KCNA5_HUMAN - dbPTM
KCNA5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCNA5_HUMAN
UniProt AC P22460
Protein Name Potassium voltage-gated channel subfamily A member 5
Gene Name KCNA5
Organism Homo sapiens (Human).
Sequence Length 613
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. [PubMed: 12130714 Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation]
Protein Sequence MEIALVPLENGGAMTVRGGDEARAGCGQATGGELQCPPTAGLSDGPKEPAPKGRGAQRDADSGVRPLPPLPDPGVRPLPPLPEELPRPRRPPPEDEEEEGDPGLGTVEDQALGTASLHHQRVHINISGLRFETQLGTLAQFPNTLLGDPAKRLRYFDPLRNEYFFDRNRPSFDGILYYYQSGGRLRRPVNVSLDVFADEIRFYQLGDEAMERFREDEGFIKEEEKPLPRNEFQRQVWLIFEYPESSGSARAIAIVSVLVILISIITFCLETLPEFRDERELLRHPPAPHQPPAPAPGANGSGVMAPPSGPTVAPLLPRTLADPFFIVETTCVIWFTFELLVRFFACPSKAGFSRNIMNIIDVVAIFPYFITLGTELAEQQPGGGGGGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADNQGTHFSSIPDAFWWAVVTMTTVGYGDMRPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDHEEPAVLKEEQGTQSQGPGLDRGVQRKVSGSRGSFCKAGGTLENADSARRGSCPLEKCNVKAKSNVDLRRSLYALCLDTSRETDL
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
15PhosphorylationLENGGAMTVRGGDEA
CCCCCEEEEECCHHH		13.4016466689
62PhosphorylationGAQRDADSGVRPLPP
CCCCCCCCCCCCCCC		40.6922496350
127PhosphorylationQRVHINISGLRFETQ
CEEEEEECCEEEEEE		27.5624719451
163PhosphorylationFDPLRNEYFFDRNRP
CCCCCCCCCCCCCCC		17.07-
192PhosphorylationLRRPVNVSLDVFADE
EECEEEEEEEEHHCC		17.41-
203PhosphorylationFADEIRFYQLGDEAM
HHCCEEEHHCCHHHH		7.93-
221SumoylationREDEGFIKEEEKPLP
HHCCCCCCCCCCCCC		57.73-
221SumoylationREDEGFIKEEEKPLP
HHCCCCCCCCCCCCC		57.7317261810
331S-nitrosocysteineFFIVETTCVIWFTFE
EEEEECCHHHHHHHH		2.46-
331S-nitrosylationFFIVETTCVIWFTFE
EEEEECCHHHHHHHH		2.4622178444
346S-palmitoylationLLVRFFACPSKAGFS
HHHHHHHCCCCCCCC		3.10-
346S-nitrosylationLLVRFFACPSKAGFS
HHHHHHHCCCCCCCC		3.1022178444
346S-nitrosocysteineLLVRFFACPSKAGFS
HHHHHHHCCCCCCCC		3.10-
412AcetylationVRVFRIFKLSRHSKG
HHHHHHHHHCCCCCH		43.0919413330
414PhosphorylationVFRIFKLSRHSKGLQ
HHHHHHHCCCCCHHH		28.6526074081
417PhosphorylationIFKLSRHSKGLQILG
HHHHCCCCCHHHHHH		27.5826074081
426PhosphorylationGLQILGKTLQASMRE
HHHHHHHHHHHHHHH		23.4626074081
430PhosphorylationLGKTLQASMRELGLL
HHHHHHHHHHHHHHH		12.8626074081
498PhosphorylationVGGKIVGSLCAIAGV
ECCCHHHHHHHHHHH		14.91-
536SumoylationHEEPAVLKEEQGTQS
CCCCCEECCCCCCCC		53.2417261810
536SumoylationHEEPAVLKEEQGTQS
CCCCCEECCCCCCCC		53.24-
557PhosphorylationRGVQRKVSGSRGSFC
HHHCEECCCCCCCCC		33.80-
559PhosphorylationVQRKVSGSRGSFCKA
HCEECCCCCCCCCCC		26.43-
575PhosphorylationGTLENADSARRGSCP
CEECCHHHHCCCCCC		22.67-
592PhosphorylationKCNVKAKSNVDLRRS
HCCCCCCCCCHHHHH		47.12-
604S-palmitoylationRRSLYALCLDTSRET
HHHHHHHHHCCCCCC		2.1618344374
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
15TPhosphorylationKinasePRKCAP17252
GPS
557SPhosphorylationKinasePKA-Uniprot
559SPhosphorylationKinaseAMPKA1Q13131
PSP
592SPhosphorylationKinaseAMPKA1Q13131
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
221KSumoylation

