dbPTM

DAB2P_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DAB2P_HUMAN
UniProt AC	Q5VWQ8
Protein Name	Disabled homolog 2-interacting protein
Gene Name	DAB2IP
Organism	Homo sapiens (Human).
Sequence Length	1189
Subcellular Localization	Cytoplasm. Cell membrane Peripheral membrane protein . Membrane. Cell projection, dendrite. Localized in soma and dendrites of Purkinje cells as well as in scattered cell bodies in the molecular layer of the cerebellum (By similarity). Colocalizes
Protein Description	Functions as a scaffold protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Involved in several processes such as innate immune response, inflammation and cell growth inhibition, apoptosis, cell survival, angiogenesis, cell migration and maturation. Plays also a role in cell cycle checkpoint control; reduces G1 phase cyclin levels resulting in G0/G1 cell cycle arrest. Mediates signal transduction by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF), interferon (IFN) or lipopolysaccharide (LPS). Modulates the balance between phosphatidylinositol 3-kinase (PI3K)-AKT-mediated cell survival and apoptosis stimulated kinase (MAP3K5)-JNK signaling pathways; sequesters both AKT1 and MAP3K5 and counterbalances the activity of each kinase by modulating their phosphorylation status in response to proinflammatory stimuli. Acts as a regulator of the endoplasmic reticulum (ER) unfolded protein response (UPR) pathway; specifically involved in transduction of the ER stress-response to the JNK cascade through ERN1. Mediates TNF-alpha-induced apoptosis activation by facilitating dissociation of inhibitor 14-3-3 from MAP3K5; recruits the PP2A phosphatase complex which dephosphorylates MAP3K5 on 'Ser-966', leading to the dissociation of 13-3-3 proteins and activation of the MAP3K5-JNK signaling pathway in endothelial cells. Mediates also TNF/TRAF2-induced MAP3K5-JNK activation, while it inhibits CHUK-NF-kappa-B signaling. Acts a negative regulator in the IFN-gamma-mediated JAK-STAT signaling cascade by inhibiting smooth muscle cell (VSMCs) proliferation and intimal expansion, and thus, prevents graft arteriosclerosis (GA). Acts as a GTPase-activating protein (GAP) for the ADP ribosylation factor 6 (ARF6) and Ras. Promotes hydrolysis of the ARF6-bound GTP and thus, negatively regulates phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent TLR4-TIRAP-MyD88 and NF-kappa-B signaling pathways in endothelial cells in response to lipopolysaccharides (LPS). Binds specifically to phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol 3-phosphate (PtdIns3P). In response to vascular endothelial growth factor (VEGFA), acts as a negative regulator of the VEGFR2-PI3K-mediated angiogenic signaling pathway by inhibiting endothelial cell migration and tube formation. In the developing brain, promotes both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex in a glial-dependent locomotion process. Probable downstream effector of the Reelin signaling pathway; promotes Purkinje cell (PC) dendrites development and formation of cerebellar synapses. Functions also as a tumor suppressor protein in prostate cancer progression; prevents cell proliferation and epithelial-to-mesenchymal transition (EMT) through activation of the glycogen synthase kinase-3 beta (GSK3B)-induced beta-catenin and inhibition of PI3K-AKT and Ras-MAPK survival downstream signaling cascades, respectively..
