CGAS for
CC DNA-binding, thereby preventing CGAS activation and subsequent damaging
CC autoinflammatory responses (PubMed:32792394). Involved in the
CC recognition of exogenous dsDNA in the cytosol: associates with
CC exogenous dsDNA immediately after its appearance in the cytosol at
CC endosome breakdown and is required to avoid autophagy
CC (PubMed:25991860). In case of poxvirus infection, has an antiviral
CC activity by blocking viral DNA replication (PubMed:18005698).
CC {ECO:0000269|PubMed:10908652, ECO:0000269|PubMed:11792822,
CC ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:18005698,
CC ECO:0000269|PubMed:25991860, ECO:0000269|PubMed:28841419,
CC ECO:0000269|PubMed:32792394, ECO:0000269|PubMed:9465049}.
CC -!- FUNCTION: (Microbial infection) Exploited by retroviruses for
CC inhibiting self-destructing autointegration of retroviral DNA, thereby
CC promoting integration of viral DNA into the host chromosome
CC (PubMed:9465049, PubMed:11005805, PubMed:16680152). EMD and BAF are
CC cooperative cofactors of HIV-1 infection (PubMed:16680152). Association
CC of EMD with the viral DNA requires the presence of BAF and viral
CC integrase (PubMed:16680152). The association of viral DNA with
CC chromatin requires the presence of BAF and EMD (PubMed:16680152).
CC {ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:16680152,
CC ECO:0000269|PubMed:9465049}.
CC -!- SUBUNIT: Homodimer (PubMed:16337940, PubMed:22399800, PubMed:28841419).
CC Heterodimerizes with BANF2 (PubMed:16337940). Interacts with
CC ANKLE2/LEM4, leading to decreased phosphorylation by VRK1 and promoting
CC dephosphorylation by protein phosphatase 2A (PP2A) (PubMed:22770216).
CC Binds non-specifically to double-stranded DNA, and is found as a
CC hexamer or dodecamer upon DNA binding. Binds to LEM domain-containing
CC nuclear proteins such as LEMD3/MAN1, TMPO/LAP2 and EMD (emerin)
CC (PubMed:11792822, PubMed:15681850). Interacts with ANKLE1 (via LEM
CC domain); the interaction may favor BANF1 dimerization
CC (PubMed:22399800). Interacts with CRX and LMNA (lamin-A). Binds linker
CC histone H1.1 and core histones H3 (PubMed:16203725). Interacts with
CC LEMD2 (via LEM domain) (PubMed:32494070). {ECO:0000269|PubMed:11792822,
CC ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725,
CC ECO:0000269|PubMed:16337940, ECO:0000269|PubMed:22399800,
CC ECO:0000269|PubMed:22770216, ECO:0000269|PubMed:28841419,
CC ECO:0000269|PubMed:32494070}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 pre-integration
CC complex in cytoplasm by binding to viral matrix protein and Gag
CC polyprotein. {ECO:0000269|PubMed:12663813,
CC ECO:0000269|PubMed:14645565}.
CC -!- INTERACTION:
CC O75531; Q8NAG6-2: ANKLE1; NbExp=2; IntAct=EBI-1055977, EBI-27052251;
CC O75531; O75531: BANF1; NbExp=3; IntAct=EBI-1055977, EBI-1055977;
CC O75531; Q9H503-2: BANF2; NbExp=3; IntAct=EBI-1055977, EBI-11977289;
CC O75531; P50402: EMD; NbExp=13; IntAct=EBI-1055977, EBI-489887;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16495336,
CC ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}. Chromosome
CC {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:28841419,
CC ECO:0000269|PubMed:32792394}. Nucleus envelope
CC {ECO:0000269|PubMed:24600006}. Cytoplasm {ECO:0000269|PubMed:16495336,
CC ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}.
CC Note=Significantly enriched at the nuclear inner membrane, diffusely
CC throughout the nucleus during interphase and concentrated at the
CC chromosomes during the M-phase (PubMed:16495336, PubMed:24600006). The
CC phosphorylated form (by VRK1) shows a cytoplasmic localization whereas
CC the unphosphorylated form locates almost exclusively in the nucleus
CC (PubMed:16495336, PubMed:24600006). May be included in HIV-1 virions
CC via its interaction with viral GAG polyprotein (PubMed:14645565).
