KCAB2_HUMAN - dbPTM
KCAB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCAB2_HUMAN
UniProt AC Q13303
Protein Name Voltage-gated potassium channel subunit beta-2
Gene Name KCNAB2
Organism Homo sapiens (Human).
Sequence Length 367
Subcellular Localization Cytoplasm . Membrane
Peripheral membrane protein
Cytoplasmic side . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cell projection, axon . Cell junction, synapse, synaptosome . Cytoplasm, cytoskeleton . Recruited to the cytoplas
Protein Description Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. [PubMed: 7649300]
Protein Sequence MYPESTTGSPARLSLRQTGSPGMIYSTRYGSPKRQLQFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSIIHEIDSILGNKPYSKKDYRS
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
2Phosphorylation------MYPESTTGS
------CCCCCCCCC		18.7326552605
3 (in isoform 3)Phosphorylation-27.9723663014
5Phosphorylation---MYPESTTGSPAR
---CCCCCCCCCCCE		27.1122115753
5 (in isoform 3)Phosphorylation-27.1123663014
6 (in isoform 3)Phosphorylation-33.2523663014
6Phosphorylation--MYPESTTGSPARL
--CCCCCCCCCCCEE		33.2522115753
7 (in isoform 3)Phosphorylation-44.9623663014
7Phosphorylation-MYPESTTGSPARLS
-CCCCCCCCCCCEEE		44.9623401153
9 (in isoform 3)Phosphorylation-17.1923663014
9PhosphorylationYPESTTGSPARLSLR
CCCCCCCCCCEEEEE		17.1923401153
12MethylationSTTGSPARLSLRQTG
CCCCCCCEEEEECCC		28.35115386339
12 (in isoform 3)Phosphorylation-28.3523663014
14PhosphorylationTGSPARLSLRQTGSP
CCCCCEEEEECCCCC		18.8925159151
14 (in isoform 3)Phosphorylation-18.8923663014
14 (in isoform 2)Phosphorylation-18.8924719451
14O-linked_GlycosylationTGSPARLSLRQTGSP
CCCCCEEEEECCCCC		18.8931492838
15 (in isoform 3)Phosphorylation-5.7923663014
18 (in isoform 2)Phosphorylation-32.94-
18PhosphorylationARLSLRQTGSPGMIY
CEEEEECCCCCCCEE		32.9423401153
20 (in isoform 2)Phosphorylation-22.9725159151
20PhosphorylationLSLRQTGSPGMIYST
EEEECCCCCCCEEEC		22.9721945579
25 (in isoform 2)Phosphorylation-8.63-
25PhosphorylationTGSPGMIYSTRYGSP
CCCCCCEEECCCCCH		8.6321945579
26PhosphorylationGSPGMIYSTRYGSPK
CCCCCEEECCCCCHH		8.7621945579
26O-linked_GlycosylationGSPGMIYSTRYGSPK
CCCCCEEECCCCCHH		8.7631492838
27PhosphorylationSPGMIYSTRYGSPKR
CCCCEEECCCCCHHH		15.7821945579
28MethylationPGMIYSTRYGSPKRQ
CCCEEECCCCCHHHH		28.0724129315
28Asymmetric dimethylargininePGMIYSTRYGSPKRQ
CCCEEECCCCCHHHH		28.07-
29PhosphorylationGMIYSTRYGSPKRQL
CCEEECCCCCHHHHH		23.2624043423
31PhosphorylationIYSTRYGSPKRQLQF
EEECCCCCHHHHHHH		20.5024043423
44UbiquitinationQFYRNLGKSGLRVSC
HHHHHHCCCCCEEEE		44.51-
51 (in isoform 3)Phosphorylation-2.9824719451
57UbiquitinationSCLGLGTWVTFGGQI
EEEECCCEEEECCEE		5.8319608861
57AcetylationSCLGLGTWVTFGGQI
EEEECCCEEEECCEE		5.8319608861
111PhosphorylationKKKGWRRSSLVITTK
HHCCCCCCCEEEEEE		21.3226657352
112PhosphorylationKKGWRRSSLVITTKI
HCCCCCCCEEEEEEE		25.5023401153
116PhosphorylationRRSSLVITTKIFWGG
CCCCEEEEEEEECCC		17.9823882029
117PhosphorylationRSSLVITTKIFWGGK
CCCEEEEEEEECCCC		15.8323882029
124AcetylationTKIFWGGKAETERGL
EEEECCCCHHCCCCC		38.8319608861
124UbiquitinationTKIFWGGKAETERGL
EEEECCCCHHCCCCC		38.8319608861
134UbiquitinationTERGLSRKHIIEGLK
CCCCCCHHHHHHHHH		35.46-
138 (in isoform 3)Ubiquitination-58.85-
157 (in isoform 3)Ubiquitination-10.26-
157AcetylationEYVDVVFANRPDPNT
EEEEEEEECCCCCCC		10.2619608861
167 (in isoform 3)Ubiquitination-52.28-
184PhosphorylationINQGMAMYWGTSRWS
