CAVN3_HUMAN - dbPTM
CAVN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAVN3_HUMAN
UniProt AC Q969G5
Protein Name Caveolae-associated protein 3 {ECO:0000312|HGNC:HGNC:9400}
Gene Name CAVIN3 {ECO:0000312|HGNC:HGNC:9400}
Organism Homo sapiens (Human).
Sequence Length 261
Subcellular Localization Cytoplasm . Membrane, caveola . Cytoplasm, cytosol . Localizes in the caveolae in a caveolin-dependent manner.
Protein Description Regulates the traffic and/or budding of caveolae. [PubMed: 19262564 Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in smooth muscle but not in the lung and heart endothelial cells. Regulates the equilibrium between cell surface-associated and cell surface-dissociated caveolae by promoting the rapid release of caveolae from the cell surface. Plays a role in the regulation of the circadian clock. Modulates the period length and phase of circadian gene expression and also regulates expression and interaction of the core clock components PER1/2 and CRY1/2 (By similarity]
Protein Sequence MRESALERGPVPEAPAGGPVHAVTVVTLLEKLASMLETLRERQGGLARRQGGLAGSVRRIQSGLGALSRSHDTTSNTLAQLLAKAERVSSHANAAQERAVRRAAQVQRLEANHGLLVARGKLHVLLFKEEGEVPASAFQKAPEPLGPADQSELGPEQLEAEVGESSDEEPVESRAQRLRRTGLQKVQSLRRALSGRKGPAAPPPTPVKPPRLGPGRSAEAQPEAQPALEPTLEPEPPQDTEEDPGRPGAAEEALLQMESVA
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
4Phosphorylation----MRESALERGPV
----CCHHHHHCCCC
17081983
31UbiquitinationTVVTLLEKLASMLET
HHHHHHHHHHHHHHH
-
34PhosphorylationTLLEKLASMLETLRE
HHHHHHHHHHHHHHH
21406692
35SulfoxidationLLEKLASMLETLRER
HHHHHHHHHHHHHHH
30846556
38PhosphorylationKLASMLETLRERQGG
HHHHHHHHHHHHHCH
21406692
56PhosphorylationRQGGLAGSVRRIQSG
HHCCCHHHHHHHHHH
28102081
62PhosphorylationGSVRRIQSGLGALSR
HHHHHHHHHHCHHHC
28355574
68PhosphorylationQSGLGALSRSHDTTS
HHHHCHHHCCCCCCH
21406692
70PhosphorylationGLGALSRSHDTTSNT
HHCHHHCCCCCCHHH
28857561
73PhosphorylationALSRSHDTTSNTLAQ
HHHCCCCCCHHHHHH
23186163
74PhosphorylationLSRSHDTTSNTLAQL
HHCCCCCCHHHHHHH
21712546
75PhosphorylationSRSHDTTSNTLAQLL
HCCCCCCHHHHHHHH
23186163
84UbiquitinationTLAQLLAKAERVSSH
HHHHHHHHHHHHHHH
21906983
121AcetylationGLLVARGKLHVLLFK
CEEEECCEEEEEEEE
26051181
121MalonylationGLLVARGKLHVLLFK
CEEEECCEEEEEEEE
26320211
128SumoylationKLHVLLFKEEGEVPA
EEEEEEEECCCCCCH
28112733
136PhosphorylationEEGEVPASAFQKAPE
CCCCCCHHHHHCCCC
-
151PhosphorylationPLGPADQSELGPEQL
CCCCCCHHHHCHHHH
23927012
165PhosphorylationLEAEVGESSDEEPVE
HHHHCCCCCCCCCHH
29255136
166PhosphorylationEAEVGESSDEEPVES
HHHCCCCCCCCCHHH
29255136
173PhosphorylationSDEEPVESRAQRLRR
CCCCCHHHHHHHHHH
23927012
185UbiquitinationLRRTGLQKVQSLRRA
HHHHHHHHHHHHHHH
21906983
188PhosphorylationTGLQKVQSLRRALSG
HHHHHHHHHHHHHCC
20068231
194PhosphorylationQSLRRALSGRKGPAA
HHHHHHHCCCCCCCC
26699800
197UbiquitinationRRALSGRKGPAAPPP
HHHHCCCCCCCCCCC
29967540
205PhosphorylationGPAAPPPTPVKPPRL
CCCCCCCCCCCCCCC
29255136
208UbiquitinationAPPPTPVKPPRLGPG
CCCCCCCCCCCCCCC
29967540
217PhosphorylationPRLGPGRSAEAQPEA
CCCCCCCCCCCCCCC
28857561

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 CAVN3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAVN3_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 CAVN3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPTN1_HUMANSPTAN1physical
22939629
RL21_HUMANRPL21physical
22939629
RS16_HUMANRPS16physical
22939629
SYSM_HUMANSARS2physical
22939629
SFXN1_HUMANSFXN1physical
22939629
TCPB_HUMANCCT2physical
22939629
RM49_HUMANMRPL49physical
22939629
PTBP3_HUMANPTBP3physical
22939629
RS3A_HUMANRPS3Aphysical
22939629
RM23_HUMANMRPL23physical
22939629
RS26_HUMANRPS26physical
22939629
PYC_HUMANPCphysical
22939629
SSRD_HUMANSSR4physical
22939629
SPTB2_HUMANSPTBN1physical
22939629
TPM4_HUMANTPM4physical
22939629
MR1L1_HUMANMRFAP1L1physical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAVN3_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP