PALB2_MOUSE - dbPTM
PALB2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PALB2_MOUSE
UniProt AC Q3U0P1
Protein Name Partner and localizer of BRCA2
Gene Name Palb2
Organism Mus musculus (Mouse).
Sequence Length 1104
Subcellular Localization Nucleus. Colocalizes with BRCA2 in nuclear foci..
Protein Description 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 (By similarity)..
Protein Sequence MEELSGKPLSYAEKEKLKEKLAFLKKEYSRTLARLQRAKRAEKAKNSKKAIEDGVPQPEASSQLSHSESINKGFPCDTLQSNHLDEETGENISQILDVEPQSFNCKQGKEVLHTPRAGDIQGQLLHSTSSPDGKKEQNTLPGTTKTPWEKSSVSQEKEDYFDTNSLALLGKHRKGQESISRKNSRTPVSEKTHLLSLRSQIPDPPALVTGIGEGILIPPSGKSERGIDTLVRGNTVSAEAAVPSCTASNSNHSQHLEHTPPKSGCKITTQGPASSTNLVAQDQKMTIFTVNSVVYKAVRAHGQLPGSPNSCSVNDLTHSNLPANSTPNSKSLKSPSNTVDERNEPLQEDEILGPSKNFNLAAVSPPSTESQIHSCTMLEGLLFPAEYYVRTTRRMSDCQRKIALEAVIQSHLGVKKKELKKKTKATKAVVLSSEDTDQSESGMLDTSTGQSSSGSLSQKLLSPAEVSSPPGPAGKATTPPPGRGHRGKRKSARTSTLGHCQLLFPPCAALAVNRSKGKFTKHKCQNRGVVIHDFELPDEDFGLLKLEKLKSCSEKLIESPDSKNCGERLPREGNHAALEELQRDSETEGLEEELTVPPGEAYRPGPTLRRQPGSKDLSSSIVLFTPADTAAPNDSGRPPPSLCSPAFPILGMTPALGSQAAGETLSTEAAQPCSTSQPPLLGDTNSLVNNSKQCNSSACSPKPDTNLQASGRQGQPACDSDSGPQATPLPVESFTFRENQLCGNACLELHEHSTEQTETADRPACDNLNPGNLQLVSELKNPSSSCSVDVSAMWWERAGAKEPCIVTACEDVVSLWKPLNSLQWEKVHTWHFTEVPVLQIVPVPDVYNLICVALGSLEIREIRALLCSSGDDSEKQVLLKSGDIKAMLGLTKRRLVSSTGTFCNQQIQIMTFADDGSSKDEQLLMPPDETVLTFAEVQGTQEALLGTTTVNSIVIWNLKTGQLLKKMHIDDSYQASVCHGAYSEKGLLFVVVSQPCAKESQALGSPVFQLLVINPKTAQSVGVLLCSLPQGQAGRFLEGDVKDHVAAAVLTSGTIAIWDLLLGHCTALLPPVSDQSWSLVKWSGTDSHLLAGQKDGNIFIYRYF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
10PhosphorylationELSGKPLSYAEKEKL
CCCCCCCCHHHHHHH
30.7224719451
11PhosphorylationLSGKPLSYAEKEKLK
CCCCCCCHHHHHHHH
26.8524719451
127PhosphorylationIQGQLLHSTSSPDGK
CCCCEEEECCCCCCC
29.9226643407
128PhosphorylationQGQLLHSTSSPDGKK
CCCEEEECCCCCCCC
23.6028066266
129PhosphorylationGQLLHSTSSPDGKKE
CCEEEECCCCCCCCC
42.7726643407
130PhosphorylationQLLHSTSSPDGKKEQ
CEEEECCCCCCCCCC
27.3928066266
154PhosphorylationPWEKSSVSQEKEDYF
CCCCCCCCCCCHHHC
34.2722006019
186PhosphorylationISRKNSRTPVSEKTH
CCCCCCCCCCCCCHH
28.0625266776
274PhosphorylationITTQGPASSTNLVAQ
EECCCCCCCCCCEEC
40.61-
334PhosphorylationPNSKSLKSPSNTVDE
CCCCCCCCCCCCCCC
38.5627841257
364PhosphorylationNFNLAAVSPPSTESQ
CCCEEEECCCCCHHH
26.77-
432PhosphorylationATKAVVLSSEDTDQS
CCEEEEECCCCCCCC
21.77-
462PhosphorylationSLSQKLLSPAEVSSP
CHHHHHCCHHHCCCC
32.2826643407
467PhosphorylationLLSPAEVSSPPGPAG
HCCHHHCCCCCCCCC
28.7425266776
468PhosphorylationLSPAEVSSPPGPAGK
CCHHHCCCCCCCCCC
40.0525266776
559PhosphorylationCSEKLIESPDSKNCG
HHHHHHCCCCCCCHH
27.3226745281
562PhosphorylationKLIESPDSKNCGERL
HHHCCCCCCCHHCCC
29.2024719451
700PhosphorylationQCNSSACSPKPDTNL
CCCCCCCCCCCCCCC
35.3625266776
783PhosphorylationVSELKNPSSSCSVDV
HHHHCCCCCCCEEEE
44.25-
784PhosphorylationSELKNPSSSCSVDVS
HHHCCCCCCCEEEEH
36.30-
787PhosphorylationKNPSSSCSVDVSAMW
CCCCCCCEEEEHHHH
24.25-
881PhosphorylationEKQVLLKSGDIKAML
HHEEEEHHCCHHHHH
41.4922807455
892UbiquitinationKAMLGLTKRRLVSST
HHHHCCCHHHHHHCC
40.3322790023
993PhosphorylationGLLFVVVSQPCAKES
CEEEEEEECCCHHHH
19.4528285833
1078PhosphorylationPVSDQSWSLVKWSGT
CCCCCCEEEEEEECC
28.6522006019

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PALB2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PALB2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PALB2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRCA1_HUMANBRCA1physical
25016020
BRCA2_HUMANBRCA2physical
25016020
PALB2_MOUSEPalb2physical
25016020
KEAP1_HUMANKEAP1physical
25016020
MO4L1_HUMANMORF4L1physical
25016020
P53_MOUSETrp53genetic
23657012
CDN1A_MOUSECdkn1agenetic
23657012
TP53B_MOUSETrp53bp1genetic
23657012

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PALB2_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP