dbPTM

PALB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PALB2_HUMAN
UniProt AC	Q86YC2
Protein Name	Partner and localizer of BRCA2
Gene Name	PALB2
Organism	Homo sapiens (Human).
Sequence Length	1186
Subcellular Localization	Nucleus . Colocalizes with BRCA2 and BRCA1 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. [PubMed: 16793542]
Protein Sequence	MDEPPGKPLSCEEKEKLKEKLAFLKREYSKTLARLQRAQRAEKIKHSIKKTVEEQDCLSQQDLSPQLKHSEPKNKICVYDKLHIKTHLDEETGEKTSITLDVGPESFNPGDGPGGLPIQRTDDTQEHFPHRVSDPSGEQKQKLPSRRKKQQKRTFISQERDCVFGTDSLRLSGKRLKEQEEISSKNPARSPVTEIRTHLLSLKSELPDSPEPVTEINEDSVLIPPTAQPEKGVDTFLRRPNFTRATTVPLQTLSDSGSSQHLEHIPPKGSSELTTHDLKNIRFTSPVSLEAQGKKMTVSTDNLLVNKAISKSGQLPTSSNLEANISCSLNELTYNNLPANENQNLKEQNQTEKSLKSPSDTLDGRNENLQESEILSQPKSLSLEATSPLSAEKHSCTVPEGLLFPAEYYVRTTRSMSNCQRKVAVEAVIQSHLDVKKKGFKNKNKDASKNLNLSNEETDQSEIRMSGTCTGQPSSRTSQKLLSLTKVSSPAGPTEDNDLSRKAVAQAPGRRYTGKRKSACTPASDHCEPLLPTSSLSIVNRSKEEVTSHKYQHEKLFIQVKGKKSRHQKEDSLSWSNSAYLSLDDDAFTAPFHRDGMLSLKQLLSFLSITDFQLPDEDFGPLKLEKVKSCSEKPVEPFESKMFGERHLKEGSCIFPEELSPKRMDTEMEDLEEDLIVLPGKSHPKRPNSQSQHTKTGLSSSILLYTPLNTVAPDDNDRPTTDMCSPAFPILGTTPAFGPQGSYEKASTEVAGRTCCTPQLAHLKDSVCLASDTKQFDSSGSPAKPHTTLQVSGRQGQPTCDCDSVPPGTPPPIESFTFKENQLCRNTCQELHKHSVEQTETAELPASDSINPGNLQLVSELKNPSGSCSVDVSAMFWERAGCKEPCIITACEDVVSLWKALDAWQWEKLYTWHFAEVPVLQIVPVPDVYNLVCVALGNLEIREIRALFCSSDDESEKQVLLKSGNIKAVLGLTKRRLVSSSGTLSDQQVEVMTFAEDGGGKENQFLMPPEETILTFAEVQGMQEALLGTTIMNNIVIWNLKTGQLLKKMHIDDSYQASVCHKAYSEMGLLFIVLSHPCAKESESLRSPVFQLIVINPKTTLSVGVMLYCLPPGQAGRFLEGDVKDHCAAAILTSGTIAIWDLLLGQCTALLPPVSDQHWSFVKWSGTDSHLLAGQKDGNIFVYHYS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	EPPGKPLSCEEKEKL CCCCCCCCHHHHHHH	28.19	29083192
59	Phosphorylation	VEEQDCLSQQDLSPQ HHHHHHCCCCCCCHH	31.93	17525332
64	Phosphorylation	CLSQQDLSPQLKHSE HCCCCCCCHHHCCCC	20.91	17525332
70	Phosphorylation	LSPQLKHSEPKNKIC CCHHHCCCCCCCCEE	54.74	29978859
86	Phosphorylation	YDKLHIKTHLDEETG EEECEEEECCCCCCC	27.37	28857561
92	Phosphorylation	KTHLDEETGEKTSIT EECCCCCCCCCEEEE	48.90	28857561
96	Phosphorylation	DEETGEKTSITLDVG CCCCCCCEEEEEEEC	22.51	28857561
97	Phosphorylation	EETGEKTSITLDVGP CCCCCCEEEEEEECC	25.33	28857561
133	Phosphorylation	EHFPHRVSDPSGEQK HHCCCCCCCCCHHHH	43.70	30266825
136	Phosphorylation	PHRVSDPSGEQKQKL CCCCCCCCHHHHCCC	61.01	30266825
145	Phosphorylation	EQKQKLPSRRKKQQK HHHCCCCHHHHHHHH	55.97	24719451