HHHHCHHHCCCCCCC		7.37-
205 (in isoform 3)Phosphorylation-7.24-
206 (in isoform 3)Phosphorylation-34.37-
207AcetylationSVARQFNLTPPICEQ
HHHHHCCCCHHHHHH		8.8619608861
208PhosphorylationVARQFNLTPPICEQA
HHHHCCCCHHHHHHH		28.2924043423
217PhosphorylationPICEQAEYHMFQREK
HHHHHHHHHHHHHHC		11.1224043423
224AcetylationYHMFQREKVEVQLPE
HHHHHHHCEEEEHHH		45.9825953088
224UbiquitinationYHMFQREKVEVQLPE
HHHHHHHCEEEEHHH		45.98-
235UbiquitinationQLPELFHKIGVGAMT
EHHHHHHHHCCCCCC		33.55-
254 (in isoform 2)Ubiquitination-38.0821890473
254UbiquitinationACGIVSGKYDSGIPP
CCCCCCCCCCCCCCC		38.0821890473
266PhosphorylationIPPYSRASLKGYQWL
CCCCCHHHHCCHHHH		29.51-
268 (in isoform 1)Ubiquitination-53.7521890473
268AcetylationPYSRASLKGYQWLKD
CCCHHHHCCHHHHHH		53.7525953088
268UbiquitinationPYSRASLKGYQWLKD
CCCHHHHCCHHHHHH		53.7521890473
268UbiquitinationPYSRASLKGYQWLKD
CCCHHHHCCHHHHHH		53.7521890473
272 (in isoform 3)Ubiquitination-9.26-
274AcetylationLKGYQWLKDKILSEE
HCCHHHHHHHHCCHH		54.7519608861
274UbiquitinationLKGYQWLKDKILSEE
HCCHHHHHHHHCCHH		54.7519608861
276AcetylationGYQWLKDKILSEEGR
CHHHHHHHHCCHHHH		43.9123749302
276UbiquitinationGYQWLKDKILSEEGR
CHHHHHHHHCCHHHH		43.9121890473
276 (in isoform 2)Ubiquitination-43.9121890473
276UbiquitinationGYQWLKDKILSEEGR
CHHHHHHHHCCHHHH		43.91-
290UbiquitinationRRQQAKLKELQAIAE
HHHHHHHHHHHHHHH		56.522189047
290UbiquitinationRRQQAKLKELQAIAE
HHHHHHHHHHHHHHH		56.5221890473
290 (in isoform 1)Ubiquitination-56.5221890473
295AcetylationKLKELQAIAERLGCT
HHHHHHHHHHHHCCC		2.3619608861
316 (in isoform 3)Ubiquitination-28.31-
316UbiquitinationAWCLRNEGVSSVLLG
HHHHHCCCCCHHECC		28.3121890473
322 (in isoform 3)Ubiquitination-5.16-
322AcetylationEGVSSVLLGASNADQ
CCCCHHECCCCCHHH		5.1619608861
324 (in isoform 3)Ubiquitination-10.28-
338UbiquitinationMENIGAIQVLPKLSS
HHHHCHHHHHHHCCH		30.1121890473
338 (in isoform 3)Ubiquitination-30.11-
358AcetylationIDSILGNKPYSKKDY
HHHHHCCCCCCCHHC		43.4625953088
358UbiquitinationIDSILGNKPYSKKDY
HHHHHCCCCCCCHHC		43.46-
360PhosphorylationSILGNKPYSKKDYRS
HHHCCCCCCCHHCCC		34.4319060867
362UbiquitinationLGNKPYSKKDYRS--
HCCCCCCCHHCCC--		43.7719608861
362AcetylationLGNKPYSKKDYRS--
HCCCCCCCHHCCC--		43.7719608861
363UbiquitinationGNKPYSKKDYRS---
CCCCCCCHHCCC---		54.79-
406 (in isoform 3)Ubiquitination--
410Acetylation--------------------------------------------------
--------------------------------------------------		19608861
410 (in isoform 3)Ubiquitination--
411 (in isoform 3)Ubiquitination--
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
31SPhosphorylationKinaseCDK2P24941
PSP
31SPhosphorylationKinaseCDK5Q00535
PSP
266SPhosphorylationKinasePRKCAP17252
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCAB2_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 KCAB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCNA5_HUMANKCNA5physical
23390957
KCNA4_HUMANKCNA4physical
23390957
SIR1_HUMANSIRT1physical
23390957
KCAB2_HUMANKCNAB2physical
25416956
KCAB1_HUMANKCNAB1physical
26186194
GAPD1_HUMANGAPVD1physical
26186194
PUR9_HUMANATICphysical
26344197
NTF2_HUMANNUTF2physical
26344197
TNNC2_HUMANTNNC2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCAB2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-124, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25, AND MASSSPECTROMETRY.

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