Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q86YC2 (PALB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Partner and localizer of BRCA2
Gene names
Name:PALB2
Synonyms:FANCN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1186 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a critical role in homologous recombination repair (HRR) through its ability to recruit BRCA2 and RAD51 to DNA breaks. Strongly stimulates the DNA strand-invasion activity of RAD51, stabilizes the nucleoprotein filament against a disruptive BRC3-BRC4 polypeptide and helps RAD51 to overcome the suppressive effect of replication protein A (RPA). Functionally cooperates with RAD51AP1 in promoting of D-loop formation by RAD51. Serves as the molecular scaffold in the formation of the BRCA1-PALB2-BRCA2 complex which is essential for homologous recombination. Via its WD repeats is proposed to scaffold a HR complex containing RAD51C and BRCA2 which is thought to play a role in HR-mediated DNA repair. Essential partner of BRCA2 that promotes the localization and stability of BRCA2. Also enables its recombinational repair and checkpoint functions of BRCA2. May act by promoting stable association of BRCA2 with nuclear structures, allowing BRCA2 to escape the effects of proteasome-mediated degradation. Binds DNA with high affinity for D loop, which comprises single-stranded, double-stranded and branched DNA structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with BRCA2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. Ref.6 Ref.11 Ref.12 Ref.16 Ref.17 Ref.22 Ref.23 Ref.24

Subunit structure

Homooligomer; dissociated upon DNA damage thus allowing association with BRCA1. Oligomerization is essential for its focal accumulation at DNA breaks. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2. Interacts with BRCA1 and this interaction is essential for its function in HRR. Interacts with RAD51AP1 and MORF4L1/MRG15. Interacts with BRCA2, RAD51C, RAD51 and XRCC3; the interactions are direct and it may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3. Interacts with POLH; the interaction is direct. Ref.6 Ref.11 Ref.12 Ref.15 Ref.16 Ref.17 Ref.23 Ref.24

Subcellular location

Nucleus. Note: Colocalizes with BRCA2 in nuclear foci. Ref.6

Domain

Interaction with BRCA2 occurs through a hydrophobic pocket at the crossover between WD repeats 4 and 5. Ref.25

The coiled coil domain mediates self-association (Ref.22). Ref.25

The chromatin-association motif (ChAM) mediates association with chromatin, probably through nucleosome core particles, independently from binding to D loop, ssDNA or dsDNA structures (Ref.20). Ref.25

Involvement in disease

Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Breast cancer susceptibility is strongly associated with PALB2 truncating mutations. Conversely, rare missense mutations do not strongly influence breast cancer risk (Ref.21).

Fanconi anemia complementation group N (FANCN) [MIM:610832]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Pancreatic cancer 3 (PNCA3) [MIM:613348]: A malignant neoplasm of the pancreas. Tumors can arise from both the exocrine and endocrine portions of the pancreas, but 95% of them develop from the exocrine portion, including the ductal epithelium, acinar cells, connective tissue, and lymphatic tissue.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Sequence similarities

Contains 7 WD repeats.

Sequence caution

The sequence BAB15140.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BRCA2P515878EBI-1222653,EBI-79792

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11861186Partner and localizer of BRCA2
PRO_0000252391

Regions

Repeat854 – 91562WD 1
Repeat917 – 96145WD 2
Repeat962 – 100948WD 3
Repeat1010 – 105243WD 4
Repeat1058 – 110952WD 5
Repeat1115 – 115339WD 6
Repeat1155 – 118632WD 7
Region1 – 579579DNA-binding (with the preference D loop > dsDNA > ssDNA)
Region1 – 319319Interaction with BRCA1
Region1 – 200200Interaction with RAD51
Region1 – 160160Required for its oligomerization and is important for its focal concentration at DNA damage sites
Region395 – 44652ChAM (Chromatin-association motif); required for chromatin association, mediates nucleosome association
Region775 – 1186412Required for interaction with POLH and POLH DNA synthesis stimulation
Region853 – 1186334Interaction with RAD51, BRCA2 and POLH
Coiled coil9 – 4133 Potential

