DFFA_HUMAN - dbPTM
DFFA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DFFA_HUMAN
UniProt AC O00273
Protein Name DNA fragmentation factor subunit alpha
Gene Name DFFA
Organism Homo sapiens (Human).
Sequence Length 331
Subcellular Localization Cytoplasm.
Protein Description Inhibitor of the caspase-activated DNase (DFF40)..
Protein Sequence MEVTGDAGVPESGEIRTLKPCLLRRNYSREQHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLPSNTKFVALASNEKWAYNNSDGGTAWISQESFDVDETDSGAGLKWKNVARQLKEDLSSIILLSEEDLQMLVDAPCSDLAQELRQSCATVQRLQHTLQQVLDQREEVRQSKQLLQLYLQALEKEGSLLSKQEESKAAFGEEVDAVDTGISRETSSDVALASHILTALREKQAPELSLSSQDLELVTKEDPKALAVALNWDIKKTETVQEACERELALRLQQTQSLHSLRSISASKASPPGDLQNPKRARQDPT
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
1Acetylation-------MEVTGDAG
-------CCCCCCCC		9.3722223895
19AcetylationSGEIRTLKPCLLRRN
CCCEEECCCCHHHCC		32.8327452117
27PhosphorylationPCLLRRNYSREQHGV
CCHHHCCCCHHHHCH		13.8022617229
28PhosphorylationCLLRRNYSREQHGVA
CHHHCCCCHHHHCHH		32.6523401153
37PhosphorylationEQHGVAASCLEDLRS
HHHCHHHHHHHHHHH		14.9723403867
38GlutathionylationQHGVAASCLEDLRSK
HHCHHHHHHHHHHHC		4.0722555962
45UbiquitinationCLEDLRSKACDILAI
HHHHHHHCCCCEEEE		46.75-
47GlutathionylationEDLRSKACDILAIDK
HHHHHCCCCEEEECC		3.7222555962
75PhosphorylationTIVDDDDYFLCLPSN
CEECCCCEEEECCCC		12.8722817900
96PhosphorylationASNEKWAYNNSDGGT
ECCCCEEEECCCCCE		17.4827251275
99PhosphorylationEKWAYNNSDGGTAWI
CCEEEECCCCCEEEE		33.7127251275
103PhosphorylationYNNSDGGTAWISQES
EECCCCCEEEECEEC		25.0927251275
107PhosphorylationDGGTAWISQESFDVD
CCCEEEECEECCCCC		19.7325159151
110PhosphorylationTAWISQESFDVDETD
EEEECEECCCCCCCC		21.0725159151
116PhosphorylationESFDVDETDSGAGLK
ECCCCCCCCCCCCHH		30.8829978859
118PhosphorylationFDVDETDSGAGLKWK
CCCCCCCCCCCHHHH		37.6527251275
188PhosphorylationQREEVRQSKQLLQLY
HHHHHHHHHHHHHHH		16.2929888752
189 (in isoform 2)Ubiquitination-36.3021890473
189 (in isoform 1)Ubiquitination-36.3021890473
189UbiquitinationREEVRQSKQLLQLYL
HHHHHHHHHHHHHHH		36.3021890473
189UbiquitinationREEVRQSKQLLQLYL
HHHHHHHHHHHHHHH		36.3021890473
195PhosphorylationSKQLLQLYLQALEKE
HHHHHHHHHHHHHHC		5.4729888752
201UbiquitinationLYLQALEKEGSLLSK
HHHHHHHHCCCCCCH		69.12-
204PhosphorylationQALEKEGSLLSKQEE
HHHHHCCCCCCHHHH		27.5124719451
208UbiquitinationKEGSLLSKQEESKAA
HCCCCCCHHHHHHHH		62.79-
213UbiquitinationLSKQEESKAAFGEEV
CCHHHHHHHHHCCCC		47.19-
225PhosphorylationEEVDAVDTGISRETS
CCCCHHCCCCCCCCC		29.8027732954
228PhosphorylationDAVDTGISRETSSDV
CHHCCCCCCCCCHHH		25.9627732954
231PhosphorylationDTGISRETSSDVALA
CCCCCCCCCHHHHHH		32.2121712546
232PhosphorylationTGISRETSSDVALAS
CCCCCCCCHHHHHHH		21.5625159151
233PhosphorylationGISRETSSDVALASH
CCCCCCCHHHHHHHH		43.4525159151
239PhosphorylationSSDVALASHILTALR
CHHHHHHHHHHHHHH		16.3523403867
243PhosphorylationALASHILTALREKQA
HHHHHHHHHHHHCCC		24.0424117733