CC {ECO:0000269|PubMed:14645565, ECO:0000269|PubMed:16495336,
CC ECO:0000269|PubMed:24600006}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in colon, brain, heart,
CC kidney, liver, lung, ovary, pancreas, placenta, prostate, skeletal
CC muscle, small intestine, spleen and testis. Not detected in thymus and
CC peripheral blood leukocytes. {ECO:0000269|PubMed:9740667}.
CC -!- DOMAIN: Has a helix-hairpin-helix (HhH) structural motif conserved
CC among proteins that bind non-specifically to DNA.
CC {ECO:0000269|PubMed:10924106}.
CC -!- DOMAIN: LEM domain proteins bind centrally on the BAF dimer.
CC {ECO:0000269|PubMed:15681850}.
CC -!- PTM: Ser-4 is the major site of phosphorylation as compared to Thr-2
CC and Thr-3. Phosphorylation on Thr-2; Thr-3 and Ser-4 disrupts its
CC ability to bind DNA and reduces its ability to bind LEM domain-
CC containing proteins. Non phosphorylated BAF seems to enhance binding
CC between EMD and LMNA. Dephosphorylated by protein phosphatase 2A (PP2A)
CC following interaction with ANKLE2/LEM4 during mitotic exit, leading to
CC mitotic nuclear envelope reassembly. {ECO:0000269|PubMed:16371512,
CC ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:22770216}.
CC -!- PTM: (Microbial infection) Phosphorylated by poxvirus B1 kinase (VPK1)
CC on serine and threonine residues, leading to BANF1 relocalization to
CC the cytoplasm, loss of dimerization and impaired DNA binding activity.
CC {ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}.
CC -!- PTM: (Microbial infection) Phosphorylated at the N-terminus by vaccinia
CC virus (VacV) B1 kinase, leading to BANF1 relocalization to the
CC cytoplasm, loss of dimerization and impaired DNA binding activity
CC (PubMed:24600006, PubMed:16495336). Hyperphosphorylation is linked to
CC the loss of ability to suppress vaccinia virus replication
CC (PubMed:24600006). {ECO:0000269|PubMed:16495336,
CC ECO:0000269|PubMed:24600006}.
CC -!- DISEASE: Nestor-Guillermo progeria syndrome (NGPS) [MIM:614008]: An
CC atypical progeroid syndrome characterized by normal development in the
CC first years of life, later followed by the emergence of generalized
CC lipoatrophy, severe osteoporosis, and marked osteolysis. The atrophic
CC facial subcutaneous fat pad and the marked osteolysis of the maxilla
CC and mandible result in a typical pseudosenile facial appearance with
CC micrognathia, prominent subcutaneous venous patterning, a convex nasal
CC ridge, and proptosis. Cognitive development is completely normal.
CC Patients do not have cardiovascular dysfunction, atherosclerosis, or
CC metabolic anomalies. {ECO:0000269|PubMed:21549337}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the BAF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC08964.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF070447; AAC23575.1; -; mRNA.
DR EMBL; AF044773; AAC08964.1; ALT_FRAME; mRNA.
DR EMBL; AF068235; AAD15901.1; -; mRNA.
DR EMBL; CR542140; CAG46937.1; -; mRNA.
DR EMBL; BC005942; AAH05942.1; -; mRNA.
DR EMBL; BC107702; AAI07703.1; -; mRNA.
DR CCDS; CCDS8125.1; -.
DR RefSeq; NP_001137457.1; NM_001143985.1.
DR RefSeq; NP_003851.1; NM_003860.3.
DR RefSeq; XP_016874003.1; XM_017018514.1.
DR RefSeq; XP_016874004.1; XM_017018515.1.
DR PDB; 1CI4; X-ray; 1.90 A; A/B=1-89.
DR PDB; 1QCK; NMR; -; A/B=1-89.
DR PDB; 2BZF; X-ray; 2.87 A; A=1-89.
DR PDB; 2EZX; NMR; -; A/B=1-89.
