dbPTM

KCMA1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCMA1_MOUSE
UniProt AC	Q08460
Protein Name	Calcium-activated potassium channel subunit alpha-1
Gene Name	Kcnma1
Organism	Mus musculus (Mouse).
Sequence Length	1209
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	MANGGGGGGGSSGGGGGGGGGSGLRMSSNIHANNLSLDASSSSSSSSSSSSSSSSSSSSSVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKTKEAQKINNGSSQADGTLKPVDEKEEVVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRSRKRILINPGNHLKIQEGTLGFFIASDAKEVKRAFFYCKACHDDVTDPKRIKKCGCRRLEDEQPPTLSPKKKQRNGGMRNSPNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELAKPGKLPLVSVNQEKNSGTHILMITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRPNRPKSRESRDKQNRKEMVYR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
22	Phosphorylation	GGGGGGGSGLRMSSN CCCCCCCCCCCCCCC	37.62	27717184
47	Phosphorylation	SSSSSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
48	Phosphorylation	SSSSSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
49	Phosphorylation	SSSSSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
50	Phosphorylation	SSSSSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
51	Phosphorylation	SSSSSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
52	Phosphorylation	SSSSSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
53	S-palmitoylation	SSSSSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	22399288
53	Phosphorylation	SSSSSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
54	S-palmitoylation	SSSSSSSSSSSSSSV CCCCCCCCCCCCCCC	35.87	22399288
56	S-palmitoylation	SSSSSSSSSSSSVHE CCCCCCCCCCCCCCC	35.87	22399288
118	S-palmitoylation	LKYLWTVCCHCGGKT HHHHHHHHHHCCCCC	0.74	-
119	S-palmitoylation	KYLWTVCCHCGGKTK HHHHHHHHHCCCCCC	2.30	-
121	S-palmitoylation	LWTVCCHCGGKTKEA HHHHHHHCCCCCCCC	4.85	-
130	Acetylation	GKTKEAQKINNGSSQ CCCCCCHHCCCCCCC	55.22	7718947
461	Phosphorylation	ALFKRHFTQVEFYQG HHHHHHCEEEEEEEC	26.11	21183079
469	Phosphorylation	QVEFYQGSVLNPHDL EEEEEECCCCCHHHH	14.12	21183079
583	Ubiquitination	FSMRSFIKIEEDTWQ HHCHHCEECCCCCHH	41.89	22790023
583 (in isoform 4)	Ubiquitination	-	41.89	22790023
642	Phosphorylation	YKSANRESRSRKRIL HHHCCCCCCCCCCEE	32.11	-
670 (in isoform 2)	Phosphorylation	-	53.27	21183079
672 (in isoform 2)	Phosphorylation	-	68.94	25521595
701 (in isoform 4)	Phosphorylation	-	46.64	-
709	Phosphorylation	LEDEQPPTLSPKKKQ CCCCCCCCCCCCCCC	46.69	25521595
711	Phosphorylation	DEQPPTLSPKKKQRN CCCCCCCCCCCCCCC	36.83	25521595
722 (in isoform 4)	Phosphorylation	-	43.69	-
724	Phosphorylation	RNGGMRNSPNTSPKL CCCCCCCCCCCCCHH	14.79	25521595
727	Phosphorylation	GMRNSPNTSPKLMRH CCCCCCCCCCHHHCC	50.19	29899451
728	Phosphorylation	MRNSPNTSPKLMRHD CCCCCCCCCHHHCCC	27.03	25521595
750	Phosphorylation	DQIDNMDSNVKKYDS CCCCCCCCCCCCCCC	32.52	27717184
757	Phosphorylation	SNVKKYDSTGMFHWC CCCCCCCCCCCCCCC	24.62	-
763 (in isoform 4)	Phosphorylation	-	2.92	27841257
765 (in isoform 4)	Phosphorylation	-	17.01	29899451
831	Phosphorylation	VFVGSIEYLKREWET EEEECHHHHHHHHHH	18.82	19887442
893	Phosphorylation	DKECILASLNIKSMQ CHHHHHHHCCCCCCC	20.64	24759943
898	Phosphorylation	LASLNIKSMQFDDSI HHHCCCCCCCCCCCC	17.64	24759943
904	Phosphorylation	KSMQFDDSIGVLQAN CCCCCCCCCCEEECC	24.08	24759943
912	Phosphorylation	IGVLQANSQGFTPPG CCEEECCCCCCCCCC	34.39	21183079
916	Phosphorylation	QANSQGFTPPGMDRS ECCCCCCCCCCCCCC	35.08	19060867
923	Phosphorylation	TPPGMDRSSPDNSPV CCCCCCCCCCCCCCC	41.79	25521595
924	Phosphorylation	PPGMDRSSPDNSPVH CCCCCCCCCCCCCCC	36.85	25521595
928	Phosphorylation	DRSSPDNSPVHGMLR CCCCCCCCCCCCCCC	35.36	25521595
938	Phosphorylation	HGMLRQPSITTGVNI CCCCCCCCCCCCCCC	24.99	20415495
940	Phosphorylation	MLRQPSITTGVNIPI CCCCCCCCCCCCCCE	23.10	22210690
941	Phosphorylation	LRQPSITTGVNIPII CCCCCCCCCCCCCEE	37.15	22210690
1000	Phosphorylation	DDPDTELYLTQPFAC CCCCCEEEEECCCCC	11.06	19887442
1059	Phosphorylation	ENALRGGYSTPQTLA HHHHCCCCCCHHHHC	16.52	20415495
1060	Phosphorylation	NALRGGYSTPQTLAN HHHCCCCCCHHHHCC	36.56	29899451
1061	Phosphorylation	ALRGGYSTPQTLANR HHCCCCCCHHHHCCH	15.78	25521595
1064	Phosphorylation	GGYSTPQTLANRDRC CCCCCHHHHCCHHHC	29.10	20415495
1092	Phosphorylation	DLGDGGCYGDLFCKA CCCCCCCCHHHHHHH	19.56	19887442
1161	Phosphorylation	NAGQSRASLSHSSHS CCCCCCHHHCCCCCC	29.33	29899451
1168	Phosphorylation	SLSHSSHSSQSSSKK HHCCCCCCCCCCCCC	31.83	29899451
1169	Phosphorylation	LSHSSHSSQSSSKKS HCCCCCCCCCCCCCC	28.76	29899451
1171	Phosphorylation	HSSHSSQSSSKKSSS CCCCCCCCCCCCCCC	38.23	29899451
1173	Phosphorylation	SHSSQSSSKKSSSVH CCCCCCCCCCCCCCC	49.72	29899451
1177	Phosphorylation	QSSSKKSSSVHSIPS CCCCCCCCCCCCCCC	45.30	29899451
1181	Phosphorylation	KKSSSVHSIPSTANR CCCCCCCCCCCCCCC	33.76	29895711
1184	Phosphorylation	SSVHSIPSTANRPNR CCCCCCCCCCCCCCC	38.18	29895711
1185	Phosphorylation	SVHSIPSTANRPNRP CCCCCCCCCCCCCCC	23.69	19367708
1194	Phosphorylation	NRPNRPKSRESRDKQ CCCCCCCCHHHCHHH	43.92	-
1197	Phosphorylation	NRPKSRESRDKQNRK CCCCCHHHCHHHHHH	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
701	S	Phosphorylation	Kinase	PKACA	P17612	PSP
722	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
899	S	Phosphorylation	Kinase	PKACA	P17612	PSP
938	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KCMA1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TERA_MOUSE	Vcp	physical	19423573
NFL_MOUSE	Nefl	physical	19423573
LMNA_MOUSE	Lmna	physical	19423573
TKT_MOUSE	Tkt	physical	19423573
SPA3K_MOUSE	Serpina3k	physical	19423573
GRP75_MOUSE	Hspa9	physical	19423573
HSP72_MOUSE	Hspa2	physical	19423573
MYH1_MOUSE	Myh1	physical	19423573
HEMO_MOUSE	Hpx	physical	19423573
CO1A1_MOUSE	Col1a1	physical	19423573
STIP1_MOUSE	Stip1	physical	19423573
APOH_MOUSE	Apoh	physical	19423573
INO1_MOUSE	Isyna1	physical	19423573
DPYL2_MOUSE	Dpysl2	physical	19423573
