Q86YC2 (PALB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Partner and localizer of BRCA2

Gene names

Name:	PALB2
Synonyms:	FANCN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1186 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Serves as the molecular scaffold in the formation of the BRCA1-PALB2-BRCA2 complex which is essential for homologous recombination. 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. 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. Ref.6 Ref.10 Ref.11 Ref.15 Ref.16
Subunit structure	Homooligomer. Oligomerization is essential for its focal accumulation at DNA breaks. Part of a trimeric complex containing BRCA1, BRCA2 and PALB2. Interacts with BRCA1 and this interaction is essential for its function in HRR. Interacts with RAD51, BRCA2, RAD51AP1 and MORF4L1/MRG15. Ref.6 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16
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.20
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.19). 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.13
Sequence similarities	Contains 7 WD repeats.
Sequence caution	The sequence BAB15140.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Fanconi anemia Tumor suppressor
Domain	Coiled coil Repeat WD repeat
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	double-strand break repair via homologous recombination Inferred from direct assay Ref.11Ref.10. Source: UniProtKB inner cell mass cell proliferation Inferred from electronic annotation. Source: Compara mesoderm development Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara organ morphogenesis Inferred from electronic annotation. Source: Compara post-anal tail morphogenesis Inferred from electronic annotation. Source: Compara somitogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Inferred from direct assay Ref.16. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1186

1186

Partner and localizer of BRCA2

PRO_0000252391

Regions

Repeat

854 – 915

62

WD 1

Repeat

917 – 961

45

WD 2

Repeat

962 – 1009

48

WD 3

Repeat

1010 – 1052

43

WD 4

Repeat

1058 – 1109

52

WD 5

Repeat

1115 – 1153

39

WD 6

Repeat

1155 – 1186

32

WD 7

Region

1 – 319

319

Interaction with BRCA1

Region

1 – 200

200

Interaction with RAD51

Region

1 – 160

160

Required for its oligomerization and is important for its focal concentration at DNA damage sites

Region

853 – 1186

334

Interaction with RAD51 and BRCA2

Coiled coil

9 – 41

33

Potential

Amino acid modifications

Modified residue

376

1

Phosphoserine Ref.9 Ref.17

Modified residue

387

1

Phosphoserine Ref.12

Natural variations

Natural variant

46

1

H → Y. Ref.22

VAR_066361

Natural variant

219

1

D → G. Ref.22

VAR_066362

Natural variant

309

1

I → V.
Corresponds to variant rs3809683 [ dbSNP | Ensembl ].

VAR_032959

Natural variant

334

1

Y → C. Ref.22

VAR_066363

Natural variant

337

1

L → S. Ref.22

VAR_066364

Natural variant

414

1

R → Q. Ref.22

VAR_066365

Natural variant

425

1

V → M. Ref.22

VAR_066366

Natural variant

491

1

A → T. Ref.22

VAR_066367

Natural variant

515

1

K → R. Ref.22

VAR_066368

Natural variant

559

1

Q → R. Ref.22

VAR_066369

Natural variant

672

1

E → Q. Ref.22

VAR_066370

Natural variant

712

1

A → V. Ref.22

VAR_066371

Natural variant

728

1

F → L. Ref.22

VAR_066372

Natural variant

864

1

P → S. Ref.21 Ref.22
Corresponds to variant rs45568339 [ dbSNP | Ensembl ].

VAR_054150

Natural variant

917

1

V → A. Ref.22

VAR_066373

Natural variant

932

1

V → M. Ref.22

VAR_066374

Natural variant

939

1

L → W May be associated with breast cancer susceptibility. Ref.22

VAR_066375

Natural variant

966

1

I → V. Ref.22

VAR_066376

Natural variant

998

1

G → E May be associated with breast cancer susceptibility. Ref.22

VAR_066377

Natural variant

1025

1

A → T. Ref.22

VAR_066378

Natural variant

1043

1

G → A May be associated with breast cancer susceptibility. Ref.22

VAR_066379

Natural variant

1075

1

S → G. Ref.22

VAR_066380

Natural variant

1105

1

V → A. Ref.22

VAR_066381

Natural variant

1114

1

Q → H. Ref.22

VAR_066382

Natural variant

1143

1

L → P May be associated with breast cancer susceptibility. Ref.22

VAR_066383

Natural variant

1170

1

H → Y. Ref.22

VAR_066384

Experimental info

Mutagenesis

14

1

K → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. Ref.11

Mutagenesis

21

1

L → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. Ref.11

Mutagenesis

28

1

Y → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. Ref.11

Mutagenesis

35

1

L → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. Ref.11

Mutagenesis

42

1

E → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. Ref.11

Secondary structure

1

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1186

Helix Strand Turn

Details...

