PALB2_MOUSE
ID PALB2_MOUSE Reviewed; 1104 AA.
AC Q3U0P1; Q6NZG9; Q7TMQ4; Q8CEA9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Partner and localizer of BRCA2;
GN Name=Palb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1086 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and FVB/N-3;
RC TISSUE=Embryonic germ cell, and Mammary tumor;
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).
CC -!- FUNCTION: Plays a critical role in homologous recombination repair
CC (HRR) through its ability to recruit BRCA2 and RAD51 to DNA breaks.
CC Strongly stimulates the DNA strand-invasion activity of RAD51,
CC stabilizes the nucleoprotein filament against a disruptive BRC3-BRC4
CC polypeptide and helps RAD51 to overcome the suppressive effect of
CC replication protein A (RPA). Functionally cooperates with RAD51AP1 in
CC promoting of D-loop formation by RAD51. Serves as the molecular
CC scaffold in the formation of the BRCA1-PALB2-BRCA2 complex which is
CC essential for homologous recombination. Via its WD repeats is proposed
CC to scaffold a HR complex containing RAD51C and BRCA2 which is thought
CC to play a role in HR-mediated DNA repair. Essential partner of BRCA2
CC that promotes the localization and stability of BRCA2. Also enables its
CC recombinational repair and checkpoint functions of BRCA2. May act by
CC promoting stable association of BRCA2 with nuclear structures, allowing
CC BRCA2 to escape the effects of proteasome-mediated degradation. Binds
CC DNA with high affinity for D loop, which comprises single-stranded,
CC double-stranded and branched DNA structures. May play a role in the
CC extension step after strand invasion at replication-dependent DNA
CC double-strand breaks; together with BRCA2 is involved in both POLH
CC localization at collapsed replication forks and DNA polymerization
CC activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer; dissociated upon DNA damage thus allowing
CC association with BRCA1. Oligomerization is essential for its focal
CC accumulation at DNA breaks. Part of a BRCA complex containing BRCA1,
CC BRCA2 and PALB2. Interacts with BRCA1 and this interaction is essential
CC for its function in HRR. Interacts with RAD51AP1 and MORF4L1/MRG15.
CC Component of the homologous recombination repair (HR) complex composed
CC of ERCC5/XPG, BRCA2, PALB2, DSS1 and RAD51 (By similarity). Within the
CC complex, interacts with ERCC5/XPG and BRCA2 (By similarity). Interacts
CC with BRCA2, RAD51C, RAD51 and XRCC3; the interactions are direct and it
CC may serve as a scaffold for a HR complex containing PALB2, BRCA2,
CC RAD51C, RAD51 and XRCC3. Interacts with POLH; the interaction is direct
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q86YC2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86YC2}.
CC Note=Colocalizes with BRCA2 in nuclear foci.
CC {ECO:0000250|UniProtKB:Q86YC2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3U0P1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U0P1-2; Sequence=VSP_020929;
CC Name=3;
CC IsoId=Q3U0P1-3; Sequence=VSP_020928;
CC Name=4;
CC IsoId=Q3U0P1-4; Sequence=VSP_020930, VSP_020931;
CC -!- DOMAIN: Interaction with BRCA2 occurs through a hydrophobic pocket at
CC the crossover between WD repeats 4 and 5. {ECO:0000250}.
CC -!- DOMAIN: The coiled coil domain mediates self-association.
CC -!- DOMAIN: The chromatin-association motif (ChAM) mediates association
CC with chromatin, probably through nucleosome core particles,
CC independently from binding to D loop, ssDNA or dsDNA structures.
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DR EMBL; AK028653; BAC26048.1; -; mRNA.
DR EMBL; AK156701; BAE33811.1; -; mRNA.
DR EMBL; BC055302; AAH55302.1; -; mRNA.
DR EMBL; BC066140; AAH66140.1; -; mRNA.
DR CCDS; CCDS40117.1; -. [Q3U0P1-1]
DR CCDS; CCDS72035.1; -. [Q3U0P1-2]
DR CCDS; CCDS80796.1; -. [Q3U0P1-3]
DR RefSeq; NP_001074707.1; NM_001081238.2. [Q3U0P1-1]
DR RefSeq; NP_001276771.1; NM_001289842.1.
