CAVN1_HUMAN - dbPTM
CAVN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAVN1_HUMAN
UniProt AC Q6NZI2
Protein Name Caveolae-associated protein 1 {ECO:0000312|HGNC:HGNC:9688}
Gene Name CAVIN1 {ECO:0000312|HGNC:HGNC:9688}
Organism Homo sapiens (Human).
Sequence Length 390
Subcellular Localization Membrane, caveola . Cell membrane . Microsome . Endoplasmic reticulum . Cytoplasm, cytosol . Mitochondrion . Nucleus . Translocates to the cytoplasm from the caveolae upon insulin stimulation (PubMed:17026959). Colocalizes with CAV1 in lipid rafts in
Protein Description Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues. [PubMed: 18056712]
Protein Sequence MEDPTLYIVERPLPGYPDAEAPEPSSAGAQAAEEPSGAGSEELIKSDQVNGVLVLSLLDKIIGAVDQIQLTQAQLEERQAEMEGAVQSIQGELSKLGKAHATTSNTVSKLLEKVRKVSVNVKTVRGSLERQAGQIKKLEVNEAELLRRRNFKVMIYQDEVKLPAKLSISKSLKESEALPEKEGEELGEGERPEEDAAALELSSDEAVEVEEVIEESRAERIKRSGLRRVDDFKKAFSKEKMEKTKVRTRENLEKTRLKTKENLEKTRHTLEKRMNKLGTRLVPAERREKLKTSRDKLRKSFTPDHVVYARSKTAVYKVPPFTFHVKKIREGQVEVLKATEMVEVGADDDEGGAERGEAGDLRRGSSPDVHALLEITEESDAVLVDKSDSD
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 Orthologous
Protein Cluster
1Acetylation-------MEDPTLYI
-------CCCCCEEE
15242332
5Phosphorylation---MEDPTLYIVERP
---CCCCCEEEEECC
20639409
7Phosphorylation-MEDPTLYIVERPLP
-CCCCCEEEEECCCC
25106551
16PhosphorylationVERPLPGYPDAEAPE
EECCCCCCCCCCCCC
20639409
25PhosphorylationDAEAPEPSSAGAQAA
CCCCCCCCCHHHHCC
26657352
26PhosphorylationAEAPEPSSAGAQAAE
CCCCCCCCHHHHCCC
26657352
36PhosphorylationAQAAEEPSGAGSEEL
HHCCCCCCCCCCHHH
29255136
40PhosphorylationEEPSGAGSEELIKSD
CCCCCCCCHHHHHHC
29255136
46PhosphorylationGSEELIKSDQVNGVL
CCHHHHHHCCCCCEE
22777824
50 (in isoform 3)Ubiquitination-21890473
53 (in isoform 3)Ubiquitination-21890473
56PhosphorylationVNGVLVLSLLDKIIG
CCCEEHHHHHHHHHH
22199227
60UbiquitinationLVLSLLDKIIGAVDQ
EHHHHHHHHHHHHHH
22817900
64 (in isoform 3)Ubiquitination-21890473
68 (in isoform 3)Ubiquitination-21890473
77 (in isoform 3)Ubiquitination-21890473
82SulfoxidationLEERQAEMEGAVQSI
HHHHHHHHHHHHHHH
30846556
88PhosphorylationEMEGAVQSIQGELSK
HHHHHHHHHHHHHHH
26657352
88 (in isoform 2)Phosphorylation-21902226
92 (in isoform 3)Ubiquitination-21890473
94PhosphorylationQSIQGELSKLGKAHA
HHHHHHHHHHCCCCC
27251275
95UbiquitinationSIQGELSKLGKAHAT
HHHHHHHHHCCCCCC
23000965
95 (in isoform 1)Ubiquitination-21890473
98UbiquitinationGELSKLGKAHATTSN
HHHHHHCCCCCCCHH
23000965
98 (in isoform 1)Ubiquitination-21890473
102PhosphorylationKLGKAHATTSNTVSK
HHCCCCCCCHHHHHH
23403867
103PhosphorylationLGKAHATTSNTVSKL
