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Q86YC2

- PALB2_HUMAN

UniProt

Q86YC2 - PALB2_HUMAN

Protein

Partner and localizer of BRCA2

Gene

PALB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    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.8 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. DNA repair Source: Reactome
    2. double-strand break repair via homologous recombination Source: UniProtKB
    3. inner cell mass cell proliferation Source: Ensembl
    4. mesoderm development Source: Ensembl
    5. negative regulation of apoptotic process Source: Ensembl
    6. organ morphogenesis Source: Ensembl
    7. post-anal tail morphogenesis Source: Ensembl
    8. somitogenesis Source: Ensembl

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_18410. Fanconi Anemia pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Partner and localizer of BRCA2
    Gene namesi
    Name:PALB2
    Synonyms:FANCN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:26144. PALB2.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Colocalizes with BRCA2 in nuclear foci.

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    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 (PubMed:22241545).1 Publication
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141K → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. 1 Publication
    Mutagenesisi21 – 211L → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. 1 Publication
    Mutagenesisi28 – 281Y → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. 1 Publication
    Mutagenesisi35 – 351L → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. 1 Publication
    Mutagenesisi42 – 421E → A: Loss of interaction with BRCA1 but no effect on interaction with BRCA2. 1 Publication
    Mutagenesisi1030 – 10301T → I: Unstable and promotes protein degradation; reduces interaction with RAD51C and RAD51. 1 Publication

    Keywords - Diseasei

    Fanconi anemia, Tumor suppressor

    Organism-specific databases

    MIMi114480. phenotype.
    227650. phenotype.
    610832. phenotype.
    613348. phenotype.
    Orphaneti1333. Familial pancreatic carcinoma.
    84. Fanconi anemia.
    145. Hereditary breast and ovarian cancer syndrome.
    PharmGKBiPA162398608.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11861186Partner and localizer of BRCA2PRO_0000252391Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei376 – 3761Phosphoserine2 Publications
    Modified residuei387 – 3871Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ86YC2.
    PaxDbiQ86YC2.
    PRIDEiQ86YC2.

    PTM databases

    PhosphoSiteiQ86YC2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ86YC2.
    BgeeiQ86YC2.
    CleanExiHS_PALB2.
    GenevestigatoriQ86YC2.

    Organism-specific databases

    HPAiCAB014895.
    HPA057000.

    Interactioni

    Subunit structurei

    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.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRCA2P5158715EBI-1222653,EBI-79792
    POLHQ9Y2537EBI-1222653,EBI-2827270
    RAD51Q066095EBI-1222653,EBI-297202
    RAD51CO4350210EBI-1222653,EBI-2267048
    XRCC3O435423EBI-1222653,EBI-2849976

    Protein-protein interaction databases

    BioGridi122843. 11 interactions.
    DIPiDIP-38427N.
    IntActiQ86YC2. 11 interactions.
    MINTiMINT-7262182.
    STRINGi9606.ENSP00000261584.

    Structurei

    Secondary structure

    1
    1186
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi855 – 8617
    Beta strandi869 – 8779
    Beta strandi884 – 91330
    Beta strandi919 – 9224
    Beta strandi932 – 9365
    Beta strandi938 – 94710
    Beta strandi958 – 97215
    Turni973 – 9753
    Beta strandi976 – 9849
    Beta strandi988 – 9947
    Beta strandi1000 – 10067
    Beta strandi1013 – 10208
    Beta strandi1025 – 10306
    Beta strandi1033 – 10397
    Turni1040 – 10423
    Beta strandi1045 – 10506
    Beta strandi1053 – 10553
    Beta strandi1059 – 10668
    Beta strandi1069 – 10757
    Beta strandi1090 – 10967
    Turni1097 – 11004
    Beta strandi1101 – 11088
    Beta strandi1118 – 11247
    Beta strandi1127 – 11326
    Beta strandi1137 – 11415
    Turni1142 – 11443
    Beta strandi1146 – 11516
    Beta strandi1161 – 11644
    Beta strandi1166 – 11749
    Beta strandi1180 – 11856

