dbPTM

VAV_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VAV_HUMAN
UniProt AC	P15498
Protein Name	Proto-oncogene vav
Gene Name	VAV1
Organism	Homo sapiens (Human).
Sequence Length	845
Subcellular Localization
Protein Description	Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation..
Protein Sequence	MELWRQCTHWLIQCRVLPPSHRVTWDGAQVCELAQALRDGVLLCQLLNNLLPHAINLREVNLRPQMSQFLCLKNIRTFLSTCCEKFGLKRSELFEAFDLFDVQDFGKVIYTLSALSWTPIAQNRGIMPFPTEEESVGDEDIYSGLSDQIDDTVEEDEDLYDCVENEEAEGDEIYEDLMRSEPVSMPPKMTEYDKRCCCLREIQQTEEKYTDTLGSIQQHFLKPLQRFLKPQDIEIIFINIEDLLRVHTHFLKEMKEALGTPGAANLYQVFIKYKERFLVYGRYCSQVESASKHLDRVAAAREDVQMKLEECSQRANNGRFTLRDLLMVPMQRVLKYHLLLQELVKHTQEAMEKENLRLALDAMRDLAQCVNEVKRDNETLRQITNFQLSIENLDQSLAHYGRPKIDGELKITSVERRSKMDRYAFLLDKALLICKRRGDSYDLKDFVNLHSFQVRDDSSGDRDNKKWSHMFLLIEDQGAQGYELFFKTRELKKKWMEQFEMAISNIYPENATANGHDFQMFSFEETTSCKACQMLLRGTFYQGYRCHRCRASAHKECLGRVPPCGRHGQDFPGTMKKDKLHRRAQDKKRNELGLPKMEVFQEYYGLPPPPGAIGPFLRLNPGDIVELTKAEAEQNWWEGRNTSTNEIGWFPCNRVKPYVHGPPQDLSVHLWYAGPMERAGAESILANRSDGTFLVRQRVKDAAEFAISIKYNVEVKHIKIMTAEGLYRITEKKAFRGLTELVEFYQQNSLKDCFKSLDTTLQFPFKEPEKRTISRPAVGSTKYFGTAKARYDFCARDRSELSLKEGDIIKILNKKGQQGWWRGEIYGRVGWFPANYVEEDYSEYC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
67	Phosphorylation	VNLRPQMSQFLCLKN HCCCHHHHHHHHHHH	16.72	26546556
73	Ubiquitination	MSQFLCLKNIRTFLS HHHHHHHHHHHHHHH	49.70	-
85	Ubiquitination	FLSTCCEKFGLKRSE HHHHHHHHHCCCHHH	30.71	-
89	Ubiquitination	CCEKFGLKRSELFEA HHHHHCCCHHHHHHH	55.01	-
110	Phosphorylation	QDFGKVIYTLSALSW HHHHHHHHHHHHCCC	12.48	25147952
113	Phosphorylation	GKVIYTLSALSWTPI HHHHHHHHHCCCCCC	21.26	-
142	Phosphorylation	SVGDEDIYSGLSDQI CCCCHHHHCCCHHHC	14.70	10669745
160	Phosphorylation	VEEDEDLYDCVENEE CCCCCCHHHHHHCCC	21.44	10669745
174	Phosphorylation	EAEGDEIYEDLMRSE CCCCCHHHHHHHHCC	11.01	10636924
180	Phosphorylation	IYEDLMRSEPVSMPP HHHHHHHCCCCCCCC	32.08	24275569
188	Ubiquitination	EPVSMPPKMTEYDKR CCCCCCCCCCHHHHH	53.21	-
192	Phosphorylation	MPPKMTEYDKRCCCL CCCCCCHHHHHHCHH	20.00	-
194	Acetylation	PKMTEYDKRCCCLRE CCCCHHHHHHCHHHH	46.57	23749302
194	Ubiquitination	PKMTEYDKRCCCLRE CCCCHHHHHHCHHHH	46.57	-
208	Ubiquitination	EIQQTEEKYTDTLGS HHHHHHHHHHHHHHH	47.41	-
212	Phosphorylation	TEEKYTDTLGSIQQH HHHHHHHHHHHHHHH	25.81	28450419
215	Phosphorylation	KYTDTLGSIQQHFLK HHHHHHHHHHHHHHH	21.97	28450419
220	Acetylation	LGSIQQHFLKPLQRF HHHHHHHHHHHHHHH	9.01	19608861
222	Ubiquitination	SIQQHFLKPLQRFLK HHHHHHHHHHHHHCC	42.62	21890473
222	Ubiquitination	SIQQHFLKPLQRFLK HHHHHHHHHHHHHCC	42.62	21906983
222	Acetylation	SIQQHFLKPLQRFLK HHHHHHHHHHHHHCC	42.62	23749302
252	Acetylation	RVHTHFLKEMKEALG HHHHHHHHHHHHHHC	55.61	19608861