HCCCCCCCHHHHHHH
23403867
104PhosphorylationGKAHATTSNTVSKLL
CCCCCCCHHHHHHHH
23403867
106PhosphorylationAHATTSNTVSKLLEK
CCCCCHHHHHHHHHH
21406692
107 (in isoform 3)Ubiquitination-21890473
108PhosphorylationATTSNTVSKLLEKVR
CCCHHHHHHHHHHHH
23403867
109AcetylationTTSNTVSKLLEKVRK
CCHHHHHHHHHHHHC
23236377
109MalonylationTTSNTVSKLLEKVRK
CCHHHHHHHHHHHHC
26320211
109UbiquitinationTTSNTVSKLLEKVRK
CCHHHHHHHHHHHHC
23000965
109 (in isoform 1)Ubiquitination-21890473
113UbiquitinationTVSKLLEKVRKVSVN
HHHHHHHHHHCCCCC
23000965
113 (in isoform 1)Ubiquitination-21890473
116SumoylationKLLEKVRKVSVNVKT
HHHHHHHCCCCCHHH
-
116SumoylationKLLEKVRKVSVNVKT
HHHHHHHCCCCCHHH
28112733
116UbiquitinationKLLEKVRKVSVNVKT
HHHHHHHCCCCCHHH
23000965
116 (in isoform 3)Ubiquitination-21890473
118PhosphorylationLEKVRKVSVNVKTVR
HHHHHCCCCCHHHHH
23911959
120 (in isoform 3)Ubiquitination-21890473
122MalonylationRKVSVNVKTVRGSLE
HCCCCCHHHHHHHHH
26320211
122SumoylationRKVSVNVKTVRGSLE
HCCCCCHHHHHHHHH
28112733
122UbiquitinationRKVSVNVKTVRGSLE
HCCCCCHHHHHHHHH
23000965
122 (in isoform 1)Ubiquitination-21890473
123PhosphorylationKVSVNVKTVRGSLER
CCCCCHHHHHHHHHH
20068231
125 (in isoform 3)Ubiquitination-21890473
127PhosphorylationNVKTVRGSLERQAGQ
CHHHHHHHHHHHCCC
28355574
128 (in isoform 3)Ubiquitination-21890473
1362-HydroxyisobutyrylationERQAGQIKKLEVNEA
HHHCCCEEEEECCHH
-
136UbiquitinationERQAGQIKKLEVNEA
HHHCCCEEEEECCHH
23000965
137MalonylationRQAGQIKKLEVNEAE
HHCCCEEEEECCHHH
26320211
137UbiquitinationRQAGQIKKLEVNEAE
HHCCCEEEEECCHHH
23000965
137 (in isoform 1)Ubiquitination-21890473
152AcetylationLLRRRNFKVMIYQDE
HHHHCCCEEEEEECC
26051181
152MalonylationLLRRRNFKVMIYQDE
HHHHCCCEEEEEECC
26320211
152UbiquitinationLLRRRNFKVMIYQDE
HHHHCCCEEEEEECC
23000965
152 (in isoform 1)Ubiquitination-21890473
154SulfoxidationRRRNFKVMIYQDEVK
HHCCCEEEEEECCCC
30846556
156PhosphorylationRNFKVMIYQDEVKLP
CCCEEEEEECCCCCC
21945579
161SumoylationMIYQDEVKLPAKLSI
EEEECCCCCCCEEEE
-
161AcetylationMIYQDEVKLPAKLSI
EEEECCCCCCCEEEE
26051181
161MalonylationMIYQDEVKLPAKLSI
EEEECCCCCCCEEEE
26320211
161SumoylationMIYQDEVKLPAKLSI
EEEECCCCCCCEEEE
25114211
161UbiquitinationMIYQDEVKLPAKLSI
EEEECCCCCCCEEEE
23000965
161 (in isoform 1)Ubiquitination-21890473
1652-HydroxyisobutyrylationDEVKLPAKLSISKSL
CCCCCCCEEEECCCH
-
165AcetylationDEVKLPAKLSISKSL
CCCCCCCEEEECCCH
19813393
165MalonylationDEVKLPAKLSISKSL
CCCCCCCEEEECCCH
26320211
165SumoylationDEVKLPAKLSISKSL
CCCCCCCEEEECCCH
28112733
165UbiquitinationDEVKLPAKLSISKSL
CCCCCCCEEEECCCH
23000965