CH60_MOUSE	Hspd1	physical	19423573
AINX_MOUSE	Ina	physical	19423573
VTDB_MOUSE	Gc	physical	19423573
FETUA_MOUSE	Ahsg	physical	19423573
NUCB1_MOUSE	Nucb1	physical	19423573
HSP7C_MOUSE	Hspa8	physical	19423573
GRP78_MOUSE	Hspa5	physical	19423573
HS71L_MOUSE	Hspa1l	physical	19423573
TBA1A_MOUSE	Tuba1a	physical	19423573
A1AT2_MOUSE	Serpina1b	physical	19423573
TBB5_MOUSE	Tubb5	physical	19423573
ATPB_MOUSE	Atp5b	physical	19423573
ACTB_MOUSE	Actb	physical	19423573
ENOG_MOUSE	Eno2	physical	19423573
PDIA3_MOUSE	Pdia3	physical	19423573
FIBB_MOUSE	Fgb	physical	19423573
SERA_MOUSE	Phgdh	physical	19423573
TCPB_MOUSE	Cct2	physical	19423573
RUVB1_MOUSE	Ruvbl1	physical	19423573
VAT1_MOUSE	Vat1	physical	19423573
DHE3_MOUSE	Glud1	physical	19423573
ATPA_MOUSE	Atp5a1	physical	19423573
FUMH_MOUSE	Fh1	physical	19423573
AMRP_MOUSE	Lrpap1	physical	19423573
PSD11_MOUSE	Psmd11	physical	19423573
NDRG1_MOUSE	Ndrg1	physical	19423573
ANXA7_MOUSE	Anxa7	physical	19423573
PRAX_MOUSE	Prx	physical	19423573
ARP3_MOUSE	Actr3	physical	19423573
NFH_MOUSE	Nefh	physical	19423573
GFAP_MOUSE	Gfap	physical	19423573
NFM_MOUSE	Nefm	physical	19423573
CADM3_MOUSE	Cadm3	physical	19423573
EIF3F_MOUSE	Eif3f	physical	19423573
ERLN2_MOUSE	Erlin2	physical	19423573
NUDC_MOUSE	Nudc	physical	19423573
ALDOA_MOUSE	Aldoa	physical	19423573
LDHB_MOUSE	Ldhb	physical	19423573
HEM2_MOUSE	Alad	physical	19423573
LDHA_MOUSE	Ldha	physical	19423573
VA0D1_MOUSE	Atp6v0d1	physical	19423573
ANXA5_MOUSE	Anxa5	physical	19423573
1433T_MOUSE	Ywhaq	physical	19423573
IDH3A_MOUSE	Idh3a	physical	19423573
ANXA3_MOUSE	Anxa3	physical	19423573
TALDO_MOUSE	Taldo1	physical	19423573
THIM_MOUSE	Acaa2	physical	19423573
VDAC1_MOUSE	Vdac1	physical	19423573
G3P_MOUSE	Gapdh	physical	19423573
TCTP_MOUSE	Tpt1	physical	19423573
APOA1_MOUSE	Apoa1	physical	19423573
RB11B_MOUSE	Rab11b	physical	19423573
ETFB_MOUSE	Etfb	physical	19423573
HPCL1_MOUSE	Hpcal1	physical	19423573
MLRS_MOUSE	Mylpf	physical	19423573
AIF1L_MOUSE	Aif1l	physical	19423573
PPIA_MOUSE	Ppia	physical	19423573
COF1_MOUSE	Cfl1	physical	19423573
1433E_MOUSE	Ywhae	physical	19423573
PCNA_MOUSE	Pcna	physical	19423573
1433G_MOUSE	Ywhag	physical	19423573
DDAH1_MOUSE	Ddah1	physical	19423573
PZP_MOUSE	Pzp	physical	19423573
PDXK_MOUSE	Pdxk	physical	19423573
ODPB_MOUSE	Pdhb	physical	19423573
CAH2_MOUSE	Car2	physical	19423573
APOE_MOUSE	Apoe	physical	19423573
PGRC2_MOUSE	Pgrmc2	physical	19423573
PEBP1_MOUSE	Pebp1	physical	19423573
PARK7_MOUSE	Park7	physical	19423573
MTAP_MOUSE	Mtap	physical	19423573
SDHB_MOUSE	Sdhb	physical	19423573
PSA7_MOUSE	Psma7	physical	19423573
LIN7C_MOUSE	Lin7c	physical	19423573
CRYAB_MOUSE	Cryab	physical	19423573
RAP1A_MOUSE	Rap1a	physical	19423573
RL12_MOUSE	Rpl12	physical	19423573
MBP_MOUSE	Mbp	physical	19423573
E41L3_MOUSE	Epb4.1l3	physical	19423573
ALBU_MOUSE	Alb	physical	19423573
KNG1_MOUSE	Kng1	physical	19423573
