dbPTM

WASL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	WASL_HUMAN
UniProt AC	O00401
Protein Name	Neural Wiskott-Aldrich syndrome protein
Gene Name	WASL
Organism	Homo sapiens (Human).
Sequence Length	505
Subcellular Localization	Nucleus . Cytoplasm . Cytoplasm, cytoskeleton . Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated. Exported from the nucleus by an nuclear export signal (NES)-dependent mechanism to the cytoplasm.
Protein Description	Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in mitosis and cytokinesis, via its role in the regulation of actin polymerization. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Plays a role in dendrite spine morphogenesis (By similarity)..
Protein Sequence	MSSVQQQPPPPRRVTNVGSLLLTPQENESLFTFLGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRDPPNGPNLPMATVDIKNPEITTNRFYGPQVNNISHTKEKKKGKAKKKRLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKNELRRQAPPPPPPSRGGPPPPPPPPHNSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPSVAVPPPPPNRMYPPPPPALPSSAPSGPPPPPPSVLGVGPVAPPPPPPPPPPPGPPPPPGLPSDGDHQVPTTAGNKAALLDQIREGAQLKKVEQNSRPVSCSGRDALLDQIRQGIQLKSVADGQESTPPTPAPTSGIVGALMEVMQKRSKAIHSSDEDEDEDDEEDFEDDDEWED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSVQQQPP ------CCCCCCCCC	38.94	19413330
15	Phosphorylation	PPPPRRVTNVGSLLL CCCCCCCCCCCCEEE	23.52	27273156
19	Phosphorylation	RRVTNVGSLLLTPQE CCCCCCCCEEECCCC	16.15	27251275
23	Phosphorylation	NVGSLLLTPQENESL CCCCEEECCCCCCCH	23.93	-
58	Phosphorylation	ADRNCMWSKKCSGVA HCCCCCCCCCCCCEE	8.71	-
62	Phosphorylation	CMWSKKCSGVACLVK CCCCCCCCCEEEEEC	45.22	29759185
95	Phosphorylation	LLWEQELYNNFVYNS EEEEEEHHHCCCCCC	13.80	-
100	Phosphorylation	ELYNNFVYNSPRGYF EHHHCCCCCCCCCEE	13.04	27642862
102	Phosphorylation	YNNFVYNSPRGYFHT HHCCCCCCCCCEEEC	9.78	24719451
132	Malonylation	EEAKKFRKAVTDLLG HHHHHHHHHHHHHHH	50.79	26320211
135	Phosphorylation	KKFRKAVTDLLGRRQ HHHHHHHHHHHHHHH	26.28	-
170	Phosphorylation	DIKNPEITTNRFYGP ECCCCCCCCCCCCCC	19.16	21945579
171	Phosphorylation	IKNPEITTNRFYGPQ CCCCCCCCCCCCCCC	30.02	21945579
175	Phosphorylation	EITTNRFYGPQVNNI CCCCCCCCCCCCCCC	25.34	21945579
183	Phosphorylation	GPQVNNISHTKEKKK CCCCCCCCCCCHHHC	27.51	28985074
185	Phosphorylation	QVNNISHTKEKKKGK CCCCCCCCCHHHCCC	33.82	25159151
186	Ubiquitination	VNNISHTKEKKKGKA CCCCCCCCHHHCCCC	63.21	32015554
205	Phosphorylation	LTKADIGTPSNFQHI CCCCCCCCCCCCCCC	24.71	25159151
207	Phosphorylation	KADIGTPSNFQHIGH CCCCCCCCCCCCCEE	50.55	25627689
242	Phosphorylation	LFDMCGISEAQLKDR HHHHHCCCHHHHCCC	16.50	16257963
251	Phosphorylation	AQLKDRETSKVIYDF HHHCCCCHHHHHHHH	34.44	28152594
252	Phosphorylation	QLKDRETSKVIYDFI HHCCCCHHHHHHHHH	21.85	28152594
253	Ubiquitination	LKDRETSKVIYDFIE HCCCCHHHHHHHHHH	39.82	29967540
256	Phosphorylation	RETSKVIYDFIEKTG CCHHHHHHHHHHHHC	14.05	19664994
261	Ubiquitination	VIYDFIEKTGGVEAV HHHHHHHHHCCHHHH	47.88	29967540
274	Methylation	AVKNELRRQAPPPPP HHHHHHHHCCCCCCC	50.03	115484371
284	Methylation	PPPPPPSRGGPPPPP CCCCCCCCCCCCCCC	60.92	115367429
305	Methylation	GPPPPPARGRGAPPP CCCCCCCCCCCCCCC	40.91	115484361
307	Methylation	PPPPARGRGAPPPPP CCCCCCCCCCCCCCC	32.33	24129315
329	Methylation	PPPPPPSRPSVAVPP CCCCCCCCCCCCCCC	33.03	115484351
426	Phosphorylation	LKKVEQNSRPVSCSG HHCHHHCCCCCCCCC	37.34	29255136
430	Phosphorylation	EQNSRPVSCSGRDAL HHCCCCCCCCCHHHH	12.78	30266825
432	Phosphorylation	NSRPVSCSGRDALLD CCCCCCCCCHHHHHH	29.38	30266825
449	Phosphorylation	RQGIQLKSVADGQES HHCCCCEECCCCCCC	31.00	22199227
456	Phosphorylation	SVADGQESTPPTPAP ECCCCCCCCCCCCCC	38.02	22199227
457	Phosphorylation	VADGQESTPPTPAPT CCCCCCCCCCCCCCC	32.32	22199227
460	Phosphorylation	GQESTPPTPAPTSGI CCCCCCCCCCCCCHH	33.03	22199227
464	Phosphorylation	TPPTPAPTSGIVGAL CCCCCCCCCHHHHHH	41.51	22199227
465	Phosphorylation	PPTPAPTSGIVGALM CCCCCCCCHHHHHHH	26.01	22199227
479	Phosphorylation	MEVMQKRSKAIHSSD HHHHHHHHHHHCCCC	33.21	25072903
484	Phosphorylation	KRSKAIHSSDEDEDE HHHHHHCCCCCCCCC	33.11	28176443
485	Phosphorylation	RSKAIHSSDEDEDED HHHHHCCCCCCCCCC	30.75	28176443

