CAV1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CAV1_MOUSE
• UniProt AC: P49817
• Protein Name: Caveolin-1
• Gene Name: Cav1
• Organism: Mus musculus (Mouse).
• Sequence Length: 178
• Subcellular Localization: Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola ; Peripheral membrane protein . Membrane raft . Golgi apparatus, trans-Golgi network . Colocalized with DPP4 in membrane rafts. Poten
• Protein Description: Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation (By similarity). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway. [PubMed: 10816572 Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae]
• Protein Sequence: MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADEVTEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSTIFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPLFEAIGKIFSNIRISTQKEI

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
2	Phosphorylation	------MSGGKYVDS ------CCCCCEECC	57.14	26824392
2	Acetylation	------MSGGKYVDS ------CCCCCEECC	57.14	23806337
5	Acetylation	---MSGGKYVDSEGH ---CCCCCEECCCCC	45.70	23806337
5	Ubiquitination	---MSGGKYVDSEGH ---CCCCCEECCCCC	45.70	22790023
6	Phosphorylation	--MSGGKYVDSEGHL --CCCCCEECCCCCE	16.86	22499769
8	Ubiquitination	MSGGKYVDSEGHLYT CCCCCEECCCCCEEE	37.57	27667366
8 (in isoform 2)	Ubiquitination	-	37.57	-
9	Phosphorylation	SGGKYVDSEGHLYTV CCCCEECCCCCEEEE	35.12	26824392
11 (in isoform 2)	Phosphorylation	-	21.76	29514104
14	Phosphorylation	VDSEGHLYTVPIREQ ECCCCCEEEEEEHHC	10.46	16943184
15	Phosphorylation	DSEGHLYTVPIREQG CCCCCEEEEEEHHCC	26.60	22499769
16 (in isoform 2)	Ubiquitination	-	2.04	-
25	Phosphorylation	IREQGNIYKPNNKAM EHHCCCEECCCCCCC	25.13	23684622
26	Ubiquitination	REQGNIYKPNNKAMA HHCCCEECCCCCCCC	37.16	22790023
26 (in isoform 2)	Ubiquitination	-	37.16	-
30	Ubiquitination	NIYKPNNKAMADEVT CEECCCCCCCCCCCC	46.29	22790023
37	Phosphorylation	KAMADEVTEKQVYDA CCCCCCCCHHHHHHH	35.10	23737553
39	Acetylation	MADEVTEKQVYDAHT CCCCCCHHHHHHHCC	35.38	23806337
39	Succinylation	MADEVTEKQVYDAHT CCCCCCHHHHHHHCC	35.38	23806337
39 (in isoform 2)	Ubiquitination	-	35.38	22790023
39	Ubiquitination	MADEVTEKQVYDAHT CCCCCCHHHHHHHCC	35.38	27667366
42	Phosphorylation	EVTEKQVYDAHTKEI CCCHHHHHHHCCCEE	12.62	21454597
46	Phosphorylation	KQVYDAHTKEIDLVN HHHHHHCCCEEECCC	31.90	21454597
47 (in isoform 2)	Ubiquitination	-	42.69	22790023
47	Ubiquitination	QVYDAHTKEIDLVNR HHHHHCCCEEECCCC	42.69	22790023
57	Ubiquitination	DLVNRDPKHLNDDVV ECCCCCCCCCCCCEE	66.08	22790023
57 (in isoform 2)	Ubiquitination	-	66.08	22790023
133	S-palmitoylation	HIWAVVPCIKSFLIE HHHHHHHHHHHHHHH	4.06	-
143	S-palmitoylation	SFLIEIQCISRVYSI HHHHHHHHHHCHHHH	3.61	-
156	S-palmitoylation	SIYVHTFCDPLFEAI HHHHHHHCHHHHHHH	5.75	28526873
176	Ubiquitination	NIRISTQKEI----- HCCEECCCCC-----	58.42	-

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
14	Y	Phosphorylation	Kinase	ABL1	P00520	Uniprot
14	Y	Phosphorylation	Kinase	INSR	P15208	Uniprot
14	Y	Phosphorylation	Kinase	SRC	P05480	PSP
14	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
14	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CAV1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CAV1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FLOT1_MOUSE	Flot1	physical	12036959
INSR_MOUSE	Insr	physical	12036959
STML3_MOUSE	Stoml3	physical	12122055
ADCY3_MOUSE	Adcy3	physical	12122055
JAK2_MOUSE	Jak2	physical	12388746
PPARG_MOUSE	Pparg	physical	15164767
TRPC4_MOUSE	Trpc4	physical	17416589
ITPR3_MOUSE	Itpr3	physical	17416589
NF1_MOUSE	Nf1	physical	16405917
PRKN_MOUSE	Park2	physical	26627850

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-14, AND MASSSPECTROMETRY.
PubMed: 19131326

"c-Abl is required for oxidative stress-induced phosphorylation ofcaveolin-1 on tyrosine 14.";
Sanguinetti A.R., Mastick C.C.;
Cell. Signal. 15:289-298(2003).
Cited for: PHOSPHORYLATION AT TYR-14.
PubMed: 12531427

"The insulin receptor catalyzes the tyrosine phosphorylation ofcaveolin-1.";
Kimura A., Mora S., Shigematsu S., Pessin J.E., Saltiel A.R.;
J. Biol. Chem. 277:30153-30158(2002).
Cited for: PHOSPHORYLATION AT TYR-14.
PubMed: 12036959