154	Phosphorylation	RKKQQKRTFISQERD HHHHHHHHHHCCCCC	32.15	23312004
157	Phosphorylation	QQKRTFISQERDCVF HHHHHHHCCCCCCCC	23.07	17525332
166	Phosphorylation	ERDCVFGTDSLRLSG CCCCCCCCHHHHHCC	15.79	23186163
168	Phosphorylation	DCVFGTDSLRLSGKR CCCCCCHHHHHCCCH	18.41	30576142
172	Phosphorylation	GTDSLRLSGKRLKEQ CCHHHHHCCCHHHHH	35.52	30576142
183	Phosphorylation	LKEQEEISSKNPARS HHHHHHHHCCCCCCC	38.24	23312004
184	Phosphorylation	KEQEEISSKNPARSP HHHHHHHCCCCCCCC	41.96	23312004
190	Phosphorylation	SSKNPARSPVTEIRT HCCCCCCCCHHHHHH	26.31	25159151
193	Phosphorylation	NPARSPVTEIRTHLL CCCCCCHHHHHHHHH	29.13	23312004
201	Phosphorylation	EIRTHLLSLKSELPD HHHHHHHHHHCCCCC	39.86	24719451
204	Phosphorylation	THLLSLKSELPDSPE HHHHHHHCCCCCCCC	50.05	28111955
209	Phosphorylation	LKSELPDSPEPVTEI HHCCCCCCCCCCCCC	29.26	30108239
214	Phosphorylation	PDSPEPVTEINEDSV CCCCCCCCCCCCCCC	41.69	30108239
220	Phosphorylation	VTEINEDSVLIPPTA CCCCCCCCCCCCCCC	16.79	30576142
226	Phosphorylation	DSVLIPPTAQPEKGV CCCCCCCCCCCCCCC	32.35	28111955
243	O-linked_Glycosylation	FLRRPNFTRATTVPL HHCCCCCCCCEECEE	26.49	30059200
246	Phosphorylation	RPNFTRATTVPLQTL CCCCCCCEECEEEEE	25.65	-
247	Phosphorylation	PNFTRATTVPLQTLS CCCCCCEECEEEEEC	21.10	-
279	Ubiquitination	ELTTHDLKNIRFTSP CCCCCCCCCCEECCC	57.28	-
284	Phosphorylation	DLKNIRFTSPVSLEA CCCCCEECCCEEEEE	23.44	28450419
285	Phosphorylation	LKNIRFTSPVSLEAQ CCCCEECCCEEEEEC	22.16	25159151
288	Phosphorylation	IRFTSPVSLEAQGKK CEECCCEEEEECCCE	24.71	28450419
294	Acetylation	VSLEAQGKKMTVSTD EEEEECCCEEEEECC	27.56	7492053
295	Acetylation	SLEAQGKKMTVSTDN EEEECCCEEEEECCC	46.78	7492061
307	Acetylation	TDNLLVNKAISKSGQ CCCHHHHHHHHCCCC	39.35	7492071
312	Phosphorylation	VNKAISKSGQLPTSS HHHHHHCCCCCCCCC	25.61	-
319	Phosphorylation	SGQLPTSSNLEANIS CCCCCCCCCCCEEEE	48.16	-
326	Phosphorylation	SNLEANISCSLNELT CCCCEEEEEECCCCH	9.47	-
354	Phosphorylation	EQNQTEKSLKSPSDT HHHHHHHHHCCCCCC	34.49	26356563
357	Phosphorylation	QTEKSLKSPSDTLDG HHHHHHCCCCCCCCC	34.62	21815630
359	Phosphorylation	EKSLKSPSDTLDGRN HHHHCCCCCCCCCCC	50.77	26356563
361	Phosphorylation	SLKSPSDTLDGRNEN HHCCCCCCCCCCCCC	30.96	26356563
372	Phosphorylation	RNENLQESEILSQPK CCCCCCHHHHHHCCC	19.58	26074081
376	Phosphorylation	LQESEILSQPKSLSL CCHHHHHHCCCCCCC	50.53	17525332
379	Ubiquitination	SEILSQPKSLSLEAT HHHHHCCCCCCCEEC	57.29	-
380	Phosphorylation	EILSQPKSLSLEATS HHHHCCCCCCCEECC	29.85	25159151
