KCMA1_RAT - dbPTM
KCMA1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCMA1_RAT
UniProt AC Q62976
Protein Name Calcium-activated potassium channel subunit alpha-1
Gene Name Kcnma1
Organism Rattus norvegicus (Rat).
Sequence Length 1209
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Isoform 7: Endoplasmic reticulum membrane
Multi-pass membrane protein. Has a dominant-negative effect on other isoforms, preventing their localization to the cell membrane.
Protein Description Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX)..
Protein Sequence MANGGGGGGGGSSGSSGGGGGGGGGETALRMSSNIHANHLSLDASSSSSSSSSSSSSSSSSVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKTKEAQKINNGSSQADGTLKPVDEKEEVVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRSRKRILINPGNHLKIQEGTLGFFIASDAKEVKRAFFYCKACHDDVTDPKRIKKCGCRRLEDEQPPTLSPKKKQRNGGMRNSPNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELAKPGKLPLVSVNQEKNSGTHILMITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRPNRPKSRESRDKQKKEMVYR
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
12PhosphorylationGGGGGGGSSGSSGGG
CCCCCCCCCCCCCCC
34.5018573811
27PhosphorylationGGGGGGETALRMSSN
CCCCCHHHHCHHCCC
33.9818573811
119S-palmitoylationLKYLWTVCCHCGGKT
HHHHHHHHHHCCCCC
0.74-
120S-palmitoylationKYLWTVCCHCGGKTK
HHHHHHHHHCCCCCC
2.30-
122S-palmitoylationLWTVCCHCGGKTKEA
HHHHHHHCCCCCCCC
4.85-
136PhosphorylationAQKINNGSSQADGTL
CHHCCCCCCCCCCCC
22.7722673903
137PhosphorylationQKINNGSSQADGTLK
HHCCCCCCCCCCCCC
30.6822673903
142PhosphorylationGSSQADGTLKPVDEK
CCCCCCCCCCCCCCC
31.9622673903
519AcetylationSIKNYHPKIRIITQM
HCCCCCHHHHHHHHH
31.1622902405
581PhosphorylationANLFSMRSFIKIEED
HHHHHCHHCEECCCC
23.7618573811
584UbiquitinationFSMRSFIKIEEDTWQ
HHCHHCEECCCCCHH
41.89-
710PhosphorylationLEDEQPPTLSPKKKQ
CCCCCCCCCCCCCCC
46.6928551015
712PhosphorylationDEQPPTLSPKKKQRN
CCCCCCCCCCCCCCC
36.8327097102
725PhosphorylationRNGGMRNSPNTSPKL
CCCCCCCCCCCCCHH
14.7918573811
728PhosphorylationGMRNSPNTSPKLMRH
CCCCCCCCCCHHHCC
50.1925403869
729PhosphorylationMRNSPNTSPKLMRHD
CCCCCCCCCHHHCCC
27.0325403869
742 (in isoform 8)Phosphorylation-43.2725403869
773 (in isoform 8)Phosphorylation-2.5530240740
805DimethylationSSALIGLRNLVMPLR
HHHHHHHHHHHHCCH
29.26-
805MethylationSSALIGLRNLVMPLR
HHHHHHHHHHHHCCH
29.264199105
847PhosphorylationLHNFPKVSILPGTPL
HHCCCCEEECCCCCC
25.2418573811
913PhosphorylationIGVLQANSQGFTPPG
CCEEECCCCCCCCCC
34.3925403869
917PhosphorylationQANSQGFTPPGMDRS
ECCCCCCCCCCCCCC
35.0825403869
924PhosphorylationTPPGMDRSSPDNSPV
CCCCCCCCCCCCCCC
41.7925403869
925PhosphorylationPPGMDRSSPDNSPVH
CCCCCCCCCCCCCCC
36.8530240740
929PhosphorylationDRSSPDNSPVHGMLR
CCCCCCCCCCCCCCC
35.3630240740
939PhosphorylationHGMLRQPSITTGVNI
CCCCCCCCCCCCCCC
24.9918573811
962PhosphorylationPGKLPLVSVNQEKNS
CCCCCEEEECCCCCC
24.0418573811
1061PhosphorylationNALRGGYSTPQTLAN
HHHCCCCCCHHHHCC
36.5622673903
1062PhosphorylationALRGGYSTPQTLANR
HHCCCCCCHHHHCCH
15.7825403869
1065PhosphorylationGGYSTPQTLANRDRC
CCCCCHHHHCCHHHC
29.1025403869
1120PhosphorylationRLRDAHLSTPSQCTK
EEHHCCCCCCCCCCE
28.5318573811
1162PhosphorylationNAGQSRASLSHSSHS
CCCCCCHHHCCCCCC
29.3318573811
1164PhosphorylationGQSRASLSHSSHSSQ
CCCCHHHCCCCCCCC
20.8727115346
1167PhosphorylationRASLSHSSHSSQSSS
CHHHCCCCCCCCCCC
23.2018573811
1173PhosphorylationSSHSSQSSSKKSSSV
CCCCCCCCCCCCCCC
38.2418573811
1174PhosphorylationSHSSQSSSKKSSSVH
CCCCCCCCCCCCCCC
49.7218573811
1177PhosphorylationSQSSSKKSSSVHSIP
CCCCCCCCCCCCCCC
31.4225575281
1178PhosphorylationQSSSKKSSSVHSIPS
CCCCCCCCCCCCCCC
45.3025575281
1179PhosphorylationSSSKKSSSVHSIPST
CCCCCCCCCCCCCCC
30.8225575281
1182PhosphorylationKKSSSVHSIPSTANR
CCCCCCCCCCCCCCC
33.7630240740
1185PhosphorylationSSVHSIPSTANRPNR
CCCCCCCCCCCCCCC
38.1825575281
1186PhosphorylationSVHSIPSTANRPNRP
CCCCCCCCCCCCCCC
23.6922668510
1195PhosphorylationNRPNRPKSRESRDKQ
CCCCCCCCCCCHHHH
43.92-
1198PhosphorylationNRPKSRESRDKQKKE
CCCCCCCCHHHHHHH
44.67-

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 KCMA1_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCMA1_RAT !!

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 KCMA1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCMA1_RAT

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Related Literatures of Post-Translational Modification

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