255	Ubiquitination	THFLKEMKEALGTPG HHHHHHHHHHHCCCC	40.71	-
267	Phosphorylation	TPGAANLYQVFIKYK CCCCHHHHHHHHHHH	11.48	20090780
272	Ubiquitination	NLYQVFIKYKERFLV HHHHHHHHHHHHHHH	38.51	-
280	Phosphorylation	YKERFLVYGRYCSQV HHHHHHHCCHHHHHH	9.68	18083107
283	Phosphorylation	RFLVYGRYCSQVESA HHHHCCHHHHHHHHH	7.65	26552605
285	Phosphorylation	LVYGRYCSQVESASK HHCCHHHHHHHHHHH	28.46	26552605
289	Phosphorylation	RYCSQVESASKHLDR HHHHHHHHHHHHHHH	38.70	26552605
291	Phosphorylation	CSQVESASKHLDRVA HHHHHHHHHHHHHHH	29.86	26552605
292	Ubiquitination	SQVESASKHLDRVAA HHHHHHHHHHHHHHH	48.15	-
307	Ubiquitination	AREDVQMKLEECSQR HHHHHHHHHHHHHHH	35.34	21890473
307	Acetylation	AREDVQMKLEECSQR HHHHHHHHHHHHHHH	35.34	25953088
321	Phosphorylation	RANNGRFTLRDLLMV HHHCCCCCHHHHHHH	21.37	24719451
335	Ubiquitination	VPMQRVLKYHLLLQE HHHHHHHHHHHHHHH	27.97	21890473
345	Ubiquitination	LLLQELVKHTQEAME HHHHHHHHHHHHHHH	54.26	-
345	Acetylation	LLLQELVKHTQEAME HHHHHHHHHHHHHHH	54.26	7374163
353	Ubiquitination	HTQEAMEKENLRLAL HHHHHHHHHHHHHHH	38.53	21890473
374	Ubiquitination	AQCVNEVKRDNETLR HHHHHHHHCCHHHHH	48.10	21890473
396	Phosphorylation	SIENLDQSLAHYGRP EEEHHHHHHHHHCCC	27.47	-
404	Ubiquitination	LAHYGRPKIDGELKI HHHHCCCCCCCEEEE	52.66	-
410	Ubiquitination	PKIDGELKITSVERR CCCCCEEEEEEHHHH	39.37	21890473
423	Phosphorylation	RRSKMDRYAFLLDKA HHHCCHHHHHHHHHH	9.46	28796482
429	Ubiquitination	RYAFLLDKALLICKR HHHHHHHHHHHHHHH	40.69	-
435	Ubiquitination	DKALLICKRRGDSYD HHHHHHHHHCCCCCC	37.83	-
435	Acetylation	DKALLICKRRGDSYD HHHHHHHHHCCCCCC	37.83	25953088
444	Acetylation	RGDSYDLKDFVNLHS CCCCCCHHHHCEEEE	46.34	25953088
444	Ubiquitination	RGDSYDLKDFVNLHS CCCCCCHHHHCEEEE	46.34	21890473
465	Ubiquitination	SSGDRDNKKWSHMFL CCCCCCCCCEEEEEE	60.97	-
487	Acetylation	QGYELFFKTRELKKK CCEEEEEEHHHHHHH	39.06	30593339
541	Phosphorylation	MLLRGTFYQGYRCHR HHHHCCCCCCCCCCC	10.81	-
555	Ubiquitination	RCRASAHKECLGRVP CCCHHHCHHHHCCCC	50.25	-
574	Phosphorylation	HGQDFPGTMKKDKLH CCCCCCCCCCHHHHH	26.51	30576142
576	Ubiquitination	QDFPGTMKKDKLHRR CCCCCCCCHHHHHHH	58.62	-
577	Ubiquitination	DFPGTMKKDKLHRRA CCCCCCCHHHHHHHH	49.63	-
588	Ubiquitination	HRRAQDKKRNELGLP HHHHHHHHHHCCCCC	69.60	-
603	Phosphorylation	KMEVFQEYYGLPPPP HHHHHHHHHCCCCCC	7.64	-
629	Ubiquitination	GDIVELTKAEAEQNW CCEEEECHHHHHHCC	57.78	-
683	Phosphorylation	MERAGAESILANRSD HHHCCCHHHHCCCCC	23.51	24670416
684	Acetylation	ERAGAESILANRSDG HHCCCHHHHCCCCCC	2.95	19608861
700	Ubiquitination	FLVRQRVKDAAEFAI EEEEEHHHHHHHHHH	43.78	-
716	Ubiquitination	IKYNVEVKHIKIMTA EEEEEEEEEEEEEEH	26.55	19608861
716	Acetylation	IKYNVEVKHIKIMTA EEEEEEEEEEEEEEH	26.55	19608861