382	Phosphorylation	LSQPKSLSLEATSPL HHCCCCCCCEECCCC	31.11	25159151
386	Phosphorylation	KSLSLEATSPLSAEK CCCCCEECCCCCCCC	22.85	30266825
387	Phosphorylation	SLSLEATSPLSAEKH CCCCEECCCCCCCCC	30.78	23401153
390	Phosphorylation	LEATSPLSAEKHSCT CEECCCCCCCCCCCC	37.45	29255136
395	Phosphorylation	PLSAEKHSCTVPEGL CCCCCCCCCCCCCCC	23.66	28122231
397	Phosphorylation	SAEKHSCTVPEGLLF CCCCCCCCCCCCCEE	41.95	28122231
454	Phosphorylation	ASKNLNLSNEETDQS HHHCCCCCCCCCCHH	40.91	25159151
458	Phosphorylation	LNLSNEETDQSEIRM CCCCCCCCCHHHEEC	32.91	30576142
466	Phosphorylation	DQSEIRMSGTCTGQP CHHHEECCCEECCCC	22.54	30576142
474	Phosphorylation	GTCTGQPSSRTSQKL CEECCCCCCHHHHHH	25.27	30576142
480	Acetylation	PSSRTSQKLLSLTKV CCCHHHHHHHHHEEE	51.68	25953088
483	Phosphorylation	RTSQKLLSLTKVSSP HHHHHHHHHEEECCC	44.42	24719451
488	Phosphorylation	LLSLTKVSSPAGPTE HHHHEEECCCCCCCC	31.96	21815630
489	Phosphorylation	LSLTKVSSPAGPTED HHHEEECCCCCCCCC	23.04	21815630
494	Phosphorylation	VSSPAGPTEDNDLSR ECCCCCCCCCCHHHH	55.86	29396449
502	Ubiquitination	EDNDLSRKAVAQAPG CCCHHHHHHHHCCCC	43.78	-
518	Phosphorylation	RYTGKRKSACTPASD CCCCCCCCCCCCCCC	32.39	25159151
533	Phosphorylation	HCEPLLPTSSLSIVN CCCCCCCCCCEEEEE	30.80	26074081
534	Phosphorylation	CEPLLPTSSLSIVNR CCCCCCCCCEEEEEC	27.60	26074081
535	Phosphorylation	EPLLPTSSLSIVNRS CCCCCCCCEEEEECC	28.72	26074081
537	Phosphorylation	LLPTSSLSIVNRSKE CCCCCCEEEEECCHH	26.83	26074081
542	Phosphorylation	SLSIVNRSKEEVTSH CEEEEECCHHHHHCC	38.93	26074081
547	Phosphorylation	NRSKEEVTSHKYQHE ECCHHHHHCCCCCCC	28.52	26074081
548	Phosphorylation	RSKEEVTSHKYQHEK CCHHHHHCCCCCCCE	24.13	26074081
551	Phosphorylation	EEVTSHKYQHEKLFI HHHHCCCCCCCEEEE	15.07	26074081
629	Phosphorylation	LKLEKVKSCSEKPVE CCHHHCCCCCCCCCC	26.34	28152594
631	Phosphorylation	LEKVKSCSEKPVEPF HHHCCCCCCCCCCCH	56.60	28152594
641	Ubiquitination	PVEPFESKMFGERHL CCCCHHHHHHCCCCC	30.93	-
652	Phosphorylation	ERHLKEGSCIFPEEL CCCCCCCCEECCHHH	12.72	23927012
660	Phosphorylation	CIFPEELSPKRMDTE EECCHHHCCCCCCCC	31.49	19664994
747	Phosphorylation	QGSYEKASTEVAGRT CCCCCCCCHHCCCCC	35.85	24532841
757	Phosphorylation	VAGRTCCTPQLAHLK CCCCCCCCHHHHHCC	19.06	25159151
778	Phosphorylation	SDTKQFDSSGSPAKP CCCCCCCCCCCCCCC	37.58	30266825
779	Phosphorylation	DTKQFDSSGSPAKPH CCCCCCCCCCCCCCC	45.17	30266825
781	Phosphorylation	KQFDSSGSPAKPHTT CCCCCCCCCCCCCCE	24.51	23401153