165 (in isoform 1)Ubiquitination-21890473
167PhosphorylationVKLPAKLSISKSLKE
CCCCCEEEECCCHHH
29255136
169PhosphorylationLPAKLSISKSLKESE
CCCEEEECCCHHHHH
30266825
1702-HydroxyisobutyrylationPAKLSISKSLKESEA
CCEEEECCCHHHHHC
-
170MalonylationPAKLSISKSLKESEA
CCEEEECCCHHHHHC
26320211
170SumoylationPAKLSISKSLKESEA
CCEEEECCCHHHHHC
28112733
170UbiquitinationPAKLSISKSLKESEA
CCEEEECCCHHHHHC
23000965
170 (in isoform 1)Ubiquitination-21890473
171PhosphorylationAKLSISKSLKESEAL
CEEEECCCHHHHHCC
28355574
173SumoylationLSISKSLKESEALPE
EEECCCHHHHHCCCH
-
173MalonylationLSISKSLKESEALPE
EEECCCHHHHHCCCH
32601280
173SumoylationLSISKSLKESEALPE
EEECCCHHHHHCCCH
-
173UbiquitinationLSISKSLKESEALPE
EEECCCHHHHHCCCH
23000965
173 (in isoform 1)Ubiquitination-21890473
175PhosphorylationISKSLKESEALPEKE
ECCCHHHHHCCCHHH
28176443
181UbiquitinationESEALPEKEGEELGE
HHHCCCHHHCCCCCC
-
202PhosphorylationDAAALELSSDEAVEV
HHHHHHCCCCCCEEH
28176443
203PhosphorylationAAALELSSDEAVEVE
HHHHHCCCCCCEEHH
28176443
209 (in isoform 2)Ubiquitination-21890473
216PhosphorylationVEEVIEESRAERIKR
HHHHHHHHHHHHHHH
28176443
227 (in isoform 2)Ubiquitination-21890473
233UbiquitinationLRRVDDFKKAFSKEK
CCCHHHHHHHHCHHH
27667366
237PhosphorylationDDFKKAFSKEKMEKT
HHHHHHHCHHHHHHH
24719451
238UbiquitinationDFKKAFSKEKMEKTK
HHHHHHCHHHHHHHC
27667366
244O-linked_GlycosylationSKEKMEKTKVRTREN
CHHHHHHHCCCCHHH
30379171
2542-HydroxyisobutyrylationRTRENLEKTRLKTKE
CCHHHHHHHCCHHHH
-
254UbiquitinationRTRENLEKTRLKTKE
CCHHHHHHHCCHHHH
29967540
258UbiquitinationNLEKTRLKTKENLEK
HHHHHCCHHHHHHHH
33845483
259PhosphorylationLEKTRLKTKENLEKT
HHHHCCHHHHHHHHH
-
260UbiquitinationEKTRLKTKENLEKTR
HHHCCHHHHHHHHHH
33845483
2652-HydroxyisobutyrylationKTKENLEKTRHTLEK
HHHHHHHHHHHHHHH
-
265UbiquitinationKTKENLEKTRHTLEK
HHHHHHHHHHHHHHH
33845483
266PhosphorylationTKENLEKTRHTLEKR
HHHHHHHHHHHHHHH
28176443
269PhosphorylationNLEKTRHTLEKRMNK
HHHHHHHHHHHHHHH
30576142
272UbiquitinationKTRHTLEKRMNKLGT
HHHHHHHHHHHHHCC
29967540
272 (in isoform 3)Ubiquitination-21890473
276UbiquitinationTLEKRMNKLGTRLVP
HHHHHHHHHCCCCCC
33845483
279PhosphorylationKRMNKLGTRLVPAER
HHHHHHCCCCCCHHH
25867546
296UbiquitinationKLKTSRDKLRKSFTP
HHHCCHHHHHHHCCC
23000965
2992-HydroxyisobutyrylationTSRDKLRKSFTPDHV
CCHHHHHHHCCCCCE
-
299AcetylationTSRDKLRKSFTPDHV
CCHHHHHHHCCCCCE
27452117
299MalonylationTSRDKLRKSFTPDHV
CCHHHHHHHCCCCCE
26320211
299UbiquitinationTSRDKLRKSFTPDHV
CCHHHHHHHCCCCCE
23000965
299 (in isoform 1)Ubiquitination-21890473
300PhosphorylationSRDKLRKSFTPDHVV
CHHHHHHHCCCCCEE
26846344
302PhosphorylationDKLRKSFTPDHVVYA
