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Barrier-to-autointegration factor (Breakpoint cluster region protein 1) (LAP2-binding protein 1) [Cleaved into: Barrier-to-autointegration factor, N-terminally processed]

 BAF_MOUSE               Reviewed;          89 AA.
O54962; Q542E6;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
22-NOV-2017, entry version 130.
RecName: Full=Barrier-to-autointegration factor;
AltName: Full=Breakpoint cluster region protein 1;
AltName: Full=LAP2-binding protein 1;
Contains:
RecName: Full=Barrier-to-autointegration factor, N-terminally processed;
Name=Banf1; Synonyms=Baf, Bcrp1, L2bp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9465049; DOI=10.1073/pnas.95.4.1528;
Lee M.S., Craigie R.;
"A previously unidentified host protein protects retroviral DNA from
autointegration.";
Proc. Natl. Acad. Sci. U.S.A. 95:1528-1533(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TMPO.
PubMed=10393804;
Furukawa K.;
"LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-
chromatin interaction.";
J. Cell Sci. 112:2485-2492(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Plays fundamental roles in nuclear assembly, chromatin
organization, gene expression and gonad development. May potently
compress chromatin structure and be involved in membrane
recruitment and chromatin decondensation during nuclear assembly.
Contains 2 non-specific dsDNA-binding sites which may promote DNA
cross-bridging. {ECO:0000250|UniProtKB:O75531}.
-!- SUBUNIT: Homodimer. Heterodimerizes with BAFL. Interacts with
ANKLE2/LEM4, leading to decreased phosphorylation by VRK1 and
promoting dephosphorylation by protein phosphatase 2A (PP2A).
Binds non-specifically to double-stranded DNA, and is found as a
hexamer or dodecamer upon DNA binding. Binds to LEM domain-
containing nuclear proteins such as LEMD3/MAN1, TMPO/LAP2 and EMD
(emerin). Interacts with ANKLE1 (via LEM domain); the interaction
may favor BANF1 dimerization. Interacts with CRX and LMNA (lamin-
A). Binds linker histone H1.1 and core histones H3.
{ECO:0000250|UniProtKB:O75531}.
-!- SUBCELLULAR LOCATION: Barrier-to-autointegration factor: Nucleus
{ECO:0000250|UniProtKB:O75531}. Cytoplasm
{ECO:0000250|UniProtKB:O75531}. Chromosome
{ECO:0000250|UniProtKB:O75531}. Nucleus envelope
{ECO:0000250|UniProtKB:O75531}. Note=Significantly enriched at the
nuclear inner membrane, diffusely throughout the nucleus during
interphase and concentrated at the chromosomes during the M-phase.
The phosphorylated form (by VRK1) shows a cytoplasmic localization
whereas the unphosphorylated form locates almost exclusively in
the nucleus. {ECO:0000250|UniProtKB:O75531}.
-!- DOMAIN: Has a helix-hairpin-helix (HhH) structural motif conserved
among proteins that bind non-specifically to DNA.
{ECO:0000250|UniProtKB:O75531}.
-!- DOMAIN: LEM domain proteins bind centrally on the BAF dimer.
{ECO:0000250|UniProtKB:O75531}.
-!- PTM: Ser-4 is the major site of phosphorylation as compared to
Thr-2 and Thr-3. Phosphorylation on Thr-2; Thr-3 and Ser-4
disrupts its ability to bind DNA and reduces its ability to bind
LEM domain-containing proteins. Non phosphorylated BAF seems to
enhance binding between EMD and LMNA. Dephosphorylated by protein
phosphatase 2A (PP2A) following interaction with ANKLE2/LEM4
during mitotic exit, leading to mitotic nuclear envelope
reassembly. {ECO:0000250|UniProtKB:O75531}.
-!- SIMILARITY: Belongs to the BAF family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF037080; AAC40032.1; -; mRNA.
EMBL; AB025349; BAA83102.1; -; mRNA.
EMBL; AK003025; BAB22518.1; -; mRNA.
EMBL; AK004212; BAB23223.1; -; mRNA.
EMBL; AK010257; BAB26800.1; -; mRNA.
EMBL; AK011079; BAB27383.1; -; mRNA.
