KCMA1_HUMAN - dbPTM
KCMA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCMA1_HUMAN
UniProt AC Q12791
Protein Name Calcium-activated potassium channel subunit alpha-1
Gene Name KCNMA1
Organism Homo sapiens (Human).
Sequence Length 1236
Subcellular Localization Cell membrane
Multi-pass membrane protein .
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 MANGGGGGGGSSGGGGGGGGSSLRMSSNIHANHLSLDASSSSSSSSSSSSSSSSSSSSSSVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKTKEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRPKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERAFPLSSVSVNDCSTSFRAFEDEQPSTLSPKKKQRNGGMRNSPNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRQNRPKSRESRDKQKYVQEERL
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
12PhosphorylationGGGGGGSSGGGGGGG
CCCCCCCCCCCCCCC		44.7418491316
21PhosphorylationGGGGGGGSSLRMSSN
CCCCCCCCCCCCCCC		29.4923403867
22PhosphorylationGGGGGGSSLRMSSNI
CCCCCCCCCCCCCCC		24.2223403867
41PhosphorylationLSLDASSSSSSSSSS
EEEECCCCCCCCCCC		31.5719664995
42PhosphorylationSLDASSSSSSSSSSS
EEECCCCCCCCCCCC		35.87-
43PhosphorylationLDASSSSSSSSSSSS
EECCCCCCCCCCCCC		35.87-
44PhosphorylationDASSSSSSSSSSSSS
ECCCCCCCCCCCCCC		35.87-
45PhosphorylationASSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
46PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
47PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
48PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
49PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.8719664994
50PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.8719664994
51PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
52PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
53PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
55PhosphorylationSSSSSSSSSSSSSVH
CCCCCCCCCCCCCCC		35.87-
118S-palmitoylationLKYLWTVCCHCGGKT
HHHHHHHHHHCCCCC		0.7422399288
119S-palmitoylationKYLWTVCCHCGGKTK
HHHHHHHHHCCCCCC		2.3022399288
121S-palmitoylationLWTVCCHCGGKTKEA
HHHHHHHCCCCCCCC		4.8522399288
511PhosphorylationSNIMRVISIKNYHPK
HHHCHHHHCCCCCHH		25.3424719451
536SulfoxidationHNKAHLLNIPSWNWK
CCCHHHCCCCCCCCC		50.9516396928
562PhosphorylationKLGFIAQSCLAQGLS
HHHHHHHHHHHHCHH		11.32-
569PhosphorylationSCLAQGLSTMLANLF
HHHHHCHHHHHHHHH		20.7022817900
580PhosphorylationANLFSMRSFIKIEED
HHHHHCHHCEECCCC		23.7624719451
685PhosphorylationKACHDDITDPKRIKK
HHCCCCCCCHHHHHH		53.9224719451
704 (in isoform 5)Phosphorylation-37.7422199227
704 (in isoform 2)Phosphorylation-37.7422199227
705 (in isoform 5)Phosphorylation-13.5822199227
705 (in isoform 2)Phosphorylation-13.5822199227
707 (in isoform 5)Phosphorylation-27.3820886841
707 (in isoform 2)Phosphorylation-27.3820886841
712SulfoxidationRMRRACCFDCGRSER
HHHHHCCCCCCCCHH		9.7816396928
724 (in isoform 4)Phosphorylation-2.4622199227
733 (in isoform 4)Phosphorylation-49.9629514088
734PhosphorylationRVRGNVDTLERAFPL
CCCCCHHHHHHHCCC		26.6623879269
734 (in isoform 4)Phosphorylation-26.6629514088
736 (in isoform 4)Phosphorylation-44.0222199227
739SulfoxidationVDTLERAFPLSSVSV
HHHHHHHCCCCCEEH		8.6116396928