DR RefSeq; NP_001276772.1; NM_001289843.1.
DR RefSeq; NP_001276773.1; NM_001289844.1. [Q3U0P1-2]
DR RefSeq; NP_001276774.1; NM_001289845.1. [Q3U0P1-3]
DR PDB; 6E4H; NMR; -; A/B=1-60.
DR PDB; 7K3S; NMR; -; B=1-60.
DR PDBsum; 6E4H; -.
DR PDBsum; 7K3S; -.
DR AlphaFoldDB; Q3U0P1; -.
DR SMR; Q3U0P1; -.
DR BioGRID; 231454; 13.
DR IntAct; Q3U0P1; 1.
DR MINT; Q3U0P1; -.
DR STRING; 10090.ENSMUSP00000095675; -.
DR iPTMnet; Q3U0P1; -.
DR PhosphoSitePlus; Q3U0P1; -.
DR EPD; Q3U0P1; -.
DR MaxQB; Q3U0P1; -.
DR PaxDb; Q3U0P1; -.
DR PRIDE; Q3U0P1; -.
DR ProteomicsDB; 295454; -. [Q3U0P1-1]
DR ProteomicsDB; 295455; -. [Q3U0P1-2]
DR ProteomicsDB; 295456; -. [Q3U0P1-3]
DR ProteomicsDB; 295457; -. [Q3U0P1-4]
DR Antibodypedia; 26008; 255 antibodies from 35 providers.
DR DNASU; 233826; -.
DR Ensembl; ENSMUST00000063587; ENSMUSP00000063514; ENSMUSG00000044702. [Q3U0P1-3]
DR Ensembl; ENSMUST00000098068; ENSMUSP00000095675; ENSMUSG00000044702. [Q3U0P1-1]
DR Ensembl; ENSMUST00000106469; ENSMUSP00000102077; ENSMUSG00000044702. [Q3U0P1-2]
DR GeneID; 233826; -.
DR KEGG; mmu:233826; -.
DR UCSC; uc009joj.2; mouse. [Q3U0P1-1]
DR UCSC; uc009jom.1; mouse. [Q3U0P1-4]
DR UCSC; uc012ftg.2; mouse. [Q3U0P1-2]
DR UCSC; uc012fth.2; mouse. [Q3U0P1-3]
DR CTD; 79728; -.
DR MGI; MGI:3040695; Palb2.
DR VEuPathDB; HostDB:ENSMUSG00000044702; -.
DR eggNOG; ENOG502QRAP; Eukaryota.
DR GeneTree; ENSGT00390000014423; -.
DR HOGENOM; CLU_008217_1_0_1; -.
DR InParanoid; Q3U0P1; -.
DR OMA; GHCQKED; -.
DR OrthoDB; 710645at2759; -.
DR PhylomeDB; Q3U0P1; -.
DR TreeFam; TF351544; -.
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
DR BioGRID-ORCS; 233826; 27 hits in 112 CRISPR screens.
DR ChiTaRS; Palb2; mouse.
DR PRO; PR:Q3U0P1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3U0P1; protein.
DR Bgee; ENSMUSG00000044702; Expressed in animal zygote and 148 other tissues.
DR ExpressionAtlas; Q3U0P1; baseline and differential.
DR Genevisible; Q3U0P1; MM.
DR GO; GO:1990391; C:DNA repair complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
DR GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR042417; PALB2.
DR InterPro; IPR031920; PALB2_WD40.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR14662; PTHR14662; 2.
DR Pfam; PF16756; PALB2_WD40; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Tumor suppressor; WD repeat.