17261810
536KSumoylation

17261810
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 KCNA5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DLG1_HUMANDLG1physical
12970345
DLG4_HUMANDLG4physical
12860415
ACTN2_HUMANACTN2physical
12860415
KCNA2_HUMANKCNA2physical
12815189
ACTN2_HUMANACTN2physical
10812072
FHL1_HUMANFHL1physical
22053194
ACTN2_HUMANACTN2physical
11389904
TFR1_HUMANTFRCphysical
18218624
KCNA3_HUMANKCNA3physical
18218624
KCNA5_HUMANKCNA5physical
18218624
RB11A_RATRab11aphysical
19706553
KCNA2_HUMANKCNA2physical
11149959
KCNA4_HUMANKCNA4physical
11149959
FYN_HUMANFYNphysical
11149959
SRC_HUMANSRCphysical
11149959
KCAB1_HUMANKCNAB1physical
22547057
RACK1_HUMANGNB2L1physical
22547057
KPCB_HUMANPRKCBphysical
22547057
KPCT_HUMANPRKCQphysical
22547057
FHL1_HUMANFHL1physical
18281375
ACK1_HUMANTNK2physical
14506255
KCAB2_HUMANKCNAB2physical
23390957
SIR1_HUMANSIRT1physical
23390957
CHIP_HUMANSTUB1physical
26232501
HSP7C_HUMANHSPA8physical
26232501
KCNA3_HUMANKCNA3physical
28514442
NPHP1_HUMANNPHP1physical
28514442
KCAB2_HUMANKCNAB2physical
28514442
NB5R1_HUMANCYB5R1physical
28514442
ADCK2_HUMANADCK2physical
28514442
AT2A3_HUMANATP2A3physical
28514442
GOLM1_HUMANGOLM1physical
28514442
DOLK_HUMANDOLKphysical
28514442
CA043_HUMANC1orf43physical
28514442
ZNT6_HUMANSLC30A6physical
28514442
SARAF_HUMANSARAFphysical
28514442
DJC18_HUMANDNAJC18physical
28514442
AT2B4_HUMANATP2B4physical
28514442
5NT3A_HUMANNT5C3Aphysical
28514442
TM223_HUMANTMEM223physical
28514442
ANKL2_HUMANANKLE2physical
28514442
RHBD3_HUMANRHBDD3physical
28514442
GHDC_HUMANGHDCphysical
28514442
YIPF4_HUMANYIPF4physical
28514442
ABCBA_HUMANABCB10physical
28514442
VANG2_HUMANVANGL2physical
28514442
LEMD2_HUMANLEMD2physical
28514442
ABCD4_HUMANABCD4physical
28514442
S27A6_HUMANSLC27A6physical
28514442
TMX2_HUMANTMX2physical
28514442
ADCY3_HUMANADCY3physical
28514442
Drug and Disease Associations
Kegg Disease
H00731 Atrial fibrillation
OMIM Disease
612240Atrial fibrillation, familial, 7 (ATFB7)
Kegg Drug
D00631 Bepridil hydrochloride hydrate (JAN); Bepridil hydrochloride (USAN); Vascor (TN)
D00640 Propafenone hydrochloride (JP16/USP); Rythmol (TN)
D01554 Pilsicainide hydrochloride hydrate (JAN); Pilsicainide hydrochloride; SUN 1165 (TN); Sunrythm (TN)
D03547 Clofilium phosphate (USAN/INN)
D07520 Bepridil (INN); Bepadin (TN)
D08377 Pilsicainide (INN)
D08435 Propafenone (INN); Propafenon hexal (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCNA5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"SUMO modification regulates inactivation of the voltage-gatedpotassium channel Kv1.5.";
Benson M.D., Li Q.J., Kieckhafer K., Dudek D., Whorton M.R.,Sunahara R.K., Iniguez-Lluhi J.A., Martens J.R.;
Proc. Natl. Acad. Sci. U.S.A. 104:1805-1810(2007).
Cited for: SUMOYLATION AT LYS-221 AND LYS-536, INTERACTION WITH UBE2I, ANDMUTAGENESIS OF ILE-220; LYS-221; LEU-535 AND LYS-536.

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