CAPRIN1
entrez
4076
canonical
uniprot
Q14444
canonical
ensembl
ENSG00000135387
resolver
ensp
ENSP00000340329
resolver
ensp
ENSP00000374296
resolver
ensp
ENSP00000434150
resolver
ensp
ENSP00000665486
resolver
ensp
ENSP00000665488
resolver
genesymbol
CAPRIN1
resolver
genesymbol_syn
GPIAP1
resolver
genesymbol_syn
GPIP137
resolver
genesymbol_syn
M11S1
resolver
genesymbol_syn
RNG105
resolver
hgnc
HGNC:6743
resolver
uniprot
A6NMY7
resolver
uniprot
D3DR06
resolver
uniprot
Q15074
resolver
uniprot
Q6IMN4
resolver
uniprot
Q6IMN7
resolver
uniprot
Q9BV09
resolver
uniprot_entry
CAPR1_HUMAN
resolver
uniprot_sec
A6NMY7
resolver
uniprot_sec
D3DR06
resolver
uniprot_sec
Q15074
resolver
uniprot_sec
Q6IMN4
resolver
uniprot_sec
Q6IMN7
resolver
uniprot_sec
Q9BV09
resolver
activity_regulation
ACTIVITY REGULATION: Ability to mediate liquid-liquid phase separation is regulated by ATP: moderate concentrations of ATP enhance phase separation, whereas high concentrations of ATP lead to inhibition of phase separation. {ECO:0000269|PubMed:34074792, ECO:0000269|PubMed:36040869}.
uniprot
proteins
amino_acid_sequence
MPSATSHSGSGSKSSGPPPPSGSSGSEAAAGAGAAAPASQHPATGTGAVQTEAMKQILGVIDKKLRNLEKKKGKLDDYQERMNKGERLNQDQLDAVSKYQEVTNNLEFAKELQRSFMALSQDIQKTIKKTARREQLMREEAEQKRLKTVLELQYVLDKLGDDEVRTDLKQGLNGVPILSEEELSLLDEFYKLVDPERDMSLRLNEQYEHASIHLWDLLEGKEKPVCGTTYKVLKEIVERVFQSNYFDSTHNHQNGLCEEEEAASAPAVEDQVPEAEPEPAEEYTEQSEVESTEYVNRQFMAETQFTSGEKEQVDEWTVETVEVVNSLQQQPQAASPSVPEPHSLTPVAQADPLVRRQRVQDLMAQMQGPYNFIQDSMLDFENQTLDPAIVSAQPMNPTQNMDMPQLVCPPVHSESRLAQPNQVPVQPEATQVPLVSSTSEGYTASQPLYQPSHATEQRPQKEPIDQIQATISLNTDQTTASSSLPAASQPQVFQAGTSKPLHSSGINVNAAPFQSMQTVFNMNAPVPPVNEPETLKQQNQYQASYNQSFSSQPHQVEQTELQQEQLQTVVGTYHGSPDQSHQVTGNHQQPPQQNTGFPRSNQPYYNSRGVSRGGSRGARGLMNGYRGPANGFRGGYDGYRPSFSNTPNSGYTQSQFSAPRDYSGYQRDGYQQNFKRGSGQSGPRGAPRGRGGPPRPNRGMPQMNTQQVN
uniprot
proteins
disease_involvement
DISEASE: Neurodegeneration, childhood-onset, with cerebellar ataxia and cognitive decline (CONDCAC) [MIM:620636]: A neurodegenerative disorder characterized by early-onset ataxia, dysarthria, cognitive decline, sensorimotor axonal neuropathy and muscle weakness. Brain imaging shows cerebellar atrophy. {ECO:0000269|PubMed:36136249}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Neurodevelopmental disorder with language impairment, autism, and attention deficit-hyperactivity disorder (NEDLAAD) [MIM:620782]: An autosomal dominant disorder with variable expressivity and incomplete penetrance. It is characterized by language impairment, speech delay, intellectual disability, attention deficit-hyperactivity disorder and autism spectrum disorder. Additional variable features include developmental delay, seizures, skeletal anomalies, respiratory difficulties, and ophthalmologic anomalies. {ECO:0000269|PubMed:35979925}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: mRNA-binding protein that acts as a regulator of mRNAs transport, translation and/or stability, and which is involved in neurogenesis, synaptic plasticity in neurons and cell proliferation and migration in multiple cell types (PubMed:17210633, PubMed:31439799, PubMed:35979925). Plays an essential role in cytoplasmic stress granule formation (PubMed:35977029). Acts as an mRNA regulator by mediating formation of some phase-separated membraneless compartment: undergoes liquid-liquid phase separation upon binding to target mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors (PubMed:31439799, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:34074792, PubMed:36040869, PubMed:36279435). Undergoes liquid-liquid phase separation following phosphorylation and interaction with FMR1, promoting formation of cytoplasmic ribonucleoprotein granules that concentrate mRNAs with factors that inhibit translation and mediate deadenylation of target mRNAs (PubMed:31439799). In these cytoplasmic ribonucleoprotein granules, CAPRIN1 mediates recruitment of CNOT7 deadenylase, leading to mRNA deadenylation and degradation (PubMed:31439799). Binds directly and selectively to MYC and CCND2 mRNAs (PubMed:17210633). In neuronal cells, directly binds to several mRNAs associated with RNA granules, including BDNF, CAMK2A, CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not to rRNAs (PubMed:17210633). {ECO:0000269|PubMed:17210633, ECO:0000269|PubMed:31439799, ECO:0000269|PubMed:32302570, ECO:0000269|PubMed:32302571, ECO:0000269|PubMed:34074792, ECO:0000269|PubMed:35977029, ECO:0000269|PubMed:35979925, ECO:0000269|PubMed:36040869, ECO:0000269|PubMed:36279435}.
uniprot
proteins
mass_dalton
78366
uniprot
proteins
mutagenesis
MUTAGEN 370; /note="Y->A,G,P,V,W,D,E,R,H,K,S,C,T,M,N,Q: Abolished interaction with G3BP1."; /evidence="ECO:0000269|PubMed:36183834"; MUTAGEN 372; /note="F->A,G,I,L,P,V,W,Y,D,E,R,H,K,S,C,T,M,N,Q: Abolished interaction with G3BP1 and ability to promote stress granule formation."; /evidence="ECO:0000269|PubMed:32302571, ECO:0000269|PubMed:36183834"; MUTAGEN 373; /note="I->A,G,P,V,D,E,R,H,K,S,C,T,M,N,Q: Abolished interaction with G3BP1."; /evidence="ECO:0000269|PubMed:36183834"; MUTAGEN 373; /note="I->F: Increased interaction with G3BP1."; /evidence="ECO:0000269|PubMed:36183834"; MUTAGEN 376; /note="S->A,G,I,L,P,V,F,E,R,H,T,M,Q: Abolished interaction with G3BP1."; /evidence="ECO:0000269|PubMed:36183834"; MUTAGEN 376; /note="S->C: Increased interaction with G3BP1."; /evidence="ECO:0000269|PubMed:36183834"; MUTAGEN 377; /note="M->F,Y: Increased interaction with G3BP1."; /evidence="ECO:0000269|PubMed:36183834"; MUTAGEN 377; /note="M->G,P,K: Abolished interaction with G3BP1."; /evidence="ECO:0000269|PubMed:36183834"; MUTAGEN 608; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 612; /note="R->A: Major reduction in MYC and CCND2 RNA-binding; when associated with A-633 and A-690."; /evidence="ECO:0000269|PubMed:17210633"; MUTAGEN 612; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 616; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 619; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 624..626; /note="GYR->ASA: Decreased ability to undergo liquid-liquid phase separation."; /evidence="ECO:0000269|PubMed:34074792"; MUTAGEN 626; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 633; /note="R->A: Major reduction in MYC and CCND2 RNA-binding; when associated with A-612 and A-690."; /evidence="ECO:0000269|PubMed:17210633"; MUTAGEN 633; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-640, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 638..640; /note="GYR->ASA: Decreased ability to undergo liquid-liquid phase separation."; /evidence="ECO:0000269|PubMed:34074792"; MUTAGEN 640; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 660..662; /note="RDY->ASA: Decreased ability to undergo liquid-liquid phase separation."; /evidence="ECO:0000269|PubMed:34074792"; MUTAGEN 660; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-667, K-676, K-684, K-688, K-690, K-695 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 667; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-676, K-684, K-688, K-690, K-695 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 676; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-684, K-688, K-690, K-695 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 680..682; /note="QSG->ASA: Does not affect ability to undergo liquid-liquid phase separation."; /evidence="ECO:0000269|PubMed:34074792"; MUTAGEN 684; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-688, K-690, K-695 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 688; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-690, K-695 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 690; /note="R->A: Major reduction in MYC and CCND2 RNA-binding; when associated with A-612 and A-633."; /evidence="ECO:0000269|PubMed:17210633"; MUTAGEN 690; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-695 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 695; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690 and K-698."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 698; /note="R->K: Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690 and K-695."; /evidence="ECO:0000269|PubMed:31439799"; MUTAGEN 704..706; /note="NTQ->ASA: Does not affect ability to undergo liquid-liquid phase separation."; /evidence="ECO:0000269|PubMed:34074792
uniprot
proteins
post_translational_modification
PTM: Tyrosine phosphorylation by EPHA4 promotes interaction with FMR1 and liquid-liquid phase separation (LLPS) for the formation of a membraneless compartment that concentrates mRNAs with associated regulatory factors. {ECO:0000269|PubMed:31439799}.; PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner (PubMed:22967762). O-glycosylation by OGT inhibit ability to undergo liquid-liquid phase separation (LLPS) (PubMed:34074792). {ECO:0000269|PubMed:22967762, ECO:0000269|PubMed:34074792}.
uniprot
proteins
protein_family
Caprin family
uniprot
proteins
pubmed
14764709
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
17210633
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20516077
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21933836
uniprot
proteins
pubmed
22967762
uniprot
proteins
pubmed
23097442
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27022092
uniprot
proteins
pubmed
28592527
uniprot
proteins
pubmed
28733330
uniprot
proteins
pubmed
28794026
uniprot
proteins
pubmed
30258011
uniprot
proteins
pubmed
31439799
uniprot
proteins
pubmed
32302570
uniprot
proteins
pubmed
32302571
uniprot
proteins
pubmed
32302572
uniprot
proteins
pubmed
34074792
uniprot
proteins
pubmed
35977029
uniprot
proteins
pubmed
35979925
uniprot
proteins
pubmed
36040869
uniprot
proteins
pubmed
36136249
uniprot
proteins
pubmed
36183834
uniprot
proteins
pubmed
36279435
uniprot
proteins
pubmed
37316325
uniprot
proteins
pubmed
7657653
uniprot
proteins
pubmed
8786113
uniprot
proteins
sequence_length
709
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:17210633, ECO:0000269|PubMed:31439799}. Cytoplasm, cytosol {ECO:0000269|PubMed:28733330}. Cell projection, dendrite {ECO:0000269|PubMed:35979925}. Cell projection, lamellipodium {ECO:0000269|PubMed:28733330}. Note=Mediates formation and localizes to cytoplasmic ribonucleoprotein membraneless compartments (PubMed:31439799). Associated with RNA granules. At the leading edge of migrating fibroblasts, colocalizes with DDX3X (PubMed:28733330). {ECO:0000269|PubMed:28733330, ECO:0000269|PubMed:31439799}.; SUBCELLULAR LOCATION: Cytoplasm, cytosol. Note=(Microbial infection) In case of reovirus infection, associates with the outer peripheries of viral factories in a G3BP1 dependent manner. {ECO:0000269|PubMed:28794026}.
uniprot
proteins