EMBL; AK011100; BAB27397.1; -; mRNA.
EMBL; AK012588; BAB28337.1; -; mRNA.
EMBL; AK088896; BAC40639.1; -; mRNA.
EMBL; BC003709; AAH03709.1; -; mRNA.
CCDS; CCDS29458.1; -.
RefSeq; NP_001033320.1; NM_001038231.2.
RefSeq; NP_001273537.1; NM_001286608.1.
RefSeq; NP_035923.1; NM_011793.3.
UniGene; Mm.358649; -.
ProteinModelPortal; O54962; -.
SMR; O54962; -.
BioGrid; 204742; 1.
IntAct; O54962; 4.
MINT; MINT-4089048; -.
STRING; 10090.ENSMUSP00000025762; -.
iPTMnet; O54962; -.
PhosphoSitePlus; O54962; -.
EPD; O54962; -.
MaxQB; O54962; -.
PaxDb; O54962; -.
PeptideAtlas; O54962; -.
PRIDE; O54962; -.
TopDownProteomics; O54962; -.
Ensembl; ENSMUST00000025762; ENSMUSP00000025762; ENSMUSG00000024844.
Ensembl; ENSMUST00000170010; ENSMUSP00000126202; ENSMUSG00000024844.
GeneID; 23825; -.
KEGG; mmu:23825; -.
UCSC; uc008gcr.2; mouse.
CTD; 8815; -.
MGI; MGI:1346330; Banf1.
eggNOG; KOG4233; Eukaryota.
eggNOG; ENOG4111URU; LUCA.
GeneTree; ENSGT00390000018613; -.
HOGENOM; HOG000231927; -.
HOVERGEN; HBG029345; -.
InParanoid; O54962; -.
KO; K21870; -.
OMA; TDWCEEF; -.
OrthoDB; EOG091G109J; -.
PhylomeDB; O54962; -.
TreeFam; TF315060; -.
Reactome; R-MMU-2993913; Clearance of Nuclear Envelope Membranes from Chromatin.
Reactome; R-MMU-2995383; Initiation of Nuclear Envelope Reformation.
PRO; PR:O54962; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024844; -.
CleanEx; MM_BANF1; -.
Genevisible; O54962; MM.
GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0097726; F:LEM domain binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0015074; P:DNA integration; IDA:MGI.
GO; GO:0075713; P:establishment of integrated proviral latency; TAS:MGI.
GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
Gene3D; 1.10.150.40; -; 1.
InterPro; IPR004122; BAF_prot.
InterPro; IPR036617; BAF_sf.
PANTHER; PTHR12912; PTHR12912; 1.
Pfam; PF02961; BAF; 1.
ProDom; PD019964; PD019964; 1.
SMART; SM01023; BAF; 1.
SUPFAM; SSF47798; SSF47798; 1.
1: Evidence at protein level;
Acetylation; Chromosome; Complete proteome; Cytoplasm; DNA-binding;
Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 89 Barrier-to-autointegration factor.
/FTId=PRO_0000423191.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:O75531}.
CHAIN 2 89 Barrier-to-autointegration factor, N-
terminally processed.
/FTId=PRO_0000221027.
DOMAIN 20 35 HhH. {ECO:0000250|UniProtKB:O75531}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:O75531}.
MOD_RES 2 2 N-acetylthreonine; in Barrier-to-
autointegration factor, N-terminally
processed.
{ECO:0000250|UniProtKB:O75531}.
MOD_RES 2 2 Phosphothreonine; by VRK1 and VRK2.
{ECO:0000250|UniProtKB:O75531}.
MOD_RES 3 3 Phosphothreonine; by VRK1 and VRK2.
{ECO:0000250|UniProtKB:O75531}.
MOD_RES 4 4 Phosphoserine; by VRK1 and VRK2.
{ECO:0000250|UniProtKB:O75531}.
SEQUENCE 89 AA; 10103 MW; 828924AFCB91E0D0 CRC64;
MTTSQKHRDF VAEPMGEKPV GSLAGIGDVL SKRLEERGFD KAYVVLGQFL VLKKDEDLFR
EWLKDTCGAN AKQSRDCFGC LREWCDAFL


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