CASR_HUMAN - dbPTM
CASR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CASR_HUMAN
UniProt AC P41180
Protein Name Extracellular calcium-sensing receptor {ECO:0000305}
Gene Name CASR {ECO:0000312|HGNC:HGNC:1514}
Organism Homo sapiens (Human).
Sequence Length 1078
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description G-protein-coupled receptor that senses changes in the extracellular concentration of calcium ions and plays a key role in maintaining calcium homeostasis. [PubMed: 7759551]
Protein Sequence MAFYSCCWVLLALTWHTSAYGPDQRAQKKGDIILGGLFPIHFGVAAKDQDLKSRPESVECIRYNFRGFRWLQAMIFAIEEINSSPALLPNLTLGYRIFDTCNTVSKALEATLSFVAQNKIDSLNLDEFCNCSEHIPSTIAVVGATGSGVSTAVANLLGLFYIPQVSYASSSRLLSNKNQFKSFLRTIPNDEHQATAMADIIEYFRWNWVGTIAADDDYGRPGIEKFREEAEERDICIDFSELISQYSDEEEIQHVVEVIQNSTAKVIVVFSSGPDLEPLIKEIVRRNITGKIWLASEAWASSSLIAMPQYFHVVGGTIGFALKAGQIPGFREFLKKVHPRKSVHNGFAKEFWEETFNCHLQEGAKGPLPVDTFLRGHEESGDRFSNSSTAFRPLCTGDENISSVETPYIDYTHLRISYNVYLAVYSIAHALQDIYTCLPGRGLFTNGSCADIKKVEAWQVLKHLRHLNFTNNMGEQVTFDECGDLVGNYSIINWHLSPEDGSIVFKEVGYYNVYAKKGERLFINEEKILWSGFSREVPFSNCSRDCLAGTRKGIIEGEPTCCFECVECPDGEYSDETDASACNKCPDDFWSNENHTSCIAKEIEFLSWTEPFGIALTLFAVLGIFLTAFVLGVFIKFRNTPIVKATNRELSYLLLFSLLCCFSSSLFFIGEPQDWTCRLRQPAFGISFVLCISCILVKTNRVLLVFEAKIPTSFHRKWWGLNLQFLLVFLCTFMQIVICVIWLYTAPPSSYRNQELEDEIIFITCHEGSLMALGFLIGYTCLLAAICFFFAFKSRKLPENFNEAKFITFSMLIFFIVWISFIPAYASTYGKFVSAVEVIAILAASFGLLACIFFNKIYIILFKPSRNTIEEVRCSTAAHAFKVAARATLRRSNVSRKRSSSLGGSTGSTPSSSISSKSNSEDPFPQPERQKQQQPLALTQQEQQQQPLTLPQQQRSQQQPRCKQKVIFGSGTVTFSLSFDEPQKNAMAHRNSTHQNSLEAQKSSDTLTRHEPLLPLQCGETDLDLTVQETGLQGPVGGDQRPEVEDPEELSPALVVSSSQSFVISGGGSTVTENVVNS
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
90N-linked_GlycosylationSSPALLPNLTLGYRI
CCCCCCCCCCCCCEE
45.709852126
90N-linked_GlycosylationSSPALLPNLTLGYRI
CCCCCCCCCCCCCEE
45.709852126
130N-linked_GlycosylationLNLDEFCNCSEHIPS
CCHHHHCCCCCCCCC
37.369852126
130N-linked_GlycosylationLNLDEFCNCSEHIPS
CCHHHHCCCCCCCCC
37.369852126
182PhosphorylationSNKNQFKSFLRTIPN
CCHHHHHHHHHHCCC
30.7024719451
186PhosphorylationQFKSFLRTIPNDEHQ
HHHHHHHHCCCCHHH
42.82-
195PhosphorylationPNDEHQATAMADIIE
CCCHHHHHHHHHHHH
15.47-
261N-linked_GlycosylationHVVEVIQNSTAKVIV
HHHHHHHCCCCEEEE
30.1527434672
261N-linked_GlycosylationHVVEVIQNSTAKVIV
HHHHHHHCCCCEEEE
30.1527434672
287N-linked_GlycosylationIKEIVRRNITGKIWL
HHHHHHCCCCCCEEE
26.1327434672
287N-linked_GlycosylationIKEIVRRNITGKIWL
HHHHHHCCCCCCEEE
26.1327434672
336AcetylationGFREFLKKVHPRKSV
CHHHHHHHHCCCCCC
48.1730587449
342PhosphorylationKKVHPRKSVHNGFAK
HHHCCCCCCCCCCHH
29.8616674116
386N-linked_GlycosylationESGDRFSNSSTAFRP
CCCCCCCCCCCCCCC
36.95UniProtKB CARBOHYD
400N-linked_GlycosylationPLCTGDENISSVETP
CCCCCCCCCCCCCCC
44.15UniProtKB CARBOHYD
446N-linked_GlycosylationPGRGLFTNGSCADIK
CCCCCCCCCCCCCHH
32.8027434672
446N-linked_GlycosylationPGRGLFTNGSCADIK
CCCCCCCCCCCCCHH
32.8027434672
468N-linked_GlycosylationLKHLRHLNFTNNMGE
HHHHHHCCCCCCCCC
35.2527434672
468N-linked_GlycosylationLKHLRHLNFTNNMGE
HHHHHHCCCCCCCCC
35.2527434672
488N-linked_GlycosylationECGDLVGNYSIINWH
HCCCEECCEEEEEEE
21.6527434672
488N-linked_GlycosylationECGDLVGNYSIINWH
HCCCEECCEEEEEEE
21.6527434672
541N-linked_GlycosylationSREVPFSNCSRDCLA
CCCCCCCCCCCCCCC
28.3227434672
594N-linked_GlycosylationDDFWSNENHTSCIAK
CCCCCCCCCCHHHHH
48.2427434672
794PhosphorylationCFFFAFKSRKLPENF
HHHHHHHCCCCCCCC
28.3529083192
875PhosphorylationTIEEVRCSTAAHAFK
CCCHHHHHHHHHHHH
15.54-
888PhosphorylationFKVAARATLRRSNVS
HHHHHHHHHHHHCCC
18.4220233724
892PhosphorylationARATLRRSNVSRKRS
HHHHHHHHCCCCCCC
34.8420798521
895PhosphorylationTLRRSNVSRKRSSSL
HHHHHCCCCCCCCCC
36.0123911959
899PhosphorylationSNVSRKRSSSLGGST
HCCCCCCCCCCCCCC
27.5820798521
900PhosphorylationNVSRKRSSSLGGSTG
CCCCCCCCCCCCCCC
33.3528857561
901PhosphorylationVSRKRSSSLGGSTGS
CCCCCCCCCCCCCCC
32.0726657352
906PhosphorylationSSSLGGSTGSTPSSS
CCCCCCCCCCCCCCC
38.13-
912PhosphorylationSTGSTPSSSISSKSN
CCCCCCCCCCCCCCC
32.6626437602
913PhosphorylationTGSTPSSSISSKSNS
CCCCCCCCCCCCCCC
30.7226437602
915PhosphorylationSTPSSSISSKSNSED
CCCCCCCCCCCCCCC
33.399694886
920PhosphorylationSISSKSNSEDPFPQP
CCCCCCCCCCCCCCH
50.93-
997PhosphorylationRNSTHQNSLEAQKSS
CCCHHHHHHHHHHCC
22.4828857561
1061PhosphorylationLVVSSSQSFVISGGG
EEEECCCCEEECCCC
24.35-