Protein Sequence	MSAGGSARKSTGRSSYYYRLLRRPRLQRQRSRSRSRTRPARESPQERPGSRRSLPGSLSEKSPSMEPSAATPFRVTGFLSRRLKGSIKRTKSQPKLDRNHSFRHILPGFRSAAAAAADNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEEVVIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTGKLKTDNVFWGEHFEFHNLPPLRTVTVHLYRETDKKKKKERNSYLGLVSLPAASVAGRQFVEKWYPVVTPNPKGGKGPGPMIRIKARYQTITILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSAADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSRGRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLEQSIVSKLGPLPRILRDVHTALSTPGSGQLPGTNDLASTPGSGSSSISAGLQKMVIENDLSGLIDFTRLPSPTPENKDLFFVTRSSGVQPSPARSSSYSEANEPDLQMANGGKSLSMVDLQDARTLDGEAGSPAGPDVLPTDGQAAAAQLVAGWPARATPVNLAGLATVRRAGQTPTTPGTSEGAPGRPQLLAPLSFQNPVYQMAAGLPLSPRGLGDSGSEGHSSLSSHSNSEELAAAAKLGSFSTAAEELARRPGELARRQMSLTEKGGQPTVPRQNSAGPQRRIDQPPPPPPPPPPAPRGRTPPNLLSTLQYPRPSSGTLASASPDWVGPSTRLRQQSSSSKGDSPELKPRAVHKQGPSPVSPNALDRTAAWLLTMNAQLLEDEGLGPDPPHRDRLRSKDELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDIQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQARNGISPTNPTKLQITENGEFRNSSNC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSAGGSARK ------CCCCCCCCC	47.10	20068231
6	Phosphorylation	--MSAGGSARKSTGR --CCCCCCCCCCCCC	24.79	20068231
10	Phosphorylation	AGGSARKSTGRSSYY CCCCCCCCCCCHHHH	30.46	20068231
11	Phosphorylation	GGSARKSTGRSSYYY CCCCCCCCCCHHHHH	39.38	29759185
25	Phosphorylation	YRLLRRPRLQRQRSR HHHHCCHHHHHHHHH	41.46	24719451
48	Phosphorylation	RESPQERPGSRRSLP CCCCCCCCCCCCCCC	44.34	24719451
50	Phosphorylation	SPQERPGSRRSLPGS CCCCCCCCCCCCCCC	27.48	22210691
53	Phosphorylation	ERPGSRRSLPGSLSE CCCCCCCCCCCCCCC	37.49	26657352
57	Phosphorylation	SRRSLPGSLSEKSPS CCCCCCCCCCCCCCC	27.12	30266825
58	Phosphorylation	RRSLPGSLSEKSPSM CCCCCCCCCCCCCCC	10.71	24719451
62	Phosphorylation	PGSLSEKSPSMEPSA CCCCCCCCCCCCCCC	20.39	23612710
64	Phosphorylation	SLSEKSPSMEPSAAT CCCCCCCCCCCCCCC	42.75	23612710
73	Phosphorylation	EPSAATPFRVTGFLS CCCCCCCCHHHHHHH	9.48	24719451
76	Phosphorylation	AATPFRVTGFLSRRL CCCCCHHHHHHHHHH	20.26	24719451
80	Phosphorylation	FRVTGFLSRRLKGSI CHHHHHHHHHHCCCC	17.06	28857561
86	Phosphorylation	LSRRLKGSIKRTKSQ HHHHHCCCCCCCCCC	24.29	24719451
92	Phosphorylation	GSIKRTKSQPKLDRN CCCCCCCCCCCCCCC	51.61	28857561
101	Phosphorylation	PKLDRNHSFRHILPG CCCCCCCCHHHHCCC	27.76	26270265
122	Phosphorylation	AAADNERSHLMPRLK HHHHHHHHCCHHHHH	18.13	-
131	Phosphorylation	LMPRLKESRSHESLL CHHHHHHHCCCCCCC	37.18	26074081
133	Phosphorylation	PRLKESRSHESLLSP HHHHHHCCCCCCCCH	40.67	26074081
161	Ubiquitination	EVVIKPVHSSILGQD CEEEECCCHHHCCCC	25.10	24816145
165 (in isoform 2)	Phosphorylation	-	5.64	24719451
205	Ubiquitination	RRAVHPNKDNSRRVE HHHHCCCCCCHHHHH	63.84	-
223	Acetylation	KLWVIEAKDLPAKKK HHHHHHCCCCCHHHH	47.19	20167786