DR PDB; 2EZY; NMR; -; A/B=1-89.
DR PDB; 2EZZ; NMR; -; A/B=1-89.
DR PDB; 2ODG; NMR; -; A/B=1-89.
DR PDB; 6GHD; X-ray; 2.10 A; A/C/D/E=2-89.
DR PDB; 6RPR; X-ray; 2.26 A; D/E=3-89.
DR PDB; 6UNT; X-ray; 1.75 A; A/B=1-89.
DR PDB; 6URE; X-ray; 1.65 A; A/B=1-89.
DR PDB; 6URJ; X-ray; 1.65 A; A/B=1-89.
DR PDB; 6URK; X-ray; 1.86 A; A/B=1-89.
DR PDB; 6URL; X-ray; 1.72 A; A/B=1-89.
DR PDB; 6URN; X-ray; 1.68 A; A/B=1-89.
DR PDB; 6URR; X-ray; 1.80 A; A/B=1-89.
DR PDB; 6URZ; X-ray; 1.65 A; A/B=1-89.
DR PDB; 6US0; X-ray; 1.65 A; A/B=1-89.
DR PDB; 6US1; X-ray; 1.65 A; A/B=1-89.
DR PDB; 6US7; X-ray; 1.65 A; A/B=1-89.
DR PDB; 6USB; X-ray; 1.68 A; A/B=1-89.
DR PDB; 6USD; X-ray; 1.65 A; A/B=1-89.
DR PDB; 6USI; X-ray; 1.65 A; A/B=1-89.
DR PDB; 7ABM; X-ray; 3.00 A; A=3-88.
DR PDB; 7NDY; X-ray; 1.44 A; A/B=2-89.
DR PDBsum; 1CI4; -.
DR PDBsum; 1QCK; -.
DR PDBsum; 2BZF; -.
DR PDBsum; 2EZX; -.
DR PDBsum; 2EZY; -.
DR PDBsum; 2EZZ; -.
DR PDBsum; 2ODG; -.
DR PDBsum; 6GHD; -.
DR PDBsum; 6RPR; -.
DR PDBsum; 6UNT; -.
DR PDBsum; 6URE; -.
DR PDBsum; 6URJ; -.
DR PDBsum; 6URK; -.
DR PDBsum; 6URL; -.
DR PDBsum; 6URN; -.
DR PDBsum; 6URR; -.
DR PDBsum; 6URZ; -.
DR PDBsum; 6US0; -.
DR PDBsum; 6US1; -.
DR PDBsum; 6US7; -.
DR PDBsum; 6USB; -.
DR PDBsum; 6USD; -.
DR PDBsum; 6USI; -.
DR PDBsum; 7ABM; -.
DR PDBsum; 7NDY; -.
DR AlphaFoldDB; O75531; -.
DR SMR; O75531; -.
DR BioGRID; 114342; 161.
DR CORUM; O75531; -.
DR DIP; DIP-50395N; -.
DR IntAct; O75531; 47.
DR MINT; O75531; -.
DR STRING; 9606.ENSP00000310275; -.
DR GlyGen; O75531; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75531; -.
DR PhosphoSitePlus; O75531; -.
DR SwissPalm; O75531; -.
DR BioMuta; BANF1; -.
DR EPD; O75531; -.
DR jPOST; O75531; -.
DR MassIVE; O75531; -.
DR MaxQB; O75531; -.
DR PaxDb; O75531; -.
DR PeptideAtlas; O75531; -.
DR PRIDE; O75531; -.
DR ProteomicsDB; 50071; -.
DR TopDownProteomics; O75531; -.
DR Antibodypedia; 30040; 275 antibodies from 29 providers.
DR DNASU; 8815; -.
DR Ensembl; ENST00000312175.7; ENSP00000310275.2; ENSG00000175334.8.
DR Ensembl; ENST00000445560.6; ENSP00000416128.2; ENSG00000175334.8.
DR Ensembl; ENST00000527348.1; ENSP00000432867.1; ENSG00000175334.8.
DR Ensembl; ENST00000533166.5; ENSP00000433760.1; ENSG00000175334.8.
DR GeneID; 8815; -.