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
888TPhosphorylationKinasePRKCAP17252
GPS
888TPhosphorylationKinasePKC-FAMILY-GPS
888TPhosphorylationKinasePKC_GROUP-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseRNF19AQ9NV58
PMID:16513638

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CASR_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 CASR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CASR_HUMANCASRphysical
9722601
FLNA_HUMANFLNAphysical
11390379
CHD8_HUMANCHD8physical
19151705
RN19A_HUMANRNF19Aphysical
16513638
STABP_HUMANSTAMBPphysical
16854379
OS9_MOUSEOs9physical
28419469
OS9_HUMANOS9physical
28419469

Drug and Disease Associations
Kegg Disease
H00239 Bartter syndrome
OMIM Disease
145980Hypocalciuric hypercalcemia, familial 1 (HHC1)
239200Hyperparathyroidism, neonatal severe (NSHPT)
601198Hypocalcemia, autosomal dominant 1 (HYPOC1)
612899Epilepsy, idiopathic generalized 8 (EIG8)
Kegg Drug
D03504 Cinacalcet (USAN)
D03505 Cinacalcet hydrochloride (JAN/USAN); Sensipar (TN)
D08991 Ronacaleret hydrochloride (USAN)
DrugBank
DB01012Cinacalcet
Regulatory Network of CASR_HUMAN

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Related Literatures of Post-Translational Modification

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