dbPTM

CAV1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CAV1_HUMAN
UniProt AC	Q03135
Protein Name	Caveolin-1
Gene Name	CAV1
Organism	Homo sapiens (Human).
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. Potent
Protein Description	May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). 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. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway. Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation. [PubMed: 25893292 Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae]
Protein Sequence	MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADELSEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTVCDPLFEAVGKIFSNVRINLQKEI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGGKYVDS ------CCCCCEECC	57.14	28355574
2 (in isoform 2)	Acetylation	-	57.14	19369195
2	Acetylation	------MSGGKYVDS ------CCCCCEECC	57.14	22814378
5	Acetylation	---MSGGKYVDSEGH ---CCCCCEECCCCC	45.70	19608861
5	Ubiquitination	---MSGGKYVDSEGH ---CCCCCEECCCCC	45.70	19608861
5	Malonylation	---MSGGKYVDSEGH ---CCCCCEECCCCC	45.70	26320211
6	Phosphorylation	--MSGGKYVDSEGHL --CCCCCEECCCCCE	16.86	21945579
6 (in isoform 2)	Phosphorylation	-	16.86	25849741
8 (in isoform 2)	Ubiquitination	-	37.57	21890473
9	Phosphorylation	SGGKYVDSEGHLYTV CCCCEECCCCCEEEE	35.12	21945579
11 (in isoform 2)	Phosphorylation	-	21.76	27642862
14	Phosphorylation	VDSEGHLYTVPIREQ ECCCCCEEEEEEHHC	10.46	16943184
15	Phosphorylation	DSEGHLYTVPIREQG CCCCCEEEEEEHHCC	26.60	21945579
16 (in isoform 2)	Ubiquitination	-	2.04	21890473
25	Phosphorylation	IREQGNIYKPNNKAM EHHCCCEECCCCHHH	25.13	21945579
26	Sumoylation	REQGNIYKPNNKAMA HHCCCEECCCCHHHH	37.16	-
26 (in isoform 1)	Ubiquitination	-	37.16	21890473
26 (in isoform 2)	Ubiquitination	-	37.16	21890473
26	Ubiquitination	REQGNIYKPNNKAMA HHCCCEECCCCHHHH	37.16	21890473
30	2-Hydroxyisobutyrylation	NIYKPNNKAMADELS CEECCCCHHHHHHHC	46.29	-
30 (in isoform 1)	Ubiquitination	-	46.29	21890473
30	Ubiquitination	NIYKPNNKAMADELS CEECCCCHHHHHHHC	46.29	21890473
32	Sulfoxidation	YKPNNKAMADELSEK ECCCCHHHHHHHCHH	5.29	30846556
37	Phosphorylation	KAMADELSEKQVYDA HHHHHHHCHHHHHCC	40.47	29255136
39	Acetylation	MADELSEKQVYDAHT HHHHHCHHHHHCCCC	41.51	23236377
39 (in isoform 1)	Ubiquitination	-	41.51	21890473
39	2-Hydroxyisobutyrylation	MADELSEKQVYDAHT HHHHHCHHHHHCCCC	41.51	-
39	Ubiquitination	MADELSEKQVYDAHT HHHHHCHHHHHCCCC	41.51	21890473
42	Phosphorylation	ELSEKQVYDAHTKEI HHCHHHHHCCCCCCE	12.62	23927012
46	Phosphorylation	KQVYDAHTKEIDLVN HHHHCCCCCCEECCC	31.90	23403867
47	2-Hydroxyisobutyrylation	QVYDAHTKEIDLVNR HHHCCCCCCEECCCC	42.69	-
47 (in isoform 1)	Ubiquitination	-	42.69	21890473
47	Ubiquitination	QVYDAHTKEIDLVNR HHHCCCCCCEECCCC	42.69	21890473
57	2-Hydroxyisobutyrylation	DLVNRDPKHLNDDVV ECCCCCCCCCCCCEE	66.08	-
57 (in isoform 1)	Ubiquitination	-	66.08	21890473
57	Ubiquitination	DLVNRDPKHLNDDVV ECCCCCCCCCCCCEE	66.08	2190698
57	Acetylation	DLVNRDPKHLNDDVV ECCCCCCCCCCCCEE	66.08	25825284
65	Ubiquitination	HLNDDVVKIDFEDVI CCCCCEEEECHHHHH	36.08	-
80	Phosphorylation	AEPEGTHSFDGIWKA CCCCCCCCCCCEEEE	25.52	11078729
88	Phosphorylation	FDGIWKASFTTFTVT CCCEEEEEEEEEHHH	21.28	21406692
90	Phosphorylation	GIWKASFTTFTVTKY CEEEEEEEEEHHHHH	20.64	21406692
91	Phosphorylation	IWKASFTTFTVTKYW EEEEEEEEEHHHHHH	18.46	21406692
93	Phosphorylation	KASFTTFTVTKYWFY EEEEEEEHHHHHHHH	25.77	21406692
95	Phosphorylation	SFTTFTVTKYWFYRL EEEEEHHHHHHHHHH	18.50	21406692
133	S-palmitoylation	HIWAVVPCIKSFLIE HHHHHHHHHHHHHHH	4.06	29575903
143	S-palmitoylation	SFLIEIQCISRVYSI HHHHHHHHHHHHHHH	3.61	29575903
145 (in isoform 2)	Ubiquitination	-	24.26	21890473
156	S-palmitoylation	SIYVHTVCDPLFEAV HHHHHHCCHHHHHHH	4.72	29575903
168	Phosphorylation	EAVGKIFSNVRINLQ HHHHHHHHHHHHEEC	37.58	11078729
176	Ubiquitination	NVRINLQKEI----- HHHHEECCCC-----	61.62	-
176 (in isoform 1)	Ubiquitination	-	61.62	21890473