DR KEGG; hsa:8815; -.
DR MANE-Select; ENST00000312175.7; ENSP00000310275.2; NM_003860.4; NP_003851.1.
DR UCSC; uc001ogo.4; human.
DR CTD; 8815; -.
DR DisGeNET; 8815; -.
DR GeneCards; BANF1; -.
DR HGNC; HGNC:17397; BANF1.
DR HPA; ENSG00000175334; Low tissue specificity.
DR MalaCards; BANF1; -.
DR MIM; 603811; gene.
DR MIM; 614008; phenotype.
DR neXtProt; NX_O75531; -.
DR OpenTargets; ENSG00000175334; -.
DR Orphanet; 280576; Nestor-Guillermo progeria syndrome.
DR PharmGKB; PA134903639; -.
DR VEuPathDB; HostDB:ENSG00000175334; -.
DR eggNOG; KOG4233; Eukaryota.
DR GeneTree; ENSGT00390000018613; -.
DR HOGENOM; CLU_167806_0_0_1; -.
DR InParanoid; O75531; -.
DR OMA; SKQQGDC; -.
DR OrthoDB; 1617480at2759; -.
DR PhylomeDB; O75531; -.
DR TreeFam; TF315060; -.
DR PathwayCommons; O75531; -.
DR Reactome; R-HSA-162592; Integration of provirus.
DR Reactome; R-HSA-164843; 2-LTR circle formation.
DR Reactome; R-HSA-175567; Integration of viral DNA into host genomic DNA.
DR Reactome; R-HSA-177539; Autointegration results in viral DNA circles.
DR Reactome; R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR Reactome; R-HSA-2980766; Nuclear Envelope Breakdown.
DR Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR SignaLink; O75531; -.
DR SIGNOR; O75531; -.
DR BioGRID-ORCS; 8815; 757 hits in 1019 CRISPR screens.
DR ChiTaRS; BANF1; human.
DR EvolutionaryTrace; O75531; -.
DR GeneWiki; Barrier_to_autointegration_factor_1; -.
DR GenomeRNAi; 8815; -.
DR Pharos; O75531; Tbio.
DR PRO; PR:O75531; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O75531; protein.
DR Bgee; ENSG00000175334; Expressed in ganglionic eminence and 193 other tissues.
DR ExpressionAtlas; O75531; baseline and differential.
DR Genevisible; O75531; HS.
DR GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0097726; F:LEM domain binding; IMP:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IMP:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IDA:UniProtKB.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; IDA:UniProtKB.
DR GO; GO:0045824; P:negative regulation of innate immune response; IDA:UniProtKB.
DR GO; GO:0032480; P:negative regulation of type I interferon production; IDA:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; TAS:ProtInc.
DR Gene3D; 1.10.150.40; -; 1.
DR InterPro; IPR004122; BAF_prot.
DR InterPro; IPR036617; BAF_sf.
DR PANTHER; PTHR12912; PTHR12912; 1.
DR Pfam; PF02961; BAF; 1.
DR SMART; SM01023; BAF; 1.
DR SUPFAM; SSF47798; SSF47798; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Cytoplasm; Disease variant;
KW DNA-binding; Host-virus interaction; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..89
FT /note="Barrier-to-autointegration factor"
FT /id="PRO_0000423190"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..89
FT /note="Barrier-to-autointegration factor, N-terminally
FT processed"
FT /id="PRO_0000221026"
FT DOMAIN 20..35
FT /note="HhH"
FT /evidence="ECO:0000269|PubMed:10924106"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2
FT /note="(Microbial infection) Phosphothreonine; by viral
FT VacV B1 kinase"
FT /evidence="ECO:0000269|PubMed:16495336"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Barrier-to-autointegration
FT factor, N-terminally processed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 2
FT /note="Phosphothreonine; by VRK1 and VRK2"
FT /evidence="ECO:0000269|PubMed:16495336"
FT MOD_RES 3
FT /note="(Microbial infection) Phosphothreonine; by viral
FT VacV B1 kinase"
FT /evidence="ECO:0000269|PubMed:16495336"
FT MOD_RES 3
FT /note="Phosphothreonine; by VRK1 and VRK2"
FT /evidence="ECO:0000269|PubMed:16495336"
FT MOD_RES 4
FT /note="Phosphoserine; by viral VacV B1 kinase, VRK1 and
FT VRK2"
FT /evidence="ECO:0000269|PubMed:16371512,
FT ECO:0000269|PubMed:16495336"
FT VARIANT 12
FT /note="A -> T (in NGPS; shows a dramatic reduction in BANF1
FT protein levels indicating that the mutation impairs protein
FT stability; dbSNP:rs387906871)"
FT /evidence="ECO:0000269|PubMed:21549337"
FT /id="VAR_065954"
FT MUTAGEN 2..4
FT /note="TTS->AAA: 95% nuclear localization. Loss of BAF
FT phosphorylation and ability to suppress vaccinia virus DNA
FT replication."
