TRPC4_HUMAN - dbPTM
TRPC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRPC4_HUMAN
UniProt AC Q9UBN4
Protein Name Short transient receptor potential channel 4
Gene Name TRPC4
Organism Homo sapiens (Human).
Sequence Length 977
Subcellular Localization Membrane
Multi-pass membrane protein. Cell membrane
Multi-pass membrane protein. Enhanced insertion into the cell membrane after activation of the EGF receptor.
Protein Description Form a receptor-activated non-selective calcium permeant cation channel. Acts as a cell-cell contact-dependent endothelial calcium entry channel. Probably operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Mediates cation entry, with an enhanced permeability to barium over calcium. May also be activated by intracellular calcium store depletion..
Protein Sequence MAQFYYKRNVNAPYRDRIPLRIVRAESELSPSEKAYLNAVEKGDYASVKKSLEEAEIYFKININCIDPLGRTALLIAIENENLELIELLLSFNVYVGDALLHAIRKEVVGAVELLLNHKKPSGEKQVPPILLDKQFSEFTPDITPIILAAHTNNYEIIKLLVQKGVSVPRPHEVRCNCVECVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDPFLTAFQLSWELQELSKVENEFKSEYEELSRQCKQFAKDLLDQTRSSRELEIILNYRDDNSLIEEQSGNDLARLKLAIKYRQKEFVAQPNCQQLLASRWYDEFPGWRRRHWAVKMVTCFIIGLLFPVFSVCYLIAPKSPLGLFIRKPFIKFICHTASYLTFLFLLLLASQHIDRSDLNRQGPPPTIVEWMILPWVLGFIWGEIKQMWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYSALNPRESWDMWHPTLVAEALFAIANIFSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYEETKGLTCKGIRCEKQNNAFSTLFETLQSLFWSIFGLINLYVTNVKAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFEEGGTLPTPFNVIPSPKSLWYLIKWIWTHLCKKKMRRKPESFGTIGRRAADNLRRHHQYQEVMRNLVKRYVAAMIRDAKTEEGLTEENFKELKQDISSFRFEVLGLLRGSKLSTIQSANASKESSNSADSDEKSDSEGNSKDKKKNFSLFDLTTLIHPRSAAIASERHNISNGSALVVQEPPREKQRKVNFVTDIKNFGLFHRRSKQNAAEQNANQIFSVSEEVARQQAAGPLERNIQLESRGLASRGDLSIPGLSEQCVLVDHRERNTDTLGLQVGKRVCPFKSEKVVVEDTVPIIPKEKHAKEEDSSIDYDLNLPDTVTHEDYVTTRL
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
5Phosphorylation---MAQFYYKRNVNA
---CCCCCCCCCCCC		8.9426074081
6Phosphorylation--MAQFYYKRNVNAP
--CCCCCCCCCCCCC		12.5426074081
14PhosphorylationKRNVNAPYRDRIPLR
CCCCCCCCCCCCCEE		23.8026074081
32PhosphorylationAESELSPSEKAYLNA
CCCCCCHHHHHHHHH		48.6422985185
167PhosphorylationLLVQKGVSVPRPHEV
HHHHCCCCCCCCCCC		34.7627174698
193PhosphorylationDVDSLRHSRSRLNIY
CHHHHHHHHHHHHHH		26.0520068231
195PhosphorylationDSLRHSRSRLNIYKA
HHHHHHHHHHHHHHH		44.1020068231
200PhosphorylationSRSRLNIYKALASPS
HHHHHHHHHHHHCCC		6.8024260401
205PhosphorylationNIYKALASPSLIALS
HHHHHHHCCCEEEEC		18.83-
207PhosphorylationYKALASPSLIALSSE
HHHHHCCCEEEECCC		29.88-
213PhosphorylationPSLIALSSEDPFLTA
CCEEEECCCCCHHHH		47.04-
390O-linked_GlycosylationASQHIDRSDLNRQGP
HHCCCCHHHHHCCCC		42.5829351928
429PhosphorylationWDGGLQDYIHDWWNL
HCCCHHHHHHHHHHH		6.2824043423
443PhosphorylationLMDFVMNSLYLATIS
HHHHHHHHHHHHHHH		10.5724043423
445PhosphorylationDFVMNSLYLATISLK
HHHHHHHHHHHHHHH		8.2924043423
448PhosphorylationMNSLYLATISLKIVA
HHHHHHHHHHHHHHH		14.4324043423
450PhosphorylationSLYLATISLKIVAFV
HHHHHHHHHHHHHHH		21.1824043423
489PhosphorylationAIANIFSSLRLISLF
HHHHHHHHHHHHHHH		13.5324719451
523PhosphorylationILKFLFIYCLVLLAF
HHHHHHHHHHHHHHH		3.4118083107
538PhosphorylationANGLNQLYFYYEETK
HCCCCHHHHEHHHHC		4.6418083107
541PhosphorylationLNQLYFYYEETKGLT
CCHHHHEHHHHCCCE		9.4418083107
624PhosphorylationIAMMNNSYQLIADHA
HHHHCCCHHHHHHCC		14.95-
688PhosphorylationKMRRKPESFGTIGRR
HHHCCCHHCCHHHHH		37.1928674419
706PhosphorylationNLRRHHQYQEVMRNL
HHHHHHHHHHHHHHH		11.4118083107
781PhosphorylationSADSDEKSDSEGNSK
CCCCCCCCCCCCCCC		44.30-
783PhosphorylationDSDEKSDSEGNSKDK
CCCCCCCCCCCCCCH		55.27-
787PhosphorylationKSDSEGNSKDKKKNF
CCCCCCCCCCHHHCC		53.76-
918PhosphorylationHRERNTDTLGLQVGK
CCCCCCCCCCCCCCC		22.2322210691
955PhosphorylationKHAKEEDSSIDYDLN
HCCCCCCCCCCCCCC		32.2624275569
956PhosphorylationHAKEEDSSIDYDLNL
CCCCCCCCCCCCCCC		31.6224275569
959PhosphorylationEEDSSIDYDLNLPDT
CCCCCCCCCCCCCCC		22.2116144838
972PhosphorylationDTVTHEDYVTTRL--
CCCCHHHHCCCCC--		9.1912154080
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
239SPhosphorylationKinasePRKG1Q13976
GPS
959YPhosphorylationKinaseFYNP06241
Uniprot
972YPhosphorylationKinaseFYNP06241
Uniprot
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:17110928
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRPC4_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 TRPC4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRPC3_HUMANTRPC3physical
12857742
TRPC6_HUMANTRPC6physical
12857742
TRPC1_HUMANTRPC1physical
12857742
TRPC4_HUMANTRPC4physical
12032305
TRPC5_HUMANTRPC5physical
12032305
ITPR2_HUMANITPR2physical
11163362
ITPR3_HUMANITPR3physical
11163362
ITPR1_HUMANITPR1physical
11163362
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRPC4_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-195, ANDMASS SPECTROMETRY.
"Epidermal growth factor induces tyrosine phosphorylation, membraneinsertion, and activation of transient receptor potential channel 4.";
Odell A.F., Scott J.L., Van Helden D.F.;
J. Biol. Chem. 280:37974-37987(2005).
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-959 ANDTYR-972, AND MUTAGENESIS OF TYR-959 AND TYR-972.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory