TRPM1_HUMAN - dbPTM
TRPM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRPM1_HUMAN
UniProt AC Q7Z4N2
Protein Name Transient receptor potential cation channel subfamily M member 1
Gene Name TRPM1 {ECO:0000312|HGNC:HGNC:7146}
Organism Homo sapiens (Human).
Sequence Length 1603
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Cation channel essential for the depolarizing photoresponse of retinal ON bipolar cells. It is part of the GRM6 signaling cascade. May play a role in metastasis suppression (By similarity). May act as a spontaneously active, calcium-permeable plasma membrane channel..
Protein Sequence MKDSNRCCCGQFTNQHIPPLPSATPSKNEEESKQVETQPEKWSVAKHTQSYPTDSYGVLEFQGGGYSNKAMYIRVSYDTKPDSLLHLMVKDWQLELPKLLISVHGGLQNFEMQPKLKQVFGKGLIKAAMTTGAWIFTGGVSTGVISHVGDALKDHSSKSRGRVCAIGIAPWGIVENKEDLVGKDVTRVYQTMSNPLSKLSVLNNSHTHFILADNGTLGKYGAEVKLRRLLEKHISLQKINTRLGQGVPLVGLVVEGGPNVVSIVLEYLQEEPPIPVVICDGSGRASDILSFAHKYCEEGGIINESLREQLLVTIQKTFNYNKAQSHQLFAIIMECMKKKELVTVFRMGSEGQQDIEMAILTALLKGTNVSAPDQLSLALAWNRVDIARSQIFVFGPHWPPLGSLAPPTDSKATEKEKKPPMATTKGGRGKGKGKKKGKVKEEVEEETDPRKIELLNWVNALEQAMLDALVLDRVDFVKLLIENGVNMQHFLTIPRLEELYNTRLGPPNTLHLLVRDVKKSNLPPDYHISLIDIGLVLEYLMGGAYRCNYTRKNFRTLYNNLFGPKRPKALKLLGMEDDEPPAKGKKKKKKKKEEEIDIDVDDPAVSRFQYPFHELMVWAVLMKRQKMAVFLWQRGEESMAKALVACKLYKAMAHESSESDLVDDISQDLDNNSKDFGQLALELLDQSYKHDEQIAMKLLTYELKNWSNSTCLKLAVAAKHRDFIAHTCSQMLLTDMWMGRLRMRKNPGLKVIMGILLPPTILFLEFRTYDDFSYQTSKENEDGKEKEEENTDANADAGSRKGDEENEHKKQRSIPIGTKICEFYNAPIVKFWFYTISYLGYLLLFNYVILVRMDGWPSLQEWIVISYIVSLALEKIREILMSEPGKLSQKIKVWLQEYWNITDLVAISTFMIGAILRLQNQPYMGYGRVIYCVDIIFWYIRVLDIFGVNKYLGPYVMMIGKMMIDMLYFVVIMLVVLMSFGVARQAILHPEEKPSWKLARNIFYMPYWMIYGEVFADQIDLYAMEINPPCGENLYDEEGKRLPPCIPGAWLTPALMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIMTFHDRPVLPPPMIILSHIYIIIMRLSGRCRKKREGDQEERDRGLKLFLSDEELKRLHEFEEQCVQEHFREKEDEQQSSSDERIRVTSERVENMSMRLEEINERETFMKTSLQTVDLRLAQLEELSNRMVNALENLAGIDRSDLIQARSRASSECEATYLLRQSSINSADGYSLYRYHFNGEELLFEDTSLSTSPGTGVRKKTCSFRIKEEKDVKTHLVPECQNSLHLSLGTSTSATPDGSHLAVDDLKNAEESKLGPDIGISKEDDERQTDSKKEETISPSLNKTDVIHGQDKSDVQNTQLTVETTNIEGTISYPLEETKITRYFPDETINACKTMKSRSFVYSRGRKLVGGVNQDVEYSSITDQQLTTEWQCQVQKITRSHSTDIPYIVSEAAVQAEHKEQFADMQDEHHVAEAIPRIPRLSLTITDRNGMENLLSVKPDQTLGFPSLRSKSLHGHPRNVKSIQGKLDRSGHASSVSSLVIVSGMTAEEKKVKKEKASTETEC
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
5 (in isoform 6)Phosphorylation-51.6629523821
22 (in isoform 5)Phosphorylation-53.0829523821
189PhosphorylationGKDVTRVYQTMSNPL
CCCHHHHHHHHCCCH		8.5824719451
191PhosphorylationDVTRVYQTMSNPLSK
CHHHHHHHHCCCHHH		12.6024719451
197PhosphorylationQTMSNPLSKLSVLNN
HHHCCCHHHHHHCCC		32.5724719451
235PhosphorylationRLLEKHISLQKINTR
HHHHHHCCHHHHHHH		25.1924719451
317PhosphorylationLLVTIQKTFNYNKAQ
HHHHHHHHCCCCHHH		10.75-
418AcetylationKATEKEKKPPMATTK
CCCHHCCCCCCCCCC		56.287479649
423PhosphorylationEKKPPMATTKGGRGK
CCCCCCCCCCCCCCC		23.8417081983
424PhosphorylationKKPPMATTKGGRGKG
CCCCCCCCCCCCCCC		20.3917081983
425AcetylationKPPMATTKGGRGKGK
CCCCCCCCCCCCCCC		55.827479659
430AcetylationTTKGGRGKGKGKKKG
CCCCCCCCCCCCCCC		56.9770663
432AcetylationKGGRGKGKGKKKGKV
CCCCCCCCCCCCCCC		71.6770667
435AcetylationRGKGKGKKKGKVKEE
CCCCCCCCCCCCCHH		75.36134053
436AcetylationGKGKGKKKGKVKEEV
CCCCCCCCCCCCHHH		68.40134057
492PhosphorylationVNMQHFLTIPRLEEL
CCHHHEECHHCHHHH		28.1728348404
813PhosphorylationNEHKKQRSIPIGTKI
CHHHHHCCCCCCCHH		30.1720873877
818PhosphorylationQRSIPIGTKICEFYN
HCCCCCCCHHHHHHC		20.25-
886UbiquitinationILMSEPGKLSQKIKV
HHHCCCCCHHHHHHH		56.5330230243
908UbiquitinationITDLVAISTFMIGAI
HHHHHHHHHHHHHHH		13.0730230243
925UbiquitinationLQNQPYMGYGRVIYC
HCCCCCCCCCCCHHH		18.8530230243
979PhosphorylationIMLVVLMSFGVARQA
HHHHHHHHHCHHHHH		18.06-
1076N-linked_GlycosylationNLLIAVFNNTFFEVK
HHHHHHHCCCCEEEH		39.78-
1095PhosphorylationQVWKFQRYQLIMTFH
CHHEEEEEEEEEEEC		9.26-
1178PhosphorylationEDEQQSSSDERIRVT
HHHHCCCCCHHHHHH		49.0623663014
1224PhosphorylationLAQLEELSNRMVNAL
HHHHHHHHHHHHHHH		26.1825159151
1251PhosphorylationQARSRASSECEATYL
HHHHHCCCHHHHHEE		45.3330576142
1257PhosphorylationSSECEATYLLRQSSI
CCHHHHHEEEHHHHC		15.7030576142
1270PhosphorylationSINSADGYSLYRYHF
HCCCCCCEEEEEEEE		8.96-
1376PhosphorylationTDSKKEETISPSLNK
CCCCCCCCCCCCCCC		28.04-
1434PhosphorylationETINACKTMKSRSFV
HHHHHHHHCCCCCEE		29.7030576142
1436AcetylationINACKTMKSRSFVYS
HHHHHHCCCCCEEEC		48.2012435089
1443PhosphorylationKSRSFVYSRGRKLVG
CCCCEEECCCCEEEC		23.9830576142
1447AcetylationFVYSRGRKLVGGVNQ
EEECCCCEEECCCCC		50.8012435097
1536PhosphorylationNGMENLLSVKPDQTL
CCHHHHHCCCCCCCC		31.1224719451
1542PhosphorylationLSVKPDQTLGFPSLR
HCCCCCCCCCCCCCC		35.91-
1570PhosphorylationIQGKLDRSGHASSVS
HCCCCCCCCCCCCCC		34.3022210691
1574PhosphorylationLDRSGHASSVSSLVI
CCCCCCCCCCCEEEE		26.1222210691
1577PhosphorylationSGHASSVSSLVIVSG
CCCCCCCCEEEEEEC		21.6522210691
1578PhosphorylationGHASSVSSLVIVSGM
CCCCCCCEEEEEECC		25.2122210691
1590"N6,N6-dimethyllysine"SGMTAEEKKVKKEKA
ECCCHHHHHHHHHHC		55.14-
1590MethylationSGMTAEEKKVKKEKA
ECCCHHHHHHHHHHC		55.14-
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 TRPM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRPM1_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 TRPM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRPM1_HUMANTRPM1physical
11535825
Drug and Disease Associations
Kegg Disease
H00787 Congenital stationary night blindness (CSNB), including: CSNB type 1 (CSNB1); CSNB type 2 (CSNB2); C
OMIM Disease
613216Night blindness, congenital stationary, 1C (CSNB1C)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRPM1_HUMAN

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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 THR-423 AND THR-424, ANDMASS SPECTROMETRY.

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