CAVN2_HUMAN - dbPTM
CAVN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAVN2_HUMAN
UniProt AC O95810
Protein Name Caveolae-associated protein 2 {ECO:0000312|HGNC:HGNC:10690}
Gene Name CAVIN2 {ECO:0000312|HGNC:HGNC:10690}
Organism Homo sapiens (Human).
Sequence Length 425
Subcellular Localization Cytoplasm, cytosol . Membrane, caveola . Localizes in the caveolae in a caveolin-dependent manner.
Protein Description Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae. [PubMed: 19525939 Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells. May play a role in targeting PRKCA to caveolae (By similarity]
Protein Sequence MGEDAAQAEKFQHPGSDMRQEKPSSPSPMPSSTPSPSLNLGNTEEAIRDNSQVNAVTVLTLLDKLVNMLDAVQENQHKMEQRQISLEGSVKGIQNDLTKLSKYQASTSNTVSKLLEKSRKVSAHTRAVKERMDRQCAQVKRLENNHAQLLRRNHFKVLIFQEENEIPASVFVKQPVSGAVEGKEELPDENKSLEETLHTVDLSSDDDLPHDEEALEDSAEEKVEESRAEKIKRSSLKKVDSLKKAFSRQNIEKKMNKLGTKIVSVERREKIKKSLTSNHQKISSGKSSPFKVSPLTFGRKKVREGESHAENETKSEDLPSSEQMPNDQEEESFAEGHSEASLASALVEGEIAEEAAEKATSRGSNSGMDSNIDLTIVEDEEEESVALEQAQKVRYEGSYALTSEEAERSDGDPVQPAVLQVHQTS
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
2Acetylation------MGEDAAQAE
------CCHHHHHHH
-
10UbiquitinationEDAAQAEKFQHPGSD
HHHHHHHHHCCCCCH
23000965
16PhosphorylationEKFQHPGSDMRQEKP
HHHCCCCCHHCCCCC
28060719
24PhosphorylationDMRQEKPSSPSPMPS
HHCCCCCCCCCCCCC
23401153
25PhosphorylationMRQEKPSSPSPMPSS
HCCCCCCCCCCCCCC
23927012
27PhosphorylationQEKPSSPSPMPSSTP
CCCCCCCCCCCCCCC
23401153
31PhosphorylationSSPSPMPSSTPSPSL
CCCCCCCCCCCCCCC
23927012
32PhosphorylationSPSPMPSSTPSPSLN
CCCCCCCCCCCCCCC
23927012
33PhosphorylationPSPMPSSTPSPSLNL
CCCCCCCCCCCCCCC
23927012
35PhosphorylationPMPSSTPSPSLNLGN
CCCCCCCCCCCCCCC
23927012
37PhosphorylationPSSTPSPSLNLGNTE
CCCCCCCCCCCCCHH
23927012
43PhosphorylationPSLNLGNTEEAIRDN
CCCCCCCHHHHHHCC
23403867
51PhosphorylationEEAIRDNSQVNAVTV
HHHHHCCCCCCHHHH
28270605
57PhosphorylationNSQVNAVTVLTLLDK
CCCCCHHHHHHHHHH
28270605
60PhosphorylationVNAVTVLTLLDKLVN
CCHHHHHHHHHHHHH
28270605
85PhosphorylationKMEQRQISLEGSVKG
HHHHHHHHHHHHHHH
25072903
89PhosphorylationRQISLEGSVKGIQND
HHHHHHHHHHHHHCC
25072903
91UbiquitinationISLEGSVKGIQNDLT
HHHHHHHHHHHCCHH
23000965
99UbiquitinationGIQNDLTKLSKYQAS
HHHCCHHHHHHHHHH
23000965
101PhosphorylationQNDLTKLSKYQASTS
HCCHHHHHHHHHHCC
18491316
102UbiquitinationNDLTKLSKYQASTSN
CCHHHHHHHHHHCCH
23000965
103PhosphorylationDLTKLSKYQASTSNT
CHHHHHHHHHHCCHH
29116813
107PhosphorylationLSKYQASTSNTVSKL
HHHHHHHCCHHHHHH
29116813
112PhosphorylationASTSNTVSKLLEKSR
HHCCHHHHHHHHHHH
22817900
113UbiquitinationSTSNTVSKLLEKSRK
HCCHHHHHHHHHHHH
23000965
117UbiquitinationTVSKLLEKSRKVSAH
HHHHHHHHHHHHHHH
23000965
156UbiquitinationLLRRNHFKVLIFQEE
HHHHCCCEEEEEECC
33845483
169PhosphorylationEENEIPASVFVKQPV
CCCCCCCEEEEECCC
28060719
173UbiquitinationIPASVFVKQPVSGAV
CCCEEEEECCCCCCC
33845483
177PhosphorylationVFVKQPVSGAVEGKE
EEEECCCCCCCCCCC
24505115
183UbiquitinationVSGAVEGKEELPDEN
CCCCCCCCCCCCCCC
33845483
192PhosphorylationELPDENKSLEETLHT
CCCCCCCCHHHHHHH
20058876
196PhosphorylationENKSLEETLHTVDLS
CCCCHHHHHHHCCCC
24972180
199PhosphorylationSLEETLHTVDLSSDD
CHHHHHHHCCCCCCC
24972180
203PhosphorylationTLHTVDLSSDDDLPH
HHHHCCCCCCCCCCC
20058876
204PhosphorylationLHTVDLSSDDDLPHD
HHHCCCCCCCCCCCC
20058876
218PhosphorylationDEEALEDSAEEKVEE
CHHHHHHHHHHHHHH
20058876
226PhosphorylationAEEKVEESRAEKIKR
HHHHHHHHHHHHHHH
28060719
241PhosphorylationSSLKKVDSLKKAFSR
HHHHHHHHHHHHHHH
26657352
247PhosphorylationDSLKKAFSRQNIEKK
HHHHHHHHHHHHHHH
23403867
257UbiquitinationNIEKKMNKLGTKIVS
HHHHHHHHHCCCEEH
23000965
260PhosphorylationKKMNKLGTKIVSVER
HHHHHHCCCEEHHHH
-
261UbiquitinationKMNKLGTKIVSVERR
HHHHHCCCEEHHHHH
23000965
264PhosphorylationKLGTKIVSVERREKI
HHCCCEEHHHHHHHH
28060719
274PhosphorylationRREKIKKSLTSNHQK
HHHHHHHHHHCCCCC
29691806
276PhosphorylationEKIKKSLTSNHQKIS
HHHHHHHHCCCCCCC
22798277
283PhosphorylationTSNHQKISSGKSSPF
HCCCCCCCCCCCCCC
23403867
284PhosphorylationSNHQKISSGKSSPFK
CCCCCCCCCCCCCCC
23401153
286UbiquitinationHQKISSGKSSPFKVS
CCCCCCCCCCCCCCC
23000965
287PhosphorylationQKISSGKSSPFKVSP
CCCCCCCCCCCCCCC
23401153
288PhosphorylationKISSGKSSPFKVSPL
CCCCCCCCCCCCCCC
23401153
291UbiquitinationSGKSSPFKVSPLTFG
CCCCCCCCCCCCCCC
23000965
293PhosphorylationKSSPFKVSPLTFGRK
CCCCCCCCCCCCCCH
26846344
296PhosphorylationPFKVSPLTFGRKKVR
CCCCCCCCCCCHHCC
30266825
307PhosphorylationKKVREGESHAENETK
HHCCCCCCCCCCCCC
27535140
313PhosphorylationESHAENETKSEDLPS
CCCCCCCCCCCCCCC
24275569
320PhosphorylationTKSEDLPSSEQMPND
CCCCCCCCCCCCCCH
20058876
321PhosphorylationKSEDLPSSEQMPNDQ
CCCCCCCCCCCCCHH
20058876
332PhosphorylationPNDQEEESFAEGHSE
CCHHHHHHHHHCCCH
27251275
338PhosphorylationESFAEGHSEASLASA
HHHHHCCCHHHHHHH
27251275
341PhosphorylationAEGHSEASLASALVE
HHCCCHHHHHHHHHH
24275569
344PhosphorylationHSEASLASALVEGEI
CCHHHHHHHHHHHHH
27251275
360PhosphorylationEEAAEKATSRGSNSG
HHHHHHHHHCCCCCC
22617229
361PhosphorylationEAAEKATSRGSNSGM
HHHHHHHHCCCCCCC
23403867
364PhosphorylationEKATSRGSNSGMDSN
HHHHHCCCCCCCCCC
30266825
366PhosphorylationATSRGSNSGMDSNID
HHHCCCCCCCCCCCC
30266825
370PhosphorylationGSNSGMDSNIDLTIV
CCCCCCCCCCCEEEE
22617229
375PhosphorylationMDSNIDLTIVEDEEE
CCCCCCEEEECCCHH
26657352
384PhosphorylationVEDEEEESVALEQAQ
ECCCHHHHHHHHHHH
26657352
395PhosphorylationEQAQKVRYEGSYALT
HHHHHHCCCCCEECC
23927012
398PhosphorylationQKVRYEGSYALTSEE
HHHCCCCCEECCHHH
23927012
399PhosphorylationKVRYEGSYALTSEEA
HHCCCCCEECCHHHH
23927012
402PhosphorylationYEGSYALTSEEAERS
CCCCEECCHHHHHHC
23927012
403PhosphorylationEGSYALTSEEAERSD
CCCEECCHHHHHHCC
23927012
409PhosphorylationTSEEAERSDGDPVQP
CHHHHHHCCCCCCCC
28192239
424PhosphorylationAVLQVHQTS------
CEEEEECCC------
28060719
425PhosphorylationVLQVHQTS-------
EEEEECCC-------
28060719

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

Oops, there are no upstream regulatory protein records of CAVN2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAVN2_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 CAVN2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUD18_HUMANNUDT18physical
16189514
PKHF2_HUMANPLEKHF2physical
16189514
CAVN2_HUMANSDPRphysical
25416956
A1CF_HUMANA1CFphysical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAVN2_HUMAN

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Related Literatures of Post-Translational Modification

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