dbPTM

FACD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FACD2_HUMAN
UniProt AC	Q9BXW9
Protein Name	Fanconi anemia group D2 protein
Gene Name	FANCD2
Organism	Homo sapiens (Human).
Sequence Length	1451
Subcellular Localization	Nucleus . Concentrates in nuclear foci during S phase and upon genotoxic stress. At the onset of mitosis, excluded from chromosomes and diffuses into the cytoplasm, returning to the nucleus at the end of cell division. Observed in a few spots localiz
Protein Description	Required for maintenance of chromosomal stability. Promotes accurate and efficient pairing of homologs during meiosis. Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing. May participate in S phase and G2 phase checkpoint activation upon DNA damage. Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress. Required for the targeting, or stabilization, of BLM to non-centromeric abnormal structures induced by replicative stress. Promotes BRCA2/FANCD1 loading onto damaged chromatin. May also be involved in B-cell immunoglobulin isotype switching..
Protein Sequence	MVSKRRLSKSEDKESLTEDASKTRKQPLSKKTKKSHIANEVEENDSIFVKLLKISGIILKTGESQNQLAVDQIAFQKKLFQTLRRHPSYPKIIEEFVSGLESYIEDEDSFRNCLLSCERLQDEEASMGASYSKSLIKLLLGIDILQPAIIKTLFEKLPEYFFENKNSDEINIPRLIVSQLKWLDRVVDGKDLTTKIMQLISIAPENLQHDIITSLPEILGDSQHADVGKELSDLLIENTSLTVPILDVLSSLRLDPNFLLKVRQLVMDKLSSIRLEDLPVIIKFILHSVTAMDTLEVISELREKLDLQHCVLPSRLQASQVKLKSKGRASSSGNQESSGQSCIILLFDVIKSAIRYEKTISEAWIKAIENTASVSEHKVFDLVMLFIIYSTNTQTKKYIDRVLRNKIRSGCIQEQLLQSTFSVHYLVLKDMCSSILSLAQSLLHSLDQSIISFGSLLYKYAFKFFDTYCQQEVVGALVTHICSGNEAEVDTALDVLLELVVLNPSAMMMNAVFVKGILDYLDNISPQQIRKLFYVLSTLAFSKQNEASSHIQDDMHLVIRKQLSSTVFKYKLIGIIGAVTMAGIMAADRSESPSLTQERANLSDEQCTQVTSLLQLVHSCSEQSPQASALYYDEFANLIQHEKLDPKALEWVGHTICNDFQDAFVVDSCVVPEGDFPFPVKALYGLEEYDTQDGIAINLLPLLFSQDFAKDGGPVTSQESGQKLVSPLCLAPYFRLLRLCVERQHNGNLEEIDGLLDCPIFLTDLEPGEKLESMSAKERSFMCSLIFLTLNWFREIVNAFCQETSPEMKGKVLTRLKHIVELQIILEKYLAVTPDYVPPLGNFDVETLDITPHTVTAISAKIRKKGKIERKQKTDGSKTSSSDTLSEEKNSECDPTPSHRGQLNKEFTGKEEKTSLLLHNSHAFFRELDIEVFSILHCGLVTKFILDTEMHTEATEVVQLGPPELLFLLEDLSQKLESMLTPPIARRVPFLKNKGSRNIGFSHLQQRSAQEIVHCVFQLLTPMCNHLENIHNYFQCLAAENHGVVDGPGVKVQEYHIMSSCYQRLLQIFHGLFAWSGFSQPENQNLLYSALHVLSSRLKQGEHSQPLEELLSQSVHYLQNFHQSIPSFQCALYLIRLLMVILEKSTASAQNKEKIASLARQFLCRVWPSGDKEKSNISNDQLHALLCIYLEHTESILKAIEEIAGVGVPELINSPKDASSSTFPTLTRHTFVVFFRVMMAELEKTVKKIEPGTAADSQQIHEEKLLYWNMAVRDFSILINLIKVFDSHPVLHVCLKYGRLFVEAFLKQCMPLLDFSFRKHREDVLSLLETFQLDTRLLHHLCGHSKIHQDTRLTQHVPLLKKTLELLVCRVKAMLTLNNCREAFWLGNLKNRDLQGEEIKSQNSQESTADESEDDMSSQASKSKATEDGEEDEVSAGEKEQDSDESYDDSD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MVSKRRLSKSEDKES CCCCCCCCCCCCHHH	32.12	29255136
10	Phosphorylation	SKRRLSKSEDKESLT CCCCCCCCCCHHHHC	47.88	29255136
15	Phosphorylation	SKSEDKESLTEDASK CCCCCHHHHCHHHHH	46.46	29255136
17	Phosphorylation	SEDKESLTEDASKTR CCCHHHHCHHHHHHH	40.89	26074081
21	Phosphorylation	ESLTEDASKTRKQPL HHHCHHHHHHHCCCC	47.05	30576142
22	Acetylation	SLTEDASKTRKQPLS HHCHHHHHHHCCCCC	54.81	25953088
23	Phosphorylation	LTEDASKTRKQPLSK HCHHHHHHHCCCCCH	40.37	30576142
29	Phosphorylation	KTRKQPLSKKTKKSH HHHCCCCCHHHCHHH	38.50	18785766
30	Ubiquitination	TRKQPLSKKTKKSHI HHCCCCCHHHCHHHH	72.62	22817900
31	Ubiquitination	RKQPLSKKTKKSHIA HCCCCCHHHCHHHHC	63.30	22817900
32	Phosphorylation	KQPLSKKTKKSHIAN CCCCCHHHCHHHHCC	47.65	18785766
33	Ubiquitination	QPLSKKTKKSHIANE CCCCHHHCHHHHCCC	62.25	22817900
33 (in isoform 1)	Ubiquitination	-	62.25	21890473
33 (in isoform 2)	Ubiquitination	-	62.25	21890473
33 (in isoform 3)	Ubiquitination	-	62.25	21890473
33 (in isoform 4)	Ubiquitination	-	62.25	21890473
34	Ubiquitination	PLSKKTKKSHIANEV CCCHHHCHHHHCCCC	53.12	22817900
34 (in isoform 1)	Ubiquitination	-	53.12	21890473
34 (in isoform 2)	Ubiquitination	-	53.12	21890473
34 (in isoform 3)	Ubiquitination	-	53.12	21890473
34 (in isoform 4)	Ubiquitination	-	53.12	21890473
35	Phosphorylation	LSKKTKKSHIANEVE CCHHHCHHHHCCCCC	22.98	28555341
50	Ubiquitination	ENDSIFVKLLKISGI CCCHHHHHHHHHCEE	37.04	29967540
53	Ubiquitination	SIFVKLLKISGIILK HHHHHHHHHCEEEEE	45.31	33845483
60	Ubiquitination	KISGIILKTGESQNQ HHCEEEEECCCCCCH	44.04	29967540
77	Ubiquitination	VDQIAFQKKLFQTLR HHHHHHHHHHHHHHH	45.02	21906983
77 (in isoform 1)	Ubiquitination	-	45.02	21890473
77 (in isoform 2)	Ubiquitination	-	45.02	21890473
77 (in isoform 3)	Ubiquitination	-	45.02	21890473
77 (in isoform 4)	Ubiquitination	-	45.02	21890473
78	Ubiquitination	DQIAFQKKLFQTLRR HHHHHHHHHHHHHHH	43.69	22817900
88	Phosphorylation	QTLRRHPSYPKIIEE HHHHHCCCCHHHHHH	48.19	24719451
126	Phosphorylation	RLQDEEASMGASYSK HHCCHHHHCCCCCHH	22.49	21815630
133	Ubiquitination	SMGASYSKSLIKLLL HCCCCCHHHHHHHHH	40.84	20603016
133 (in isoform 1)	Ubiquitination	-	40.84	21890473
133 (in isoform 2)	Ubiquitination	-	40.84	21890473
133 (in isoform 3)	Ubiquitination	-	40.84	21890473
133 (in isoform 4)	Ubiquitination	-	40.84	21890473
134	Phosphorylation	MGASYSKSLIKLLLG CCCCCHHHHHHHHHC	29.41	24719451
137	Ubiquitination	SYSKSLIKLLLGIDI CCHHHHHHHHHCHHH	38.07	22817900
151	Ubiquitination	ILQPAIIKTLFEKLP HHHHHHHHHHHHHCH	32.82	22817900
156	Ubiquitination	IIKTLFEKLPEYFFE HHHHHHHHCHHHHHC	63.11	21906983
156 (in isoform 1)	Ubiquitination	-	63.11	21890473
156 (in isoform 2)	Ubiquitination	-	63.11	21890473
156 (in isoform 3)	Ubiquitination	-	63.11	21890473
156 (in isoform 4)	Ubiquitination	-	63.11	21890473
165	Ubiquitination	PEYFFENKNSDEINI HHHHHCCCCCCCCCC	51.10	21906983
165 (in isoform 1)	Ubiquitination	-	51.10	21890473
165 (in isoform 2)	Ubiquitination	-	51.10	21890473
165 (in isoform 3)	Ubiquitination	-	51.10	21890473
165 (in isoform 4)	Ubiquitination	-	51.10	21890473
167	Phosphorylation	YFFENKNSDEINIPR HHHCCCCCCCCCCCH	37.92	17525332
178	Phosphorylation	NIPRLIVSQLKWLDR CCCHHHHHHHHHHHH	23.85	17525332
181	Ubiquitination	RLIVSQLKWLDRVVD HHHHHHHHHHHHHCC	37.77	21890473
181 (in isoform 1)	Ubiquitination	-	37.77	21890473
181 (in isoform 2)	Ubiquitination	-	37.77	21890473
181 (in isoform 3)	Ubiquitination	-	37.77	21890473
181 (in isoform 4)	Ubiquitination	-	37.77	21890473
190	2-Hydroxyisobutyrylation	LDRVVDGKDLTTKIM HHHHCCCCCHHHHHH	45.13	-
190	Ubiquitination	LDRVVDGKDLTTKIM HHHHCCCCCHHHHHH	45.13	27667366
201	Phosphorylation	TKIMQLISIAPENLQ HHHHHHHHHCCHHCC	22.69	-
222	Phosphorylation	LPEILGDSQHADVGK HHHHHCCCCCCCHHH	23.28	25159151
250	Phosphorylation	VPILDVLSSLRLDPN CCHHHHHHHCCCCHH	27.46	30301811
251	Phosphorylation	PILDVLSSLRLDPNF CHHHHHHHCCCCHHH	17.22	25954137
261	Ubiquitination	LDPNFLLKVRQLVMD CCHHHHHHHHHHHHH	37.20	23000965
261 (in isoform 1)	Ubiquitination	-	37.20	21890473
261 (in isoform 2)	Ubiquitination	-	37.20	21890473
261 (in isoform 3)	Ubiquitination	-	37.20	21890473
271	Phosphorylation	QLVMDKLSSIRLEDL HHHHHHHHCCCHHHH	29.47	30301811
272	Phosphorylation	LVMDKLSSIRLEDLP HHHHHHHCCCHHHHH	23.36	25954137
299	Phosphorylation	MDTLEVISELREKLD HHHHHHHHHHHHHCC	35.44	24719451
319	Phosphorylation	LPSRLQASQVKLKSK CCHHHCHHHEEECCC	23.65	30266825
322	Ubiquitination	RLQASQVKLKSKGRA HHCHHHEEECCCCCC	42.43	22505724
330	Phosphorylation	LKSKGRASSSGNQES ECCCCCCCCCCCCCC	24.55	18691976
331	Phosphorylation	KSKGRASSSGNQESS CCCCCCCCCCCCCCC	41.08	22817900
332	Phosphorylation	SKGRASSSGNQESSG CCCCCCCCCCCCCCC	38.99	28122231
337	Phosphorylation	SSSGNQESSGQSCII CCCCCCCCCCCCEEH	29.97	28122231
338	Phosphorylation	SSGNQESSGQSCIIL CCCCCCCCCCCEEHH	39.85	29496963
341	Phosphorylation	NQESSGQSCIILLFD CCCCCCCCEEHHHHH	15.71	28122231
358	Ubiquitination	KSAIRYEKTISEAWI HHHHHHCCCCCHHHH	42.07	29967540
366	Ubiquitination	TISEAWIKAIENTAS CCCHHHHHHHHHCCC	32.39	29967540
389	Phosphorylation	LVMLFIIYSTNTQTK HEEEHHHHCCCCCCH	12.48	22817900
458	Phosphorylation	ISFGSLLYKYAFKFF HHHHHHHHHHHHHHH	13.77	-
524	Neddylation	ILDYLDNISPQQIRK HHHHHHCCCHHHHHH	6.75	32015554
524	Ubiquitination	ILDYLDNISPQQIRK HHHHHHCCCHHHHHH	6.75	29901268
561	Neddylation	DMHLVIRKQLSSTVF CHHHHHHHHHHHHHH	44.46	32015554
561	Ubiquitination	DMHLVIRKQLSSTVF CHHHHHHHHHHHHHH	44.46	23000965
561 (in isoform 1)	Ubiquitination	-	44.46	21890473
561 (in isoform 2)	Ubiquitination	-	44.46	21890473
561 (in isoform 3)	Ubiquitination	-	44.46	21890473
569	Ubiquitination	QLSSTVFKYKLIGII HHHHHHHHHHHHHHH	36.82	25015289
590	Phosphorylation	GIMAADRSESPSLTQ HHHHCCCCCCCCCCH	42.87	22167270
