KCC2B_HUMAN - dbPTM
KCC2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCC2B_HUMAN
UniProt AC Q13554
Protein Name Calcium/calmodulin-dependent protein kinase type II subunit beta
Gene Name CAMK2B
Organism Homo sapiens (Human).
Sequence Length 666
Subcellular Localization Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Sarcoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side . Cell junction, synapse . In slow-twitch muscle, evenly distributed betwee
Protein Description Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle. In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Participates in the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2..
Protein Sequence MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSVGRQTTAPATMSTAASGTTMGLVEQAKSLLNKKADGVKPQTNSTKNSAAATSPKGTLPPAALEPQTTVIHNPVDGIKESSDSANTTIEDEDAKAPRVPDILSSVRRGSGAPEAEGPLPCPSPAPFSPLPAPSPRISDILNSVRRGSGTPEAEGPLSAGPPPCLSPALLGPLSSPSPRISDILNSVRRGSGTPEAEGPSPVGPPPCPSPTIPGPLPTPSRKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWQNVHFHCSGAPVAPLQ
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
17PhosphorylationFTDEYQLYEDIGKGA
CCCCCHHHHHHCCCH
8.9521082442
26PhosphorylationDIGKGAFSVVRRCVK
HHCCCHHHHHHHHHH
21.1128857561
36PhosphorylationRRCVKLCTGHEYAAK
HHHHHHHCCCHHHHH
52.5929978859
40PhosphorylationKLCTGHEYAAKIINT
HHHCCCHHHHHHHHC
13.2429978859
47PhosphorylationYAAKIINTKKLSARD
HHHHHHHCCCCCHHH
21.1029978859
57UbiquitinationLSARDHQKLEREARI
CCHHHHHHHHHHHHH
49.23-
71PhosphorylationICRLLKHSNIVRLHD
HHHHHHHCCEEEECC
27.0226437602
79PhosphorylationNIVRLHDSISEEGFH
CEEEECCCCCCCCCE
19.7824275569
138UbiquitinationGVVHRDLKPENLLLA
CCCCCCCCHHHHHHH
55.35-
146PhosphorylationPENLLLASKCKGAAV
HHHHHHHHCCCCCCE
38.2628857561
182PhosphorylationAGTPGYLSPEVLRKE
CCCCCCCCHHHHHHH
15.5521815630
227AcetylationHKLYQQIKAGAYDFP
HHHHHHHHHCCCCCC
36.1126051181
227UbiquitinationHKLYQQIKAGAYDFP
HHHHHHHHHCCCCCC
36.112190698
227 (in isoform 1)Ubiquitination-36.1121906983
227 (in isoform 2)Ubiquitination-36.1121906983
227 (in isoform 3)Ubiquitination-36.1121906983
227 (in isoform 4)Ubiquitination-36.1121906983
227 (in isoform 5)Ubiquitination-36.1121906983
227 (in isoform 7)Ubiquitination-36.1121906983
227 (in isoform 6)Ubiquitination-36.1121906983
231PhosphorylationQQIKAGAYDFPSPEW
HHHHHCCCCCCCCCH
19.7328857561
235PhosphorylationAGAYDFPSPEWDTVT
HCCCCCCCCCHHCCC
35.1328857561
240PhosphorylationFPSPEWDTVTPEAKN
CCCCCHHCCCHHHHH
27.6128857561
246UbiquitinationDTVTPEAKNLINQML
HCCCHHHHHHHHHHH
51.10-
254PhosphorylationNLINQMLTINPAKRI
HHHHHHHCCCHHHCC
17.2329396449
259AcetylationMLTINPAKRITAHEA
HHCCCHHHCCCHHHH
45.6625953088
259UbiquitinationMLTINPAKRITAHEA
HHCCCHHHCCCHHHH
45.66-
259MalonylationMLTINPAKRITAHEA
HHCCCHHHCCCHHHH
45.6626320211
268UbiquitinationITAHEALKHPWVCQR
CCHHHHHCCCCHHCH
55.45-
276PhosphorylationHPWVCQRSTVASMMH
CCCHHCHHHHHHHHH
11.0123882029
277PhosphorylationPWVCQRSTVASMMHR
CCHHCHHHHHHHHHH
23.4523663014
280PhosphorylationCQRSTVASMMHRQET
HCHHHHHHHHHHHHH
16.5930631047
287PhosphorylationSMMHRQETVECLKKF
HHHHHHHHHHHHHHH
17.1723882029
299MethylationKKFNARRKLKGAILT
HHHCHHHHHHHHHHH
49.34-
301MethylationFNARRKLKGAILTTM
HCHHHHHHHHHHHHH
49.7024129315
306PhosphorylationKLKGAILTTMLATRN
HHHHHHHHHHHHCCC
12.2121082442
307PhosphorylationLKGAILTTMLATRNF
HHHHHHHHHHHCCCC
13.5221082442
311 (in isoform 8)Phosphorylation-23.3729514088
311PhosphorylationILTTMLATRNFSVGR
HHHHHHHCCCCCCCC
23.3721406692
315 (in isoform 4)Phosphorylation-27.49-
315 (in isoform 8)Phosphorylation-27.4918691976