756 (in isoform 7)Phosphorylation-12.0922199227
763PhosphorylationFEDEQPSTLSPKKKQ
CCCCCCCCCCCCCCC		37.63-
765 (in isoform 7)Phosphorylation-34.4629514088
765PhosphorylationDEQPSTLSPKKKQRN
CCCCCCCCCCCCCCC		34.4622496350
766 (in isoform 7)Phosphorylation-56.4429514088
768 (in isoform 7)Phosphorylation-58.4822199227
778PhosphorylationRNGGMRNSPNTSPKL
CCCCCCCCCCCCCHH		14.7922199227
781PhosphorylationGMRNSPNTSPKLMRH
CCCCCCCCCCHHHCC		50.1922199227
782PhosphorylationMRNSPNTSPKLMRHD
CCCCCCCCCHHHCCC		27.0322199227
970PhosphorylationQANSQGFTPPGMDRS
ECCCCCCCCCCCCCC		35.0828348404
977PhosphorylationTPPGMDRSSPDNSPV
CCCCCCCCCCCCCCC		41.7928857561
978PhosphorylationPPGMDRSSPDNSPVH
CCCCCCCCCCCCCCC		36.8511078709
982PhosphorylationDRSSPDNSPVHGMLR
CCCCCCCCCCCCCCC		35.3627732954
992PhosphorylationHGMLRQPSITTGVNI
CCCCCCCCCCCCCCC		24.9911078709
1086PhosphorylationENALRGGYSTPQTLA
HHHHCCCCCCHHHHC		16.5219060867
1088PhosphorylationALRGGYSTPQTLANR
HHCCCCCCHHHHCCH		15.7824076635
1091PhosphorylationGGYSTPQTLANRDRC
CCCCCHHHHCCHHHC		29.1025307156
1146PhosphorylationRLRDAHLSTPSQCTK
EEHHCCCCCCCCCCE		28.53-
1149PhosphorylationDAHLSTPSQCTKRYV
HCCCCCCCCCCEEEE		37.67-
1152PhosphorylationLSTPSQCTKRYVITN
CCCCCCCCEEEEECC		15.77-
1188PhosphorylationNAGQSRASLSHSSHS
CCCCCCHHHCCCCCC		29.3328348404
1190PhosphorylationGQSRASLSHSSHSSQ
CCCCHHHCCCCCCCC		20.8728348404
1193PhosphorylationRASLSHSSHSSQSSS
CHHHCCCCCCCCCCC		23.2026657352
1196PhosphorylationLSHSSHSSQSSSKKS
HCCCCCCCCCCCCCC		28.76-
1200PhosphorylationSHSSQSSSKKSSSVH
CCCCCCCCCCCCCCC		49.7219592459
1203PhosphorylationSQSSSKKSSSVHSIP
CCCCCCCCCCCCCCC		31.4228857561
1204PhosphorylationQSSSKKSSSVHSIPS
CCCCCCCCCCCCCCC		45.3026657352
1205PhosphorylationSSSKKSSSVHSIPST
CCCCCCCCCCCCCCC		30.8226657352
1208PhosphorylationKKSSSVHSIPSTANR
CCCCCCCCCCCCCCC		33.7627732954
1211PhosphorylationSSVHSIPSTANRQNR
CCCCCCCCCCCCCCC		38.1827732954
1212PhosphorylationSVHSIPSTANRQNRP
CCCCCCCCCCCCCCC		23.6927732954
1215MethylationSIPSTANRQNRPKSR
CCCCCCCCCCCCCCC		32.4624391403
1221PhosphorylationNRQNRPKSRESRDKQ
CCCCCCCCCHHHHHH		43.92-
1224PhosphorylationNRPKSRESRDKQKYV
CCCCCCHHHHHHHHH		44.67-
1230PhosphorylationESRDKQKYVQEERL-
HHHHHHHHHHHHCC-		12.60-
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
1200SPhosphorylationKinasePRKCAP17252
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCMA1_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 KCMA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAV1_HUMANCAV1physical
15703204
CAV2_HUMANCAV2physical
15703204
CAV3_HUMANCAV3physical
15703204
ACTA_HUMANACTA2physical
15703204
ACTH_HUMANACTG2physical
15703204
TA2R_HUMANTBXA2Rphysical
20959415
KCMA1_HUMANKCNMA1physical
20959415
Drug and Disease Associations
Kegg Disease
H01258 Generalized epilepsy and paroxysmal dyskinesia (GEPD)
OMIM Disease
609446Generalized epilepsy and paroxysmal dyskinesia (GEPD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCMA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1086, AND MASSSPECTROMETRY.

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