787	Phosphorylation	GSPAKPHTTLQVSGR CCCCCCCCEEEECCC	37.42	30108239
788	Phosphorylation	SPAKPHTTLQVSGRQ CCCCCCCEEEECCCC	16.50	30108239
792	Phosphorylation	PHTTLQVSGRQGQPT CCCEEEECCCCCCCC	18.46	25159151
799	Phosphorylation	SGRQGQPTCDCDSVP CCCCCCCCCCCCCCC	17.06	28111955
804	Phosphorylation	QPTCDCDSVPPGTPP CCCCCCCCCCCCCCC	42.74	28111955
809	Phosphorylation	CDSVPPGTPPPIESF CCCCCCCCCCCCHHC	38.09	28111955
815	Phosphorylation	GTPPPIESFTFKENQ CCCCCCHHCCCCCCH	30.24	28111955
817	Phosphorylation	PPPIESFTFKENQLC CCCCHHCCCCCCHHH	42.97	28111955
993	Phosphorylation	DQQVEVMTFAEDGGG CCEEEEEEEEECCCC	25.52	29759185
1055	Phosphorylation	KMHIDDSYQASVCHK HCCCCCCHHHHHHHH	18.32	-
1165	Phosphorylation	HWSFVKWSGTDSHLL CCEEEEEECCCCEEE	26.54	21712546
1167	Phosphorylation	SFVKWSGTDSHLLAG EEEEEECCCCEEECC	28.90	21712546
1169	Phosphorylation	VKWSGTDSHLLAGQK EEEECCCCEEECCCC	18.84	26471730

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
-	K	Ubiquitination	E3 ubiquitin ligase	KEAP1	Q14145	PMID:26649820

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PALB2_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAD51_HUMAN	RAD51	physical	20871616
R51A1_HUMAN	RAD51AP1	physical	20871616
MO4L1_HUMAN	MORF4L1	physical	20332121
BRCA2_HUMAN	BRCA2	physical	20332121
RAD51_HUMAN	RAD51	physical	20332121
BRCA1_HUMAN	BRCA1	physical	19584259
BRCA2_HUMAN	BRCA2	physical	19584259
RAD51_HUMAN	RAD51	physical	19584259
BRCA2_HUMAN	BRCA2	physical	19553677
BRCA1_HUMAN	BRCA1	physical	19553677
MO4L1_HUMAN	MORF4L1	physical	19553677
MO4L2_HUMAN	MORF4L2	physical	19553677
BRCA2_HUMAN	BRCA2	physical	19268590
BRCA1_HUMAN	BRCA1	physical	19268590
BRCA2_HUMAN	BRCA2	physical	17200672
RAD51_HUMAN	RAD51	physical	16793542
BRCA2_HUMAN	BRCA2	physical	16793542
BRCA2_HUMAN	BRCA2	physical	19369211
BRCA1_HUMAN	BRCA1	physical	19369211
CTIP_HUMAN	RBBP8	physical	19369211
BACH1_HUMAN	BACH1	physical	19369211
PALB2_HUMAN	PALB2	physical	23038782
BRCA1_HUMAN	BRCA1	physical	23038782
BRCA2_HUMAN	BRCA2	physical	23038782
BRCA2_HUMAN	BRCA2	physical	19609323
BRCA1_HUMAN	BRCA1	physical	23585894
BRCA2_HUMAN	BRCA2	physical	23585894
RAD51_HUMAN	RAD51	physical	23585894
MO4L1_HUMAN	MORF4L1	physical	23585894
HNRPC_HUMAN	HNRNPC	physical	23585894
POLH_HUMAN	POLH	physical	24485656
BRCA1_HUMAN	BRCA1	physical	22193777
BRCA2_HUMAN	BRCA2	physical	22193777
RAD51_HUMAN	RAD51	physical	22193777
