WHAMM_HUMAN - dbPTM
WHAMM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WHAMM_HUMAN
UniProt AC Q8TF30
Protein Name WASP homolog-associated protein with actin, membranes and microtubules
Gene Name WHAMM
Organism Homo sapiens (Human).
Sequence Length 809
Subcellular Localization Cytoplasm . Endoplasmic reticulum-Golgi intermediate compartment . Cytoplasmic vesicle membrane . Golgi apparatus, cis-Golgi network . Localized to a perinuclear compartment near the microtubule-organizing center (MTOC). Also detected on tubulo-vesic
Protein Description Acts as a nucleation-promoting factor (NPF) that stimulates Arp2/3-mediated actin polymerization both at the Golgi apparatus and along tubular membranes. Its activity in membrane tubulation requires F-actin and interaction with microtubules. Proposed to use coordinated actin-nucleating and microtubule-binding activities of distinct WHAMM molecules to drive membrane tubule elongation; when MT-bound can recruit and remodel membrane vesicles but is prevented to activate the Arp2/3 complex. Involved as a regulator of Golgi positioning and morphology. Participates in vesicle transport between the reticulum endoplasmic and the Golgi complex. Required for RhoD-dependent actin reorganization such as in cell adhesion and cell migration..
Protein Sequence MEDEQPDSLEGWVPVREGLFAEPERHRLRFLVAWNGAEGKFAVTCHDRTAQQRRLREGARLGPEPEPKPEAAVSPSSWAGLLSAAGLRGAHRQLAALWPPLERCFPRLPPELDVGGGGAWGLGLGLWALLWPTRAGPGEAALQELCGQLERYLGAAADGCGGATVRDALFPAEGGAADCESPREFRERALRARWVEADARLRQVIQGHGKANTMVALMNVYQEEDEAYQELVTVATMFFQYLLQPFRAMREVATLCKLDILKSLDEDDLGPRRVVALEKEAEEWTRRAEEAVVSIQDITVNYFKETVKALAGMQKEMEQDAKRFGQAAWATAIPRLEKLQLMLARETLQLMRAKELCLNHKRAEIQGKMEDLPEQEKNTNVVDELEIQFYEIQLELYEVKFEILKNEEILLTTQLDSLKRLIKEKQDEVVYYDPCENPEELKVIDCVVGLQDDKNLEVKELRRQCQQLESKRGRICAKRASLRSRKDQCKENHRFRLQQAEESIRYSRQHHSIQMKRDKIKEEEQKKKEWINQERQKTLQRLRSFKDKRLAQSVRNTSGSEPVAPNLPSDLSQQMCLPASHAVSVIHPSSRKTRGVPLSEAGNVKSPKCQNCHGNIPVQVFVPVGDQTHSKSSEELSLPPPPPPPPPPPPPPPPPPPPLRALSSSSQAATHQNLGFRAPVKDDQPRPLVCESPAERPRDSLESFSCPGSMDEVLASLRHGRAPLRKVEVPAVRPPHASINEHILAAIRQGVKLKKVHPDLGPNPSSKPTSNRRTSDLERSIKAALQRIKRVSADSEEDSDEQDPGQWDG
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
8PhosphorylationMEDEQPDSLEGWVPV
CCCCCCCCCCCCEEC		34.7024850871
181PhosphorylationGGAADCESPREFRER
CCCCCCCCHHHHHHH		35.2721815630
262UbiquitinationLCKLDILKSLDEDDL
HHHHHHHHCCCCCCC		49.6729967540
279UbiquitinationRRVVALEKEAEEWTR
HHEEEHHHHHHHHHH		64.1729967540
299PhosphorylationVVSIQDITVNYFKET
EEEHHHHHHHHHHHH		15.81-
302PhosphorylationIQDITVNYFKETVKA
HHHHHHHHHHHHHHH		16.22-
354UbiquitinationTLQLMRAKELCLNHK
HHHHHHHHHHHHHHH		40.6329967540
419UbiquitinationTTQLDSLKRLIKEKQ
HHCHHHHHHHHHHCC		49.4629967540
431PhosphorylationEKQDEVVYYDPCENP
HCCCCEEEECCCCCH		13.8128796482
432PhosphorylationKQDEVVYYDPCENPE
CCCCEEEECCCCCHH		11.2028796482
459UbiquitinationDDKNLEVKELRRQCQ
CCCCHHHHHHHHHHH		41.4729967540
470PhosphorylationRQCQQLESKRGRICA
HHHHHHHHHHHHHHH		35.9224719451
481PhosphorylationRICAKRASLRSRKDQ
HHHHHHHHHHCCHHH		28.48-
544PhosphorylationKTLQRLRSFKDKRLA
HHHHHHHHHCCHHHH		41.04-
593PhosphorylationIHPSSRKTRGVPLSE
ECCCCCCCCCCCHHH		31.39-
594MethylationHPSSRKTRGVPLSEA
CCCCCCCCCCCHHHC		47.34115920057
599PhosphorylationKTRGVPLSEAGNVKS
CCCCCCHHHCCCCCC		21.2326437602
606PhosphorylationSEAGNVKSPKCQNCH
HHCCCCCCCCCCCCC		25.8818669648
663PhosphorylationPPPLRALSSSSQAAT
CCCCHHCCCCCCCCC		27.4729978859
664PhosphorylationPPLRALSSSSQAATH
CCCHHCCCCCCCCCC		34.5529978859
665PhosphorylationPLRALSSSSQAATHQ
CCHHCCCCCCCCCCC		24.0829978859
666PhosphorylationLRALSSSSQAATHQN
CHHCCCCCCCCCCCC		26.2829978859
670PhosphorylationSSSSQAATHQNLGFR
CCCCCCCCCCCCCCC		27.3227080861
692PhosphorylationPRPLVCESPAERPRD
CCCCEECCCCCCCCC		25.0425159151
716PhosphorylationSMDEVLASLRHGRAP
CHHHHHHHHHCCCCC		23.0624719451
765PhosphorylationPDLGPNPSSKPTSNR
CCCCCCCCCCCCCCC		58.6024719451
774PhosphorylationKPTSNRRTSDLERSI
CCCCCCCCHHHHHHH		24.2926699800
775PhosphorylationPTSNRRTSDLERSIK
CCCCCCCHHHHHHHH		38.0826699800
782UbiquitinationSDLERSIKAALQRIK
HHHHHHHHHHHHHHH		28.9329967540
792PhosphorylationLQRIKRVSADSEEDS
HHHHHHHCCCCCCCC		30.3223090842
795PhosphorylationIKRVSADSEEDSDEQ
HHHHCCCCCCCCCCC		42.4722199227
799PhosphorylationSADSEEDSDEQDPGQ
CCCCCCCCCCCCCCC		46.4520363803
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

Oops, there are no upstream regulatory protein records of WHAMM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WHAMM_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 WHAMM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of WHAMM_HUMAN !!
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 WHAMM_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-606, AND MASSSPECTROMETRY.

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