248UbiquitinationILTALREKQAPELSL
HHHHHHHCCCCCCCC		45.38-
248 (in isoform 2)Ubiquitination-45.3821890473
254 (in isoform 2)Phosphorylation-25.2520068231
254PhosphorylationEKQAPELSLSSQDLE
HCCCCCCCCCHHHHE		25.2520068231
256PhosphorylationQAPELSLSSQDLELV
CCCCCCCCHHHHEEE		23.6822199227
256 (in isoform 2)Phosphorylation-23.6820068231
257PhosphorylationAPELSLSSQDLELVT
CCCCCCCHHHHEEEE		32.7617525332
257 (in isoform 2)Phosphorylation-32.7617525332
264PhosphorylationSQDLELVTKEDPKAL
HHHHEEEECCCHHHH		41.1425002506
296MethylationCERELALRLQQTQSL
HHHHHHHHHHHHHHH		25.50-
300PhosphorylationLALRLQQTQSLHSLR
HHHHHHHHHHHHHHH		13.7328857561
302PhosphorylationLRLQQTQSLHSLRSI
HHHHHHHHHHHHHHH		31.2828857561
305PhosphorylationQQTQSLHSLRSISAS
HHHHHHHHHHHHCCC		30.6728857561
308PhosphorylationQSLHSLRSISASKAS
HHHHHHHHHCCCCCC		26.6223927012
310PhosphorylationLHSLRSISASKASPP
HHHHHHHCCCCCCCC		27.9530278072
312PhosphorylationSLRSISASKASPPGD
HHHHHCCCCCCCCCC		23.2030278072
313UbiquitinationLRSISASKASPPGDL
HHHHCCCCCCCCCCC		53.23-
313AcetylationLRSISASKASPPGDL
HHHHCCCCCCCCCCC		53.2325953088
315PhosphorylationSISASKASPPGDLQN
HHCCCCCCCCCCCCC		35.0529255136
324AcetylationPGDLQNPKRARQDPT
CCCCCCHHHHCCCCC		67.2669851
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 DFFA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DFFA_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 DFFA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NECA2_HUMANNECAB2physical
16189514
EWS_HUMANEWSR1physical
16189514
DFFB_HUMANDFFBphysical
17353931
HERC1_HUMANHERC1physical
17353931
CRCM_HUMANMCCphysical
17353931
NP1L5_HUMANNAP1L5physical
17353931
UBP15_HUMANUSP15physical
17353931
DFFB_HUMANDFFBphysical
10527860
SEPT5_HUMANSEPT5physical
22939629
TM1L2_HUMANTOM1L2physical
22939629
BZW2_HUMANBZW2physical
22863883
KCRB_HUMANCKBphysical
22863883
CNBP_HUMANCNBPphysical
22863883
IF6_HUMANEIF6physical
22863883
G3P_HUMANGAPDHphysical
22863883
ISOC1_HUMANISOC1physical
22863883
METK2_HUMANMAT2Aphysical
22863883
MAT2B_HUMANMAT2Bphysical
22863883
PUR4_HUMANPFASphysical
22863883
PPP5_HUMANPPP5Cphysical
22863883
TBA1A_HUMANTUBA1Aphysical
22863883
TBB5_HUMANTUBBphysical
22863883
TSYL4_HUMANTSPYL4physical
26186194
GBB4_HUMANGNB4physical
26186194
DFFB_HUMANDFFBphysical
26186194
DFFB_HUMANDFFBphysical
28514442
TSYL4_HUMANTSPYL4physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DFFA_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-315, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-315, AND MASS SPECTROMETRY.
"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-315, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-315, ANDMASS SPECTROMETRY.
"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-257, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND MASSSPECTROMETRY.

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