CABP1
entrez
9478
canonical
uniprot
Q9NZU7
canonical
ensembl
ENSG00000157782
resolver
ensp
ENSP00000288615
resolver
ensp
ENSP00000288616
resolver
ensp
ENSP00000317310
resolver
ensp
ENSP00000398959
resolver
enst
ENST00000453000
resolver
genesymbol
CABP1
resolver
hgnc
HGNC:1384
resolver
uniprot
C9J8G2
resolver
uniprot
O95663
resolver
uniprot
Q8N6H5
resolver
uniprot
Q9NZU8
resolver
uniprot_entry
C9J8G2_HUMAN
resolver
uniprot_entry
CABP1_HUMAN
resolver
uniprot_sec
O95663
resolver
uniprot_sec
Q8N6H5
resolver
uniprot_sec
Q9NZU8
resolver
amino_acid_sequence
MGGGDGAAFKRPGDGARLQRVLGLGSRREPRSLPAGGPAPRRTAPPPPGHASAGPAAMSSHIAKSESKTSLLKAAAAAASGGSRAPRHGPARDPGLPSRRLPGSCPATPQSSGDPSSRRPLCRPAPREEGARGSQRVLPQAHCRPREALPAAASRPSPSSPLPPARGRDGEERGLSPALGLRGSLRARGRGDSVPAAASEADPFLHRLRPMLSSAFGQDRSLRPEEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDGEISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR
uniprot
proteins
function
FUNCTION: Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs) (PubMed:14570872). Inhibits agonist-induced intracellular calcium signaling (PubMed:15980432). Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels (PubMed:11865310). Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but has an opposite effect on channel function (PubMed:15140941). Suppresses the calcium-dependent inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels (PubMed:15895247). Prevents NMDA receptor-induced cellular degeneration. Required for the normal transfer of light signals through the retina (By similarity). {ECO:0000250|UniProtKB:O88751, ECO:0000250|UniProtKB:Q9JLK7, ECO:0000269|PubMed:11865310, ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:15140941, ECO:0000269|PubMed:15895247, ECO:0000269|PubMed:15980432}.
uniprot
proteins
mass_dalton
39838
uniprot
proteins
mutagenesis
MUTAGEN 238; /note="D->A: Loss of magnesium-binding. Loss of binding to ITPRs; when associated with A-240; A-315; A-317; A-352 and A-354."; /evidence="ECO:0000269|PubMed:12032348, ECO:0000269|PubMed:19008222"; MUTAGEN 240; /note="D->A: Loss of magnesium-binding. Loss of binding to ITPRs; when associated with A-238; A-315; A-317; A-352 and A-354."; /evidence="ECO:0000269|PubMed:12032348, ECO:0000269|PubMed:19008222"; MUTAGEN 242; /note="D->A: Loss of magnesium-binding."; /evidence="ECO:0000269|PubMed:19008222"; MUTAGEN 249; /note="D->A: No effect on magnesium-binding."; /evidence="ECO:0000269|PubMed:19008222"; MUTAGEN 315; /note="D->A: Loss of binding to ITPRs; when associated with A-238; A-240; A-317; A-352 and A-354."; /evidence="ECO:0000269|PubMed:12032348"; MUTAGEN 317; /note="N->A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-352 and A-354."; /evidence="ECO:0000269|PubMed:12032348"; MUTAGEN 323; /note="S->A: Loss of phosphorylation and loss of calcium release by InsP(3)."; /evidence="ECO:0000269|PubMed:14685260"; MUTAGEN 352; /note="D->A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-354."; /evidence="ECO:0000269|PubMed:12032348"; MUTAGEN 354; /note="N->A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-352."; /evidence="ECO:0000269|PubMed:12032348
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. The phosphorylation regulates the activity. {ECO:0000269|PubMed:14685260}.
uniprot
proteins
pubmed
10625670
uniprot
proteins
pubmed
11865310
uniprot
proteins
pubmed
12032348
uniprot
proteins
pubmed
14570872
uniprot
proteins
pubmed
14685260
uniprot
proteins
pubmed
15095872
uniprot
proteins
pubmed
15140941
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15895247
uniprot
proteins
pubmed
15980432
uniprot
proteins
pubmed
16147998
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
19008222
uniprot
proteins
pubmed
9694893
uniprot
proteins
pubmed
9920909
uniprot
proteins
sequence_length
370
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10625670}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14685260}. Cell membrane {ECO:0000269|PubMed:10625670, ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:14685260}; Lipid-anchor; Cytoplasmic side. Golgi apparatus {ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:14685260}. Postsynaptic density {ECO:0000305}. Note=L-CaBP1 is associated most likely with the cytoskeletal structures, whereas S-CaBP1 is localized at or near the plasma membrane. {ECO:0000269|PubMed:10625670}.; SUBCELLULAR LOCATION: [Isoform L-CaBP1]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10625670}. Note=L-CaBP1 is associated most likely with the cytoskeletal structures. {ECO:0000269|PubMed:10625670}.; SUBCELLULAR LOCATION: [Isoform S-CaBP1]: Cytoplasm, cell cortex. Cell membrane {ECO:0000305|PubMed:10625670}; Lipid-anchor {ECO:0000305}. Note=S-CaBP1 is localized at or near the plasma membrane.
uniprot
proteins