FT /evidence="ECO:0000269|PubMed:16495336,
FT ECO:0000269|PubMed:24600006"
FT MUTAGEN 2..4
FT /note="TTS->DDD: 85% cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:24600006"
FT MUTAGEN 2..3
FT /note="TT->AA: No effect on the initial rate of
FT phosphorylation but a second slow phase of phosphorylation
FT is absent."
FT /evidence="ECO:0000269|PubMed:16495336"
FT MUTAGEN 4
FT /note="S->A: Delayed phosphorylation with a 10-fold
FT decrease in the initial phosphorylation rate. 71% loss of
FT binding to lamin A."
FT /evidence="ECO:0000269|PubMed:16371512,
FT ECO:0000269|PubMed:16495336"
FT MUTAGEN 4
FT /note="S->D: 75% cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:24600006"
FT MUTAGEN 4
FT /note="S->E: Complete loss of phosphorylation and
FT mislocalization of EMD in nucleus."
FT /evidence="ECO:0000269|PubMed:16371512"
FT MUTAGEN 6
FT /note="K->A: Complete loss of LEMD3/MAN1 and histone H1/H3
FT binding."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850,
FT ECO:0000269|PubMed:16203725"
FT MUTAGEN 6
FT /note="K->E: Complete loss of dsDNA and LEMD3/MAN1
FT binding."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850,
FT ECO:0000269|PubMed:16203725"
FT MUTAGEN 8
FT /note="R->A: Enhances histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:15681850,
FT ECO:0000269|PubMed:16203725"
FT MUTAGEN 8
FT /note="R->E: Complete loss of LEMD3/MAN1 binding."
FT /evidence="ECO:0000269|PubMed:15681850,
FT ECO:0000269|PubMed:16203725"
FT MUTAGEN 9
FT /note="D->A: Reduces binding to dsDNA, LEMD3/MAN1 and
FT histone H1/H3."
FT /evidence="ECO:0000269|PubMed:12163470,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 14
FT /note="P->A: No effect on LEMD3/MAN1 and enhances histone
FT H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 18
FT /note="K->A: No effect on histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:16203725"
FT MUTAGEN 25
FT /note="G->E: Complete loss of dsDNA, EMD, histone H1/H3 and
FT LEMD3/MAN1 binding."
FT /evidence="ECO:0000269|PubMed:12163470,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 25
FT /note="G->Q: Complete loss of EMD binding and reduces dsDNA
FT binding."
FT /evidence="ECO:0000269|PubMed:12163470,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 26
FT /note="I->A: Reduces histone H1/H3 and LEMD3/MAN1 binding.
FT Fails to promote HIV-1 genome integration."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 26
FT /note="I->K: Fails to promote HIV-1 genome integration."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 27
FT /note="G->E: Fails to bind dsDNA."
FT /evidence="ECO:0000269|PubMed:12163470"
FT MUTAGEN 27
FT /note="G->Q: Reduces binding to dsDNA."
FT /evidence="ECO:0000269|PubMed:12163470"
FT MUTAGEN 29
FT /note="V->A: No effect on histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:16203725"
FT MUTAGEN 32
FT /note="K->E: No effect on histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:16203725"
FT MUTAGEN 33
FT /note="K->E: No effect on histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:16203725"
FT MUTAGEN 37
FT /note="R->A: No effect on histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:15681850,
FT ECO:0000269|PubMed:16203725"
FT MUTAGEN 37
FT /note="R->E: Reduces LEMD3/MAN1 binding."