722	Phosphorylation	VKHIKIMTAEGLYRI EEEEEEEEHHHHHHH	25.65	29449344
727	Phosphorylation	IMTAEGLYRITEKKA EEEHHHHHHHHHHHH	15.72	29449344
732	Ubiquitination	GLYRITEKKAFRGLT HHHHHHHHHHHCCHH	40.53	-
732	Acetylation	GLYRITEKKAFRGLT HHHHHHHHHHHCCHH	40.53	7306861
733	Acetylation	LYRITEKKAFRGLTE HHHHHHHHHHCCHHH	46.67	7306871
745	Phosphorylation	LTELVEFYQQNSLKD HHHHHHHHHHCCHHH	8.83	20028078
751	Ubiquitination	FYQQNSLKDCFKSLD HHHHCCHHHHHHHCC	52.88	21890473
755	Ubiquitination	NSLKDCFKSLDTTLQ CCHHHHHHHCCCCCC	57.34	-
756	Phosphorylation	SLKDCFKSLDTTLQF CHHHHHHHCCCCCCC	15.95	30108239
759	Phosphorylation	DCFKSLDTTLQFPFK HHHHHCCCCCCCCCC	34.40	30108239
760	Phosphorylation	CFKSLDTTLQFPFKE HHHHCCCCCCCCCCC	20.44	30108239
766	Ubiquitination	TTLQFPFKEPEKRTI CCCCCCCCCCCCCCC	73.01	-
770	Ubiquitination	FPFKEPEKRTISRPA CCCCCCCCCCCCCCC	66.61	-
774	Phosphorylation	EPEKRTISRPAVGST CCCCCCCCCCCCCCC	31.44	-
780	Phosphorylation	ISRPAVGSTKYFGTA CCCCCCCCCCCCCCC	18.35	29978859
781	Phosphorylation	SRPAVGSTKYFGTAK CCCCCCCCCCCCCCH	24.68	29978859
782	Acetylation	RPAVGSTKYFGTAKA CCCCCCCCCCCCCHH	40.04	25953088
782	Ubiquitination	RPAVGSTKYFGTAKA CCCCCCCCCCCCCHH	40.04	-
783	Phosphorylation	PAVGSTKYFGTAKAR CCCCCCCCCCCCHHH	13.82	-
786	Phosphorylation	GSTKYFGTAKARYDF CCCCCCCCCHHHHEE	18.32	-
788	Ubiquitination	TKYFGTAKARYDFCA CCCCCCCHHHHEECC	32.98	-
791	Phosphorylation	FGTAKARYDFCARDR CCCCHHHHEECCCCC	20.45	25147952
799	Phosphorylation	DFCARDRSELSLKEG EECCCCCCCCCCCCC	47.37	30108239
802	Phosphorylation	ARDRSELSLKEGDII CCCCCCCCCCCCCEE	33.09	30108239
804	Ubiquitination	DRSELSLKEGDIIKI CCCCCCCCCCCEEEE	57.16	-
810	Ubiquitination	LKEGDIIKILNKKGQ CCCCCEEEEEECCCC	41.28	-
815	Ubiquitination	IIKILNKKGQQGWWR EEEEEECCCCCCEEC	61.96	-
826	Phosphorylation	GWWRGEIYGRVGWFP CEECCEEECEECCEE	8.45	30576142
836	Phosphorylation	VGWFPANYVEEDYSE ECCEEHHHCCCCHHH	16.02	26552605
841	Phosphorylation	ANYVEEDYSEYC--- HHHCCCCHHHHC---	13.49	28796482
842	Phosphorylation	NYVEEDYSEYC---- HHCCCCHHHHC----	34.12	28796482
844	Phosphorylation	VEEDYSEYC------ CCCCHHHHC------	9.49	19605366

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
142	Y	Phosphorylation	Kinase	LCK	P06239	PSP
160	Y	Phosphorylation	Kinase	LCK	P06239	PSP
174	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
174	Y	Phosphorylation	Kinase	LCK	P06239	PSP
267	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:11087752
-	K	Ubiquitination	E3 ubiquitin ligase	SOCS1	O15524	PMID:10747851

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XRCC6_HUMAN	XRCC6	physical	8524317
EZH2_HUMAN	EZH2	physical	8649418
