Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
PALB2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PALB2 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. Defects in PALB2 are a cause of susceptibility to breast cancer (BC). 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. Breast cancer susceptibility is strongly associated with PALB2 truncating mutations. Conversely, rare missense mutations do not strongly influence breast cancer risk (PubMed:22241545). Defects in PALB2 are the cause of Fanconi anemia complementation group N (FANCN). It is 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. Defects in PALB2 are the cause of pancreatic cancer type 3 (PNCA3). It is 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: This description may include information from UniProtKB.
Protein type: Unknown function
Chromosomal Location of Human Ortholog: 16p12.2
Cellular Component: nucleoplasm; nucleolus; nucleus
Molecular Function: protein binding; DNA binding
Biological Process: somitogenesis; organ morphogenesis; mesoderm development; DNA repair; inner cell mass cell proliferation; double-strand break repair via homologous recombination; negative regulation of apoptosis
Reference #:  Q86YC2 (UniProtKB)
Alt. Names/Synonyms: DKFZp667I166; DKFZp686E1054; FANCN; FLJ21816; PALB2; Partner and localizer of BRCA2
Gene Symbols: PALB2
Molecular weight: 131,295 Da
Basal Isoelectric point: 6.03  Predict pI for various phosphorylation states
Select Structure to View Below

PALB2

Protein Structure Not Found.


STRING  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 3 S59-p VEEQDCLsQQDLsPQ
0 7 S64-p CLsQQDLsPQLKHSE
0 1 R131 TQEHFPHRVSDPSGE
0 1 S157-p QQKRTFIsQERDCVF
0 2 S172-p GTDSLRLsGKRLKEQ
0 2 S190-p SSKNPARsPVTEIRT
0 1 S209-p LKSELPDsPEPVTEI
0 1 T246-p RPNFTRAttVPLQTL
0 1 T247-p PNFTRAttVPLQTLS
0 1 T284-p DLKNIRFtsPVsLEA
0 3 S285-p LKNIRFtsPVsLEAQ
0 1 S288-p IRFtsPVsLEAQGkk
0 1 K294-ac VsLEAQGkkMTVSTD
0 1 K295-ac sLEAQGkkMTVSTDN
0 1 K307-ac TDNLLVNkAISKsGQ
0 1 S312-p VNkAISKsGQLPTSs
0 1 S319-p sGQLPTSsNLEANIs
0 1 S326-p sNLEANIsCSLNELT
0 1 S357-p QTEKSLKsPSDTLDG
0 7 S376-p LQESEILsQPKsLsL
0 1 S380-p EILsQPKsLsLEATs
0 1 S382-p LsQPKsLsLEATsPL
0 6 S387-p sLsLEATsPLsAEKH
0 1 S390-p LEATsPLsAEKHSCT
0 3 S454-p ASKNLNLsNEETDQS
0 1 S488-p LLSLTKVssPAGPTE
0 3 S489-p LSLTKVssPAGPTED
0 1 S518-p RYTGKRKsACTPASD
0 1 S631-p LEKVKSCsEKPVEPF
0 8 S660-p CIFPEELsPKRMDTE
0 1 T757-p VAGRTCCtPQLAHLK
0 1 S781-p KQFDSSGsPAKPHTT
0 1 S792-p PHTTLQVsGRQGQPT
0 1 S865 VSELKNPSGSCSVDV
0 1 G866 SELKNPSGSCSVDVS
0 1 S869 KNPSGSCSVDVSAMF
0 1 S963 EKQVLLKSGNIKAVL
0 1 K974 KAVLGLTKRRLVSSS
0 1 S1165-p HWSFVKWsGtDSHLL
0 1 T1167-p SFVKWsGtDSHLLAG
  mouse

 
P56 KAIEDGVPQPEASSQ
S61 GVPQPEASSQLSHSE
S127-p IQGQLLHsTSSPDGK
S154 PWEKSSVSQEKEDYF
L169 DTNSLALLGKHRKGQ
T186 ISRKNSRTPVSEKTH
P204 LRSQIPDPPALVTGI
A240 GNTVSAEAAVPSCTA
A241 NTVSAEAAVPSCTAS
A273 KITTQGPASSTNLVA
S274 ITTQGPASSTNLVAQ
N277 QGPASSTNLVAQDQK
Q283 TNLVAQDQKMTIFTV
K284 NLVAQDQKMTIFTVN
K296 TVNSVVYKAVRAHGQ
H301 VYKAVRAHGQLPGSP
P308 HGQLPGSPNSCSVND
S310 QLPGSPNSCSVNDLT
S334 PNSKSLKSPSNTVDE
G353 LQEDEILGPSKNFNL
N357 EILGPSKNFNLAAVS
N359 LGPSKNFNLAAVSPP
S364 NFNLAAVSPPSTESQ
S367 LAAVSPPSTESQIHS
S432 ATKAVVLSSEDTDQS
S467 LLSPAEVSSPPGPAG
S468 LSPAEVSSPPGPAGK
S491 GHRGKRKSARTSTLG
S553 LEKLKSCSEKLIESP
Q582 HAALEELQRDSETEG
T675 EAAQPCSTSQPPLLG
C699 KQCNSSACSPKPDTN
S710 PDTNLQASGRQGQPA
S783-p VSELKNPssSCsVDV
S784-p SELKNPssSCsVDVS
S787-p KNPssSCsVDVSAMW
S881-p EKQVLLKsGDIKAML
K892-ub KAMLGLTkRRLVSST
S1083 SWSLVKWSGTDSHLL
T1085 SLVKWSGTDSHLLAG
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.