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2W18X-ray1.90A835-1186[»]
    3EU7X-ray2.20A835-1186[»]
    ProteinModelPortaliQ86YC2.
    SMRiQ86YC2. Positions 854-1186.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ86YC2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati854 – 91562WD 1Add
    BLAST
    Repeati917 – 96145WD 2Add
    BLAST
    Repeati962 – 100948WD 3Add
    BLAST
    Repeati1010 – 105243WD 4Add
    BLAST
    Repeati1058 – 110952WD 5Add
    BLAST
    Repeati1115 – 115339WD 6Add
    BLAST
    Repeati1155 – 118632WD 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 579579DNA-binding (with the preference D loop > dsDNA > ssDNA)Add
    BLAST
    Regioni1 – 319319Interaction with BRCA1Add
    BLAST
    Regioni1 – 200200Interaction with RAD51Add
    BLAST
    Regioni1 – 160160Required for its oligomerization and is important for its focal concentration at DNA damage sitesAdd
    BLAST
    Regioni395 – 44652ChAM (Chromatin-association motif); required for chromatin association, mediates nucleosome associationAdd
    BLAST
    Regioni775 – 1186412Required for interaction with POLH and POLH DNA synthesis stimulationAdd
    BLAST
    Regioni853 – 1186334Interaction with RAD51, BRCA2 and POLHAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili9 – 4133Sequence AnalysisAdd
    BLAST

    Domaini

    Interaction with BRCA2 occurs through a hydrophobic pocket at the crossover between WD repeats 4 and 5.1 Publication
    The coiled coil domain mediates self-association.2 Publications
    The chromatin-association motif (ChAM) mediates association with chromatin, probably through nucleosome core particles, independently from binding to D loop, ssDNA or dsDNA structures.2 Publications

    Sequence similaritiesi

    Contains 7 WD repeats.Curated

    Keywords - Domaini

    Coiled coil, Repeat, WD repeat

    Phylogenomic databases

    eggNOGiNOG73403.
    HOGENOMiHOG000115428.
    HOVERGENiHBG082102.
    InParanoidiQ86YC2.
    KOiK10897.
    OMAiNIVIWNL.
    OrthoDBiEOG72C51Z.
    PhylomeDBiQ86YC2.
    TreeFamiTF351544.

