Names & Taxonomy

Uniprot ID:
O14936
Entry Name:
CSKP_HUMAN
Status:
reviewed
Protein Names:
Peripheral plasma membrane protein CASK (hCASK) (EC 2.7.11.1) (Calcium/calmodulin-dependent serine protein kinase) (Protein lin-2 homolog)
Gene Names:
CASK LIN2
Gene Names Primary:
CASK
Organism:
Homo sapiens (Human)

Structure

Length:
926
Sequence:
MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAERAVSQVLDSLEEIHALTDCSEKDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNPPSDAVQRAKEVLEEISCYPENNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEALRVTPPPTSPYLNGDSPESANGDMDMENVTRVRLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIVPSYRTQSSSCERDSPSTSRQSPANGHSSTNNSVSDLPSTTQPKGRQIYVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPELQEWRVACIAMEKTKQEQQASCTWFGKKKKQYKDKYLAKHNAVFDQLDLVTYEEVVKLPAFKRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNEDESLQRLQKESDILQRTYAHYFDLTIINNEIDETIRHLEEAVELVCTAPQWVPVSWVY
Proteomes:
UP000005640

Subcellular location

Subcellular Location:
Nucleus

Function

Function:
Multidomain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel trafficking. Contributes to neural development and regulation of gene expression via interaction with the transcription factor TBR1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1.
Catalytic Activity:
ATP + a protein = ADP + a phosphoprotein.
Cofactor:
COFACTOR: ; Note=Unlike other protein kinases, does not require a divalent cation such as magnesium for catalytic activity.
Kinetics:
BIOPHYSICOCHEMICAL PROPERTIES: ; Kinetic parameters: KM=563 uM for ATP
Enzyme Regulation:
ENZYME REGULATION: Differs from archetypal CaMK members in that the kinase domain exhibits a constitutively active conformation and the autoinhibitory region does not engage in direct contact with the ATP-binding cleft, although it still binds Ca(2+)/CAM.
Active Site:
ACT_SITE 141 141
Gene Ontology Go:
actin cytoskeleton
basement membrane
basolateral plasma membrane
cell-cell junction
ciliary membrane
cytoplasm
cytosol
focal adhesion
nuclear lamina
nuclear matrix
nucleolus
plasma membrane
presynaptic membrane
vesicle
ATP binding
guanylate kinase activity
protein serine/threonine kinase activity
calcium ion import
cell adhesion
extracellular matrix organization
GDP metabolic process
GMP metabolic process
negative regulation of cell-matrix adhesion
negative regulation of cellular response to growth factor stimulus
negative regulation of keratinocyte proliferation
negative regulation of wound healing
neurotransmitter secretion
positive regulation of calcium ion import
positive regulation of transcription from RNA polymerase II promoter
synaptic transmission
Gene Ontology Biological Process:
calcium ion import
cell adhesion
extracellular matrix organization
GDP metabolic process
GMP metabolic process
negative regulation of cell-matrix adhesion
negative regulation of cellular response to growth factor stimulus
negative regulation of keratinocyte proliferation
negative regulation of wound healing
neurotransmitter secretion
positive regulation of calcium ion import
positive regulation of transcription from RNA polymerase II promoter
synaptic transmission
Gene Ontology Molecular Function:
ATP binding
guanylate kinase activity
protein serine/threonine kinase activity
Gene Ontology Cellular Component:
actin cytoskeleton
basement membrane
basolateral plasma membrane
cell-cell junction
ciliary membrane
cytoplasm
cytosol
focal adhesion
nuclear lamina
nuclear matrix
nucleolus
plasma membrane
presynaptic membrane
vesicle
Keywords:
3D-structure
ATP-binding
Alternative splicing
Calmodulin-binding
Cell membrane
Complete proteome
Cytoplasm
Disease mutation
Kinase
Membrane
Mental retardation
Nucleotide-binding
Nucleus
Phosphoprotein
Polymorphism
Reference proteome
Repeat
SH3 domain
Serine/threonine-protein kinase
Transferase
Interacts With:
Q8WXD9; Q12929; P41134; O14910; Q63373; Q9Y2J0; P34741; Q9H788; Q13425

Publication

PubMed ID:
9660868 15772651 15489334 11003712 19012874 24275569 9546224 18423203 17344846 19165920 19200522 19377476