dbPTM

WASP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	WASP_HUMAN
UniProt AC	P42768
Protein Name	Wiskott-Aldrich syndrome protein
Gene Name	WAS
Organism	Homo sapiens (Human).
Sequence Length	502
Subcellular Localization	Cytoplasm, cytoskeleton.
Protein Description	Effector protein for Rho-type GTPases. Regulates actin filament reorganization via its interaction with the Arp2/3 complex. Important for efficient actin polymerization. Possible regulator of lymphocyte and platelet function. Mediates actin filament reorganization and the formation of actin pedestals upon infection by pathogenic bacteria..
Protein Sequence	MSGGPMGGRPGGRGAPAVQQNIPSTLLQDHENQRLFEMLGRKCLTLATAVVQLYLALPPGAEHWTKEHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFFHTFAGDDCQAGLNFADEDEAQAFRALVQEKIQKRNQRQSGDRRQLPPPPTPANEERRGGLPPLPLHPGGDQGGPPVGPLSLGLATVDIQNPDITSSRYRGLPAPGPSPADKKRSGKKKISKADIGAPSGFKHVSHVGWDPQNGFDVNNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFIEDQGGLEAVRQEMRRQEPLPPPPPPSRGGNQLPRPPIVGGNKGRSGPLPPVPLGIAPPPPTPRGPPPPGRGGPPPPPPPATGRSGPLPPPPPGAGGPPMPPPPPPPPPPPSSGNGPAPPPLPPALVPAGGLAPGGGRGALLDQIRQGIQLNKTPGAPESSALQPPPQSSEGLVGALMHVMQKRSRAIHSSDEGEDQAGDEDEDDEWDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGGPMGGR ------CCCCCCCCC	53.08	23401153
45	Phosphorylation	MLGRKCLTLATAVVQ HHHHHHHHHHHHHHH	24.66	20049867
54	Phosphorylation	ATAVVQLYLALPPGA HHHHHHHHHHCCCCC	3.48	20049867
76	Sumoylation	CGAVCFVKDNPQKSY CCCEEEECCCCCCEE	31.38	-
76	Ubiquitination	CGAVCFVKDNPQKSY CCCEEEECCCCCCEE	31.38	-
76	Sumoylation	CGAVCFVKDNPQKSY CCCEEEECCCCCCEE	31.38	-
81	Ubiquitination	FVKDNPQKSYFIRLY EECCCCCCEEEEEHH	48.67	-
83	Phosphorylation	KDNPQKSYFIRLYGL CCCCCCEEEEEHHHH	15.29	-
88	Phosphorylation	KSYFIRLYGLQAGRL CEEEEEHHHHHHHHH	13.12	30257219
102	Phosphorylation	LLWEQELYSQLVYST HHHHHHHHHHHHHCC	8.13	-
144	Sumoylation	FRALVQEKIQKRNQR HHHHHHHHHHHHHHH	33.09	-
144	Ubiquitination	FRALVQEKIQKRNQR HHHHHHHHHHHHHHH	33.09	21890473
144	Sumoylation	FRALVQEKIQKRNQR HHHHHHHHHHHHHHH	33.09	-
147	Acetylation	LVQEKIQKRNQRQSG HHHHHHHHHHHHHCC	57.71	25953088
147	Sumoylation	LVQEKIQKRNQRQSG HHHHHHHHHHHHHCC	57.71	-
147	Sumoylation	LVQEKIQKRNQRQSG HHHHHHHHHHHHHCC	57.71	-
147	Ubiquitination	LVQEKIQKRNQRQSG HHHHHHHHHHHHHCC	57.71	-
194	Phosphorylation	GPPVGPLSLGLATVD CCCCCCCEEEEEEEE	24.43	29438985
210	Phosphorylation	QNPDITSSRYRGLPA CCCCCCCCCCCCCCC	25.36	29438985
212	Phosphorylation	PDITSSRYRGLPAPG CCCCCCCCCCCCCCC	15.81	27155012
221	Phosphorylation	GLPAPGPSPADKKRS CCCCCCCCHHHHCCC	38.34	23401153
234	Phosphorylation	RSGKKKISKADIGAP CCCCCCCCHHHCCCC	30.58	30108239
235	Ubiquitination	SGKKKISKADIGAPS CCCCCCCHHHCCCCC	54.26	-
277	Phosphorylation	LFSRAGISEAQLTDA HHHHHCCCHHHCCCH	26.43	28450419
282	Phosphorylation	GISEAQLTDAETSKL CCCHHHCCCHHHHHH	22.53	28450419