592	Phosphorylation	MAADRSESPSLTQER HHCCCCCCCCCCHHH	22.49	19664994
594	Phosphorylation	ADRSESPSLTQERAN CCCCCCCCCCHHHHC	54.02	30266825
596	Phosphorylation	RSESPSLTQERANLS CCCCCCCCHHHHCCC	32.49	17525332
608	Phosphorylation	NLSDEQCTQVTSLLQ CCCHHHHHHHHHHHH	26.26	22817900
684	Phosphorylation	PFPVKALYGLEEYDT CCCHHHHHCCCCCCC	25.23	17053785
689	Phosphorylation	ALYGLEEYDTQDGIA HHHCCCCCCCCCCEE	18.21	29523821
691	Phosphorylation	YGLEEYDTQDGIAIN HCCCCCCCCCCEEHH	27.88	28464451
716	Phosphorylation	AKDGGPVTSQESGQK HHCCCCCCCHHHCCC	28.03	25850435
717	Phosphorylation	KDGGPVTSQESGQKL HCCCCCCCHHHCCCC	31.98	17525332
720	Phosphorylation	GPVTSQESGQKLVSP CCCCCHHHCCCCCHH	38.60	25850435
723	Ubiquitination	TSQESGQKLVSPLCL CCHHHCCCCCHHHHH	55.15	21963094
777	Ubiquitination	KLESMSAKERSFMCS HHHCCCHHHHHHHHH	46.48	-
784	Phosphorylation	KERSFMCSLIFLTLN HHHHHHHHHHHHHHH	16.83	30387612
789	Phosphorylation	MCSLIFLTLNWFREI HHHHHHHHHHHHHHH	13.80	30387612
841	Ubiquitination	PDYVPPLGNFDVETL CCCCCCCCCCCCEEC	38.23	33845483
868	Ubiquitination	KIRKKGKIERKQKTD HHHHCCCCCEEECCC	9.38	33845483
873	Ubiquitination	GKIERKQKTDGSKTS CCCCEEECCCCCCCC	52.17	22817900
878	Ubiquitination	KQKTDGSKTSSSDTL EECCCCCCCCCCCCC	58.94	33845483
878 (in isoform 1)	Ubiquitination	-	58.94	21890473
878 (in isoform 2)	Ubiquitination	-	58.94	21890473
878 (in isoform 3)	Ubiquitination	-	58.94	21890473
879	Phosphorylation	QKTDGSKTSSSDTLS ECCCCCCCCCCCCCC	35.22	23186163
880	Phosphorylation	KTDGSKTSSSDTLSE CCCCCCCCCCCCCCH	31.42	23186163
881	Phosphorylation	TDGSKTSSSDTLSEE CCCCCCCCCCCCCHH	37.15	23186163
882	Phosphorylation	DGSKTSSSDTLSEEK CCCCCCCCCCCCHHH	34.09	21815630
884	Phosphorylation	SKTSSSDTLSEEKNS CCCCCCCCCCHHHCC	33.85	23401153
886	Phosphorylation	TSSSDTLSEEKNSEC CCCCCCCCHHHCCCC	45.89	23401153
889	Acetylation	SDTLSEEKNSECDPT CCCCCHHHCCCCCCC	62.82	26051181
889	Ubiquitination	SDTLSEEKNSECDPT CCCCCHHHCCCCCCC	62.82	21963094
891	Phosphorylation	TLSEEKNSECDPTPS CCCHHHCCCCCCCCC	51.15	25849741
896	Phosphorylation	KNSECDPTPSHRGQL HCCCCCCCCCCCCCC	24.95	30576142
898	Phosphorylation	SECDPTPSHRGQLNK CCCCCCCCCCCCCCC	28.44	23186163
905	Ubiquitination	SHRGQLNKEFTGKEE CCCCCCCCCCCCCHH	63.90	33845483
910	Ubiquitination	LNKEFTGKEEKTSLL CCCCCCCCHHHHEEE	60.69	22817900
913	Ubiquitination	EFTGKEEKTSLLLHN CCCCCHHHHEEEEEC	44.50	21890473
913 (in isoform 1)	Ubiquitination	-	44.50	21890473
913 (in isoform 2)	Ubiquitination	-	44.50	21890473
913 (in isoform 3)	Ubiquitination	-	44.50	21890473
978	Phosphorylation	DLSQKLESMLTPPIA HHHHHHHHHCCCCHH	29.54	-
981	Phosphorylation	QKLESMLTPPIARRV HHHHHHCCCCHHHCC	20.55	-
992	Ubiquitination	ARRVPFLKNKGSRNI HHCCCCCCCCCCCCC	57.92	29967540
1059	Phosphorylation	VQEYHIMSSCYQRLL HHHHHHHHHHHHHHH	19.36	25627689