224	Ubiquitination	LWVIEAKDLPAKKKY HHHHHCCCCCHHHHH	66.00	24816145
237	Ubiquitination	KYLCELCLDDVLYAR HHHHHHHHHCHHHHC	11.15	24816145
257	Ubiquitination	KTDNVFWGEHFEFHN CCCCEEECCCEECCC	13.67	24816145
260	Ubiquitination	NVFWGEHFEFHNLPP CEEECCCEECCCCCC	10.50	24816145
261	Phosphorylation	VFWGEHFEFHNLPPL EEECCCEECCCCCCC	48.15	24719451
278	Ubiquitination	VTVHLYRETDKKKKK EEEEEEECCCCCCHH	48.04	24816145
285	Ubiquitination	ETDKKKKKERNSYLG CCCCCCHHHCCCCCC	71.44	24816145
289	Phosphorylation	KKKKERNSYLGLVSL CCHHHCCCCCCCHHH	28.14	22617229
290	Phosphorylation	KKKERNSYLGLVSLP CHHHCCCCCCCHHHC	14.34	26657352
295	Phosphorylation	NSYLGLVSLPAASVA CCCCCCHHHCHHHHH	33.41	23403867
296	Ubiquitination	SYLGLVSLPAASVAG CCCCCHHHCHHHHHC	2.33	29967540
300	Phosphorylation	LVSLPAASVAGRQFV CHHHCHHHHHCHHHH	18.01	23403867
334	Phosphorylation	MIRIKARYQTITILP CEEEEEEEEEEEEEE	18.18	26074081
336	Phosphorylation	RIKARYQTITILPME EEEEEEEEEEEEEHH	15.91	26074081
338	Phosphorylation	KARYQTITILPMEMY EEEEEEEEEEEHHHH	21.61	26074081
345	Phosphorylation	TILPMEMYKEFAEHI EEEEHHHHHHHHHHH	8.28	26074081
377	Phosphorylation	KTKEEMASALVHILQ CCHHHHHHHHHHHHH	22.33	30576142
385	Phosphorylation	ALVHILQSTGKVKDF HHHHHHHHCCCHHHH	35.36	30576142
392	Ubiquitination	STGKVKDFLTDLMMS HCCCHHHHHHHHHHH	7.01	29967540
416	Phosphorylation	HLIFRENTLATKAIE CEEECCCHHHHHHHH	17.02	22468782
578	Phosphorylation	EEYMSFMNQFLEHEW HHHHHHHHHHHHHCC	27.69	32142685
578 (in isoform 2)	Phosphorylation	-	27.69	24719451
602	Phosphorylation	ISNPETLSNTAGFEG CCCHHHHHCCCCCCC	39.28	18669648
602 (in isoform 2)	Phosphorylation	-	39.28	-
605 (in isoform 2)	Phosphorylation	-	25.57	-
610	Phosphorylation	NTAGFEGYIDLGREL CCCCCCCCHHHHHHH	5.53	20736484
623	Phosphorylation	ELSSLHSLLWEAVSQ HHHHHHHHHHHHHHH	4.48	32142685
623 (in isoform 2)	Phosphorylation	-	4.48	-
639	Phosphorylation	EQSIVSKLGPLPRIL HHHHHHHHCCHHHHH	7.13	32142685
639 (in isoform 2)	Phosphorylation	-	7.13	-
666 (in isoform 2)	Phosphorylation	-	43.37	-
669	Phosphorylation	PGTNDLASTPGSGSS CCCCCCCCCCCCCCC	42.29	29523821
670	Phosphorylation	GTNDLASTPGSGSSS CCCCCCCCCCCCCCH	26.51	29523821
673	Phosphorylation	DLASTPGSGSSSISA CCCCCCCCCCCHHHH	36.38	29523821
674	Phosphorylation	LASTPGSGSSSISAG CCCCCCCCCCHHHHH	37.15	20068231
692	Phosphorylation	MVIENDLSGLIDFTR HHEECCCCCCCCCCC	34.12	28450419
698	Phosphorylation	LSGLIDFTRLPSPTP CCCCCCCCCCCCCCC	27.78	28450419
699	Phosphorylation	SGLIDFTRLPSPTPE CCCCCCCCCCCCCCC	44.59	27251275
701	Phosphorylation	LIDFTRLPSPTPENK CCCCCCCCCCCCCCC	34.66	18669648
702	Phosphorylation	IDFTRLPSPTPENKD CCCCCCCCCCCCCCC	46.10	29255136
704	Phosphorylation	FTRLPSPTPENKDLF CCCCCCCCCCCCCCE	47.80	21712546
714	Phosphorylation	NKDLFFVTRSSGVQP CCCCEEEECCCCCCC	21.48	24117733
716	Phosphorylation	DLFFVTRSSGVQPSP CCEEEECCCCCCCCC	23.29	28857561
