dbPTM

DBNL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DBNL_HUMAN
UniProt AC	Q9UJU6
Protein Name	Drebrin-like protein
Gene Name	DBNL
Organism	Homo sapiens (Human).
Sequence Length	430
Subcellular Localization	Cytoplasm, cytoskeleton . Cell projection, lamellipodium . Cell projection, ruffle . Cytoplasm, cell cortex . Cytoplasm, cytosol . Cell junction, synapse . Cell projection . Cell membrane Peripheral membrane protein Cytoplasmic side. Cytoplasmic vesicl
Protein Description	Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes (By similarity). May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes..
Protein Sequence	MAANLSRNGPALQEAYVRVVTEKSPTDWALFTYEGNSNDIRVAGTGEGGLEEMVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACASHVSTMASFLKGAHVTINARAEEDVEPECIMEKVAKASGANYSFHKESGRFQDVGPQAPVGSVYQKTNAVSEIKRVGKDSFWAKAEKEEENRRLEEKRRAEEAQRQLEQERRERELREAARREQRYQEQGGEASPQRTWEQQQEVVSRNRNEQESAVHPREIFKQKERAMSTTSISSPQPGKLRSPFLQKQLTQPETHFGREPAAAISRPRADLPAEEPAPSTPPCLVQAEEEAVYEEPPEQETFYEQPPLVQQQGAGSEHIDHHIQGQGLSGQGLCARALYDYQAADDTEISFDPENLITGIEVIDEGWWRGYGPDGHFGMFPANYVELIE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MAANLSRNGPALQ --CCCCCCCCCHHHH	24.41	22199227
16	Phosphorylation	GPALQEAYVRVVTEK CHHHHEEEEEEEECC	6.50	21253578
21	Phosphorylation	EAYVRVVTEKSPTDW EEEEEEEECCCCCCE	34.53	28102081
23	Ubiquitination	YVRVVTEKSPTDWAL EEEEEECCCCCCEEE	52.98	21906983
23	Acetylation	YVRVVTEKSPTDWAL EEEEEECCCCCCEEE	52.98	23236377
23	Ubiquitination	YVRVVTEKSPTDWAL EEEEEECCCCCCEEE	52.98	21906983
23 (in isoform 1)	Ubiquitination	-	52.98	21890473
23 (in isoform 2)	Ubiquitination	-	52.98	21890473
23 (in isoform 3)	Ubiquitination	-	52.98	21890473
24	Phosphorylation	VRVVTEKSPTDWALF EEEEECCCCCCEEEE	27.14	23898821
26	Phosphorylation	VVTEKSPTDWALFTY EEECCCCCCEEEEEE	51.79	22617229
32	Phosphorylation	PTDWALFTYEGNSND CCCEEEEEEECCCCE	22.86	23186163
33	Phosphorylation	TDWALFTYEGNSNDI CCEEEEEEECCCCEE	17.95	23186163
37	Phosphorylation	LFTYEGNSNDIRVAG EEEEECCCCEEEEEC	46.89	23186163
45	Phosphorylation	NDIRVAGTGEGGLEE CEEEEECCCCCCHHH	23.48	17855441
53	Sulfoxidation	GEGGLEEMVEELNSG CCCCHHHHHHHHHCC	3.16	21406390
61	Ubiquitination	VEELNSGKVMYAFCR HHHHHCCCEEEEEEE	24.53	21890473
69	Ubiquitination	VMYAFCRVKDPNSGL EEEEEEEECCCCCCC	9.67	21890473
70	Acetylation	MYAFCRVKDPNSGLP EEEEEEECCCCCCCC	48.38	26051181
73	Acetylation	FCRVKDPNSGLPKFV EEEECCCCCCCCEEE	59.86	19608861
99	Phosphorylation	VRKGACASHVSTMAS HHHCCHHHHHHHHHH	25.06	-
99 (in isoform 6)	Phosphorylation	-	25.06	24532841
102	Phosphorylation	GACASHVSTMASFLK CCHHHHHHHHHHHHC	13.67	28857561
102 (in isoform 6)	Phosphorylation	-	13.67	24532841
103	Phosphorylation	ACASHVSTMASFLKG CHHHHHHHHHHHHCC	18.70	28857561
103 (in isoform 6)	Phosphorylation	-	18.70	24532841
106	Phosphorylation	SHVSTMASFLKGAHV HHHHHHHHHHCCCEE	21.93	28857561
106 (in isoform 6)	Phosphorylation	-	21.93	24532841
114	Phosphorylation	FLKGAHVTINARAEE HHCCCEEEEECCCCC	9.92	-
120 (in isoform 6)	Phosphorylation	-	49.53	24532841
129	Sulfoxidation	DVEPECIMEKVAKAS CCCCHHHHHHHHHHH	6.53	21406390
129 (in isoform 4)	Phosphorylation	-	6.53	28796482
131	Acetylation	EPECIMEKVAKASGA CCHHHHHHHHHHHCC	30.07	23749302
131	Ubiquitination	EPECIMEKVAKASGA CCHHHHHHHHHHHCC	30.07	-
134	Ubiquitination	CIMEKVAKASGANYS HHHHHHHHHHCCCCE	46.18	-
134 (in isoform 3)	Ubiquitination	-	46.18	-
136	Phosphorylation	MEKVAKASGANYSFH HHHHHHHHCCCCEEE	37.42	21945579
137 (in isoform 4)	Phosphorylation	-	23.77	25159151
140	Phosphorylation	AKASGANYSFHKESG HHHHCCCCEEECCCC	16.51	21945579
140 (in isoform 4)	Phosphorylation	-	16.51	21712546
141	Phosphorylation	KASGANYSFHKESGR HHHCCCCEEECCCCC	22.23	23401153
144	Methylation	GANYSFHKESGRFQD CCCCEEECCCCCCCC	52.11	-
144	Ubiquitination	GANYSFHKESGRFQD CCCCEEECCCCCCCC	52.11	-
144 (in isoform 3)	Ubiquitination	-	52.11	-
146	Phosphorylation	NYSFHKESGRFQDVG CCEEECCCCCCCCCC	39.82	23312004
160	Phosphorylation	GPQAPVGSVYQKTNA CCCCCCCCHHHHCCC	20.20	23401153
162	Phosphorylation	QAPVGSVYQKTNAVS CCCCCCHHHHCCCHH	13.14	21945579
164	Methylation	PVGSVYQKTNAVSEI CCCCHHHHCCCHHHH	26.51	-
164	Ubiquitination	PVGSVYQKTNAVSEI CCCCHHHHCCCHHHH	26.51	21890473
164 (in isoform 1)	Ubiquitination	-	26.51	21890473
164 (in isoform 2)	Ubiquitination	-	26.51	21890473
164 (in isoform 3)	Ubiquitination	-	26.51	21890473
165	Phosphorylation	VGSVYQKTNAVSEIK CCCHHHHCCCHHHHH	16.94	-
169	Phosphorylation	YQKTNAVSEIKRVGK HHHCCCHHHHHHHCC	31.06	29970186
172	Acetylation	TNAVSEIKRVGKDSF CCCHHHHHHHCCCCH	36.66	25953088
172	Methylation	TNAVSEIKRVGKDSF CCCHHHHHHHCCCCH	36.66	-
172	Ubiquitination	TNAVSEIKRVGKDSF CCCHHHHHHHCCCCH	36.66	-
175 (in isoform 6)	Phosphorylation	-	31.89	28796482
176	Acetylation	SEIKRVGKDSFWAKA HHHHHHCCCCHHHHH	47.55	19608861
176	Malonylation	SEIKRVGKDSFWAKA HHHHHHCCCCHHHHH	47.55	26320211
176	Ubiquitination	SEIKRVGKDSFWAKA HHHHHHCCCCHHHHH	47.55	-
176 (in isoform 3)	Malonylation	-	47.55	26320211
176 (in isoform 3)	Ubiquitination	-	47.55	-
178	Phosphorylation	IKRVGKDSFWAKAEK HHHHCCCCHHHHHHH	26.61	22617229
183 (in isoform 6)	Phosphorylation	-	25.91	25159151
185	Acetylation	SFWAKAEKEEENRRL CHHHHHHHHHHHHHH	75.24	19608861
186 (in isoform 6)	Phosphorylation	-	63.15	21712546
224	Phosphorylation	AARREQRYQEQGGEA HHHHHHHHHHCCCCC	18.98	21945579
224 (in isoform 2)	Phosphorylation	-	18.98	28796482
224 (in isoform 3)	Phosphorylation	-	18.98	28796482
