dbPTM

CAMKV_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CAMKV_MOUSE
UniProt AC	Q3UHL1
Protein Name	CaM kinase-like vesicle-associated protein
Gene Name	Camkv
Organism	Mus musculus (Mouse).
Sequence Length	512
Subcellular Localization	Cell membrane Peripheral membrane protein. Cytoplasmic vesicle membrane Peripheral membrane protein. Predominantly observed in association with the plasma membrane of soma and in neurites, both axons and dendrites. May be associated with vesicular
Protein Description	Does not appear to have detectable kinase activity..
Protein Sequence	MPFGCVTLGDKKNYNQPSEVTDRYDLGQVIKTEEFCEIFRAKDKTTGKLHTCKKFQKRDGRKVRKAAKNEIGILKMVKHPNILQLVDVFVTRKEYFIFLELATGREVFDWILDQGYYSERDTSNVVRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDFHLAKLENGLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYEEVEEDDYENHDKNLFRKILAGDYEFDSPYWDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWISGNAASDKNIKDGVCAQIEKNFARAKWKKAVRVTTLMKRLRAPEQSGTAATQSASDAATPGAAGGAIAAAAAAAAAGGAASASGASATAATEGGAGCAAKSDDIASADRSATPATDGSATPATDGSVTPATDGSITPATDGSVTPATDRSATPATDGRATPATEESTVPATQSSALPAAKAAATPEPAVAQPDSTALEGATGQAPPSSKGEEATGCAQESQRVETS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	S-palmitoylation	---MPFGCVTLGDKK ---CCCCCEECCCCC	1.85	28680068
5	S-nitrosylation	---MPFGCVTLGDKK ---CCCCCEECCCCC	1.85	24895380
11	Acetylation	GCVTLGDKKNYNQPS CCEECCCCCCCCCCC	40.91	19857947
11	Ubiquitination	GCVTLGDKKNYNQPS CCEECCCCCCCCCCC	40.91	22790023
12	Ubiquitination	CVTLGDKKNYNQPSE CEECCCCCCCCCCCC	70.20	27667366
75	Ubiquitination	KNEIGILKMVKHPNI HHHCCHHHHCCCCCH	39.46	22790023
147	Ubiquitination	KIVHRNLKLENLVYY HHHHCCCCHHHHEEH	58.25	22790023
153	Phosphorylation	LKLENLVYYNRLKNS CCHHHHEEHHCCCCC	9.74	29899451
154	Phosphorylation	KLENLVYYNRLKNSK CHHHHEEHHCCCCCE	6.07	18034455
239	Ubiquitination	HDKNLFRKILAGDYE CCHHHHHHHHHCCCC	34.44	22790023
251	Phosphorylation	DYEFDSPYWDDISQA CCCCCCCCHHHHHHH	25.97	-
294	Ubiquitination	SGNAASDKNIKDGVC CCCCCCCCCCCCCCH	59.06	22790023
320	Phosphorylation	WKKAVRVTTLMKRLR HHHHHHHHHHHHHHC	12.03	22324799
321	Phosphorylation	KKAVRVTTLMKRLRA HHHHHHHHHHHHHCC	23.23	29899451
324	Ubiquitination	VRVTTLMKRLRAPEQ HHHHHHHHHHCCCCC	51.93	27667366
345	Phosphorylation	QSASDAATPGAAGGA CCHHHCCCCCHHHHH	24.79	-
387	Phosphorylation	GAGCAAKSDDIASAD CCCCCCCCCCCCCCC	35.47	20415495
392	Phosphorylation	AKSDDIASADRSATP CCCCCCCCCCCCCCC	30.91	25521595
396	Phosphorylation	DIASADRSATPATDG CCCCCCCCCCCCCCC	36.72	20415495
398	Phosphorylation	ASADRSATPATDGSA CCCCCCCCCCCCCCC	18.07	29899451
401	Phosphorylation	DRSATPATDGSATPA CCCCCCCCCCCCCCC	41.94	20415495
404	Phosphorylation	ATPATDGSATPATDG CCCCCCCCCCCCCCC	31.60	22807455
406	Phosphorylation	PATDGSATPATDGSV CCCCCCCCCCCCCCC	18.36	22807455
409	Phosphorylation	DGSATPATDGSVTPA CCCCCCCCCCCCCCC	41.94	29899451
414	Phosphorylation	PATDGSVTPATDGSI CCCCCCCCCCCCCCC	14.65	19060867
417	Phosphorylation	DGSVTPATDGSITPA CCCCCCCCCCCCCCC	41.94	25521595
420	Phosphorylation	VTPATDGSITPATDG CCCCCCCCCCCCCCC	26.54	22817900
422	Phosphorylation	PATDGSITPATDGSV CCCCCCCCCCCCCCC	14.47	25521595
425	Phosphorylation	DGSITPATDGSVTPA CCCCCCCCCCCCCCC	41.94	22817900
428	Phosphorylation	ITPATDGSVTPATDR CCCCCCCCCCCCCCC	26.15	25521595
430	Phosphorylation	PATDGSVTPATDRSA CCCCCCCCCCCCCCC	14.65	25521595
433	Phosphorylation	DGSVTPATDRSATPA CCCCCCCCCCCCCCC	32.90	29899451
436	Phosphorylation	VTPATDRSATPATDG CCCCCCCCCCCCCCC	39.03	25521595
438	Phosphorylation	PATDRSATPATDGRA CCCCCCCCCCCCCCC	18.07	28382018
441	Phosphorylation	DRSATPATDGRATPA CCCCCCCCCCCCCCC	39.94	25521595
446	Phosphorylation	PATDGRATPATEEST CCCCCCCCCCCCCCC	16.46	25521595
449	Phosphorylation	DGRATPATEESTVPA CCCCCCCCCCCCCCC	41.30	25521595
452	Phosphorylation	ATPATEESTVPATQS CCCCCCCCCCCCCCC	28.59	25521595
453	Phosphorylation	TPATEESTVPATQSS CCCCCCCCCCCCCCC	33.51	25521595
457	O-linked_Glycosylation	EESTVPATQSSALPA CCCCCCCCCCCHHHH	23.94	22517741
457	Phosphorylation	EESTVPATQSSALPA CCCCCCCCCCCHHHH	23.94	24925903
459	Phosphorylation	STVPATQSSALPAAK CCCCCCCCCHHHHHH	17.14	24925903
460	Phosphorylation	TVPATQSSALPAAKA CCCCCCCCHHHHHHH	24.81	24925903
470	Phosphorylation	PAAKAAATPEPAVAQ HHHHHHCCCCCCCCC	24.37	15345747
493	Phosphorylation	ATGQAPPSSKGEEAT CCCCCCCCCCCCCCC	43.56	25521595
511	Phosphorylation	QESQRVETS------ CHHHCCCCC------	36.56	29899451
512	Phosphorylation	ESQRVETS------- HHHCCCCC-------	25.39	29899451

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
345	T	Phosphorylation	Kinase	CDK5	Q00535	PSP
345	T	Phosphorylation	Kinase	CDK5	P49615	PSP

Functions of PTM Sites

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

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 CAMKV_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CAMKV_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of CAMKV_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-414; THR-446; THR-449AND SER-452, AND MASS SPECTROMETRY.	17114649 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-470, AND MASSSPECTROMETRY.	15345747 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-154, AND MASSSPECTROMETRY.	18034455 [Abstract]