Amino acid modifications

Modified residue3761Phosphoserine Ref.9 Ref.18
Modified residue3871Phosphoserine Ref.13

Natural variations

Natural variant461H → Y. Ref.27
VAR_066361
Natural variant2191D → G. Ref.27
VAR_066362
Natural variant3091I → V.
Corresponds to variant rs3809683 [ dbSNP | Ensembl ].
VAR_032959
Natural variant3341Y → C. Ref.27
VAR_066363
Natural variant3371L → S. Ref.27
Corresponds to variant rs45494092 [ dbSNP | Ensembl ].
VAR_066364
Natural variant4141R → Q. Ref.27
VAR_066365
Natural variant4251V → M. Ref.27
VAR_066366
Natural variant4911A → T. Ref.27
VAR_066367
Natural variant5151K → R. Ref.27
VAR_066368
Natural variant5591Q → R. Ref.27
Corresponds to variant rs152451 [ dbSNP | Ensembl ].
VAR_066369
Natural variant6721E → Q. Ref.27
Corresponds to variant rs45532440 [ dbSNP | Ensembl ].
VAR_066370
Natural variant7121A → V. Ref.27
Corresponds to variant rs141458731 [ dbSNP | Ensembl ].
VAR_066371
Natural variant7281F → L. Ref.27
VAR_066372
Natural variant8641P → S. Ref.26 Ref.27
Corresponds to variant rs45568339 [ dbSNP | Ensembl ].
VAR_054150
Natural variant9171V → A. Ref.27
VAR_066373
Natural variant9321V → M. Ref.27
Corresponds to variant rs45624036 [ dbSNP | Ensembl ].
VAR_066374
Natural variant9391L → W May be associated with breast cancer susceptibility; reduces interaction with BRCA2, RAD51 and XRCC3; decreases double-stranded DNA break-initiated homologous recombination; increases sensitivity to IR. Ref.23 Ref.27
Corresponds to variant rs45478192 [ dbSNP | Ensembl ].
VAR_066375
Natural variant9661I → V. Ref.27
VAR_066376
Natural variant9981G → E May be associated with breast cancer susceptibility. Ref.27
Corresponds to variant rs45551636 [ dbSNP | Ensembl ].
VAR_066377
Natural variant10251A → T. Ref.27
VAR_066378
Natural variant10431G → A May be associated with breast cancer susceptibility; reduces interaction with BRCA2, RAD51C, RAD51 and XRCC3; decreases double-stranded DNA break-initiated homologous recombination; increases sensitivity to IR. Ref.27
VAR_066379
Natural variant10751S → G. Ref.27
VAR_066380
Natural variant11051V → A. Ref.27
VAR_066381
Natural variant11141Q → H. Ref.27
VAR_066382
Natural variant11431L → P May be associated with breast cancer susceptibility. Ref.23 Ref.27
VAR_066383
Natural variant11701H → Y. Ref.27
VAR_066384

Experimental info

Mutagenesis141K → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. Ref.12
Mutagenesis211L → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. Ref.12
Mutagenesis281Y → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. Ref.12
Mutagenesis351L → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. Ref.12
Mutagenesis421E → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. Ref.12
Mutagenesis10301T → I: Unstable and promotes protein degradation; reduces interaction with RAD51C and RAD51. Ref.23

Secondary structure

....................................................... 1186
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q86YC2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 215EC32291315FA2

FASTA1,186131,295
        10         20         30         40         50         60 
MDEPPGKPLS CEEKEKLKEK LAFLKREYSK TLARLQRAQR AEKIKHSIKK TVEEQDCLSQ 

        70         80         90        100        110        120 
QDLSPQLKHS EPKNKICVYD KLHIKTHLDE ETGEKTSITL DVGPESFNPG DGPGGLPIQR 

       130        140        150        160        170        180 
TDDTQEHFPH RVSDPSGEQK QKLPSRRKKQ QKRTFISQER DCVFGTDSLR LSGKRLKEQE 

       190        200        210        220        230        240 
EISSKNPARS PVTEIRTHLL SLKSELPDSP EPVTEINEDS VLIPPTAQPE KGVDTFLRRP 