MO4L1_HUMAN	MORF4L1	physical	22193777
H31_HUMAN	HIST1H3A	physical	22193777
H2B2E_HUMAN	HIST2H2BE	physical	22193777
BCAS3_HUMAN	BCAS3	physical	25640309
CASZ1_HUMAN	CASZ1	physical	25640309
CCL5_HUMAN	CCL5	physical	25640309
CYTM_HUMAN	CST6	physical	25640309
DIRA3_HUMAN	DIRAS3	physical	25640309
ERRFI_HUMAN	ERRFI1	physical	25640309
FA84B_HUMAN	FAM84B	physical	25640309
GREB1_HUMAN	GREB1	physical	25640309
I13R2_HUMAN	IL13RA2	physical	25640309
IL24_HUMAN	IL24	physical	25640309
KLK6_HUMAN	KLK6	physical	25640309
LYPD3_HUMAN	LYPD3	physical	25640309
MRC2_HUMAN	MRC2	physical	25640309
ARY2_HUMAN	NAT2	physical	25640309
PRD14_HUMAN	PRDM14	physical	25640309
RHBT2_HUMAN	RHOBTB2	physical	25640309
SPB5_HUMAN	SERPINB5	physical	25640309
SNAI1_HUMAN	SNAI1	physical	25640309
THRSP_HUMAN	THRSP	physical	25640309
BRCA1_HUMAN	BRCA1	physical	26649820
BRCA2_HUMAN	BRCA2	physical	26649820
CUL3_HUMAN	CUL3	physical	26649820
KEAP1_HUMAN	KEAP1	physical	26649820
UBP11_HUMAN	USP11	physical	26649820
ERCC5_HUMAN	ERCC5	physical	26833090
BRCA2_HUMAN	BRCA2	physical	26833090
RAD51_HUMAN	RAD51	physical	26833090
PALB2_HUMAN	PALB2	physical	25016020
RAD51_HUMAN	RAD51	physical	25016020
BRCA2_HUMAN	BRCA2	physical	25016020
BRCA1_HUMAN	BRCA1	physical	25016020
KEAP1_HUMAN	KEAP1	physical	25016020
MO4L1_HUMAN	MORF4L1	physical	25016020
BRCA2_HUMAN	BRCA2	physical	26990772
RA51C_HUMAN	RAD51C	physical	24141787
BRCA2_HUMAN	BRCA2	physical	24141787
RAD51_HUMAN	RAD51	physical	24141787
XRCC3_HUMAN	XRCC3	physical	24141787
BRCA1_HUMAN	BRCA1	physical	22331464
BRCA2_HUMAN	BRCA2	physical	22331464
PALB2_HUMAN	PALB2	physical	22331464
KEAP1_HUMAN	KEAP1	physical	22331464
MO4L1_HUMAN	MORF4L1	physical	22331464
RAD51_HUMAN	RAD51	physical	22331464
RN168_HUMAN	RNF168	physical	28240985
RAD51_HUMAN	RAD51	physical	28240985
BRCA2_HUMAN	BRCA2	physical	28240985

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
114480	Breast cancer (BC)
610832	Fanconi anemia complementation group N (FANCN)
613348	Pancreatic cancer 3 (PNCA3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PALB2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387 AND SER-660, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-64; SER-157 ANDSER-376, AND MASS SPECTROMETRY.	17525332 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660, AND MASSSPECTROMETRY.	15302935 [Abstract]