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RAT:CSKP

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Species (Taxon ID) Rattus norvegicus (Rat). (10116)
Gene Name(s) Cask
Protein Name(s) Peripheral plasma membrane protein CASK

Calcium/calmodulin-dependent serine protein kinase

External Links
UniProt Q62915
EMBL U47110
RefSeq NP_071520.1
UniGene Rn.72627
PDB 1RSO
PDBsum 1RSO
ProteinModelPortal Q62915
SMR Q62915
BioGrid 248269
IntAct Q62915
MINT MINT-220139
STRING 10116.ENSRNOP00000063381
PhosphoSite Q62915
PaxDb Q62915
PRIDE Q62915
GeneID 29647
KEGG rno:29647
UCSC RGD:62004
CTD 8573
RGD 62004
eggNOG COG0515
HOGENOM HOG000233034
HOVERGEN HBG001858
InParanoid Q62915
KO K06103
PhylomeDB Q62915
BRENDA 2.7.11.1
Reactome REACT_198300
REACT_258050
EvolutionaryTrace Q62915
NextBio 609922
Proteomes UP000002494
Genevestigator Q62915
GO GO:0060170
GO:0005737
GO:0005829
GO:0030425
GO:0016020
GO:0005634
GO:0005886
GO:0042734
GO:0043234
GO:0097060
GO:0005524
GO:0005516
GO:0004683
GO:0042043
GO:0030165
GO:0008022
GO:0032403
GO:0003713
GO:0006886
GO:0006461
GO:1903506
Gene3D 2.30.42.10
3.40.50.300
InterPro IPR008145
IPR008144
IPR020590
IPR011009
IPR004172
IPR014775
IPR027417
IPR001478
IPR000719
IPR002290
IPR011511
IPR001452
Pfam PF00625
PF02828
PF00595
PF00069
PF07653
SMART SM00072
SM00569
SM00228
SM00220
SM00326
SUPFAM SSF50044
SSF50156
SSF52540
SSF56112
PROSITE PS00856
PS50052
PS51022
PS50106
PS50011
PS50002

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0097060

synaptic membrane

PMID:8786425[1]

ECO:0000314

C

Subfractionated rat brain homogenates into different membrane fraction. Enriched in synapse plasma membrane, figure 4.

complete
CACAO 2690

GO:0005886

plasma membrane

PMID:8786425[1]

ECO:0000314

C

Subfractionated rat brain homogenates into different membrane fraction. Enriched in synapse plasma membrane, figure 4.

complete

GO:0042734

presynaptic membrane

PMID:18596612[2]

ECO:0000314

C

Subcellular fractionation, Figure 4 A and B showed Cask found in membrane fraction enriched with presynaptic markers.

complete
CACAO 3198

part_of

GO:0042734

presynaptic membrane

PMID:18596612[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0097060

synaptic membrane

PMID:8786425[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0097060

synaptic membrane

PMID:8786425[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0060170

ciliary membrane

PMID:18596612[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0042734

presynaptic membrane

PMID:18596612[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:18664494[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0098846

podocyte foot

PMID:15994232[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0097440

apical dendrite

PMID:9660869[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0097060

synaptic membrane

PMID:9660869[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0072659

protein localization to plasma membrane

PMID:14960569[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0061003

positive regulation of dendritic spine morphogenesis

PMID:18606847[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0045121

membrane raft

PMID:11679592[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0044877

protein-containing complex binding

PMID:15331416[9]

ECO:0000353

physical interaction evidence used in manual assertion

RGD:620460

F

Seeded From UniProt

complete

part_of

GO:0043025

neuronal cell body

PMID:9660869[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042043

neurexin family protein binding

PMID:8786425[1]

ECO:0000353

physical interaction evidence used in manual assertion

RGD:620211
RGD:620212
RGD:628659

F

Seeded From UniProt

complete

part_of

GO:0032991

protein-containing complex

PMID:15331416[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0032991

protein-containing complex

PMID:11356864[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0032024

positive regulation of insulin secretion

PMID:24140090[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0030425

dendrite

PMID:12641734[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0030165

PDZ domain binding

PMID:9660869[5]

ECO:0000353

physical interaction evidence used in manual assertion

RGD:3649

F

Seeded From UniProt

complete

enables

GO:0030165

PDZ domain binding

PMID:17084383[13]

ECO:0000353

physical interaction evidence used in manual assertion

RGD:620108

F

Seeded From UniProt

complete

enables

GO:0030165

PDZ domain binding

PMID:15024025[14]

ECO:0000353

physical interaction evidence used in manual assertion

RGD:733316

F

Seeded From UniProt

complete

enables

GO:0030165

PDZ domain binding

PMID:15024025[14]

ECO:0000353

physical interaction evidence used in manual assertion

RGD:62261

F

Seeded From UniProt

complete

enables

GO:0030165

PDZ domain binding

PMID:15024025[14]

ECO:0000353

physical interaction evidence used in manual assertion

RGD:621660

F

Seeded From UniProt

complete

enables

GO:0030165

PDZ domain binding

PMID:12641734[12]