315PhosphorylationMLATRNFSVGRQTTA
HHHCCCCCCCCCCCC
27.4924670416
315 (in isoform 5)Phosphorylation-27.49-
315 (in isoform 3)Phosphorylation-27.49-
319 (in isoform 4)Phosphorylation-36.96-
319 (in isoform 3)Phosphorylation-36.96-
319 (in isoform 5)Phosphorylation-36.96-
320O-linked_GlycosylationNFSVGRQTTAPATMS
CCCCCCCCCCCCCCC
24.4622564745
320PhosphorylationNFSVGRQTTAPATMS
CCCCCCCCCCCCCCC
24.4620068231
321O-linked_GlycosylationFSVGRQTTAPATMST
CCCCCCCCCCCCCCC
23.4722564745
321PhosphorylationFSVGRQTTAPATMST
CCCCCCCCCCCCCCC
23.4726437602
325PhosphorylationRQTTAPATMSTAASG
CCCCCCCCCCCCCCC
15.5920068231
327PhosphorylationTTAPATMSTAASGTT
CCCCCCCCCCCCCCC
15.5620068231
328PhosphorylationTAPATMSTAASGTTM
CCCCCCCCCCCCCCH
18.5420068231
331PhosphorylationATMSTAASGTTMGLV
CCCCCCCCCCCHHHH
33.9220068231
333PhosphorylationMSTAASGTTMGLVEQ
CCCCCCCCCHHHHHH
15.8922210691
334 (in isoform 4)Phosphorylation-16.87-
334PhosphorylationSTAASGTTMGLVEQA
CCCCCCCCHHHHHHH
16.8722210691
342AcetylationMGLVEQAKSLLNKKA
HHHHHHHHHHHHHCC
41.137662425
343 (in isoform 3)Phosphorylation-40.9024719451
343PhosphorylationGLVEQAKSLLNKKAD
HHHHHHHHHHHHCCC
40.9024719451
355 (in isoform 3)Phosphorylation-47.8224076635
356 (in isoform 3)Phosphorylation-39.4024076635
356PhosphorylationADGVKPQTNSTKNSA
CCCCCCCCCCCCCCC
39.4020068231
357 (in isoform 6)Phosphorylation-42.2920068231
358PhosphorylationGVKPQTNSTKNSAAA
CCCCCCCCCCCCCCC
44.1126437602
358 (in isoform 6)Phosphorylation-44.1120068231
358 (in isoform 3)Phosphorylation-44.1119369195
361 (in isoform 3)Phosphorylation-36.6528348404
362 (in isoform 3)Phosphorylation-22.3526471730
366PhosphorylationTKNSAAATSPKGTLP
CCCCCCCCCCCCCCC
40.6126033855
367PhosphorylationKNSAAATSPKGTLPP
CCCCCCCCCCCCCCH
21.6425849741
371PhosphorylationAATSPKGTLPPAALE
CCCCCCCCCCHHHCC
42.0724076635
381PhosphorylationPAALEPQTTVIHNPV
HHHCCCCCEEEECCC
33.4720068231
382PhosphorylationAALEPQTTVIHNPVD
HHCCCCCEEEECCCC
16.5320068231
394PhosphorylationPVDGIKESSDSANTT
CCCCCCCCCCCCCCC
34.1518510355
395PhosphorylationVDGIKESSDSANTTI
CCCCCCCCCCCCCCC
36.3518510355
397PhosphorylationGIKESSDSANTTIED
CCCCCCCCCCCCCCC
25.9320068231
400PhosphorylationESSDSANTTIEDEDA
CCCCCCCCCCCCHHH
28.9420068231
401PhosphorylationSSDSANTTIEDEDAK
CCCCCCCCCCCHHHC
23.3720068231
417PhosphorylationPRVPDILSSVRRGSG
CCCHHHHHHHHCCCC
27.4124719451
418PhosphorylationRVPDILSSVRRGSGA
CCHHHHHHHHCCCCC
19.0526437602
423PhosphorylationLSSVRRGSGAPEAEG
HHHHHCCCCCCCCCC
29.9425849741
436PhosphorylationEGPLPCPSPAPFSPL
CCCCCCCCCCCCCCC
40.1722673903
441PhosphorylationCPSPAPFSPLPAPSP
CCCCCCCCCCCCCCC
25.1922673903
456PhosphorylationRISDILNSVRRGSGT
CHHHHHHHHHCCCCC
17.3528857561
461PhosphorylationLNSVRRGSGTPEAEG
HHHHHCCCCCCCCCC
37.3722798277
463PhosphorylationSVRRGSGTPEAEGPL
HHHCCCCCCCCCCCC
21.4719764811
471PhosphorylationPEAEGPLSAGPPPCL
CCCCCCCCCCCCCCC
34.0219764811
479PhosphorylationAGPPPCLSPALLGPL
CCCCCCCCHHHHCCC
18.1628348404
490PhosphorylationLGPLSSPSPRISDIL
HCCCCCCCCHHHHHH
28.8517081983
499PhosphorylationRISDILNSVRRGSGT
HHHHHHHHHHCCCCC
17.3528857561
504PhosphorylationLNSVRRGSGTPEAEG
HHHHHCCCCCCCCCC
37.3719764811
506PhosphorylationSVRRGSGTPEAEGPS
HHHCCCCCCCCCCCC
21.4719764811
513PhosphorylationTPEAEGPSPVGPPPC
CCCCCCCCCCCCCCC
42.9728348404
522PhosphorylationVGPPPCPSPTIPGPL
CCCCCCCCCCCCCCC
41.2026437602
524PhosphorylationPPPCPSPTIPGPLPT
CCCCCCCCCCCCCCC
44.1128348404
623PhosphorylationCIAYIRLTQYIDGQG
HHHHHHHHHEECCCC
14.9628152594
625PhosphorylationAYIRLTQYIDGQGRP
HHHHHHHEECCCCCC
8.8528152594

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
287TPhosphorylationKinaseCAMK2BQ13554
GPS
382TPhosphorylationKinaseCAMK2BQ13554
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
287TPhosphorylation

16690701
287TPhosphorylation

16690701

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 KCC2B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTN4_HUMANACTN4physical
11160423
1433B_HUMANYWHABphysical
12619878
KCC2B_HUMANCAMK2Bphysical
15604093
SMYD3_HUMANSMYD3physical
21988832
KCC2B_HUMANCAMK2Bphysical
25416956
KPBB_HUMANPHKBphysical
25416956
RAP2B_HUMANRAP2Bphysical
25416956
RL11_HUMANRPL11physical
25416956
MD2L2_HUMANMAD2L2physical
25416956
MO4L1_HUMANMORF4L1physical
25416956
RBPMS_HUMANRBPMSphysical
25416956
BACH_HUMANACOT7physical
25416956
RFOX2_HUMANRBFOX2physical
25416956
POP5_HUMANPOP5physical
25416956
MED18_HUMANMED18physical
25416956
SPRY7_HUMANSPRYD7physical
25416956
SEM4G_HUMANSEMA4Gphysical
25416956
RM11_HUMANMRPL11physical
25416956
AP5B1_HUMANAP5B1physical
25416956
TTC5_HUMANTTC5physical
25416956
CCM2L_HUMANCCM2Lphysical
25416956
MGT5B_HUMANMGAT5Bphysical
25416956
F1712_HUMANFAM171A2physical
25416956
KR195_HUMANKRTAP19-5physical
25416956
KR197_HUMANKRTAP19-7physical
25416956
KR10B_HUMANKRTAP10-11physical
25416956

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 KCC2B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND MASSSPECTROMETRY.
"Ca2+-calmodulin-dependent protein kinase expression and signalling inskeletal muscle during exercise.";
Rose A.J., Kiens B., Richter E.A.;
J. Physiol. (Lond.) 574:889-903(2006).
Cited for: FUNCTION IN SKELETAL MUSCLE, PHOSPHORYLATION AT THR-287, FUNCTION INPHOSPHORYLATION OF PLN, TISSUE SPECIFICITY, AND INDUCTION.

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