FT CHAIN 1..1104
FT /note="Partner and localizer of BRCA2"
FT /id="PRO_0000252392"
FT REPEAT 772..833
FT /note="WD 1"
FT REPEAT 835..879
FT /note="WD 2"
FT REPEAT 880..927
FT /note="WD 3"
FT REPEAT 928..970
FT /note="WD 4"
FT REPEAT 976..1027
FT /note="WD 5"
FT REPEAT 1033..1071
FT /note="WD 6"
FT REPEAT 1073..1104
FT /note="WD 7"
FT REGION 1..308
FT /note="Interaction with BRCA1"
FT /evidence="ECO:0000250"
FT REGION 1..195
FT /note="Interaction with RAD51"
FT /evidence="ECO:0000250"
FT REGION 1..157
FT /note="Required for its oligomerization and is important
FT for its focal concentration at DNA damage sites"
FT /evidence="ECO:0000250"
FT REGION 39..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..424
FT /note="ChAM (Chromatin-association motif); required for
FT chromatin association, mediates nucleosome association"
FT /evidence="ECO:0000250"
FT REGION 417..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..1104
FT /note="Required for interaction with POLH and POLH DNA
FT synthesis stimulation"
FT /evidence="ECO:0000250"
FT REGION 771..1104
FT /note="Interaction with RAD51 and BRCA2"
FT /evidence="ECO:0000250"
FT REGION 771..1104
FT /note="Interaction with RAD51, BRCA2 and POLH"
FT /evidence="ECO:0000250"
FT COILED 9..48
FT /evidence="ECO:0000255"
FT COMPBIAS 58..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YC2"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YC2"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YC2"
FT VAR_SEQ 36..755
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020928"
FT VAR_SEQ 170..532
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020929"
FT VAR_SEQ 533..544
FT /note="DFELPDEDFGLL -> GKSRRRVRLRLM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020930"
FT VAR_SEQ 545..1104
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020931"
FT HELIX 11..39
FT /evidence="ECO:0007829|PDB:6E4H"
SQ SEQUENCE 1104 AA; 119097 MW; D8E027609707D03D CRC64;
MEELSGKPLS YAEKEKLKEK LAFLKKEYSR TLARLQRAKR AEKAKNSKKA IEDGVPQPEA
SSQLSHSESI NKGFPCDTLQ SNHLDEETGE NISQILDVEP QSFNCKQGKE VLHTPRAGDI
QGQLLHSTSS PDGKKEQNTL PGTTKTPWEK SSVSQEKEDY FDTNSLALLG KHRKGQESIS
RKNSRTPVSE KTHLLSLRSQ IPDPPALVTG IGEGILIPPS GKSERGIDTL VRGNTVSAEA
AVPSCTASNS NHSQHLEHTP PKSGCKITTQ GPASSTNLVA QDQKMTIFTV NSVVYKAVRA
HGQLPGSPNS CSVNDLTHSN LPANSTPNSK SLKSPSNTVD ERNEPLQEDE ILGPSKNFNL
AAVSPPSTES QIHSCTMLEG LLFPAEYYVR TTRRMSDCQR KIALEAVIQS HLGVKKKELK
KKTKATKAVV LSSEDTDQSE SGMLDTSTGQ SSSGSLSQKL LSPAEVSSPP GPAGKATTPP
PGRGHRGKRK SARTSTLGHC QLLFPPCAAL AVNRSKGKFT KHKCQNRGVV IHDFELPDED
FGLLKLEKLK SCSEKLIESP DSKNCGERLP REGNHAALEE LQRDSETEGL EEELTVPPGE
AYRPGPTLRR QPGSKDLSSS IVLFTPADTA APNDSGRPPP SLCSPAFPIL GMTPALGSQA
AGETLSTEAA QPCSTSQPPL LGDTNSLVNN SKQCNSSACS PKPDTNLQAS GRQGQPACDS
DSGPQATPLP VESFTFRENQ LCGNACLELH EHSTEQTETA DRPACDNLNP GNLQLVSELK
NPSSSCSVDV SAMWWERAGA KEPCIVTACE DVVSLWKPLN SLQWEKVHTW HFTEVPVLQI
VPVPDVYNLI CVALGSLEIR EIRALLCSSG DDSEKQVLLK SGDIKAMLGL TKRRLVSSTG
TFCNQQIQIM TFADDGSSKD EQLLMPPDET VLTFAEVQGT QEALLGTTTV NSIVIWNLKT
GQLLKKMHID DSYQASVCHG AYSEKGLLFV VVSQPCAKES QALGSPVFQL LVINPKTAQS
VGVLLCSLPQ GQAGRFLEGD VKDHVAAAVL TSGTIAIWDL LLGHCTALLP PVSDQSWSLV
KWSGTDSHLL AGQKDGNIFI YRYF