FT /evidence="ECO:0000269|PubMed:15681850,
FT ECO:0000269|PubMed:16203725"
FT MUTAGEN 41
FT /note="K->A: No effect on histone H1/H3 and LEMD3/MAN1
FT binding."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 41
FT /note="K->E: Reduces histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 46
FT /note="L->E: Complete loss of dsDNA, histone H1/H3 and
FT LEMD3/MAN1 binding."
FT /evidence="ECO:0000269|PubMed:12163470,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 47
FT /note="G->E: Abolishes homodimerization, preventing ability
FT to cross-bridge DNA. Abolished ability to mediate nuclear
FT membrane reformation at the end of mitosis. Abolished
FT ability to outcompete CGAS for DNA-binding, leading to
FT innate immune activation. Complete loss of EMD, histone
FT H1/H3 and LEMD3/MAN1 binding."
FT /evidence="ECO:0000269|PubMed:12163470,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725,
FT ECO:0000269|PubMed:28841419, ECO:0000269|PubMed:32792394"
FT MUTAGEN 50
FT /note="L->A: Reduces LEMD3/MAN1 binding. No effect on
FT Histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 50
FT /note="L->K: Fails to promote HIV-1 genome integration."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 51
FT /note="V->E: Complete loss of EMD, and histone H1/H3
FT binding. Reduces dsDNA and LEMD3/MAN1 binding."
FT /evidence="ECO:0000269|PubMed:12163470,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 53
FT /note="K->A: No effect on LEMD3/MAN1 binding. Enhances
FT histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850,
FT ECO:0000269|PubMed:16203725"
FT MUTAGEN 53
FT /note="K->E: Complete loss of EMD binding. Reduces
FT LEMD3/MAN1 binding. Enhances histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850,
FT ECO:0000269|PubMed:16203725"
FT MUTAGEN 54
FT /note="K->A: Reduces LEMD3/MAN1 binding. No effect on
FT histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850,
FT ECO:0000269|PubMed:16203725"
FT MUTAGEN 54
FT /note="K->E: Reduces binding to dsDNA."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850,
FT ECO:0000269|PubMed:16203725"
FT MUTAGEN 58
FT /note="L->R: Abolishes interaction with LEM domain-
FT containing proteins without affecting homodimerization and
FT DNA-binding. Does not affect its involvement in nuclear
FT membrane reformation at the end of mitosis. Does not affect
FT ability to outcompete CGAS for DNA-binding."
FT /evidence="ECO:0000269|PubMed:28841419,
FT ECO:0000269|PubMed:32792394"
FT MUTAGEN 60
FT /note="R->E: No effect on histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:16203725"
FT MUTAGEN 62
FT /note="W->A: Complete loss of LEMD3/MAN1 binding. Enhances
FT histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 64
FT /note="K->E: Enhances histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:16203725"
FT MUTAGEN 75
FT /note="R->E: Reduces binding to dsDNA. No effect on histone
FT H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:12163470,
FT ECO:0000269|PubMed:16203725"
FT MUTAGEN 80
FT /note="C->A: No effect on histone H1/H3 and LEMD3/MAN1
FT binding."
FT /evidence="ECO:0000269|PubMed:11005805,
FT ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"
FT MUTAGEN 82
FT /note="R->E: No effect on histone H1/H3 binding."
FT /evidence="ECO:0000269|PubMed:16203725"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:7NDY"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:7NDY"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:7NDY"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:7NDY"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:7NDY"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:7NDY"
FT HELIX 71..88
FT /evidence="ECO:0007829|PDB:7NDY"
SQ SEQUENCE 89 AA; 10059 MW; 9A2180A2D284F5D0 CRC64;
MTTSQKHRDF VAEPMGEKPV GSLAGIGEVL GKKLEERGFD KAYVVLGQFL VLKKDEDLFR
EWLKDTCGAN AKQSRDCFGC LREWCDAFL
