KCC2B_RAT - dbPTM
KCC2B_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCC2B_RAT
UniProt AC P08413
Protein Name Calcium/calmodulin-dependent protein kinase type II subunit beta
Gene Name Camk2b
Organism Rattus norvegicus (Rat).
Sequence Length 542
Subcellular Localization Sarcoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side. Cell junction, synapse . Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Colocalizes with the cortical actin cytoskeleton by
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 MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSVGRQTTAPATMSTAASGTTMGLVEQAKSLLNKKADGVKPQTNSTKNSSAITSPKGSLPPAALEPQTTVIHNPVDGIKESSDSTNTTIEDEDAKARKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRPDGKWQNVHFHCSGAPVAPLQ
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
14PhosphorylationCTRFTDEYQLYEDIG
ECCCCCCCHHHHHHC
13.46-
17PhosphorylationFTDEYQLYEDIGKGA
CCCCCHHHHHHCCCH
8.95-
22UbiquitinationQLYEDIGKGAFSVVR
HHHHHHCCCHHHHHH
47.61-
26PhosphorylationDIGKGAFSVVRRCVK
HHCCCHHHHHHHHHH
21.1125403869
33AcetylationSVVRRCVKLCTGHEY
HHHHHHHHHHCCCHH
41.2825786129
33UbiquitinationSVVRRCVKLCTGHEY
HHHHHHHHHHCCCHH
41.28-
40PhosphorylationKLCTGHEYAAKIINT
HHHCCCHHHHHHHHC
13.24-
43UbiquitinationTGHEYAAKIINTKKL
CCCHHHHHHHHCCCC
35.63-
48UbiquitinationAAKIINTKKLSARDH
HHHHHHCCCCCHHHH
47.42-
49UbiquitinationAKIINTKKLSARDHQ
HHHHHCCCCCHHHHH
45.71-
57AcetylationLSARDHQKLEREARI
CCHHHHHHHHHHHHH
49.2322902405
69UbiquitinationARICRLLKHSNIVRL
HHHHHHHHHCCEEEE
49.97-
69AcetylationARICRLLKHSNIVRL
HHHHHHHHHCCEEEE
49.9722902405
107PhosphorylationEDIVAREYYSEADAS
HHHHHHHHCCCCCHH
13.51-
138UbiquitinationGVVHRDLKPENLLLA
CCCCCCCCHHHHHHH
55.35-
138AcetylationGVVHRDLKPENLLLA
CCCCCCCCHHHHHHH
55.357767833
146PhosphorylationPENLLLASKCKGAAV
HHHHHHHHCCCCCCE
38.2627097102
147UbiquitinationENLLLASKCKGAAVK
HHHHHHHCCCCCCEE
34.07-
149UbiquitinationLLLASKCKGAAVKLA
HHHHHCCCCCCEEHH
56.15-
154UbiquitinationKCKGAAVKLADFGLA
CCCCCCEEHHHCCEE
32.98-
182PhosphorylationAGTPGYLSPEVLRKE
CCCCCCCCHHHHHHH
15.5530181290
221MethylationFWDEDQHKLYQQIKA
CCCHHHHHHHHHHHH
43.1712692561
221"N6,N6-dimethyllysine"FWDEDQHKLYQQIKA
CCCHHHHHHHHHHHH
43.17-
223PhosphorylationDEDQHKLYQQIKAGA
CHHHHHHHHHHHHCC
11.81-
227UbiquitinationHKLYQQIKAGAYDFP
HHHHHHHHHCCCCCC
36.11-
227AcetylationHKLYQQIKAGAYDFP
HHHHHHHHHCCCCCC
36.1122902405
231PhosphorylationQQIKAGAYDFPSPEW
HHHHHCCCCCCCCCH
19.73-
235PhosphorylationAGAYDFPSPEWDTVT
HCCCCCCCCCHHCCC
35.1328551015
240PhosphorylationFPSPEWDTVTPEAKN
CCCCCHHCCCHHHHH
27.61-
242PhosphorylationSPEWDTVTPEAKNLI
CCCHHCCCHHHHHHH
19.94-
246UbiquitinationDTVTPEAKNLINQML
HCCCHHHHHHHHHHH
51.10-
254PhosphorylationNLINQMLTINPAKRI
HHHHHHHCCCHHHCC
17.2327097102
259UbiquitinationMLTINPAKRITAHEA
HHCCCHHHCCCHHHH
45.66-
259AcetylationMLTINPAKRITAHEA
HHCCCHHHCCCHHHH
45.66134805
268UbiquitinationITAHEALKHPWVCQR
CCHHHHHCCCCHHCH
55.45-
268AcetylationITAHEALKHPWVCQR
CCHHHHHCCCCHHCH
55.4522902405
276PhosphorylationHPWVCQRSTVASMMH
CCCHHCHHHHHHHHH
11.0130411139
277PhosphorylationPWVCQRSTVASMMHR
CCHHCHHHHHHHHHH
23.4527097102
280PhosphorylationCQRSTVASMMHRQET
HCHHHHHHHHHHHHH
16.5927097102
