UniProt ID | KCC2B_HUMAN | |
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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 |
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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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
17 | Phosphorylation | FTDEYQLYEDIGKGA CCCCCHHHHHHCCCH | 8.95 | 21082442 | |
26 | Phosphorylation | DIGKGAFSVVRRCVK HHCCCHHHHHHHHHH | 21.11 | 28857561 | |
36 | Phosphorylation | RRCVKLCTGHEYAAK HHHHHHHCCCHHHHH | 52.59 | 29978859 | |
40 | Phosphorylation | KLCTGHEYAAKIINT HHHCCCHHHHHHHHC | 13.24 | 29978859 | |
47 | Phosphorylation | YAAKIINTKKLSARD HHHHHHHCCCCCHHH | 21.10 | 29978859 | |
57 | Ubiquitination | LSARDHQKLEREARI CCHHHHHHHHHHHHH | 49.23 | - | |
71 | Phosphorylation | ICRLLKHSNIVRLHD HHHHHHHCCEEEECC | 27.02 | 26437602 | |
79 | Phosphorylation | NIVRLHDSISEEGFH CEEEECCCCCCCCCE | 19.78 | 24275569 | |
138 | Ubiquitination | GVVHRDLKPENLLLA CCCCCCCCHHHHHHH | 55.35 | - | |
146 | Phosphorylation | PENLLLASKCKGAAV HHHHHHHHCCCCCCE | 38.26 | 28857561 | |
182 | Phosphorylation | AGTPGYLSPEVLRKE CCCCCCCCHHHHHHH | 15.55 | 21815630 | |
227 | Acetylation | HKLYQQIKAGAYDFP HHHHHHHHHCCCCCC | 36.11 | 26051181 | |
227 | Ubiquitination | HKLYQQIKAGAYDFP HHHHHHHHHCCCCCC | 36.11 | 2190698 | |
227 (in isoform 1) | Ubiquitination | - | 36.11 | 21906983 | |
227 (in isoform 2) | Ubiquitination | - | 36.11 | 21906983 | |
227 (in isoform 3) | Ubiquitination | - | 36.11 | 21906983 | |
227 (in isoform 4) | Ubiquitination | - | 36.11 | 21906983 | |
227 (in isoform 5) | Ubiquitination | - | 36.11 | 21906983 | |
227 (in isoform 7) | Ubiquitination | - | 36.11 | 21906983 | |
227 (in isoform 6) | Ubiquitination | - | 36.11 | 21906983 | |
231 | Phosphorylation | QQIKAGAYDFPSPEW HHHHHCCCCCCCCCH | 19.73 | 28857561 | |
235 | Phosphorylation | AGAYDFPSPEWDTVT HCCCCCCCCCHHCCC | 35.13 | 28857561 | |
240 | Phosphorylation | FPSPEWDTVTPEAKN CCCCCHHCCCHHHHH | 27.61 | 28857561 | |
246 | Ubiquitination | DTVTPEAKNLINQML HCCCHHHHHHHHHHH | 51.10 | - | |
254 | Phosphorylation | NLINQMLTINPAKRI HHHHHHHCCCHHHCC | 17.23 | 29396449 | |
259 | Acetylation | MLTINPAKRITAHEA HHCCCHHHCCCHHHH | 45.66 | 25953088 | |
259 | Ubiquitination | MLTINPAKRITAHEA HHCCCHHHCCCHHHH | 45.66 | - | |
259 | Malonylation | MLTINPAKRITAHEA HHCCCHHHCCCHHHH | 45.66 | 26320211 | |
268 | Ubiquitination | ITAHEALKHPWVCQR CCHHHHHCCCCHHCH | 55.45 | - | |
276 | Phosphorylation | HPWVCQRSTVASMMH CCCHHCHHHHHHHHH | 11.01 | 23882029 | |
277 | Phosphorylation | PWVCQRSTVASMMHR CCHHCHHHHHHHHHH | 23.45 | 23663014 | |
280 | Phosphorylation | CQRSTVASMMHRQET HCHHHHHHHHHHHHH | 16.59 | 30631047 | |
287 | Phosphorylation | SMMHRQETVECLKKF HHHHHHHHHHHHHHH | 17.17 | 23882029 | |
299 | Methylation | KKFNARRKLKGAILT HHHCHHHHHHHHHHH | 49.34 | - | |
301 | Methylation | FNARRKLKGAILTTM HCHHHHHHHHHHHHH | 49.70 | 24129315 | |
306 | Phosphorylation | KLKGAILTTMLATRN HHHHHHHHHHHHCCC | 12.21 | 21082442 | |
307 | Phosphorylation | LKGAILTTMLATRNF HHHHHHHHHHHCCCC | 13.52 | 21082442 | |
311 (in isoform 8) | Phosphorylation | - | 23.37 | 29514088 | |
311 | Phosphorylation | ILTTMLATRNFSVGR HHHHHHHCCCCCCCC | 23.37 | 21406692 | |
315 (in isoform 4) | Phosphorylation | - | 27.49 | - | |
315 (in isoform 8) | Phosphorylation | - | 27.49 | 18691976 | |
315 | Phosphorylation | MLATRNFSVGRQTTA HHHCCCCCCCCCCCC | 27.49 | 24670416 | |
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 | - | |
320 | O-linked_Glycosylation | NFSVGRQTTAPATMS CCCCCCCCCCCCCCC | 24.46 | 22564745 | |
320 | Phosphorylation | NFSVGRQTTAPATMS CCCCCCCCCCCCCCC | 24.46 | 20068231 | |
321 | O-linked_Glycosylation | FSVGRQTTAPATMST CCCCCCCCCCCCCCC | 23.47 | 22564745 | |
321 | Phosphorylation | FSVGRQTTAPATMST CCCCCCCCCCCCCCC | 23.47 | 26437602 | |
325 | Phosphorylation | RQTTAPATMSTAASG CCCCCCCCCCCCCCC | 15.59 | 20068231 | |
327 | Phosphorylation | TTAPATMSTAASGTT CCCCCCCCCCCCCCC | 15.56 | 20068231 | |
328 | Phosphorylation | TAPATMSTAASGTTM CCCCCCCCCCCCCCH | 18.54 | 20068231 | |
331 | Phosphorylation | ATMSTAASGTTMGLV CCCCCCCCCCCHHHH | 33.92 | 20068231 | |
333 | Phosphorylation | MSTAASGTTMGLVEQ CCCCCCCCCHHHHHH | 15.89 | 22210691 | |
334 (in isoform 4) | Phosphorylation | - | 16.87 | - | |
334 | Phosphorylation | STAASGTTMGLVEQA CCCCCCCCHHHHHHH | 16.87 | 22210691 | |
342 | Acetylation | MGLVEQAKSLLNKKA HHHHHHHHHHHHHCC | 41.13 | 7662425 | |
343 (in isoform 3) | Phosphorylation | - | 40.90 | 24719451 | |
343 | Phosphorylation | GLVEQAKSLLNKKAD HHHHHHHHHHHHCCC | 40.90 | 24719451 | |
355 (in isoform 3) | Phosphorylation | - | 47.82 | 24076635 | |
356 (in isoform 3) | Phosphorylation | - | 39.40 | 24076635 | |
356 | Phosphorylation | ADGVKPQTNSTKNSA CCCCCCCCCCCCCCC | 39.40 | 20068231 | |
357 (in isoform 6) | Phosphorylation | - | 42.29 | 20068231 | |
358 | Phosphorylation | GVKPQTNSTKNSAAA CCCCCCCCCCCCCCC | 44.11 | 26437602 | |
358 (in isoform 6) | Phosphorylation | - | 44.11 | 20068231 | |
358 (in isoform 3) | Phosphorylation | - | 44.11 | 19369195 | |
361 (in isoform 3) | Phosphorylation | - | 36.65 | 28348404 | |
362 (in isoform 3) | Phosphorylation | - | 22.35 | 26471730 | |
366 | Phosphorylation | TKNSAAATSPKGTLP CCCCCCCCCCCCCCC | 40.61 | 26033855 | |
367 | Phosphorylation | KNSAAATSPKGTLPP CCCCCCCCCCCCCCH | 21.64 | 25849741 | |
371 | Phosphorylation | AATSPKGTLPPAALE CCCCCCCCCCHHHCC | 42.07 | 24076635 | |
381 | Phosphorylation | PAALEPQTTVIHNPV HHHCCCCCEEEECCC | 33.47 | 20068231 | |
382 | Phosphorylation | AALEPQTTVIHNPVD HHCCCCCEEEECCCC | 16.53 | 20068231 | |
394 | Phosphorylation | PVDGIKESSDSANTT CCCCCCCCCCCCCCC | 34.15 | 18510355 | |
395 | Phosphorylation | VDGIKESSDSANTTI CCCCCCCCCCCCCCC | 36.35 | 18510355 | |
397 | Phosphorylation | GIKESSDSANTTIED CCCCCCCCCCCCCCC | 25.93 | 20068231 | |
400 | Phosphorylation | ESSDSANTTIEDEDA CCCCCCCCCCCCHHH | 28.94 | 20068231 | |
401 | Phosphorylation | SSDSANTTIEDEDAK CCCCCCCCCCCHHHC | 23.37 | 20068231 | |
417 | Phosphorylation | PRVPDILSSVRRGSG CCCHHHHHHHHCCCC | 27.41 | 24719451 | |
418 | Phosphorylation | RVPDILSSVRRGSGA CCHHHHHHHHCCCCC | 19.05 | 26437602 | |
423 | Phosphorylation | LSSVRRGSGAPEAEG HHHHHCCCCCCCCCC | 29.94 | 25849741 | |
436 | Phosphorylation | EGPLPCPSPAPFSPL CCCCCCCCCCCCCCC | 40.17 | 22673903 | |
441 | Phosphorylation | CPSPAPFSPLPAPSP CCCCCCCCCCCCCCC | 25.19 | 22673903 | |
456 | Phosphorylation | RISDILNSVRRGSGT CHHHHHHHHHCCCCC | 17.35 | 28857561 | |
461 | Phosphorylation | LNSVRRGSGTPEAEG HHHHHCCCCCCCCCC | 37.37 | 22798277 | |
463 | Phosphorylation | SVRRGSGTPEAEGPL HHHCCCCCCCCCCCC | 21.47 | 19764811 | |
471 | Phosphorylation | PEAEGPLSAGPPPCL CCCCCCCCCCCCCCC | 34.02 | 19764811 | |
479 | Phosphorylation | AGPPPCLSPALLGPL CCCCCCCCHHHHCCC | 18.16 | 28348404 | |
490 | Phosphorylation | LGPLSSPSPRISDIL HCCCCCCCCHHHHHH | 28.85 | 17081983 | |
499 | Phosphorylation | RISDILNSVRRGSGT HHHHHHHHHHCCCCC | 17.35 | 28857561 | |
504 | Phosphorylation | LNSVRRGSGTPEAEG HHHHHCCCCCCCCCC | 37.37 | 19764811 | |
506 | Phosphorylation | SVRRGSGTPEAEGPS HHHCCCCCCCCCCCC | 21.47 | 19764811 | |
513 | Phosphorylation | TPEAEGPSPVGPPPC CCCCCCCCCCCCCCC | 42.97 | 28348404 | |
522 | Phosphorylation | VGPPPCPSPTIPGPL CCCCCCCCCCCCCCC | 41.20 | 26437602 | |
524 | Phosphorylation | PPPCPSPTIPGPLPT CCCCCCCCCCCCCCC | 44.11 | 28348404 | |
623 | Phosphorylation | CIAYIRLTQYIDGQG HHHHHHHHHEECCCC | 14.96 | 28152594 | |
625 | Phosphorylation | AYIRLTQYIDGQGRP HHHHHHHEECCCCCC | 8.85 | 28152594 |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ACTN4_HUMAN | ACTN4 | physical | 11160423 | |
1433B_HUMAN | YWHAB | physical | 12619878 | |
KCC2B_HUMAN | CAMK2B | physical | 15604093 | |
SMYD3_HUMAN | SMYD3 | physical | 21988832 | |
KCC2B_HUMAN | CAMK2B | physical | 25416956 | |
KPBB_HUMAN | PHKB | physical | 25416956 | |
RAP2B_HUMAN | RAP2B | physical | 25416956 | |
RL11_HUMAN | RPL11 | physical | 25416956 | |
MD2L2_HUMAN | MAD2L2 | physical | 25416956 | |
MO4L1_HUMAN | MORF4L1 | physical | 25416956 | |
RBPMS_HUMAN | RBPMS | physical | 25416956 | |
BACH_HUMAN | ACOT7 | physical | 25416956 | |
RFOX2_HUMAN | RBFOX2 | physical | 25416956 | |
POP5_HUMAN | POP5 | physical | 25416956 | |
MED18_HUMAN | MED18 | physical | 25416956 | |
SPRY7_HUMAN | SPRYD7 | physical | 25416956 | |
SEM4G_HUMAN | SEMA4G | physical | 25416956 | |
RM11_HUMAN | MRPL11 | physical | 25416956 | |
AP5B1_HUMAN | AP5B1 | physical | 25416956 | |
TTC5_HUMAN | TTC5 | physical | 25416956 | |
CCM2L_HUMAN | CCM2L | physical | 25416956 | |
MGT5B_HUMAN | MGAT5B | physical | 25416956 | |
F1712_HUMAN | FAM171A2 | physical | 25416956 | |
KR195_HUMAN | KRTAP19-5 | physical | 25416956 | |
KR197_HUMAN | KRTAP19-7 | physical | 25416956 | |
KR10B_HUMAN | KRTAP10-11 | physical | 25416956 |
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. |
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Phosphorylation | |
Reference | PubMed |
"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. |