717	Phosphorylation	LFFVTRSSGVQPSPA CEEEECCCCCCCCCC	39.43	29396449
719	Phosphorylation	FVTRSSGVQPSPARS EEECCCCCCCCCCCC	9.04	19651622
722	Phosphorylation	RSSGVQPSPARSSSY CCCCCCCCCCCCCCC	17.69	21815630
726	Phosphorylation	VQPSPARSSSYSEAN CCCCCCCCCCCCCCC	26.24	23927012
727	Phosphorylation	QPSPARSSSYSEANE CCCCCCCCCCCCCCC	27.95	25159151
728	Phosphorylation	PSPARSSSYSEANEP CCCCCCCCCCCCCCC	33.65	23927012
729	Phosphorylation	SPARSSSYSEANEPD CCCCCCCCCCCCCCC	16.69	23927012
730	Phosphorylation	PARSSSYSEANEPDL CCCCCCCCCCCCCCC	31.98	23663014
735	Phosphorylation	SYSEANEPDLQMANG CCCCCCCCCCCCCCC	47.63	32142685
745	Phosphorylation	QMANGGKSLSMVDLQ CCCCCCCCCCEEEHH	29.02	30266825
747	Phosphorylation	ANGGKSLSMVDLQDA CCCCCCCCEEEHHCC	24.69	29255136
750 (in isoform 2)	Phosphorylation	-	29.94	24719451
756	Phosphorylation	VDLQDARTLDGEAGS EEHHCCCCCCCCCCC	30.81	27251275
762	Phosphorylation	RTLDGEAGSPAGPDV CCCCCCCCCCCCCCC	29.84	18669648
763	Phosphorylation	TLDGEAGSPAGPDVL CCCCCCCCCCCCCCC	20.72	25106551
771 (in isoform 2)	Phosphorylation	-	28.43	24719451
772	Phosphorylation	AGPDVLPTDGQAAAA CCCCCCCCCHHHHHH	48.91	22199227
790	Phosphorylation	AGWPARATPVNLAGL HCCCCCCCCCCHHHH	23.40	21815630
799	Phosphorylation	VNLAGLATVRRAGQT CCHHHHHHHHHCCCC	21.42	29255136
808	Phosphorylation	RRAGQTPTTPGTSEG HHCCCCCCCCCCCCC	49.35	20068231
811	Phosphorylation	GQTPTTPGTSEGAPG CCCCCCCCCCCCCCC	39.52	32142685
811 (in isoform 2)	Phosphorylation	-	39.52	24719451
812	Phosphorylation	QTPTTPGTSEGAPGR CCCCCCCCCCCCCCC	25.47	20068231
813	Phosphorylation	TPTTPGTSEGAPGRP CCCCCCCCCCCCCCC	39.69	20068231
814	Phosphorylation	PTTPGTSEGAPGRPQ CCCCCCCCCCCCCCC	60.25	27251275
818 (in isoform 2)	Phosphorylation	-	54.06	-
821 (in isoform 2)	Phosphorylation	-	47.98	-
825 (in isoform 2)	Phosphorylation	-	28.62	-
831 (in isoform 2)	Phosphorylation	-	18.53	-
833	Phosphorylation	LSFQNPVYQMAAGLP CCCCCHHHHHHCCCC	8.20	27259358
833 (in isoform 2)	Phosphorylation	-	8.20	-
842	Phosphorylation	MAAGLPLSPRGLGDS HHCCCCCCCCCCCCC	15.60	26356563
846	Phosphorylation	LPLSPRGLGDSGSEG CCCCCCCCCCCCCCC	7.91	24719451
849	Phosphorylation	SPRGLGDSGSEGHSS CCCCCCCCCCCCCCC	42.28	28857561
851	Phosphorylation	RGLGDSGSEGHSSLS CCCCCCCCCCCCCCC	44.34	23312004
854	Phosphorylation	GDSGSEGHSSLSSHS CCCCCCCCCCCCCCC	15.34	33259812
854 (in isoform 2)	Phosphorylation	-	15.34	24719451
855	Phosphorylation	DSGSEGHSSLSSHSN CCCCCCCCCCCCCCC	43.78	23312004
856	Phosphorylation	SGSEGHSSLSSHSNS CCCCCCCCCCCCCCH	26.96	23312004
858	Phosphorylation	SEGHSSLSSHSNSEE CCCCCCCCCCCCHHH	28.14	23312004
859	Phosphorylation	EGHSSLSSHSNSEEL CCCCCCCCCCCHHHH	35.91	23312004
861	Phosphorylation	HSSLSSHSNSEELAA CCCCCCCCCHHHHHH	43.96	23312004
863	Phosphorylation	SLSSHSNSEELAAAA CCCCCCCHHHHHHHH	35.15	23312004