286	Phosphorylation	AQLTDAETSKLIYDF HHCCCHHHHHHHHHH	32.65	28450419
287	Phosphorylation	QLTDAETSKLIYDFI HCCCHHHHHHHHHHH	19.57	28450419
291	Phosphorylation	AETSKLIYDFIEDQG HHHHHHHHHHHHHCC	18.42	16472662
320	Phosphorylation	LPPPPPPSRGGNQLP CCCCCCCCCCCCCCC	49.70	-
321	Methylation	PPPPPPSRGGNQLPR CCCCCCCCCCCCCCC	63.91	115385621
328	Methylation	RGGNQLPRPPIVGGN CCCCCCCCCCCCCCC	59.21	115385627
338	Methylation	IVGGNKGRSGPLPPV CCCCCCCCCCCCCCC	39.80	52723715
339	Phosphorylation	VGGNKGRSGPLPPVP CCCCCCCCCCCCCCC	54.13	27080861
355	Phosphorylation	GIAPPPPTPRGPPPP CCCCCCCCCCCCCCC	31.24	27080861
357	Methylation	APPPPTPRGPPPPGR CCCCCCCCCCCCCCC	73.12	115391857
357	Dimethylation	APPPPTPRGPPPPGR CCCCCCCCCCCCCCC	73.12	-
364	Methylation	RGPPPPGRGGPPPPP CCCCCCCCCCCCCCC	53.31	16287795
364	Dimethylation	RGPPPPGRGGPPPPP CCCCCCCCCCCCCCC	53.31	-
377	Methylation	PPPPATGRSGPLPPP CCCCCCCCCCCCCCC	33.80	115391853
431	Methylation	GLAPGGGRGALLDQI CCCCCCCHHHHHHHH	30.41	115385633
439	Methylation	GALLDQIRQGIQLNK HHHHHHHHHHHCCCC	24.04	115385639
483	Phosphorylation	KRSRAIHSSDEGEDQ HHHHHHHCCCCCCCC	33.11	28674151
484	Phosphorylation	RSRAIHSSDEGEDQA HHHHHHCCCCCCCCC	26.06	7753869

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
102	Y	Phosphorylation	Kinase	NPM-ALK	AAA58698	PSP
291	Y	Phosphorylation	Kinase	NPM-ALK	AAA58698	PSP
291	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
291	Y	Phosphorylation	Kinase	TNK2	Q07912	GPS
291	Y	Phosphorylation	Kinase	BTK	Q06187	PhosphoELM
291	Y	Phosphorylation	Kinase	FYN	P06241	Uniprot
291	Y	Phosphorylation	Kinase	HCK	P08631	Uniprot
291	Y	Phosphorylation	Kinase	HCK	P08103	PSP
291	Y	Phosphorylation	Kinase	LCK	P06239	PSP
291	Y	Phosphorylation	Kinase	LYN	P07948	PSP
483	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
483	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
483	S	Phosphorylation	Kinase	CK2	-	Uniprot
484	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
484	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
484	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FYN_HUMAN	FYN	physical	8805332
GRB2_HUMAN	GRB2	physical	9307968
EGFR_HUMAN	EGFR	physical	9307968
FYN_HUMAN	FYN	physical	10532312
VASP_HUMAN	VASP	physical	11598004
WIPF1_HUMAN	WIPF1	physical	9405671
FYB1_HUMAN	FYB	physical	10747096
NCK1_HUMAN	NCK1	physical	10747096
LCP2_HUMAN	LCP2	physical	10747096
CDC42_HUMAN	CDC42	physical	10724160
WIPF2_HUMAN	WIPF2	physical	12213210
RAC1_HUMAN	RAC1	physical	8643625
CDC42_HUMAN	CDC42	physical	8643625
FYN_HUMAN	FYN	physical	7565724
FGR_HUMAN	FGR	physical	7565724
NCK1_HUMAN	NCK1	physical	7565724
ITSN2_HUMAN	ITSN2	physical	11748279
CDC42_HUMAN	CDC42	physical	8625410
RBBP5_HUMAN	RBBP5	physical	20574068