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
242	S	Phosphorylation	Kinase	TNK2	Q07912	Uniprot
256	Y	Phosphorylation	Kinase	ABL2	Q4JIM5	GPS
256	Y	Phosphorylation	Kinase	TNK2	Q07912	Uniprot
256	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS
484	S	Phosphorylation	Kinase	PAK4	O96013	PSP
485	S	Phosphorylation	Kinase	PAK4	O96013	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
242	S	Phosphorylation	16257963
Phosphorylation at Ser-242, Tyr-256, Ser-484 and Ser-485 enhances actin polymerization activity.
484	S	Phosphorylation	20068231
Phosphorylation at Ser-242, Tyr-256, Ser-484 and Ser-485 enhances actin polymerization activity.
485	S	Phosphorylation	20068231
Phosphorylation at Ser-242, Tyr-256, Ser-484 and Ser-485 enhances actin polymerization activity.

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 WASL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRC8_HUMAN	CTTN	physical	11830518
NCK1_HUMAN	NCK1	physical	11340081
RHOQ_HUMAN	RHOQ	physical	12456725
CDC42_HUMAN	CDC42	physical	10781580
GRB2_HUMAN	GRB2	physical	10781580
PROF1_HUMAN	PFN1	physical	9822597
WIPF1_HUMAN	WIPF1	physical	12372256
A4_HUMAN	APP	physical	21832049
WIPF2_HUMAN	WIPF2	physical	22939629
ZN638_HUMAN	ZNF638	physical	22939629
HS90A_BOVIN	HSP90AA1	physical	15791211
HS90B_BOVIN	HSP90AB1	physical	15791211
HS90A_HUMAN	HSP90AA1	physical	15791211
HS90B_HUMAN	HSP90AB1	physical	15791211
ARC1B_HUMAN	ARPC1B	physical	15894313
ARP2_HUMAN	ACTR2	physical	12732638
ARP3_HUMAN	ACTR3	physical	12732638
WIPF1_HUMAN	WIPF1	physical	11331876
ZN395_HUMAN	ZNF395	physical	21988832
GELS_HUMAN	GSN	physical	16531231
RNF8_HUMAN	RNF8	physical	25416956
ARPC3_HUMAN	ARPC3	physical	25416956
RHOJ_HUMAN	RHOJ	physical	25416956
FBP1L_HUMAN	FNBP1L	physical	26344197
CIP4_HUMAN	TRIP10	physical	26344197
WASF1_HUMAN	WASF1	physical	26344197
WASF2_HUMAN	WASF2	physical	26344197
WASF3_HUMAN	WASF3	physical	26344197
RNF8_HUMAN	RNF8	physical	21516116
WIPF2_HUMAN	WIPF2	physical	28514442
WIPF3_HUMAN	WIPF3	physical	28514442
WIPF1_HUMAN	WIPF1	physical	28514442
ATG4C_HUMAN	ATG4C	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
ACY2_HUMAN	ASPA	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 WASL_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-484 AND SER-485, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Phosphorylation of WASP by the Cdc42-associated kinase ACK1: dualhydroxyamino acid specificity in a tyrosine kinase."; Yokoyama N., Lougheed J., Miller W.T.; J. Biol. Chem. 280:42219-42226(2005). Cited for: PHOSPHORYLATION AT SER-242 AND TYR-256 BY TNK2, AND INTERACTION WITHWASL.	16257963 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-256, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-256, AND MASSSPECTROMETRY.	17389395 [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-256, AND MASSSPECTROMETRY.	18083107 [Abstract]

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