867	Phosphorylation	HSNSEELAAAAKLGS CCCHHHHHHHHHHCC	9.80	24719451
868 (in isoform 2)	Phosphorylation	-	22.15	-
871 (in isoform 2)	Phosphorylation	-	48.97	24719451
874	Phosphorylation	AAAAKLGSFSTAAEE HHHHHHCCHHHHHHH	26.85	25850435
876	Phosphorylation	AAKLGSFSTAAEELA HHHHCCHHHHHHHHH	20.87	23186163
877	Phosphorylation	AKLGSFSTAAEELAR HHHCCHHHHHHHHHC	28.07	23186163
895	Phosphorylation	ELARRQMSLTEKGGQ HHHHHHHHHHHCCCC	24.65	28355574
897	Phosphorylation	ARRQMSLTEKGGQPT HHHHHHHHHCCCCCC	28.48	23312004
907	Phosphorylation	GGQPTVPRQNSAGPQ CCCCCCCCCCCCCCC	43.93	24719451
910	Phosphorylation	PTVPRQNSAGPQRRI CCCCCCCCCCCCCCC	26.68	-
914	Phosphorylation	RQNSAGPQRRIDQPP CCCCCCCCCCCCCCC	46.49	18669648
917	Phosphorylation	SAGPQRRIDQPPPPP CCCCCCCCCCCCCCC	6.68	18669648
921	Phosphorylation	QRRIDQPPPPPPPPP CCCCCCCCCCCCCCC	48.69	18669648
924	Ubiquitination	IDQPPPPPPPPPPAP CCCCCCCCCCCCCCC	60.86	29967540
927	Phosphorylation	PPPPPPPPPPAPRGR CCCCCCCCCCCCCCC	53.96	18669648
929	Phosphorylation	PPPPPPPPAPRGRTP CCCCCCCCCCCCCCC	61.75	18669648
931	Ubiquitination	PPPPPPAPRGRTPPN CCCCCCCCCCCCCCC	45.06	29967540
932	Methylation	PPPPPAPRGRTPPNL CCCCCCCCCCCCCCH	49.70	-
934	Methylation	PPPAPRGRTPPNLLS CCCCCCCCCCCCHHH	45.39	-
935	Phosphorylation	PPAPRGRTPPNLLST CCCCCCCCCCCHHHH	46.02	26657352
941	Phosphorylation	RTPPNLLSTLQYPRP CCCCCHHHHCCCCCC	30.18	28348404
942	Phosphorylation	TPPNLLSTLQYPRPS CCCCHHHHCCCCCCC	20.18	18669648
945	Phosphorylation	NLLSTLQYPRPSSGT CHHHHCCCCCCCCCC	12.34	18669648
949	Phosphorylation	TLQYPRPSSGTLASA HCCCCCCCCCCCCCC	42.55	25850435
950	Phosphorylation	LQYPRPSSGTLASAS CCCCCCCCCCCCCCC	38.18	33259812
952	Phosphorylation	YPRPSSGTLASASPD CCCCCCCCCCCCCCC	22.54	28348404
955	Phosphorylation	PSSGTLASASPDWVG CCCCCCCCCCCCCCC	32.18	25850435
957	Phosphorylation	SGTLASASPDWVGPS CCCCCCCCCCCCCCC	22.39	25106551
964	Phosphorylation	SPDWVGPSTRLRQQS CCCCCCCCHHHHCCC	21.89	20068231
967	Phosphorylation	WVGPSTRLRQQSSSS CCCCCHHHHCCCCCC	6.17	24719451
971	Phosphorylation	STRLRQQSSSSKGDS CHHHHCCCCCCCCCC	24.69	27273156
972	Phosphorylation	TRLRQQSSSSKGDSP HHHHCCCCCCCCCCC	34.00	27273156
973	Phosphorylation	RLRQQSSSSKGDSPE HHHCCCCCCCCCCCC	41.12	27273156
974	Phosphorylation	LRQQSSSSKGDSPEL HHCCCCCCCCCCCCC	42.48	23927012
978	Phosphorylation	SSSSKGDSPELKPRA CCCCCCCCCCCCCCH	29.01	29255136
984 (in isoform 2)	Phosphorylation	-	47.88	24719451
992	Phosphorylation	AVHKQGPSPVSPNAL HHHCCCCCCCCCCHH	44.77	30266825
995	Phosphorylation	KQGPSPVSPNALDRT CCCCCCCCCCHHHHH	18.80	30266825
1003	Phosphorylation	PNALDRTAAWLLTMN CCHHHHHHHHHHHHH	9.49	27251275
1020	Ubiquitination	LLEDEGLGPDPPHRD HHHCCCCCCCCCCHH	35.11	29967540
1027	Ubiquitination	GPDPPHRDRLRSKDE CCCCCCHHHHCCHHH	51.43	29967540
1031	Phosphorylation	PHRDRLRSKDELSQA CCHHHHCCHHHHHHH	49.39	26657352