1060	Phosphorylation	QEYHIMSSCYQRLLQ HHHHHHHHHHHHHHH	10.24	25627689
1096	Phosphorylation	SALHVLSSRLKQGEH HHHHHHHHHHHCCCC	37.15	24719451
1154	Ubiquitination	ASAQNKEKIASLARQ CCCCCHHHHHHHHHH	45.22	29967540
1172	Acetylation	RVWPSGDKEKSNISN HHCCCCCHHHCCCCH	71.25	19829121
1195	Phosphorylation	IYLEHTESILKAIEE HHHHCHHHHHHHHHH	34.08	24719451
1198	Acetylation	EHTESILKAIEEIAG HCHHHHHHHHHHHHC	45.72	18530725
1214	Phosphorylation	GVPELINSPKDASSS CHHHHHCCCCCCCCC	26.74	28122231
1216	Ubiquitination	PELINSPKDASSSTF HHHHCCCCCCCCCCC	66.79	21906983
1216 (in isoform 1)	Ubiquitination	-	66.79	21890473
1216 (in isoform 2)	Ubiquitination	-	66.79	21890473
1216 (in isoform 3)	Ubiquitination	-	66.79	21890473
1234 (in isoform 3)	Phosphorylation	-	2.45	26552605
1235 (in isoform 3)	Phosphorylation	-	3.78	26552605
1236 (in isoform 3)	Phosphorylation	-	12.17	26552605
1238 (in isoform 3)	Phosphorylation	-	1.51	26552605
1243 (in isoform 3)	Phosphorylation	-	37.88	26552605
1244 (in isoform 3)	Phosphorylation	-	71.84	26552605
1246 (in isoform 3)	Phosphorylation	-	9.83	26552605
1247 (in isoform 3)	Phosphorylation	-	53.95	26552605
1248	Ubiquitination	ELEKTVKKIEPGTAA HHHHHHHHCCCCCCC	48.22	29967540
1248 (in isoform 3)	Phosphorylation	-	48.22	26552605
1249 (in isoform 3)	Phosphorylation	-	6.82	26552605
1253	Phosphorylation	VKKIEPGTAADSQQI HHHCCCCCCCCHHHH	29.41	20068231
1257	Phosphorylation	EPGTAADSQQIHEEK CCCCCCCHHHHHHHH	21.18	25159151
1316	Phosphorylation	CMPLLDFSFRKHRED HHHHHCCCCHHHHHH	24.65	24719451
1346	Ubiquitination	HHLCGHSKIHQDTRL HHHHCCCHHCCCCCH	38.23	29967540
1361	Acetylation	TQHVPLLKKTLELLV HHHHHHHHHHHHHHH	51.93	25953088
1361	Ubiquitination	TQHVPLLKKTLELLV HHHHHHHHHHHHHHH	51.93	29967540
1362	Ubiquitination	QHVPLLKKTLELLVC HHHHHHHHHHHHHHH	59.31	-
1363	Phosphorylation	HVPLLKKTLELLVCR HHHHHHHHHHHHHHH	24.71	-
1372	Ubiquitination	ELLVCRVKAMLTLNN HHHHHHHHHHHHHCC	14.55	-
1390	Ubiquitination	AFWLGNLKNRDLQGE HHHHCCCCCCCCCCH	54.67	21963094
1390 (in isoform 1)	Ubiquitination	-	54.67	21890473
1390 (in isoform 2)	Ubiquitination	-	54.67	21890473
1400	Ubiquitination	DLQGEEIKSQNSQES CCCCHHCCCCCCCCC	49.63	23503661
1400 (in isoform 2)	Ubiquitination	-	49.63	-
1401	Phosphorylation	LQGEEIKSQNSQEST CCCHHCCCCCCCCCC	40.01	23403867
1404	Phosphorylation	EEIKSQNSQESTADE HHCCCCCCCCCCCCC	27.91	28176443
1407	Phosphorylation	KSQNSQESTADESED CCCCCCCCCCCCCHH	22.66	28176443
1408	Phosphorylation	SQNSQESTADESEDD CCCCCCCCCCCCHHH	37.06	28176443
1412	Phosphorylation	QESTADESEDDMSSQ CCCCCCCCHHHHHHH	47.04	19664994
1417	Phosphorylation	DESEDDMSSQASKSK CCCHHHHHHHHHHHC	26.71	28176443
1418	Phosphorylation	ESEDDMSSQASKSKA CCHHHHHHHHHHHCC	24.11	17525332
1418 (in isoform 1)	Phosphorylation	-	24.11	17525332