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	ABL	P00519	PSP
14	Y	Phosphorylation	Kinase	FYN	P06241	PSP
14	Y	Phosphorylation	Kinase	SRC	P12931	PSP
14	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
88	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
88	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	ZNRF1	Q8ND25	PMID:28593998

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CAV1_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 CAV1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANDR_HUMAN	AR	physical	11278309
NLTP_HUMAN	SCP2	physical	15182174
PLD2_HUMAN	PLD2	physical	14675200
AQP3_HUMAN	AQP3	physical	14675200
EDNRB_HUMAN	EDNRB	physical	12694195
NOS3_HUMAN	NOS3	physical	8910295
NOS2_HUMAN	NOS2	physical	11114180
BTK_HUMAN	BTK	physical	11751885
GRK5_HUMAN	GRK5	physical	10085129
RK_HUMAN	GRK1	physical	10085129
ARBK1_HUMAN	ADRBK1	physical	10085129
TRADD_HUMAN	TRADD	physical	11112773
NTRK1_HUMAN	NTRK1	physical	9867838
NEUR3_HUMAN	NEU3	physical	12011038
CAV2_HUMAN	CAV2	physical	9361015
S1PR1_HUMAN	S1PR1	physical	10921915
FLOT1_HUMAN	FLOT1	physical	10212252
FLOT2_HUMAN	FLOT2	physical	10212252
PGH2_HUMAN	PTGS2	physical	11432874
PGFRB_HUMAN	PDGFRB	physical	10066366
PGFRA_HUMAN	PDGFRA	physical	10066366
TRAF2_HUMAN	TRAF2	physical	11805080
CSK_HUMAN	CSK	physical	11805080
SRC_HUMAN	SRC	physical	8910575
SMAD2_HUMAN	SMAD2	physical	11102446
CXA1_HUMAN	GJA1	physical	11980479
RAC1_HUMAN	RAC1	physical	20460433
PGH2_HUMAN	PTGS2	physical	19960513
MK03_HUMAN	MAPK3	physical	12388423
MK01_HUMAN	MAPK1	physical	12388423
EGFR_HUMAN	EGFR	physical	12388423
KCNA3_HUMAN	KCNA3	physical	18218624
KCNA5_HUMAN	KCNA5	physical	18218624
PP1A_HUMAN	PPP1CA	physical	14645548
2AAA_HUMAN	PPP2R1A	physical	14645548
2AAB_HUMAN	PPP2R1B	physical	14645548
PP2AA_HUMAN	PPP2CA	physical	14645548
PTPA_HUMAN	PPP2R4	physical	14645548
SYUA_HUMAN	SNCA	physical	21693152
SYUA_MOUSE	Snca	physical	21693152
NOS3_HUMAN	NOS3	physical	11425855
CAVN1_HUMAN	PTRF	physical	22939629
ESR1_HUMAN	ESR1	physical	19595769
VDAC1_HUMAN	VDAC1	physical	19595769
TERA_HUMAN	VCP	physical	23335559
UBXN6_HUMAN	UBXN6	physical	23335559
KCNN3_HUMAN	KCNN3	physical	22952906
MCL1_HUMAN	MCL1	physical	22277751
TRPC1_HUMAN	TRPC1	physical	19052258
PTC1_HUMAN	PTCH1	physical	11278759
TNS2_HUMAN	TENC1	physical	16951145
RHG07_HUMAN	DLC1	physical	16951145
PP2AA_HUMAN	PPP2CA	physical	17855368
ID1_HUMAN	ID1	physical	17855368
NF1_HUMAN	NF1	physical	16405917
MALL_HUMAN	MALL	physical	11294831
KCMA1_HUMAN	KCNMA1	physical	15703204
LRP6_HUMAN	LRP6	physical	16890161
NOS3_HUMAN	NOS3	physical	12852865
TNR6_HUMAN	FAS	physical	21382479
BID_HUMAN	BID	physical	21382479
