VANG2_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VANG2_RAT
• UniProt AC: P84889
• Protein Name: Vang-like protein 2
• Gene Name: Vangl2 {ECO:0000312|RGD:1309442}
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 521
• Subcellular Localization: Cell membrane; Multi-pass membrane protein.
• Protein Description: Involved in the control of early morphogenesis and patterning of both axial midline structures and the development of neural plate. Plays a role in the regulation of planar cell polarity, particularly in the orientation of stereociliary bundles in the cochlea. Required for polarization and movement of myocardializing cells in the outflow tract and seems to act via RHOA signaling to regulate this process. Required for cell surface localization of FZD3 and FZD6 in the inner ear (By similarity)..
• Protein Sequence: MDTESQYSGYSYKSGHSRSSRKHRDRRDRHRSKSRDGSRGDKSVTIQAPGEPLLDNESTRGDERDDNWGETTTVVTGTSEHSISHDDLTRIAKDMEDSVPLDCSRHLGVAAGAILALLSFLTPLAFLLLPPLLWREELEPCGTACEGLFISVAFKLLILLLGSWALFFRRPKASLPRVFVLRALLMVLVFLLVISYWLFYGVRILDARERSYQGVVQFAVSLVDALLFVHYLAVVLLELRQLQPQFTLKVVRSTDGASRFYNVGHLSIQRVAVWILEKYYHDFPVYNPALLNLPKSVLAKKVSGFKVYSLGEENSTNNSTGQSRAVIAAAARRRDNSHNEYYYEEAEHERRVRKRRARLVVAVEEAFTHIKRLQEEEQKNPREVMDPREAAQAIFASMARAMQKYLRTTKQQPYHTMESILQHLEFCITHDMTPKAFLERYLAAGPTIQYHKERWLAKQWTLVSEEPVTNGLKDGIVFLLKRQDFSLVVSTKKVPFFKLSEEFVDPKSHKFVMRLQSETSV

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
58	Phosphorylation	EPLLDNESTRGDERD CCCCCCCCCCCCCCC	29.65	27097102
59	Phosphorylation	PLLDNESTRGDERDD CCCCCCCCCCCCCCC	32.28	27097102
71	Phosphorylation	RDDNWGETTTVVTGT CCCCCCCCEEEEEEC	24.67	27097102
72	Phosphorylation	DDNWGETTTVVTGTS CCCCCCCEEEEEECC	17.19	27097102
73	Phosphorylation	DNWGETTTVVTGTSE CCCCCCEEEEEECCC	22.02	27097102
76	Phosphorylation	GETTTVVTGTSEHSI CCCEEEEEECCCCCC	30.33	27097102
78	Phosphorylation	TTTVVTGTSEHSISH CEEEEEECCCCCCCH	22.90	27097102
79	Phosphorylation	TTVVTGTSEHSISHD EEEEEECCCCCCCHH	34.36	27097102
82	Phosphorylation	VTGTSEHSISHDDLT EEECCCCCCCHHHHH	23.02	27097102
84	Phosphorylation	GTSEHSISHDDLTRI ECCCCCCCHHHHHHH	24.71	27097102
89	Phosphorylation	SISHDDLTRIAKDME CCCHHHHHHHHHHCC	27.33	27097102
308	Phosphorylation	KVSGFKVYSLGEENS HCCCCEEEECCCCCC	9.96	27097102
309	Phosphorylation	VSGFKVYSLGEENST CCCCEEEECCCCCCC	32.65	27097102
315	Phosphorylation	YSLGEENSTNNSTGQ EECCCCCCCCCCCHH	35.47	27097102
316	Phosphorylation	SLGEENSTNNSTGQS ECCCCCCCCCCCHHH	50.42	27097102
319	Phosphorylation	EENSTNNSTGQSRAV CCCCCCCCCHHHHHH	35.66	27097102
320	Phosphorylation	ENSTNNSTGQSRAVI CCCCCCCCHHHHHHH	41.17	27097102
507	Ubiquitination	SEEFVDPKSHKFVMR CHHHCCCCCCCHHHH	61.81	-
519	Phosphorylation	VMRLQSETSV----- HHHHHHCCCC-----	39.78	28551015
520	Phosphorylation	MRLQSETSV------ HHHHHCCCC------	23.06	28551015

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of VANG2_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of VANG2_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of VANG2_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of VANG2_RAT !!

Drug and Disease Associations

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