    Family and domain databases

    Gene3Di2.130.10.10. 3 hits.
    InterProiIPR015943. WD40/YVTN_repeat-like_dom.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q86YC2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDEPPGKPLS CEEKEKLKEK LAFLKREYSK TLARLQRAQR AEKIKHSIKK     50
    TVEEQDCLSQ QDLSPQLKHS EPKNKICVYD KLHIKTHLDE ETGEKTSITL 100
    DVGPESFNPG DGPGGLPIQR TDDTQEHFPH RVSDPSGEQK QKLPSRRKKQ 150
    QKRTFISQER DCVFGTDSLR LSGKRLKEQE EISSKNPARS PVTEIRTHLL 200
    SLKSELPDSP EPVTEINEDS VLIPPTAQPE KGVDTFLRRP NFTRATTVPL 250
    QTLSDSGSSQ HLEHIPPKGS SELTTHDLKN IRFTSPVSLE AQGKKMTVST 300
    DNLLVNKAIS KSGQLPTSSN LEANISCSLN ELTYNNLPAN ENQNLKEQNQ 350
    TEKSLKSPSD TLDGRNENLQ ESEILSQPKS LSLEATSPLS AEKHSCTVPE 400
    GLLFPAEYYV RTTRSMSNCQ RKVAVEAVIQ SHLDVKKKGF KNKNKDASKN 450
    LNLSNEETDQ SEIRMSGTCT GQPSSRTSQK LLSLTKVSSP AGPTEDNDLS 500
    RKAVAQAPGR RYTGKRKSAC TPASDHCEPL LPTSSLSIVN RSKEEVTSHK 550
    YQHEKLFIQV KGKKSRHQKE DSLSWSNSAY LSLDDDAFTA PFHRDGMLSL 600
    KQLLSFLSIT DFQLPDEDFG PLKLEKVKSC SEKPVEPFES KMFGERHLKE 650
    GSCIFPEELS PKRMDTEMED LEEDLIVLPG KSHPKRPNSQ SQHTKTGLSS 700
    SILLYTPLNT VAPDDNDRPT TDMCSPAFPI LGTTPAFGPQ GSYEKASTEV 750
    AGRTCCTPQL AHLKDSVCLA SDTKQFDSSG SPAKPHTTLQ VSGRQGQPTC 800
    DCDSVPPGTP PPIESFTFKE NQLCRNTCQE LHKHSVEQTE TAELPASDSI 850
    NPGNLQLVSE LKNPSGSCSV DVSAMFWERA GCKEPCIITA CEDVVSLWKA 900
    LDAWQWEKLY TWHFAEVPVL QIVPVPDVYN LVCVALGNLE IREIRALFCS 950
    SDDESEKQVL LKSGNIKAVL GLTKRRLVSS SGTLSDQQVE VMTFAEDGGG 1000
    KENQFLMPPE ETILTFAEVQ GMQEALLGTT IMNNIVIWNL KTGQLLKKMH 1050
    IDDSYQASVC HKAYSEMGLL FIVLSHPCAK ESESLRSPVF QLIVINPKTT 1100
    LSVGVMLYCL PPGQAGRFLE GDVKDHCAAA ILTSGTIAIW DLLLGQCTAL 1150
    LPPVSDQHWS FVKWSGTDSH LLAGQKDGNI FVYHYS 1186
    Length:1,186
    Mass (Da):131,295
    Last modified:June 1, 2003 - v1
    Checksum:i215EC32291315FA2
    GO

    Sequence cautioni

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti46 – 461H → Y.1 Publication
    VAR_066361
    Natural varianti219 – 2191D → G.1 Publication
    VAR_066362
    Natural varianti309 – 3091I → V.
    Corresponds to variant rs3809683 [ dbSNP | Ensembl ].
    VAR_032959
    Natural varianti334 – 3341Y → C.1 Publication
    VAR_066363
    Natural varianti337 – 3371L → S.1 Publication
    Corresponds to variant rs45494092 [ dbSNP | Ensembl ].
    VAR_066364
    Natural varianti414 – 4141R → Q.1 Publication
    VAR_066365
    Natural varianti425 – 4251V → M.1 Publication
    VAR_066366
    Natural varianti491 – 4911A → T.1 Publication
    VAR_066367
    Natural varianti515 – 5151K → R.1 Publication
    VAR_066368
    Natural varianti559 – 5591Q → R.1 Publication
    Corresponds to variant rs152451 [ dbSNP | Ensembl ].
    VAR_066369
    Natural varianti672 – 6721E → Q.1 Publication
    Corresponds to variant rs45532440 [ dbSNP | Ensembl ].
    VAR_066370
    Natural varianti712 – 7121A → V.1 Publication
    Corresponds to variant rs141458731 [ dbSNP | Ensembl ].
    VAR_066371
    Natural varianti728 – 7281F → L.1 Publication
    VAR_066372
    Natural varianti864 – 8641P → S.2 Publications
    Corresponds to variant rs45568339 [ dbSNP | Ensembl ].
    VAR_054150
    Natural varianti917 – 9171V → A.1 Publication
    VAR_066373
    Natural varianti932 – 9321V → M.1 Publication
    Corresponds to variant rs45624036 [ dbSNP | Ensembl ].
    VAR_066374
    Natural varianti939 – 9391L → 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. 1 Publication
    Corresponds to variant rs45478192 [ dbSNP | Ensembl ].
    VAR_066375
    Natural varianti966 – 9661I → V.1 Publication
    VAR_066376
    Natural varianti998 – 9981G → E May be associated with breast cancer susceptibility. 1 Publication
    Corresponds to variant rs45551636 [ dbSNP | Ensembl ].
    VAR_066377
    Natural varianti1025 – 10251A → T.1 Publication
    VAR_066378
    Natural varianti1043 – 10431G → 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. 1 Publication
    VAR_066379
    Natural varianti1075 – 10751S → G.1 Publication
    VAR_066380
    Natural varianti1105 – 11051V → A.1 Publication
    VAR_066381
    Natural varianti1114 – 11141Q → H.1 Publication
    VAR_066382
    Natural varianti1143 – 11431L → P May be associated with breast cancer susceptibility. 1 Publication
    VAR_066383
    Natural varianti1170 – 11701H → Y.1 Publication
    VAR_066384