KPCT_HUMAN	PRKCQ	genetic	10725744
KPCT_HUMAN	PRKCQ	physical	10725744
PLCG1_HUMAN	PLCG1	physical	9891995
P85A_HUMAN	PIK3R1	physical	9891995
JUN_HUMAN	JUN	physical	11287617
EPOR_HUMAN	EPOR	physical	9162069
P85A_HUMAN	PIK3R1	physical	9162069
PRLR_HUMAN	PRLR	physical	7768923
3BP2_HUMAN	SH3BP2	physical	11390470
PGFRB_HUMAN	PDGFRB	physical	10938113
EGFR_HUMAN	EGFR	physical	10938113
ABL1_HUMAN	ABL1	physical	11790798
RGAP1_HUMAN	RACGAP1	physical	10748082
KSYK_HUMAN	SYK	physical	8986718
RAF1_HUMAN	RAF1	physical	8900182
MK01_HUMAN	MAPK1	physical	8900182
MP2K1_HUMAN	MAP2K1	physical	8900182
GRB2_HUMAN	GRB2	physical	8900182
KSYK_HUMAN	SYK	physical	8900182
GDIR2_HUMAN	ARHGDIB	physical	10664460
PHAG1_HUMAN	PAG1	physical	10790433
GRB2_HUMAN	GRB2	physical	7809090
CBL_HUMAN	CBL	physical	9200440
KSYK_HUMAN	SYK	physical	11331248
LCP2_HUMAN	LCP2	physical	9047237
PTN6_HUMAN	PTPN6	physical	8632004
SIAH2_HUMAN	SIAH2	physical	10207103
GRB2_HUMAN	GRB2	physical	10207103
MK01_HUMAN	MAPK1	physical	9013873
GRB2_HUMAN	GRB2	physical	9013873
S100B_HUMAN	S100B	physical	10394361
ZAP70_HUMAN	ZAP70	physical	7798261
LCP2_HUMAN	LCP2	physical	8703037
INSR_HUMAN	INSR	physical	7535775
EZH2_HUMAN	EZH2	physical	15882624
SUZ12_HUMAN	SUZ12	physical	15882624
EED_HUMAN	EED	physical	15882624
PHAX_HUMAN	PHAX	physical	21900206
TBA1A_HUMAN	TUBA1A	physical	8530437
TBB5_HUMAN	TUBB	physical	8530437
CBL_HUMAN	CBL	physical	12881521
CBL_HUMAN	CBL	physical	16356860
CBL_HUMAN	CBL	physical	19635790
LCP2_HUMAN	LCP2	physical	19635790
CBL_HUMAN	CBL	physical	16289966
CBLB_HUMAN	CBLB	physical	9399639
CD5_HUMAN	CD5	physical	23376399
SPI1_HUMAN	SPI1	physical	19747912
PLCG1_HUMAN	PLCG1	physical	16467851
FCERB_HUMAN	MS4A2	physical	8900182
KLK7_HUMAN	KLK7	physical	28514442
PLBL1_HUMAN	PLBD1	physical	28514442
NUB1_HUMAN	NUB1	physical	28514442
CYTSA_HUMAN	SPECC1L	physical	28514442
SPA12_HUMAN	SERPINA12	physical	28514442
APLP2_HUMAN	APLP2	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
DR9C7_HUMAN	SDR9C7	physical	28514442
PAI2_HUMAN	SERPINB2	physical	28514442
APBB2_HUMAN	APBB2	physical	28514442
CDSN_HUMAN	CDSN	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
CYTM_HUMAN	CST6	physical	28514442
DNJC1_HUMAN	DNAJC1	physical	28514442
SBSN_HUMAN	SBSN	physical	28514442
DSG1_HUMAN	DSG1	physical	28514442
AT2B2_HUMAN	ATP2B2	physical	28514442
CHK1_HUMAN	CHEK1	physical	28514442

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of VAV_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-222; LYS-252 AND LYS-716,AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-826, AND MASSSPECTROMETRY.	15592455 [Abstract]