1421	Phosphorylation	DDMSSQASKSKATED HHHHHHHHHHCCCCC	29.80	23403867
1422	Ubiquitination	DMSSQASKSKATEDG HHHHHHHHHCCCCCC	60.02	-
1423	Phosphorylation	MSSQASKSKATEDGE HHHHHHHHCCCCCCC	25.65	30576142
1426	Phosphorylation	QASKSKATEDGEEDE HHHHHCCCCCCCCCC	40.43	25159151
1435	Phosphorylation	DGEEDEVSAGEKEQD CCCCCCCCCCCCCCC	64.16	29255136
1443	Phosphorylation	AGEKEQDSDESYDDS CCCCCCCCCCCCCCC	2.88	25137130
1446	Phosphorylation	KEQDSDESYDDSD-- CCCCCCCCCCCCC--	3.32	25137130
1447	Phosphorylation	EQDSDESYDDSD--- CCCCCCCCCCCC---	2.55	24144214
1450	Phosphorylation	SDESYDDSD------ CCCCCCCCC------	3.73	25137130

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
222	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
331	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
596	T	Phosphorylation	Kinase	ATR	Q13535	PSP
608	T	Phosphorylation	Kinase	ATR	Q13535	PSP
691	T	Phosphorylation	Kinase	ATM	Q13315	PSP
691	T	Phosphorylation	Kinase	ATR	Q13535	PSP
717	S	Phosphorylation	Kinase	ATM	Q13315	PSP
717	S	Phosphorylation	Kinase	ATR	Q13535	PSP
1257	S	Phosphorylation	Kinase	ATM	Q13315	PhosphoELM
1401	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
1404	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
1418	S	Phosphorylation	Kinase	ATM	Q13315	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	BRCA1	P38398	PMID:12887909
-	K	Ubiquitination	E3 ubiquitin ligase	FANCL	Q9NW38	PMID:12973351
-	K	Ubiquitination	E3 ubiquitin ligase	RAD18	Q9NS91	PMID:20675655

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
222	S	Phosphorylation	12086603
Phosphorylation on Ser-222 is required for S-phase checkpoint activation, but not for ubiquitination, foci formation, or DNA repair.
222	S	Phosphorylation	12086603
Ubiquitination is required for binding to chromatin, interaction with BRCA1, BRCA2 and MTMR15/FAN1, DNA repair, and normal cell cycle progression, but not for phosphorylation on Ser-222 or interaction with MEN1.
222	S	Phosphorylation	12086603
Upon ionizing radiation, phosphorylated by ATM on Ser-222 and Ser-1404.
222	S	ubiquitylation	12086603
Phosphorylation on Ser-222 is required for S-phase checkpoint activation, but not for ubiquitination, foci formation, or DNA repair.
222	S	ubiquitylation	12086603
Ubiquitination is required for binding to chromatin, interaction with BRCA1, BRCA2 and MTMR15/FAN1, DNA repair, and normal cell cycle progression, but not for phosphorylation on Ser-222 or interaction with MEN1.
561	K	ubiquitylation	11239454
Monoubiquitinated on Lys-561 during S phase and upon genotoxic stress by FANCL in complex with E2 ligases UBE2T or UBE2W (isoform 1 and isoform 2).
1404	S	Phosphorylation	12086603
Upon ionizing radiation, phosphorylated by ATM on Ser-222 and Ser-1404.