287PhosphorylationSMMHRQETVECLKKF
HHHHHHHHHHHHHHH
17.178443414
292AcetylationQETVECLKKFNARRK
HHHHHHHHHHCHHHH
67.9622902405
292UbiquitinationQETVECLKKFNARRK
HHHHHHHHHHCHHHH
67.96-
293UbiquitinationETVECLKKFNARRKL
HHHHHHHHHCHHHHH
30.79-
299UbiquitinationKKFNARRKLKGAILT
HHHCHHHHHHHHHHH
49.34-
301UbiquitinationFNARRKLKGAILTTM
HCHHHHHHHHHHHHH
49.70-
306PhosphorylationKLKGAILTTMLATRN
HHHHHHHHHHHHCCC
12.2128432305
307PhosphorylationLKGAILTTMLATRNF
HHHHHHHHHHHCCCC
13.5228432305
311PhosphorylationILTTMLATRNFSVGR
HHHHHHHCCCCCCCC
23.3727097102
315PhosphorylationMLATRNFSVGRQTTA
HHHCCCCCCCCCCCC
27.4925403869
320PhosphorylationNFSVGRQTTAPATMS
CCCCCCCCCCCCCCC
24.46-
321PhosphorylationFSVGRQTTAPATMST
CCCCCCCCCCCCCCC
23.47-
325PhosphorylationRQTTAPATMSTAASG
CCCCCCCCCCCCCCC
15.59-
327PhosphorylationTTAPATMSTAASGTT
CCCCCCCCCCCCCCC
15.56-
328PhosphorylationTAPATMSTAASGTTM
CCCCCCCCCCCCCCH
18.54-
331PhosphorylationATMSTAASGTTMGLV
CCCCCCCCCCCHHHH
33.92-
333PhosphorylationMSTAASGTTMGLVEQ
CCCCCCCCCHHHHHH
15.89-
334PhosphorylationSTAASGTTMGLVEQA
CCCCCCCCHHHHHHH
16.87-
342UbiquitinationMGLVEQAKSLLNKKA
HHHHHHHHHHHHHCC
41.13-
343PhosphorylationGLVEQAKSLLNKKAD
HHHHHHHHHHHHCCC
40.9030181290
347UbiquitinationQAKSLLNKKADGVKP
HHHHHHHHCCCCCCC
49.67-
348UbiquitinationAKSLLNKKADGVKPQ
HHHHHHHCCCCCCCC
51.11-
353UbiquitinationNKKADGVKPQTNSTK
HHCCCCCCCCCCCCC
36.62-
356PhosphorylationADGVKPQTNSTKNSS
CCCCCCCCCCCCCCC
39.4028432305
358PhosphorylationGVKPQTNSTKNSSAI
CCCCCCCCCCCCCCC
44.1127097102
359PhosphorylationVKPQTNSTKNSSAIT
CCCCCCCCCCCCCCC
35.9928432305
360UbiquitinationKPQTNSTKNSSAITS
CCCCCCCCCCCCCCC
55.44-
362PhosphorylationQTNSTKNSSAITSPK
CCCCCCCCCCCCCCC
23.7828432305
363PhosphorylationTNSTKNSSAITSPKG
CCCCCCCCCCCCCCC
32.8427097102
366PhosphorylationTKNSSAITSPKGSLP
CCCCCCCCCCCCCCC
38.4027097102
367PhosphorylationKNSSAITSPKGSLPP
CCCCCCCCCCCCCCH
20.6430411139
369UbiquitinationSSAITSPKGSLPPAA
CCCCCCCCCCCCHHH
61.98-
371PhosphorylationAITSPKGSLPPAALE
CCCCCCCCCCHHHCC
43.7725403869
381PhosphorylationPAALEPQTTVIHNPV
HHHCCCCCEEEECCC
33.4722673903
382PhosphorylationAALEPQTTVIHNPVD
HHCCCCCEEEECCCC
16.5322673903
394PhosphorylationPVDGIKESSDSTNTT
CCCCCCCCCCCCCCC
34.1525403869
395PhosphorylationVDGIKESSDSTNTTI
CCCCCCCCCCCCCCC
36.3530240740
397PhosphorylationGIKESSDSTNTTIED
CCCCCCCCCCCCCCH
26.0430411139
398PhosphorylationIKESSDSTNTTIEDE
CCCCCCCCCCCCCHH
41.3925403869
400PhosphorylationESSDSTNTTIEDEDA
CCCCCCCCCCCHHHH
29.2825403869
401PhosphorylationSSDSTNTTIEDEDAK
CCCCCCCCCCHHHHH
25.1630240740
411UbiquitinationDEDAKARKQEIIKTT
HHHHHHHHHHHHHHH
58.08-
416UbiquitinationARKQEIIKTTEQLIE
HHHHHHHHHHHHHHH
55.87-
469UbiquitinationYFENLLAKNSKPIHT
HHHHHHHCCCCCCEE
62.82-
472UbiquitinationNLLAKNSKPIHTTIL
HHHHCCCCCCEEEEC
58.34-
501PhosphorylationAYIRLTQYIDGQGRP
HHHHHHHEECCCCCC
8.85-
510PhosphorylationDGQGRPRTSQSEETR
CCCCCCCCCCCCCEE
33.5325403869
511PhosphorylationGQGRPRTSQSEETRV
CCCCCCCCCCCCEEE
32.7525403869
513PhosphorylationGRPRTSQSEETRVWH
CCCCCCCCCCEEEEE
36.8525403869
516PhosphorylationRTSQSEETRVWHRPD
CCCCCCCEEEEECCC
26.8625403869
534PhosphorylationQNVHFHCSGAPVAPL
EEEEEEECCCCCCCC
29.4427097102

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
254TPhosphorylationKinaseCAMK2AP11275
PSP
254TPhosphorylationKinaseCAMK2BP08413
PSP
280SPhosphorylationKinaseCAMK2BP08413
PSP
287TPhosphorylationKinaseCAM-KII_GROUP-PhosphoELM
287TPhosphorylationKinaseCAMK2AP11275
PSP
287TPhosphorylationKinaseCAMK2-FAMILY-GPS
287TPhosphorylationKinaseCAMK2BP08413
PSP
306TPhosphorylationKinaseCAMK2BP08413
PSP
307TPhosphorylationKinaseCAMK2BP08413
PSP
311TPhosphorylationKinaseCAMK2BP08413
PSP
315SPhosphorylationKinaseCAMK2AP11275
PSP
315SPhosphorylationKinaseCAMK2BP08413
PSP
320TPhosphorylationKinaseCAMK2BP08413
PSP
321TPhosphorylationKinaseCAMK2BP08413
PSP
325TPhosphorylationKinaseCAMK2BP08413
PSP
327SPhosphorylationKinaseCAMK2BP08413
PSP
328TPhosphorylationKinaseCAMK2BP08413
PSP
331SPhosphorylationKinaseCAMK2BP08413
PSP
333TPhosphorylationKinaseCAMK2BP08413
PSP
334TPhosphorylationKinaseCAMK2BP08413
PSP
343SPhosphorylationKinaseCAMK2BP08413
PSP
358SPhosphorylationKinaseCAMK2BP08413
PSP
363SPhosphorylationKinaseCAMK2BP08413
PSP
367SPhosphorylationKinaseCAMK2BP08413
PSP
371SPhosphorylationKinaseCAMK2BP08413
PSP
381TPhosphorylationKinaseCAMK2BP08413
PSP
382TPhosphorylationKinaseCAMK2BP08413
PSP
397SPhosphorylationKinaseCAMK2BP08413
PSP
400TPhosphorylationKinaseCAMK2BP08413
PSP
401TPhosphorylationKinaseCAMK2BP08413
PSP

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

12873385
287TPhosphorylation

12873385

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC20_RATCdc20physical
21725312
1433E_RATYwhaephysical
21725312
TBG1_RATTubg1physical
21725312

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCC2B_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Regulation and function of Ca2+-calmodulin-dependent protein kinaseII of fast-twitch rat skeletal muscle.";
Rose A.J., Alsted T.J., Kobberoe J.B., Richter E.A.;
J. Physiol. (Lond.) 580:993-1005(2007).
Cited for: FUNCTION, INDUCTION, AND PHOSPHORYLATION AT THR-287.

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