JMJD6_HUMAN	JMJD6	physical	20574068
KDM4A_HUMAN	KDM4A	physical	20574068
KDM6B_HUMAN	KDM6B	physical	20574068
ARPC3_HUMAN	ARPC3	physical	12769847
ARPC4_HUMAN	ARPC4	physical	12769847
ACK1_HUMAN	TNK2	physical	16257963
ARPC2_HUMAN	ARPC2	physical	11943145
CDC42_HUMAN	CDC42	physical	15075243
CBL_HUMAN	CBL	physical	23684068
CBLB_HUMAN	CBLB	physical	23684068
WIPF2_HUMAN	WIPF2	physical	21988832
WIPF1_HUMAN	WIPF1	physical	21988832
FNBP1_HUMAN	FNBP1	physical	16418535
NCK1_HUMAN	NCK1	physical	24287595
NCK2_HUMAN	NCK2	physical	24287595
WIPF1_HUMAN	WIPF1	physical	25416956
NCK2_HUMAN	NCK2	physical	25416956
SRBS2_HUMAN	SORBS2	physical	25416956
APBP2_HUMAN	APPBP2	physical	25416956
ABI3_HUMAN	ABI3	physical	25416956
CIP4_HUMAN	TRIP10	physical	21516116
GAS7_HUMAN	GAS7	physical	26506240
SAE1_HUMAN	SAE1	physical	26261240
SAE2_HUMAN	UBA2	physical	26261240
UBC9_HUMAN	UBE2I	physical	26261240
RBP2_HUMAN	RANBP2	physical	26261240
TF65_HUMAN	RELA	physical	26261240
ALDOA_RABIT	ALDOA	physical	20129922
CDC42_HUMAN	CDC42	physical	28539360

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
301000	Wiskott-Aldrich syndrome (WAS)
313900	Thrombocytopenia 1 (THC1)
300299	Neutropenia, severe congenital, X-linked (XLN)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of WASP_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 TYR-291; SER-483 ANDSER-484, AND MASS SPECTROMETRY.	19690332 [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 TYR-291; SER-483 ANDSER-484, AND MASS SPECTROMETRY.	18088087 [Abstract]
"Phosphorylation of the WASP-VCA domain increases its affinity for theArp2/3 complex and enhances actin polymerization by WASP."; Cory G.O.C., Cramer R., Blanchoin L., Ridley A.J.; Mol. Cell 11:1229-1239(2003). Cited for: PHOSPHORYLATION AT SER-483 AND SER-484, AND INTERACTION WITH THEARP2/3 COMPLEX.	12769847 [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-291, AND MASSSPECTROMETRY.	18083107 [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-291, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Fyn and PTP-PEST-mediated regulation of Wiskott-Aldrich syndromeprotein (WASp) tyrosine phosphorylation is required for coupling Tcell antigen receptor engagement to WASp effector function and T cellactivation."; Badour K., Zhang J., Shi F., Leng Y., Collins M., Siminovitch K.A.; J. Exp. Med. 199:99-112(2004). Cited for: PHOSPHORYLATION AT TYR-291 BY FYN.	14707117 [Abstract]
"Phosphorylation of tyrosine 291 enhances the ability of WASp tostimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein."; Cory G.O., Garg R., Cramer R., Ridley A.J.; J. Biol. Chem. 277:45115-45121(2002). Cited for: FUNCTION, PHOSPHORYLATION AT TYR-291 BY HCK, MASS SPECTROMETRY, ANDINTERACTION WITH HCK.	12235133 [Abstract]