       250        260        270        280        290        300 
NFTRATTVPL QTLSDSGSSQ HLEHIPPKGS SELTTHDLKN IRFTSPVSLE AQGKKMTVST 

       310        320        330        340        350        360 
DNLLVNKAIS KSGQLPTSSN LEANISCSLN ELTYNNLPAN ENQNLKEQNQ TEKSLKSPSD 

       370        380        390        400        410        420 
TLDGRNENLQ ESEILSQPKS LSLEATSPLS AEKHSCTVPE GLLFPAEYYV RTTRSMSNCQ 

       430        440        450        460        470        480 
RKVAVEAVIQ SHLDVKKKGF KNKNKDASKN LNLSNEETDQ SEIRMSGTCT GQPSSRTSQK 

       490        500        510        520        530        540 
LLSLTKVSSP AGPTEDNDLS RKAVAQAPGR RYTGKRKSAC TPASDHCEPL LPTSSLSIVN 

       550        560        570        580        590        600 
RSKEEVTSHK YQHEKLFIQV KGKKSRHQKE DSLSWSNSAY LSLDDDAFTA PFHRDGMLSL 

       610        620        630        640        650        660 
KQLLSFLSIT DFQLPDEDFG PLKLEKVKSC SEKPVEPFES KMFGERHLKE GSCIFPEELS 

       670        680        690        700        710        720 
PKRMDTEMED LEEDLIVLPG KSHPKRPNSQ SQHTKTGLSS SILLYTPLNT VAPDDNDRPT 

       730        740        750        760        770        780 
TDMCSPAFPI LGTTPAFGPQ GSYEKASTEV AGRTCCTPQL AHLKDSVCLA SDTKQFDSSG 

       790        800        810        820        830        840 
SPAKPHTTLQ VSGRQGQPTC DCDSVPPGTP PPIESFTFKE NQLCRNTCQE LHKHSVEQTE 

       850        860        870        880        890        900 
TAELPASDSI NPGNLQLVSE LKNPSGSCSV DVSAMFWERA GCKEPCIITA CEDVVSLWKA 

       910        920        930        940        950        960 
LDAWQWEKLY TWHFAEVPVL QIVPVPDVYN LVCVALGNLE IREIRALFCS SDDESEKQVL 

       970        980        990       1000       1010       1020 
LKSGNIKAVL GLTKRRLVSS SGTLSDQQVE VMTFAEDGGG KENQFLMPPE ETILTFAEVQ 

      1030       1040       1050       1060       1070       1080 
GMQEALLGTT IMNNIVIWNL KTGQLLKKMH IDDSYQASVC HKAYSEMGLL FIVLSHPCAK 

      1090       1100       1110       1120       1130       1140 
ESESLRSPVF QLIVINPKTT LSVGVMLYCL PPGQAGRFLE GDVKDHCAAA ILTSGTIAIW 