Beta strand

855 – 861

7

Beta strand

869 – 877

9

Beta strand

884 – 913

30

Beta strand

919 – 922

4

Beta strand

932 – 936

5

Beta strand

938 – 947

10

Beta strand

958 – 972

15

Turn

973 – 975

3

Beta strand

976 – 984

9

Beta strand

988 – 994

7

Beta strand

1000 – 1006

7

Beta strand

1013 – 1020

8

Beta strand

1025 – 1030

6

Beta strand

1033 – 1039

7

Turn

1040 – 1042

3

Beta strand

1045 – 1050

6

Beta strand

1053 – 1055

3

Beta strand

1059 – 1066

8

Beta strand

1069 – 1075

7

Beta strand

1090 – 1096

7

Turn

1097 – 1100

4

Beta strand

1101 – 1108

8

Beta strand

1118 – 1124

7

Beta strand

1127 – 1132

6

Beta strand

1137 – 1141

5

Turn

1142 – 1144

3

Beta strand

1146 – 1151

6

Beta strand

1161 – 1164

4

Beta strand

1166 – 1174

9

Beta strand

1180 – 1185

6

Sequences

	Sequence		Length	Mass (Da)
	Q86YC2 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 215EC32291315FA2	FASTA	1,186	131,295
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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 BREAST CANCER SUSCEPTIBILITY.
[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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"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.
[11]	"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 COMPLEX WITH BRCA1 AND BRCA2, INTERACTION WITH BRCA1, MUTAGENESIS OF LYS-14; LEU-21; TYR-28; LEU-35 AND GLU-42.
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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].
[19]	"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.
[20]	"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.
[21]	"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. , 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.
[22]	"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

GeneReviews

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.

IPI

IPI00172559.

RefSeq

NP_078951.2. NM_024675.3.

UniGene

Hs.444664.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2W18	X-ray	1.90	A	835-1186	[»]
3EU7	X-ray	2.20	A	835-1186	[»]

ProteinModelPortal

Q86YC2.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38427N.

IntAct

Q86YC2. 1 interaction.

MINT

MINT-7262182.

STRING

9606.ENSP00000261584.

PTM databases

PhosphoSite

Q86YC2.

Polymorphism databases

DMDM

74727919.

Proteomic databases

PaxDb

Q86YC2.

PRIDE

Q86YC2.

Protocols and materials databases

DNASU

79728.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261584; ENSP00000261584; ENSG00000083093.

GeneID

79728.

KEGG

hsa:79728.

UCSC

uc002dlx.1. human.

Organism-specific databases

CTD

79728.

GeneCards

GC16M023614.

HGNC

HGNC:26144. PALB2.

HPA

CAB014895.

MIM

114480. phenotype.
227650. phenotype.
610355. gene.
610832. phenotype.
613348. phenotype.

neXtProt

NX_Q86YC2.

Orphanet

1333. Familial pancreatic carcinoma.
84. Fanconi anemia.
145. Hereditary breast and ovarian cancer syndrome.

PharmGKB

PA162398608.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG73403.

HOGENOM

HOG000115428.

HOVERGEN

HBG082102.

InParanoid

Q86YC2.

KO

K10897.

OMA

VCHKAYS.

OrthoDB

EOG41NTK6.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

Q86YC2.

Bgee

Q86YC2.

CleanEx

HS_PALB2.

Genevestigator

Q86YC2.

GermOnline

ENSG00000083093. Homo sapiens.

Family and domain databases

Gene3D

2.130.10.10. 3 hits.

InterPro

IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]

SUPFAM

SSF50978. WD40_like. 1 hit.

PROSITE

PS00678. WD_REPEATS_1. False negative.
PS50082. WD_REPEATS_2. False negative.
PS50294. WD_REPEATS_REGION. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q86YC2.

GenomeRNAi

79728.

NextBio

69102.

SOURCE

Search...

Entry information

Entry name

PALB2_HUMAN

Accession

Primary (citable) accession number: Q86YC2
Secondary accession number(s): A6NIE1 , Q8N7Y6, Q8ND31, Q9H6W1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 17, 2006
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.