AMPB_MOUSE	Rnpep	physical	19423573
HNRPK_MOUSE	Hnrnpk	physical	19423573
PLSL_MOUSE	Lcp1	physical	19423573
ACON_MOUSE	Aco2	physical	19423573
TRFE_MOUSE	Trf	physical	19423573
CALR_MOUSE	Calr	physical	19423573
VIME_MOUSE	Vim	physical	19423573
GDIA_MOUSE	Gdi1	physical	19423573
SPRC_MOUSE	Sparc	physical	19423573
INPP_MOUSE	Inpp1	physical	19423573
RCN3_MOUSE	Rcn3	physical	19423573
SUCB1_MOUSE	Sucla2	physical	19423573
IF4A2_MOUSE	Eif4a2	physical	19423573
KCRM_MOUSE	Ckm	physical	19423573
MMSA_MOUSE	Aldh6a1	physical	19423573
DLDH_MOUSE	Dld	physical	19423573
ENOB_MOUSE	Eno3	physical	19423573
CTBP1_MOUSE	Ctbp1	physical	19423573
AATC_MOUSE	Got1	physical	19423573
OAT_MOUSE	Oat	physical	19423573
SPB6_MOUSE	Serpinb6a	physical	19423573
1433B_MOUSE	Ywhab	physical	19423573
CALB2_MOUSE	Calb2	physical	19423573
1433F_MOUSE	Ywhah	physical	19423573
UCHL1_MOUSE	Uchl1	physical	19423573
GDIR2_MOUSE	Arhgdib	physical	19423573
CBX1_MOUSE	Cbx1	physical	19423573
LGUL_MOUSE	Glo1	physical	19423573
HEBP1_MOUSE	Hebp1	physical	19423573
PRDX2_MOUSE	Prdx2	physical	19423573
1433Z_MOUSE	Ywhaz	physical	19423573
KAD1_MOUSE	Ak1	physical	19423573
RAB1A_MOUSE	Rab1	physical	19423573
KCY_MOUSE	Cmpk1	physical	19423573
IDI1_MOUSE	Idi1	physical	19423573
INMT_MOUSE	Inmt	physical	19423573
APT_MOUSE	Aprt	physical	19423573
GPX1_MOUSE	Gpx1	physical	19423573
TPIS_MOUSE	Tpi1	physical	19423573
MET7B_MOUSE	Mettl7b	physical	19423573
LEG1_MOUSE	Lgals1	physical	19423573
STMN1_MOUSE	Stmn1	physical	19423573
MDHM_MOUSE	Mdh2	physical	19423573
HBB1_MOUSE	Hbb-b1	physical	19423573
HBB2_MOUSE	Hbb-b2	physical	19423573
GSTM1_MOUSE	Gstm1	physical	19423573
TAGL_MOUSE	Tagln	physical	19423573
SODM_MOUSE	Sod2	physical	19423573
CO1A2_MOUSE	Col1a2	physical	19423573
ACTG_MOUSE	Actg1	physical	19423573
MYP0_MOUSE	Mpz	physical	19423573
MGST1_MOUSE	Mgst1	physical	19423573
AMPD2_MOUSE	Ampd2	physical	20114047
GCP4_MOUSE	Tubgcp4	physical	20114047
GCP2_MOUSE	Tubgcp2	physical	20114047
AT1A1_MOUSE	Atp1a1	physical	20114047
PI3R4_MOUSE	Pik3r4	physical	20114047
ACTY_MOUSE	Actr1b	physical	20114047
K1107_MOUSE	A830010M20Rik	physical	20114047
AT1A2_MOUSE	Atp1a2	physical	20114047
AT1A3_MOUSE	Atp1a3	physical	20114047
PK3C3_MOUSE	Pik3c3	physical	20114047
KHDR1_MOUSE	Khdrbs1	physical	20114047
TBG1_MOUSE	Tubg1	physical	20114047
HSP7C_MOUSE	Hspa8	physical	20114047
ACTZ_MOUSE	Actr1a	physical	20114047
GCP3_MOUSE	Tubgcp3	physical	20114047
DYN1_MOUSE	Dnm1	physical	20114047
KIF5C_MOUSE	Kif5c	physical	20114047
EF1A1_MOUSE	Eef1a1	physical	20114047
ACK1_MOUSE	Tnk2	physical	20114047
STXB1_MOUSE	Stxbp1	physical	20114047
SIA8B_MOUSE	St8sia2	physical	20114047
P53_MOUSE	Trp53	physical	25581503
FADD_MOUSE	Fadd	physical	25581503

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KCMA1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-711 AND THR-1061, ANDMASS SPECTROMETRY.	17114649 [Abstract]