      1150       1160       1170       1180 
DLLLGQCTAL LPPVSDQHWS FVKWSGTDSH LLAGQKDGNI FVYHYS 

« Hide

References

« Hide 'large scale' references
[1]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Endometrium.
[2]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-440 AND 476-1186.
Tissue: Testis.
[6]"Control of BRCA2 cellular and clinical functions by a nuclear partner, PALB2."
Xia B., Sheng Q., Nakanishi K., Ohashi A., Wu J., Christ N., Liu X., Jasin M., Couch F.J., Livingston D.M.
Mol. Cell 22:719-729(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA2.
[7]"A recurrent mutation in PALB2 in Finnish cancer families."
Erkko H., Xia B., Nikkilae J., Schleutker J., Syrjaekoski K., Mannermaa A., Kallioniemi A., Pylkaes K., Karppinen S.-M., Rapakko K., Miron A., Sheng Q., Li G., Mattila H., Bell D.W., Haber D.A., Grip M., Reiman M. expand/collapse author list , Jukkola-Vuorinen A., Mustonen A., Kere J., Aaltonen L.A., Kosma V.-M., Kataja V., Soini Y., Drapkin R.I., Livingston D.M., Winqvist R.
Nature 446:316-319(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO BREAST CANCER.
[8]"Fanconi anemia is associated with a defect in the BRCA2 partner PALB2."
Xia B., Dorsman J.C., Ameziane N., de Vries Y., Rooimans M.A., Sheng Q., Pals G., Errami A., Gluckman E., Llera J., Wang W., Livingston D.M., Joenje H., de Winter J.P.
Nat. Genet. 39:159-161(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN FANCN.
[9]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"PALB2 regulates recombinational repair through chromatin association and oligomerization."
Sy S.M., Huen M.S., Zhu Y., Chen J.
J. Biol. Chem. 284:18302-18310(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH BRCA2.
[12]"PALB2 is an integral component of the BRCA complex required for homologous recombination repair."
Sy S.M., Huen M.S., Chen J.
Proc. Natl. Acad. Sci. U.S.A. 106:7155-7160(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A BRCA COMPLEX WITH BRCA1 AND BRCA2, INTERACTION WITH BRCA1, MUTAGENESIS OF LYS-14; LEU-21; TYR-28; LEU-35 AND GLU-42.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Exomic sequencing identifies PALB2 as a pancreatic cancer susceptibility gene."
Jones S., Hruban R.H., Kamiyama M., Borges M., Zhang X., Parsons D.W., Lin J.C., Palmisano E., Brune K., Jaffee E.M., Iacobuzio-Donahue C.A., Maitra A., Parmigiani G., Kern S.E., Velculescu V.E., Kinzler K.W., Vogelstein B., Eshleman J.R., Goggins M., Klein A.P.
Science 324:217-217(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PNCA3.
[15]"MRG15 binds directly to PALB2 and stimulates homology-directed repair of chromosomal breaks."
Hayakawa T., Zhang F., Hayakawa N., Ohtani Y., Shinmyozu K., Nakayama J., Andreassen P.R.
J. Cell Sci. 123:1124-1130(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MORF4L1.
[16]"Cooperation of breast cancer proteins PALB2 and piccolo BRCA2 in stimulating homologous recombination."
Buisson R., Dion-Cote A.M., Coulombe Y., Launay H., Cai H., Stasiak A.Z., Stasiak A., Xia B., Masson J.Y.
Nat. Struct. Mol. Biol. 17:1247-1254(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAD51.
[17]"Enhancement of RAD51 recombinase activity by the tumor suppressor PALB2."
Dray E., Etchin J., Wiese C., Saro D., Williams G.J., Hammel M., Yu X., Galkin V.E., Liu D., Tsai M.S., Sy S.M., Schild D., Egelman E., Chen J., Sung P.
Nat. Struct. Mol. Biol. 17:1255-1259(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAD51 AND RAD51AP1.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"ChAM, a novel motif that mediates PALB2 intrinsic chromatin binding and facilitates DNA repair."
Bleuyard J.Y., Buisson R., Masson J.Y., Esashi F.
EMBO Rep. 13:135-141(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH CHROMATIN, ASSOCIATION WITH NUCLEOSOMES.
[21]"Rare germline mutations in PALB2 and breast cancer risk: a population-based study."
Tischkowitz M., Capanu M., Sabbaghian N., Li L., Liang X., Vallee M.P., Tavtigian S.V., Concannon P., Foulkes W.D., Bernstein L., Bernstein J.L., Begg C.B.
Hum. Mutat. 33:674-680(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO BREAST CANCER.
[22]"PALB2 self-interaction controls homologous recombination."
Buisson R., Masson J.Y.
Nucleic Acids Res. 40:10312-10323(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SELF-ASSOCIATION.
[23]"Breast cancer-associated missense mutants of the PALB2 WD40 domain, which directly binds RAD51C, RAD51 and BRCA2, disrupt DNA repair."
Park J.Y., Singh T.R., Nassar N., Zhang F., Freund M., Hanenberg H., Meetei A.R., Andreassen P.R.
Oncogene 0:0-0(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BRCA2; RAD51C; RAD51 AND XRCC3, MUTAGENESIS OF THR-1030, CHARACTERIZATION OF VARIANTS TRP-939 AND PRO-1143.
[24]"Breast cancer proteins PALB2 and BRCA2 stimulate polymerase eta in recombination-associated DNA synthesis at blocked replication forks."
Buisson R., Niraj J., Pauty J., Maity R., Zhao W., Coulombe Y., Sung P., Masson J.Y.
Cell Rep. 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH POLH.
[25]"Structural basis for recruitment of BRCA2 by PALB2."
Oliver A.W., Swift S., Lord C.J., Ashworth A., Pearl L.H.
EMBO Rep. 10:990-996(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 835-1186 ALONE AND IN COMPLEX WITH A BRCA2 PEPTIDE, DOMAIN WD REPEATS.
[26]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. expand/collapse author list , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K.
Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-864.
[27]"Germline mutations in the PALB2 gene are population specific and occur with low frequencies in familial breast cancer."
Hellebrand H., Sutter C., Honisch E., Gross E., Wappenschmidt B., Schem C., Deissler H., Ditsch N., Gress V., Kiechle M., Bartram C.R., Schmutzler R.K., Niederacher D., Arnold N., Meindl A.
Hum. Mutat. 32:E2176-E2188(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TYR-46; GLY-219; CYS-334; SER-337; GLN-414; MET-425; THR-491; ARG-515; ARG-559; GLN-672; VAL-712; LEU-728; SER-864; ALA-917; MET-932; TRP-939; VAL-966; GLU-998; THR-1025; ALA-1043; GLY-1075; ALA-1105; HIS-1114; PRO-1143 AND TYR-1170.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL834425 mRNA. Translation: CAD39086.1.
CR749637 mRNA. Translation: CAH18431.1.
AC008870 Genomic DNA. No translation available.
CH471145 Genomic DNA. Translation: EAW55813.1.
BC044254 mRNA. Translation: AAH44254.1.
AK025469 mRNA. Translation: BAB15140.1. Different initiation.
AK097533 mRNA. Translation: BAC05090.1.
RefSeqNP_078951.2. NM_024675.3.
UniGeneHs.444664.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2W18X-ray1.90A835-1186[»]
3EU7X-ray2.20A835-1186[»]
ProteinModelPortalQ86YC2.
SMRQ86YC2. Positions 854-1186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122843. 11 interactions.
DIPDIP-38427N.
IntActQ86YC2. 7 interactions.
MINTMINT-7262182.
STRING9606.ENSP00000261584.