1036	Phosphorylation	LRSKDELSQAEKDLA HCCHHHHHHHHHHHH	25.87	23403867
1044 (in isoform 2)	Phosphorylation	-	6.84	-
1059	Phosphorylation	STKKLEEYETLFKCQ CHHHHHHHHHHHHCC	12.58	28796482
1061	Phosphorylation	KKLEEYETLFKCQEE HHHHHHHHHHHCCHH	36.27	28796482
1080	Phosphorylation	LVLEYQARLEEGEER HHHHHHHHHHHHHHH	27.40	24719451
1108	Phosphorylation	GIISRLMSVEEELKK HHHHHHHCHHHHHHH	30.85	29255136
1112	Phosphorylation	RLMSVEEELKKDHAE HHHCHHHHHHHHHHH	53.00	27251275
1126	Phosphorylation	EMQAAVDSKQKIIDA HHHHHHHHHHHHHHH	30.32	21406692
1128	Methylation	QAAVDSKQKIIDAQE HHHHHHHHHHHHHHH	46.24	-
1136	Ubiquitination	KIIDAQEKRIASLDA HHHHHHHHHHHHHHH	36.70	-
1140	Phosphorylation	AQEKRIASLDAANAR HHHHHHHHHHHHHHH	25.14	21406692
1150	Phosphorylation	AANARLMSALTQLKE HHHHHHHHHHHHHHH	25.39	21406692
1153	Phosphorylation	ARLMSALTQLKERYS HHHHHHHHHHHHHHH	31.41	21406692
1168	Phosphorylation	MQARNGISPTNPTKL HHCCCCCCCCCCCCE	27.37	30266825
1170	Phosphorylation	ARNGISPTNPTKLQI CCCCCCCCCCCCEEE	47.22	30266825
1173	Phosphorylation	GISPTNPTKLQITEN CCCCCCCCCEEECCC	46.59	30266825

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
728	S	Phosphorylation	Kinase	MAP3K5	Q99683	Uniprot
728	S	Phosphorylation	Kinase	RIPK1	Q13546	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
728	S	Phosphorylation		17389591
In response to TNF-alpha-induction, phosphorylated at Ser-728; phosphorylation leads to a conformational change, and thus, increases its association with 14-3-3 proteins, MAP3K5, RIPK1 and TRAF2 in endothelial cells; also stimulates regulatory p85 subunit sequestring and PI3K-p85 complex activity inhibition.

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 DAB2P_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
M3K5_HUMAN	MAP3K5	physical	19903888
P85A_HUMAN	PIK3R1	physical	19903888
AKT1_HUMAN	AKT1	physical	19903888
CUL1_HUMAN	CUL1	physical	24912918
CUL4A_HUMAN	CUL4A	physical	24912918
SKP1_HUMAN	SKP1	physical	24912918
RBX1_HUMAN	RBX1	physical	24912918
FBXW7_HUMAN	FBXW7	physical	24912918
M3K5_HUMAN	MAP3K5	physical	15310755
M3K5_HUMAN	MAP3K5	physical	24985705
ANS1A_HUMAN	ANKS1A	physical	28514442
CLIP1_HUMAN	CLIP1	physical	28514442
CRCM_HUMAN	MCC	physical	28514442
CING_HUMAN	CGN	physical	28514442
SNX17_HUMAN	SNX17	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 DAB2P_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-747, AND MASSSPECTROMETRY.	19690332 [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-992 AND SER-995, ANDMASS SPECTROMETRY.	18669648 [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-1168, AND MASSSPECTROMETRY.	19007248 [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-702, AND MASSSPECTROMETRY.	16964243 [Abstract]

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