ECO:0000353

physical interaction evidence used in manual assertion

RGD:631330

F

Seeded From UniProt

complete

involved_in

GO:0021987

cerebral cortex development

PMID:10749215[15]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016323

basolateral plasma membrane

PMID:10710551[16]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:11356864[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0014069

postsynaptic density

PMID:11679592[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008022

protein C-terminus binding

PMID:9660869[5]

ECO:0000353

physical interaction evidence used in manual assertion

RGD:3649

F

Seeded From UniProt

complete

enables

GO:0008022

protein C-terminus binding

PMID:12511555[17]

ECO:0000353

physical interaction evidence used in manual assertion

RGD:1348952

F

Seeded From UniProt

complete

involved_in

GO:0006357

regulation of transcription by RNA polymerase II

PMID:19275891[18]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:9660869[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:12641734[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:20623620[19]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004672

protein kinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000719

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000719

F

Seeded From UniProt

complete

involved_in

GO:0006468

protein phosphorylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000719

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

Reactome:R-RNO-6794334
Reactome:R-RNO-451396
Reactome:R-RNO-2750184

ECO:0000304

author statement supported by traceable reference used in manual assertion



C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0016301

kinase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0039

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0005516

calmodulin binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0112

F

Seeded From UniProt

complete

enables

GO:0004674

protein serine/threonine kinase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0723

F

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 1.4 Hata, Y et al. (1996) CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins. J. Neurosci. 16 2488-94 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 Saavedra, MV et al. (2008) Scaffolding proteins in highly purified rat olfactory cilia membranes. Neuroreport 19 1123-6 PubMed GONUTS page
  3. Ojeh, N et al. (2008) The MAGUK-family protein CASK is targeted to nuclei of the basal epidermis and controls keratinocyte proliferation. J. Cell. Sci. 121 2705-17 PubMed GONUTS page
  4. Lehtonen, S et al. (2005) Cell junction-associated proteins IQGAP1, MAGI-2, CASK, spectrins, and alpha-actinin are components of the nephrin multiprotein complex. Proc. Natl. Acad. Sci. U.S.A. 102 9814-9 PubMed GONUTS page
  5. 5.0 5.1 5.2 5.3 5.4 5.5 Hsueh, YP et al. (1998) Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses. J. Cell Biol. 142 139-51 PubMed GONUTS page
  6. Leonoudakis, D et al. (2004) A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels. J. Biol. Chem. 279 19051-63 PubMed GONUTS page
  7. Chao, HW et al. (2008) SUMOylation of the MAGUK protein CASK regulates dendritic spinogenesis. J. Cell Biol. 182 141-55 PubMed GONUTS page
  8. 8.0 8.1 Fallon, L et al. (2002) Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain. J. Biol. Chem. 277 486-91 PubMed GONUTS page
  9. 9.0 9.1 Lehtonen, S et al. (2004) Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin. Am. J. Pathol. 165 923-36 PubMed GONUTS page
  10. 10.0 10.1 Hsueh, YP et al. (2001) Bipartite interaction between neurofibromatosis type I protein (neurofibromin) and syndecan transmembrane heparan sulfate proteoglycans. J. Neurosci. 21 3764-70 PubMed GONUTS page
  11. Zhu, ZQ et al. (2014) Calcium/calmodulin-dependent serine protein kinase is involved in exendin-4-induced insulin secretion in INS-1 cells. Metab. Clin. Exp. 63 120-6 PubMed GONUTS page
  12. 12.0 12.1 12.2 Yap, CC et al. (2003) CIP98, a novel PDZ domain protein, is expressed in the central nervous system and interacts with calmodulin-dependent serine kinase. J. Neurochem. 85 123-34 PubMed GONUTS page
  13. Hong, CJ & Hsueh, YP (2006) CASK associates with glutamate receptor interacting protein and signaling molecules. Biochem. Biophys. Res. Commun. 351 771-6 PubMed GONUTS page
  14. 14.0 14.1 14.2 Leonoudakis, D et al. (2004) Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins. J. Biol. Chem. 279 22331-46 PubMed GONUTS page
  15. Hsueh, YP et al. (2000) Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2. Nature 404 298-302 PubMed GONUTS page
  16. Straight, SW et al. (2000) mLin-7 is localized to the basolateral surface of renal epithelia via its NH(2) terminus. Am. J. Physiol. Renal Physiol. 278 F464-75 PubMed GONUTS page
  17. Schuh, K et al. (2003) Interaction of the plasma membrane Ca2+ pump 4b/CI with the Ca2+/calmodulin-dependent membrane-associated kinase CASK. J. Biol. Chem. 278 9778-83 PubMed GONUTS page
  18. Huang, TN & Hsueh, YP (2009) CASK point mutation regulates protein-protein interactions and NR2b promoter activity. Biochem. Biophys. Res. Commun. 382 219-22 PubMed GONUTS page
  19. Kuo, TY et al. (2010) X-linked mental retardation gene CASK interacts with Bcl11A/CTIP1 and regulates axon branching and outgrowth. J. Neurosci. Res. 88 2364-73 PubMed GONUTS page