PAR1_HUMAN	F2R	physical	17848177
PAR1_HUMAN	F2R	physical	20826780
EPCR_HUMAN	PROCR	physical	20826780
CAV2_HUMAN	CAV2	physical	18081315
DERL1_HUMAN	DERL1	physical	24089527
SELS_HUMAN	VIMP	physical	24089527
TERA_HUMAN	VCP	physical	24089527
UFD1_HUMAN	UFD1L	physical	24089527
PGH2_HUMAN	PTGS2	physical	24089527
PGH1_HUMAN	PTGS1	physical	15230350
PTGIS_HUMAN	PTGIS	physical	11339822
ATG5_HUMAN	ATG5	physical	24727585
ATG12_HUMAN	ATG12	physical	24727585
MRP1_HUMAN	ABCC1	physical	14627714
TFR1_HUMAN	TFRC	physical	14627714
PPARG_HUMAN	PPARG	physical	12813462
VAV2_HUMAN	VAV2	physical	20808760
PLCG1_HUMAN	PLCG1	physical	20808760
CTNB1_HUMAN	CTNNB1	physical	18356165
HDAC6_HUMAN	HDAC6	physical	18356165
SEPR_HUMAN	FAP	physical	26209915
AN13A_HUMAN	ANKRD13A	physical	26797118
CTNB1_HUMAN	CTNNB1	physical	19244345
ADCY6_HUMAN	ADCY6	physical	21228062
ADCY5_HUMAN	ADCY5	physical	21228062
RHG07_HUMAN	DLC1	physical	22693251
TLR4_HUMAN	TLR4	physical	21715681
EGFR_HUMAN	EGFR	physical	10781609
KCNA3_HUMAN	KCNA3	physical	26931497
KCNA5_HUMAN	KCNA5	physical	26931497
EGFR_HUMAN	EGFR	physical	15273741
MCR_HUMAN	NR3C2	physical	28734243
MLP3A_HUMAN	MAP1LC3A	physical	28734243
UBC_HUMAN	UBC	physical	28734243
ACTB_HUMAN	ACTB	physical	28734243

Drug and Disease Associations

Kegg Disease
OMIM Disease
612526	Congenital generalized lipodystrophy 3 (CGL3)
615343	Pulmonary hypertension, primary, 3 (PPH3)
606721	Partial lipodystrophy, congenital cataracts, and neurodegeneration syndrome (LCCNS)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CAV1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"N-terminal processing and modifications of caveolin-1 in caveolaefrom human adipocytes."; Vainonen J.P., Aboulaich N., Turkina M.V., Stralfors P., Vener A.V.; Biochem. Biophys. Res. Commun. 320:480-486(2004). Cited for: PROTEIN SEQUENCE OF 2-66, SUBCELLULAR LOCATION, ACETYLATION AT SER-2,AND PHOSPHORYLATION.	15219854 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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-37, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASSSPECTROMETRY.	19007248 [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 SER-37, AND MASSSPECTROMETRY.	17081983 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6; TYR-14; TYR-25 ANDTYR-42, AND MASS SPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6 AND TYR-14, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-14, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-14, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6; TYR-14 AND TYR-25,AND MASS SPECTROMETRY.	15951569 [Abstract]
"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.	12531427 [Abstract]