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 FACD2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BLM_HUMAN	BLM	physical	15257300
BRCA2_HUMAN	BRCA2	physical	15199141
NBN_HUMAN	NBN	physical	12447395
ATM_HUMAN	ATM	physical	14499622
BRCA1_HUMAN	BRCA1	physical	14499622
FANCE_HUMAN	FANCE	physical	15115758
FANCE_HUMAN	FANCE	physical	12649160
FANCE_HUMAN	FANCE	physical	12093742
KAT5_HUMAN	KAT5	physical	18263878
BRCA2_HUMAN	BRCA2	physical	18263878
RAD18_HUMAN	RAD18	physical	21355096
TNKS1_HUMAN	TNKS	physical	21314979
TERF1_HUMAN	TERF1	physical	21314979
DPOLN_HUMAN	POLN	physical	20967207
CEBPD_HUMAN	CEBPD	physical	20805509
FAN1_HUMAN	FAN1	physical	20603073
FAN1_HUMAN	FAN1	physical	20603016
FAN1_HUMAN	FAN1	physical	20603015
BRCA2_HUMAN	BRCA2	physical	20450923
FOXO3_HUMAN	FOXO3	physical	20040763
H2AX_HUMAN	H2AFX	physical	17304220
PCNA_HUMAN	PCNA	physical	19704162
TERF1_HUMAN	TERF1	physical	19129235
DCR1B_HUMAN	DCLRE1B	physical	18469862
BRCA2_HUMAN	BRCA2	physical	18212739
FANCG_HUMAN	FANCG	physical	18212739
FANCC_HUMAN	FANCC	physical	16127171
FANCE_HUMAN	FANCE	physical	16127171
BRCA1_HUMAN	BRCA1	physical	11239454
MSH2_HUMAN	MSH2	physical	21865299
MLH1_HUMAN	MLH1	physical	21865299
FANCI_HUMAN	FANCI	physical	22855611
FANCL_HUMAN	FANCL	physical	21775430
POLH_HUMAN	POLH	physical	23388460
DYN1_HUMAN	DNM1	physical	22863883
I2BPL_HUMAN	IRF2BPL	physical	22863883
FANCE_HUMAN	FANCE	physical	24451376
FANCI_HUMAN	FANCI	physical	24451376
FAN1_HUMAN	FAN1	physical	25135477
FZR1_HUMAN	FZR1	physical	22854063
RAD18_HUMAN	RAD18	physical	25893307
RAD51_HUMAN	RAD51	physical	25893307
PCNA_HUMAN	PCNA	physical	25893307
REV1_HUMAN	REV1	physical	26187992
FANCE_HUMAN	FANCE	physical	26277624
BRCA2_HUMAN	BRCA2	physical	19861535
FANCI_HUMAN	FANCI	physical	27773793
FANCA_HUMAN	FANCA	physical	23303816
FANCC_HUMAN	FANCC	physical	23303816
FANCE_HUMAN	FANCE	physical	23303816
CTBP1_HUMAN	CTBP1	physical	23303816
MSH2_HUMAN	MSH2	genetic	24966277
DNA2_HUMAN	DNA2	physical	22987153
CTIP_HUMAN	RBBP8	physical	24794434
FANCJ_HUMAN	BRIP1	physical	26336824
LAMB2_HUMAN	LAMB2	physical	24658369
MYC_HUMAN	MYC	physical	24658369
MCM2_HUMAN	MCM2	physical	24658369
MCM3_HUMAN	MCM3	physical	24658369
MCM4_HUMAN	MCM4	physical	24658369
ATPA_HUMAN	ATP5A1	physical	28687786
CTIP_HUMAN	RBBP8	physical	24794430
FAN1_HUMAN	FAN1	physical	24794430
FANCI_HUMAN	FANCI	physical	24794430
XPF_HUMAN	ERCC4	physical	24794430
RFA1_HUMAN	RPA1	physical	24794430
SLX4_HUMAN	SLX4	physical	24794430
UBC_HUMAN	UBC	physical	21464321
PARP1_HUMAN	PARP1	genetic	28628639
PARP2_HUMAN	PARP2	genetic	28628639
TOP3A_HUMAN	TOP3A	physical	25659033
FANCI_HUMAN	FANCI	physical	25489943
SPTN1_HUMAN	SPTAN1	physical	26297932
SPTA1_HUMAN	SPTA1	physical	16889989
CHK1_HUMAN	CHEK1	genetic	14988723
FANCI_HUMAN	FANCI	physical	23993743
MCM2_HUMAN	MCM2	physical	23993743
MCM4_HUMAN	MCM4	physical	23993743
MCM6_HUMAN	MCM6	physical	23993743
MCM3_HUMAN	MCM3	physical	23993743
MCM5_HUMAN	MCM5	physical	23993743
MCM7_HUMAN	MCM7	physical	23993743
H2B1B_HUMAN	HIST1H2BB	physical	22828868
H31_HUMAN	HIST1H3A	physical	22828868
ABCB6_HUMAN	ABCB6	physical	22258451
BRCA2_HUMAN	BRCA2	physical	28684355