PTM databases

PhosphoSiteQ86YC2.

Polymorphism databases

DMDM74727919.

Proteomic databases

PaxDbQ86YC2.
PRIDEQ86YC2.

Protocols and materials databases

DNASU79728.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261584; ENSP00000261584; ENSG00000083093.
GeneID79728.
KEGGhsa:79728.
UCSCuc002dlx.1. human.

Organism-specific databases

CTD79728.
GeneCardsGC16M023614.
HGNCHGNC:26144. PALB2.
HPACAB014895.
HPA057000.
MIM114480. phenotype.
227650. phenotype.
610355. gene.
610832. phenotype.
613348. phenotype.
neXtProtNX_Q86YC2.
Orphanet1333. Familial pancreatic carcinoma.
84. Fanconi anemia.
145. Hereditary breast and ovarian cancer syndrome.
PharmGKBPA162398608.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG73403.
HOGENOMHOG000115428.
HOVERGENHBG082102.
InParanoidQ86YC2.
KOK10897.
OMANIVIWNL.
OrthoDBEOG72C51Z.
PhylomeDBQ86YC2.
TreeFamTF351544.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressQ86YC2.
BgeeQ86YC2.
CleanExHS_PALB2.
GenevestigatorQ86YC2.

Family and domain databases

Gene3D2.130.10.10. 3 hits.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
SUPFAMSSF50978. SSF50978. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceQ86YC2.
GeneWikiPALB2.
GenomeRNAi79728.
NextBio69102.
PROQ86YC2.
SOURCESearch...

Entry information

Entry namePALB2_HUMAN
AccessionPrimary (citable) accession number: Q86YC2
Secondary accession number(s): A6NIE1 expand/collapse secondary AC list , Q8N7Y6, Q8ND31, Q9H6W1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM