dbPTM

CAV2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CAV2_HUMAN
UniProt AC	P51636
Protein Name	Caveolin-2
Gene Name	CAV2
Organism	Homo sapiens (Human).
Sequence Length	162
Subcellular Localization	Nucleus. Cytoplasm. Golgi apparatus membrane Peripheral membrane protein. Cell membrane Peripheral membrane protein. Membrane, caveola Peripheral membrane protein. Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr
Protein Description	May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity)..
Protein Sequence	MGLETEKADVQLFMDDDSYSHHSGLEYADPEKFADSDQDRDPHRLNSHLKLGFEDVIAEPVTTHSFDKVWICSHALFEISKYVMYKFLTVFLAIPLAFIAGILFATLSCLHIWILMPFVKTCLMVLPSVQTIWKSVTDVIIAPLCTSVGRCFSSVSLQLSQD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MGLETEKADVQL ---CCCCCCCCCEEE	48.07	29396449
5 (in isoform 2)	Phosphorylation	-	48.07	24719451
6 (in isoform 2)	Phosphorylation	-	36.55	27642862
7	Ubiquitination	-MGLETEKADVQLFM -CCCCCCCCCEEEEC	58.25	-
7 (in isoform 2)	Phosphorylation	-	58.25	27642862
10 (in isoform 2)	Phosphorylation	-	6.78	25056879
14 (in isoform 2)	Phosphorylation	-	8.20	27642862
18	Phosphorylation	QLFMDDDSYSHHSGL EEECCCCCCCCCCCC	35.21	22322096
18 (in isoform 3)	Phosphorylation	-	35.21	-
19	Phosphorylation	LFMDDDSYSHHSGLE EECCCCCCCCCCCCC	21.01	22322096
19 (in isoform 3)	Phosphorylation	-	21.01	-
20 (in isoform 3)	Phosphorylation	-	20.76	-
20	Phosphorylation	FMDDDSYSHHSGLEY ECCCCCCCCCCCCCC	20.76	22322096
23 (in isoform 3)	Phosphorylation	-	39.38	-
23	Phosphorylation	DDSYSHHSGLEYADP CCCCCCCCCCCCCCH	39.38	22322096
27	Phosphorylation	SHHSGLEYADPEKFA CCCCCCCCCCHHHHC	22.73	22322096
27 (in isoform 3)	Phosphorylation	-	22.73	-
36	Phosphorylation	DPEKFADSDQDRDPH CHHHHCCCCCCCCHH	33.47	29255136
36 (in isoform 3)	Phosphorylation	-	33.47	29743597
47	Phosphorylation	RDPHRLNSHLKLGFE CCHHHHHHHHHCCCC	34.49	29514088
50	Ubiquitination	HRLNSHLKLGFEDVI HHHHHHHHCCCCHHC	40.93	-
121	Phosphorylation	ILMPFVKTCLMVLPS HHHHHHHHHHHHCHH	12.93	20068231
128	Phosphorylation	TCLMVLPSVQTIWKS HHHHHCHHHHHHHHH	23.77	20068231
131	Phosphorylation	MVLPSVQTIWKSVTD HHCHHHHHHHHHHHH	27.01	20068231
135	Phosphorylation	SVQTIWKSVTDVIIA HHHHHHHHHHHHHHH	18.43	22817900
145	S-palmitoylation	DVIIAPLCTSVGRCF HHHHHHHCCCHHHHH	2.31	29575903
151	S-palmitoylation	LCTSVGRCFSSVSLQ HCCCHHHHHHHHHHH	2.97	29575903

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
19	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
19	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
23	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
27	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
36	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
23	S	Phosphorylation	18081315
CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae.
36	S	Phosphorylation	18081315
Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells (By similarity).
727	S	Phosphorylation	-
Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation of STAT3 and its activation.

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 CAV2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAV1_HUMAN	CAV1	physical	12414992
CAV1_HUMAN	CAV1	physical	9361015
SRC_HUMAN	SRC	physical	12091389
NCK1_HUMAN	NCK1	physical	12091389
RASA1_HUMAN	RASA1	physical	12091389
DNJA1_HUMAN	DNAJA1	physical	21900206
KCMA1_HUMAN	KCNMA1	physical	15703204
PGH1_HUMAN	PTGS1	physical	15230350
EGFR_HUMAN	EGFR	physical	15273741

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 CAV2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Serine 23 and 36 phosphorylation of caveolin-2 is differentiallyregulated by targeting to lipid raft/caveolae and in mitoticendothelial cells."; Sowa G., Xie L., Xu L., Sessa W.C.; Biochemistry 47:101-111(2008). Cited for: PHOSPHORYLATION AT SER-23 AND SER-36, FUNCTION, SUBCELLULAR LOCATION,AND MUTAGENESIS OF SER-23 AND SER-36.	18081315 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19; SER-20; SER-23;TYR-27 AND SER-36, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Tyrosine phosphorylation of caveolin-2 at residue 27: differences inthe spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)."; Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W.,Campos-Gonzalez R., Lisanti M.P.; Biochemistry 43:13694-13706(2004). Cited for: PHOSPHORYLATION AT TYR-19 AND TYR-27, SUBCELLULAR LOCATION,INTERACTION WITH CAV1; NCK1; RASA1 AND SRC, FUNCTION, AND MUTAGENESISOF TYR-19 AND TYR-27.	15504032 [Abstract]
"Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remainsassociated with lipid rafts/caveolae, but no longer forms a highmolecular mass hetero-oligomer with caveolin-1."; Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E.,Lisanti M.P.; J. Biol. Chem. 277:34556-34567(2002). Cited for: PHOSPHORYLATION AT TYR-19, SUBCELLULAR LOCATION, AND INTERACTION WITHCAV1; SRC; RASA1 AND NCK1.	12091389 [Abstract]

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