232	Phosphorylation	QEQGGEASPQRTWEQ HHCCCCCCCCCHHHH	19.77	29255136
232 (in isoform 2)	Phosphorylation	-	19.77	25159151
232 (in isoform 3)	Phosphorylation	-	19.77	25159151
235 (in isoform 2)	Phosphorylation	-	45.23	21712546
235 (in isoform 3)	Phosphorylation	-	45.23	21712546
236	Phosphorylation	GEASPQRTWEQQQEV CCCCCCCHHHHHHHH	28.27	20201521
245	Phosphorylation	EQQQEVVSRNRNEQE HHHHHHHHCCCCHHH	29.07	23927012
253	Phosphorylation	RNRNEQESAVHPREI CCCCHHHHCCCHHHH	34.97	28555341
258 (in isoform 3)	Phosphorylation	-	34.46	-
268	Sulfoxidation	FKQKERAMSTTSISS HHHHHHHHHCCCCCC	4.59	21406390
269	Phosphorylation	KQKERAMSTTSISSP HHHHHHHHCCCCCCC	27.78	19664994
270	Phosphorylation	QKERAMSTTSISSPQ HHHHHHHCCCCCCCC	16.10	29255136
271	Phosphorylation	KERAMSTTSISSPQP HHHHHHCCCCCCCCC	19.43	22167270
272	O-linked_Glycosylation	ERAMSTTSISSPQPG HHHHHCCCCCCCCCC	22.14	30379171
272	Phosphorylation	ERAMSTTSISSPQPG HHHHHCCCCCCCCCC	22.14	22167270
274	O-linked_Glycosylation	AMSTTSISSPQPGKL HHHCCCCCCCCCCCC	35.42	30379171
274	Phosphorylation	AMSTTSISSPQPGKL HHHCCCCCCCCCCCC	35.42	29255136
275	Phosphorylation	MSTTSISSPQPGKLR HHCCCCCCCCCCCCC	26.36	19664994
280	Acetylation	ISSPQPGKLRSPFLQ CCCCCCCCCCCHHHH	47.62	23954790
280	Malonylation	ISSPQPGKLRSPFLQ CCCCCCCCCCCHHHH	47.62	26320211
280	Ubiquitination	ISSPQPGKLRSPFLQ CCCCCCCCCCCHHHH	47.62	-
281 (in isoform 2)	Ubiquitination	-	8.98	-
283	Phosphorylation	PQPGKLRSPFLQKQL CCCCCCCCHHHHHHH	30.36	29255136
288	Acetylation	LRSPFLQKQLTQPET CCCHHHHHHHCCCCC	49.80	19608861
288	Methylation	LRSPFLQKQLTQPET CCCHHHHHHHCCCCC	49.80	-
288	Ubiquitination	LRSPFLQKQLTQPET CCCHHHHHHHCCCCC	49.80	-
289 (in isoform 3)	Malonylation	-	36.46	26320211
289 (in isoform 3)	Ubiquitination	-	36.46	-
291	Phosphorylation	PFLQKQLTQPETHFG HHHHHHHCCCCCCCC	39.31	29255136
295	O-linked_Glycosylation	KQLTQPETHFGREPA HHHCCCCCCCCCCCC	29.23	30379171
295	Phosphorylation	KQLTQPETHFGREPA HHHCCCCCCCCCCCC	29.23	22167270
297	Acetylation	LTQPETHFGREPAAA HCCCCCCCCCCCCHH	14.94	19608861
297 (in isoform 3)	Ubiquitination	-	14.94	-
306	Phosphorylation	REPAAAISRPRADLP CCCCHHHCCCCCCCC	31.35	26330541
320	Phosphorylation	PAEEPAPSTPPCLVQ CCCCCCCCCCCCEEE	56.50	20058876
321	Phosphorylation	AEEPAPSTPPCLVQA CCCCCCCCCCCEEEE	30.14	20058876
334	Phosphorylation	QAEEEAVYEEPPEQE EECHHHHHCCCCCCC	22.94	20736484
344	Phosphorylation	PPEQETFYEQPPLVQ CCCCCCCCCCCCCCC	22.52	20736484
412	Phosphorylation	DEGWWRGYGPDGHFG ECCCCCCCCCCCCCC	19.53	28796482
420	Sulfoxidation	GPDGHFGMFPANYVE CCCCCCCCCCHHHEE	3.39	30846556
425	Phosphorylation	FGMFPANYVELIE-- CCCCCHHHEEECC--	9.45	28796482

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
334	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
344	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SH24A_HUMAN	SH2D4A	physical	16189514
HERC2_HUMAN	HERC2	physical	17353931
GPS2_HUMAN	GPS2	physical	17353931
DNPEP_HUMAN	DNPEP	physical	17353931
CDK4_HUMAN	CDK4	physical	17353931
E2AK2_HUMAN	EIF2AK2	physical	17353931
RBCC1_HUMAN	RB1CC1	physical	17353931
CP4F8_HUMAN	CYP4F8	physical	17353931
ZAP70_HUMAN	ZAP70	physical	14557276
M4K1_HUMAN	MAP4K1	physical	10567356
3BP2_HUMAN	SH3BP2	physical	17306257
CBL_HUMAN	CBL	physical	17306257
AGFG1_HUMAN	AGFG1	physical	22863883
HEM2_HUMAN	ALAD	physical	22863883
GON7_HUMAN	C14orf142	physical	22863883
CBS_HUMAN	CBS	physical	22863883
DDX5_HUMAN	DDX5	physical	22863883
NC2B_HUMAN	DR1	physical	22863883
ERO1A_HUMAN	ERO1L	physical	22863883
GPN1_HUMAN	GPN1	physical	22863883
HPBP1_HUMAN	HSPBP1	physical	22863883
P3H1_HUMAN	P3H1	physical	22863883
LRSM1_HUMAN	LRSAM1	physical	22863883
OGT1_HUMAN	OGT	physical	22863883
PLIN3_HUMAN	PLIN3	physical	22863883
PPME1_HUMAN	PPME1	physical	22863883
RAGP1_HUMAN	RANGAP1	physical	22863883
TPRKB_HUMAN	TPRKB	physical	22863883
UBA5_HUMAN	UBA5	physical	22863883
UBE3A_HUMAN	UBE3A	physical	22863883
WDR4_HUMAN	WDR4	physical	22863883
SH24A_HUMAN	SH2D4A	physical	25416956
HERC2_HUMAN	HERC2	physical	26186194
FGD6_HUMAN	FGD6	physical	26186194
ECI2_HUMAN	ECI2	physical	26186194
NEUA_HUMAN	CMAS	physical	26186194
UBP20_HUMAN	USP20	physical	26186194
NEUL4_HUMAN	NEURL4	physical	26186194
FGD6_HUMAN	FGD6	physical	28514442
NEUL4_HUMAN	NEURL4	physical	28514442
HERC2_HUMAN	HERC2	physical	28514442
UBP20_HUMAN	USP20	physical	28514442
ECI2_HUMAN	ECI2	physical	28514442
NEUA_HUMAN	CMAS	physical	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 DBNL_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176 AND LYS-288, AND MASSSPECTROMETRY.	19608861 [Abstract]
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-232; SER-269 ANDSER-275, AND MASS SPECTROMETRY.	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-232; SER-269; THR-270AND SER-275, AND MASS SPECTROMETRY.	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-232; SER-269 ANDSER-283, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-275, ANDMASS SPECTROMETRY.	18088087 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-269; SER-272;SER-275; SER-283 AND THR-291, AND MASS SPECTROMETRY.	17287340 [Abstract]
"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-283, AND MASSSPECTROMETRY.	17924679 [Abstract]
"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-232, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, AND MASSSPECTROMETRY.	16094384 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, AND MASSSPECTROMETRY.	15592455 [Abstract]