TRPV6_HUMAN - dbPTM
TRPV6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRPV6_HUMAN
UniProt AC Q9H1D0
Protein Name Transient receptor potential cation channel subfamily V member 6
Gene Name TRPV6
Organism Homo sapiens (Human).
Sequence Length 765
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine. [PubMed: 11097838]
Protein Sequence MGPLQGDGGPALGGADVAPRLSPVRVWPRPQAPKEPALHPMGLSLPKEKGLILCLWSKFCRWFQRRESWAQSRDEQNLLQQKRIWESPLLLAAKDNDVQALNKLLKYEDCKVHQRGAMGETALHIAALYDNLEAAMVLMEAAPELVFEPMTSELYEGQTALHIAVVNQNMNLVRALLARRASVSARATGTAFRRSPCNLIYFGEHPLSFAACVNSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDRHGDHLQPLDLVPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHTQWTYGPLTSTLYDLTEIDSSGDEQSLLELIITTKKREARQILDQTPVKELVSLKWKRYGRPYFCMLGAIYLLYIICFTMCCIYRPLKPRTNNRTSPRDNTLLQQKLLQEAYMTPKDDIRLVGELVTVIGAIIILLVEVPDIFRMGVTRFFGQTILGGPFHVLIITYAFMVLVTMVMRLISASGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPEELGHFYDYPMALFSTFELFLTIIDGPANYNVDLPFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQIVATTVMLERKLPRCLWPRSGICGREYGLGDRWFLRVEDRQDLNRQRIQRYAQAFHTRGSEDLDKDSVEKLELGCPFSPHLSLPMPSVSRSTSRSSANWERLRQGTLRRDLRGIINRGLEDGESWEYQI
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
107PhosphorylationALNKLLKYEDCKVHQ
HHHHHHCCCCCCCCC
15.86-
144PhosphorylationVLMEAAPELVFEPMT
HHHHHCHHHHEECCC
15.00-
182PhosphorylationALLARRASVSARATG
HHHHHHHHHHHHHCC
2.79-
184PhosphorylationLARRASVSARATGTA
HHHHHHHHHHHCCCC
35.92-
188PhosphorylationASVSARATGTAFRRS
HHHHHHHCCCCCCCC
35.1822210691
190PhosphorylationVSARATGTAFRRSPC
HHHHHCCCCCCCCCC
27.0922210691
201PhosphorylationRSPCNLIYFGEHPLS
CCCCEEEEEECCCCC
14.42-
208N-linked_GlycosylationYFGEHPLSFAACVNS
EEECCCCCEEECCCH
42.93-
248N-linked_GlycosylationHILILQPNKTFACQM
EEEEECCCCCCHHHH
28.5712765696
318PhosphorylationGPLTSTLYDLTEIDS
CCCHHCEEECCCCCC
36.53-
358N-linked_GlycosylationTPVKELVSLKWKRYG
CCHHHHHHHCCHHHC
48.25-
396PhosphorylationYRPLKPRTNNRTSPR
HCCCCCCCCCCCCCC
4.4329052541
398N-linked_GlycosylationPLKPRTNNRTSPRDN
CCCCCCCCCCCCCCC
1.4712765696
398N-linked_GlycosylationPLKPRTNNRTSPRDN
CCCCCCCCCCCCCCC
1.47UniProtKB CARBOHYD
400PhosphorylationKPRTNNRTSPRDNTL
CCCCCCCCCCCCCHH
2.8623090842
401PhosphorylationPRTNNRTSPRDNTLL
CCCCCCCCCCCCHHH
1.8623090842
406PhosphorylationRTSPRDNTLLQQKLL
CCCCCCCHHHHHHHH
58.8123090842
417PhosphorylationQKLLQEAYMTPKDDI
HHHHHHHHCCCHHHH
22.4723090842
419PhosphorylationLLQEAYMTPKDDIRL
HHHHHHCCCHHHHHH
20.6723090842
601PhosphorylationMYSITYAAFAIIATL
HHHHHHHHHHHHHHH
8.3218669648
641PhosphorylationRAQIVATTVMLERKL
HHHHHHHHHHHHCCC
34.1618669648
688PhosphorylationRQRIQRYAQAFHTRG
HHHHHHHHHHHHHCC
27.35-
696PhosphorylationQAFHTRGSEDLDKDS
HHHHHCCCCCCCHHH
41.4628102081
702PhosphorylationGSEDLDKDSVEKLEL
CCCCCCHHHHHHHCC
14.5711248124
703PhosphorylationSEDLDKDSVEKLELG
CCCCCHHHHHHHCCC
5.5928102081
714PhosphorylationLELGCPFSPHLSLPM
HCCCCCCCCCCCCCC
29.0028270605
718PhosphorylationCPFSPHLSLPMPSVS
CCCCCCCCCCCCCCC
22.8228270605
723PhosphorylationHLSLPMPSVSRSTSR
CCCCCCCCCCCCCCC
12.7828270605
727PhosphorylationPMPSVSRSTSRSSAN
CCCCCCCCCCCCCCC
-
728PhosphorylationMPSVSRSTSRSSANW
CCCCCCCCCCCCCCH
22817900
731PhosphorylationVSRSTSRSSANWERL
CCCCCCCCCCCHHHH
-
732PhosphorylationSRSTSRSSANWERLR
CCCCCCCCCCHHHHH
-
742PhosphorylationWERLRQGTLRRDLRG
HHHHHHCCHHHHHHH
11278579
760PhosphorylationRGLEDGESWEYQI--
CCCCCCCCCCCCC--
25159151

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
184SPhosphorylationKinasePRKCBP05771-2
GPS
201YPhosphorylationKinaseSRCP12931
Uniprot
702TPhosphorylationKinaseKPCAP17252
PhosphoELM
728TPhosphorylationKinasePRKCBP05771-2
GPS
742TPhosphorylationKinasePKCAP17252
PSP
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:20843805

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRPV6_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 TRPV6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEDD4_HUMANNEDD4physical
20843805
K1C40_HUMANKRT40physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRPV6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Competitive regulation of CaT-like-mediated Ca2+ entry by proteinkinase C and calmodulin.";
Niemeyer B.A., Bergs C., Wissenbach U., Flockerzi V., Trost C.;
Proc. Natl. Acad. Sci. U.S.A. 98:3600-3605(2001).
Cited for: FUNCTION, INTERACTION WITH CALMODULIN, PHOSPHORYLATION AT THR-702, ANDMUTAGENESIS OF THR-702.

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