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
227646	Fanconi anemia complementation group D2 (FANCD2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of FACD2_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-592, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.	19369195 [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-1412, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1412, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND MASSSPECTROMETRY.	19007248 [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-167; SER-178; SER-592;THR-596; SER-717; SER-1412 AND SER-1418, 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-592; SER-717 ANDSER-1412 (ISOFORMS 1/2/3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] ATSER-1435 (ISOFORM 2), AND MASS SPECTROMETRY.	15302935 [Abstract]
"Convergence of the fanconi anemia and ataxia telangiectasia signalingpathways."; Taniguchi T., Garcia-Higuera I., Xu B., Andreassen P.R., Gregory R.C.,Kim S.-T., Lane W.S., Kastan M.B., D'Andrea A.D.; Cell 109:459-472(2002). Cited for: FUNCTION, PHOSPHORYLATION AT SER-222 AND SER-1404, MUTAGENESIS OFSER-222; LYS-561; SER-1257; SER-1401; SER-1404 AND SER-1418, AND MASSSPECTROMETRY.	12086603 [Abstract]
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-684, AND MASSSPECTROMETRY.	17053785 [Abstract]
Ubiquitylation
Reference	PubMed
"A genetic screen identifies FAN1, a Fanconi anemia-associatednuclease necessary for DNA interstrand crosslink repair."; Smogorzewska A., Desetty R., Saito T.T., Schlabach M., Lach F.P.,Sowa M.E., Clark A.B., Kunkel T.A., Harper J.W., Colaiacovo M.P.,Elledge S.J.; Mol. Cell 39:36-47(2010). Cited for: UBIQUITINATION AT LYS-561, INTERACTION WITH MTMR15, AND MUTAGENESIS OFLYS-561.	20603073 [Abstract]
"Deficiency of FANCD2-associated nuclease KIAA1018/FAN1 sensitizescells to interstrand crosslinking agents."; Kratz K., Schopf B., Kaden S., Sendoel A., Eberhard R., Lademann C.,Cannavo E., Sartori A.A., Hengartner M.O., Jiricny J.; Cell 142:77-88(2010). Cited for: UBIQUITINATION AT LYS-561, INTERACTION WITH MTMR15, AND MUTAGENESIS OFLYS-561.	20603016 [Abstract]
"Identification of KIAA1018/FAN1, a DNA repair nuclease recruited toDNA damage by monoubiquitinated FANCD2."; MacKay C., Declais A.C., Lundin C., Agostinho A., Deans A.J.,MacArtney T.J., Hofmann K., Gartner A., West S.C., Helleday T.,Lilley D.M., Rouse J.; Cell 142:65-76(2010). Cited for: UBIQUITINATION AT LYS-561, INTERACTION WITH MTMR15, AND MUTAGENESIS OFLYS-561.	20603015 [Abstract]
"Mechanistic insight into site-restricted monoubiquitination of FANCD2by Ube2t, FANCL, and FANCI."; Alpi A.F., Pace P.E., Babu M.M., Patel K.J.; Mol. Cell 32:767-777(2008). Cited for: UBIQUITINATION AT LYS-561, AND MUTAGENESIS OF LYS-561.	19111657 [Abstract]
"Interaction of the Fanconi anemia proteins and BRCA1 in a commonpathway."; Garcia-Higuera I., Taniguchi T., Ganesan S., Meyn M.S., Timmers C.,Hejna J., Grompe M., D'Andrea A.D.; Mol. Cell 7:249-262(2001). Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-561, MASSSPECTROMETRY, MUTAGENESIS OF LYS-561, AND INTERACTION WITH BRCA1.	11239454 [Abstract]

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