WASF1_HUMAN - dbPTM
WASF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WASF1_HUMAN
UniProt AC Q92558
Protein Name Wiskott-Aldrich syndrome protein family member 1
Gene Name WASF1
Organism Homo sapiens (Human).
Sequence Length 559
Subcellular Localization Cytoplasm, cytoskeleton . Cell junction, synapse . Cell junction, focal adhesion . Dot-like pattern in the cytoplasm. Concentrated in Rac-regulated membrane-ruffling areas (PubMed:9889097). Partial translocation to focal adhesion sites might be media
Protein Description Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity)..
Protein Sequence MPLVKRNIDPRHLCHTALPRGIKNELECVTNISLANIIRQLSSLSKYAEDIFGELFNEAHSFSFRVNSLQERVDRLSVSVTQLDPKEEELSLQDITMRKAFRSSTIQDQQLFDRKTLPIPLQETYDVCEQPPPLNILTPYRDDGKEGLKFYTNPSYFFDLWKEKMLQDTEDKRKEKRKQKQKNLDRPHEPEKVPRAPHDRRREWQKLAQGPELAEDDANLLHKHIEVANGPASHFETRPQTYVDHMDGSYSLSALPFSQMSELLTRAEERVLVRPHEPPPPPPMHGAGDAKPIPTCISSATGLIENRPQSPATGRTPVFVSPTPPPPPPPLPSALSTSSLRASMTSTPPPPVPPPPPPPATALQAPAVPPPPAPLQIAPGVLHPAPPPIAPPLVQPSPPVARAAPVCETVPVHPLPQGEVQGLPPPPPPPPLPPPGIRPSSPVTVTALAHPPSGLHPTPSTAPGPHVPLMPPSPPSQVIPASEPKRHPSTLPVISDARSVLLEAIRKGIQLRKVEEQREQEAKHERIENDVATILSRRIAVEYSDSEDDSEFDEVDWLE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
45PhosphorylationIRQLSSLSKYAEDIF
HHHHHHHHHHHHHHH		26.1025999147
61PhosphorylationELFNEAHSFSFRVNS
HHHHHHHHCEEEHHH		29.6324719451
63PhosphorylationFNEAHSFSFRVNSLQ
HHHHHHCEEEHHHHH		18.3724719451
79PhosphorylationRVDRLSVSVTQLDPK
HHHHEEEEEEECCCC		18.9726546556
91PhosphorylationDPKEEELSLQDITMR
CCCCCCCCHHHHHHH		27.5420068231
96PhosphorylationELSLQDITMRKAFRS
CCCHHHHHHHHHHHC		21.1520068231
103PhosphorylationTMRKAFRSSTIQDQQ
HHHHHHHCCCCCCHH		25.9426074081
104PhosphorylationMRKAFRSSTIQDQQL
HHHHHHCCCCCCHHC		25.8526074081
105PhosphorylationRKAFRSSTIQDQQLF
HHHHHCCCCCCHHCC		24.7320363803
116PhosphorylationQQLFDRKTLPIPLQE
HHCCCCCCCCCCCHH		38.3626074081
124PhosphorylationLPIPLQETYDVCEQP
CCCCCHHHHCCCCCC		16.4426074081
125PhosphorylationPIPLQETYDVCEQPP
CCCCHHHHCCCCCCC		12.9626074081
151PhosphorylationGKEGLKFYTNPSYFF
CCCCCEECCCHHHHH		12.2027642862
162UbiquitinationSYFFDLWKEKMLQDT
HHHHHHHHHHHCCCC		55.5422817900
164UbiquitinationFFDLWKEKMLQDTED
HHHHHHHHHCCCCHH		40.9822817900
169PhosphorylationKEKMLQDTEDKRKEK
HHHHCCCCHHHHHHH		32.8723684312
182AcetylationEKRKQKQKNLDRPHE
HHHHHHHHCCCCCCC		67.527978691
192AcetylationDRPHEPEKVPRAPHD
CCCCCCCCCCCCCCH		69.157978701
295PhosphorylationGDAKPIPTCISSATG
CCCCCCCCHHHHCCC		24.1626074081
298PhosphorylationKPIPTCISSATGLIE
CCCCCHHHHCCCCCC		18.9620068231
299PhosphorylationPIPTCISSATGLIEN
CCCCHHHHCCCCCCC		15.2222496350
301PhosphorylationPTCISSATGLIENRP
CCHHHHCCCCCCCCC		34.1722167270
307MethylationATGLIENRPQSPATG
CCCCCCCCCCCCCCC		20.18115919885
310PhosphorylationLIENRPQSPATGRTP
CCCCCCCCCCCCCCC		21.1329255136
313PhosphorylationNRPQSPATGRTPVFV
CCCCCCCCCCCCEEE		30.4929255136
315MethylationPQSPATGRTPVFVSP
CCCCCCCCCCEEECC		31.34115919889
316PhosphorylationQSPATGRTPVFVSPT
CCCCCCCCCEEECCC		25.7526074081
321PhosphorylationGRTPVFVSPTPPPPP
CCCCEEECCCCCCCC		16.1626074081
323PhosphorylationTPVFVSPTPPPPPPP
CCEEECCCCCCCCCC		40.7028555341
333PhosphorylationPPPPPLPSALSTSSL
CCCCCCCCCCCCHHH		49.9126074081
336PhosphorylationPPLPSALSTSSLRAS
CCCCCCCCCHHHCCC		26.4228464451
337PhosphorylationPLPSALSTSSLRASM
CCCCCCCCHHHCCCC		24.1626074081
338PhosphorylationLPSALSTSSLRASMT
CCCCCCCHHHCCCCC		24.8126074081
339PhosphorylationPSALSTSSLRASMTS
CCCCCCHHHCCCCCC		23.2028464451
341Asymmetric dimethylarginineALSTSSLRASMTSTP
CCCCHHHCCCCCCCC		26.94-
341MethylationALSTSSLRASMTSTP
CCCCHHHCCCCCCCC		26.94-
397PhosphorylationAPPLVQPSPPVARAA
CCCCCCCCCCCCCCC		25.4116862120
441PhosphorylationPPGIRPSSPVTVTAL
CCCCCCCCCEEEEEC		26.5216862120
489PhosphorylationSEPKRHPSTLPVISD
CCCCCCCCCCCHHCH		36.1328348404
490PhosphorylationEPKRHPSTLPVISDA
CCCCCCCCCCHHCHH		39.2625690035
533PhosphorylationRIENDVATILSRRIA
HHHHHHHHHHHHHHE		23.4626270265
536PhosphorylationNDVATILSRRIAVEY
HHHHHHHHHHHEEEE		18.7016275905
543PhosphorylationSRRIAVEYSDSEDDS
HHHHEEEECCCCCCC		15.92-
546PhosphorylationIAVEYSDSEDDSEFD
HEEEECCCCCCCCCC		36.66-
550PhosphorylationYSDSEDDSEFDEVDW
ECCCCCCCCCCCCCC		53.11-
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
125YPhosphorylationKinaseSRCP12931
PSP
125YPhosphorylationKinaseSRC64-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WASF1_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 WASF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PROF1_HUMANPFN1physical
9843499
BAIP2_HUMANBAIAP2physical
11130076
ABL1_HUMANABL1physical
18559503
ZC3HF_HUMANZC3H15physical
22939629
KAPCA_HUMANPRKACAphysical
10970852
ABL1_HUMANABL1physical
10970852
KAP2_HUMANPRKAR2Aphysical
10970852
CIP4_HUMANTRIP10physical
25416956
IFT20_HUMANIFT20physical
25416956
FBP1L_HUMANFNBP1Lphysical
26344197
CIP4_HUMANTRIP10physical
26344197
RAC1_HUMANRAC1physical
9843499
ARP3_HUMANACTR3physical
12829704
MAPK2_HUMANMAPKAPK2physical
12829704
CAD23_HUMANCDH23physical
27173435
NCKP1_HUMANNCKAP1physical
27173435
ABI1_HUMANABI1physical
27173435
NXN_HUMANNXNphysical
27173435
AIPL1_HUMANAIPL1physical
27173435
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 WASF1_HUMAN

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Related Literatures of Post-Translational Modification

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