HHHHHHCCCCCEEEE
26846344
308PhosphorylationFTPDHVVYARSKTAV
CCCCCEEEEECCCEE
25159151
311PhosphorylationDHVVYARSKTAVYKV
CCEEEEECCCEEEEC
26437602
312UbiquitinationHVVYARSKTAVYKVP
CEEEEECCCEEEECC
23000965
313PhosphorylationVVYARSKTAVYKVPP
EEEEECCCEEEECCC
26657352
316PhosphorylationARSKTAVYKVPPFTF
EECCCEEEECCCCEE
28152594
317UbiquitinationRSKTAVYKVPPFTFH
ECCCEEEECCCCEEE
23000965
317 (in isoform 1)Ubiquitination-21890473
3262-HydroxyisobutyrylationPPFTFHVKKIREGQV
CCCEEEEEECCCCCC
-
326AcetylationPPFTFHVKKIREGQV
CCCEEEEEECCCCCC
30591687
326SumoylationPPFTFHVKKIREGQV
CCCEEEEEECCCCCC
28112733
326UbiquitinationPPFTFHVKKIREGQV
CCCEEEEEECCCCCC
32015554
327AcetylationPFTFHVKKIREGQVE
CCEEEEEECCCCCCE
30591693
337UbiquitinationEGQVEVLKATEMVEV
CCCCEEEEEEEEEEE
-
341SulfoxidationEVLKATEMVEVGADD
EEEEEEEEEEECCCC
28465586
365PhosphorylationAGDLRRGSSPDVHAL
CCCCCCCCCCCHHHH
30266825
366PhosphorylationGDLRRGSSPDVHALL
CCCCCCCCCCHHHHH
30266825
376PhosphorylationVHALLEITEESDAVL
HHHHHHCCCCCCCEE
30266825
379PhosphorylationLLEITEESDAVLVDK
HHHCCCCCCCEEEEC
30266825
387PhosphorylationDAVLVDKSDSD----
CCEEEECCCCC----
30266825
389PhosphorylationVLVDKSDSD------
EEEECCCCC------
30266825

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
300SPhosphorylationKinaseAURKBQ96GD4
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAVN1_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 CAVN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN148_HUMANZNF148physical
10727401
TFF1_HUMANTFF1physical
9582279
TRI72_HUMANTRIM72physical
21343302
TF3C4_HUMANGTF3C4physical
22939629
TMEDA_HUMANTMED10physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
LIPS_HUMANLIPEphysical
17026959
MAGI3_HUMANMAGI3physical
28514442
M21D2_HUMANMB21D2physical
28514442
MD1L1_HUMANMAD1L1physical
28514442
ZBTB1_HUMANZBTB1physical
28514442
ZN622_HUMANZNF622physical
28514442
FHL2_HUMANFHL2physical
28514442
ZZEF1_HUMANZZEF1physical
28514442
UTRO_HUMANUTRNphysical
28514442
FBX28_HUMANFBXO28physical
28514442
TRI26_HUMANTRIM26physical
28514442
TERF2_HUMANTERF2physical
28514442
HECD3_HUMANHECTD3physical
28514442
KLH15_HUMANKLHL15physical
28514442
SNTB2_HUMANSNTB2physical
28514442
OBSL1_HUMANOBSL1physical
28514442
CRBN_HUMANCRBNphysical
28514442
HSP7C_HUMANHSPA8physical
28514442
EXOC7_HUMANEXOC7physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAVN1_HUMAN

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Related Literatures of Post-Translational Modification

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