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS32406.1.
    RefSeqiNP_078951.2. NM_024675.3.
    UniGeneiHs.444664.

    Genome annotation databases

    EnsembliENST00000261584; ENSP00000261584; ENSG00000083093.
    GeneIDi79728.
    KEGGihsa:79728.
    UCSCiuc002dlx.1. human.

    Polymorphism databases

    DMDMi74727919.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS32406.1.
    RefSeqi NP_078951.2. NM_024675.3.
    UniGenei Hs.444664.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2W18 X-ray 1.90 A 835-1186 [» ]
    3EU7 X-ray 2.20 A 835-1186 [» ]
    ProteinModelPortali Q86YC2.
    SMRi Q86YC2. Positions 854-1186.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122843. 11 interactions.
    DIPi DIP-38427N.
    IntActi Q86YC2. 11 interactions.
    MINTi MINT-7262182.
    STRINGi 9606.ENSP00000261584.

    PTM databases

    PhosphoSitei Q86YC2.

    Polymorphism databases

    DMDMi 74727919.

    Proteomic databases

    MaxQBi Q86YC2.
    PaxDbi Q86YC2.
    PRIDEi Q86YC2.

    Protocols and materials databases

    DNASUi 79728.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261584 ; ENSP00000261584 ; ENSG00000083093 .
    GeneIDi 79728.
    KEGGi hsa:79728.
    UCSCi uc002dlx.1. human.

    Organism-specific databases

    CTDi 79728.
    GeneCardsi GC16M023614.
    GeneReviewsi PALB2.
    HGNCi HGNC:26144. PALB2.
    HPAi CAB014895.
    HPA057000.
    MIMi 114480. phenotype.
    227650. phenotype.
    610355. gene.
    610832. phenotype.
    613348. phenotype.
    neXtProti NX_Q86YC2.
    Orphaneti 1333. Familial pancreatic carcinoma.
    84. Fanconi anemia.
    145. Hereditary breast and ovarian cancer syndrome.
    PharmGKBi PA162398608.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG73403.
    HOGENOMi HOG000115428.
    HOVERGENi HBG082102.
    InParanoidi Q86YC2.
    KOi K10897.
    OMAi NIVIWNL.
    OrthoDBi EOG72C51Z.
    PhylomeDBi Q86YC2.
    TreeFami TF351544.

    Enzyme and pathway databases

    Reactomei REACT_18410. Fanconi Anemia pathway.

    Miscellaneous databases

    EvolutionaryTracei Q86YC2.
    GeneWikii PALB2.
    GenomeRNAii 79728.
    NextBioi 69102.
    PROi Q86YC2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86YC2.
    Bgeei Q86YC2.
    CleanExi HS_PALB2.
    Genevestigatori Q86YC2.

    Family and domain databases

    Gene3Di 2.130.10.10. 3 hits.
    InterProi IPR015943. WD40/YVTN_repeat-like_dom.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. 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. 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. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO BREAST CANCER.
    8. Cited for: INVOLVEMENT IN FANCN.
    9. 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. 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. 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. 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. 6:553-564(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. 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.

    Entry informationi

    Entry nameiPALB2_HUMAN
    AccessioniPrimary (citable) accession number: Q86YC2
    Secondary accession number(s): A6NIE1
    , Q8N7Y6, Q8ND31, Q9H6W1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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