PRAG1
entrez
157285
canonical
uniprot
Q86YV5
canonical
ensembl
ENSG00000275342
resolver
ensp
ENSP00000481109
resolver
ensp
ENSP00000603752
resolver
enst
ENST00000615670
resolver
enst
ENST00000933693
resolver
genesymbol
PRAG1
resolver
genesymbol_syn
SGK223
resolver
hgnc
HGNC:25438
resolver
uniprot
Q8N3N5
resolver
uniprot_entry
PRAG1_HUMAN
resolver
uniprot_sec
Q8N3N5
resolver
amino_acid_sequence
MHQTLCLNPESLKMSACSDFVEHIWKPGSCKNCFCLRSDHQLVAGPPQPRAGSLPPPPRLPPRPENCRLEDEGVNSSPYSKPTIAVKPTMMSSEASDVWTEANLSAEVSQVIWRRAPGKLPLPKQEDAPVVYLGSFRGVQKPAGPSTSPDGNSRCPPAYTMVGLHNLEPRGERNIAFHPVSFPEEKAVHKEKPSFPYQDRPSTQESFRQKLAAFAGTTSGCHQGPGPLRESLPSEDDSDQRCSPSGDSEGGEYCSILDCCPGSPVAKAASQTAGSRGRHGGRDCSPTCWEQGKCSGPAEQEKRGPSFPKECCSQGPTAHPSCLGPKKLSLTSEAAISSDGLSCGSGSGSGSGASSPFVPHLESDYCSLMKEPAPEKQQDPGCPGVTPSRCLGLTGEPQPPAHPREATQPEPIYAESTKRKKAAPVPSKSQAKIEHAAAAQGQGQVCTGNAWAQKAASGWGRDSPDPTPQVSATITVMAAHPEEDHRTIYLSSPDSAVGVQWPRGPVSQNSEVGEEETSAGQGLSSRESHAHSASESKPKERPAIPPKLSKSSPVGSPVSPSAGGPPVSPLADLSDGSSGGSSIGPQPPSQGPADPAPSCRTNGVAISDPSRCPQPAASSASEQRRPRFQAGTWSRQCRIEEEEEVEQELLSHSWGRETKNGPTDHSNSTTWHRLHPTDGSSGQNSKVGTGMSKSASFAFEFPKDRSGIETFSPPPPPPKSRHLLKMNKSSSDLEKVSQGSAESLSPSFRGVHVSFTTGSTDSLASDSRTCSDGGPSSELAHSPTNSGKKLFAPVPFPSGSTEDVSPSGPQQPPPLPQKKIVSRAASSPDGFFWTQGSPKPGTASPKLNLSHSETNVHDESHFSYSLSPGNRHHPVFSSSDPLEKAFKGSGHWLPAAGLAGNRGGCGSPGLQCKGAPSASSSQLSVSSQASTGSTQLQLHGLLSNISSKEGTYAKLGGLYTQSLARLVAKCEDLFMGGQKKELHFNENNWSLFKLTCNKPCCDSGDAIYYCATCSEDPGSTYAVKICKAPEPKTVSYCSPSVPVHFNIQQDCGHFVASVPSSMLSSPDAPKDPVPALPTHPPAQEQDCVVVITREVPHQTASDFVRDSAASHQAEPEAYERRVCFLLLQLCNGLEHLKEHGIIHRDLCLENLLLVHCTLQAGPGPAPAPAPAPAPAAAAPPCSSAAPPAGGTLSPAAGPASPEGPREKQLPRLIISNFLKAKQKPGGTPNLQQKKSQARLAPEIVSASQYRKFDEFQTGILIYELLHQPNPFEVRAQLRERDYRQEDLPPLPALSLYSPGLQQLAHLLLEADPIKRIRIGEAKRVLQCLLWGPRRELVQQPGTSEEALCGTLHNWIDMKRALMMMKFAEKAVDRRRGVELEDWLCCQYLASAEPGALLQSLKLLQLL
uniprot
proteins
function
FUNCTION: Catalytically inactive protein kinase that acts as a scaffold protein. Functions as an effector of the small GTPase RND2, which stimulates RhoA activity and inhibits NGF-induced neurite outgrowth (By similarity). Promotes Src family kinase (SFK) signaling by regulating the subcellular localization of CSK, a negative regulator of these kinases, leading to the regulation of cell morphology and motility by a CSK-dependent mechanism (By similarity). Acts as a critical coactivator of Notch signaling (By similarity). {ECO:0000250|UniProtKB:D3ZMK9, ECO:0000250|UniProtKB:Q571I4}.
uniprot
proteins
mass_dalton
149624
uniprot
proteins
mutagenesis
MUTAGEN 955; /note="L->A: Decreases homodimerization. Abolished interaction with PEAK1. No effect on cell migration."; /evidence="ECO:0000269|PubMed:29079850"; MUTAGEN 966; /note="L->A: Decreases homodimerization. Abolished interaction with PEAK1. Decreases cell migration."; /evidence="ECO:0000269|PubMed:29079850"; MUTAGEN 1243; /note="I->A: No effect on homodimerization. Decreases oligomerization. Decreases interaction with PEAK1."; /evidence="ECO:0000269|PubMed:29079850"; MUTAGEN 1271; /note="F->A: Decreases homodimerization. Decreases interaction with PEAK1."; /evidence="ECO:0000269|PubMed:29079850"; MUTAGEN 1278; /note="R->A: Decreases homodimerization."; /evidence="ECO:0000269|PubMed:29079850"; MUTAGEN 1282; /note="Y->A: No effect on homodimerization. Decreases oligomerization. Decreases interaction with PEAK1. No effect on cell migration."; /evidence="ECO:0000269|PubMed:29079850"; MUTAGEN 1366; /note="F->A: Decreases homodimerization. Abolished interaction with PEAK1. Decreases cell migration."; /evidence="ECO:0000269|PubMed:29079850"; MUTAGEN 1382; /note="W->A: Decreases homodimerization. Abolished interaction with PEAK1. Decreases cell migration."; /evidence="ECO:0000269|PubMed:29079850
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by CSK on Tyr-253, Tyr-365, and Tyr-413; Tyr-413 is a primary site of phosphorylation. {ECO:0000250|UniProtKB:D3ZMK9}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
12471243
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27116701
uniprot
proteins
pubmed
29079850
uniprot
proteins
sequence_length
1406
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:D3ZMK9}. Cell junction, focal adhesion {ECO:0000269|PubMed:27116701}. Nucleus {ECO:0000250|UniProtKB:Q571I4}. Note=Colocalized with NOTCH1 in the nucleus. {ECO:0000250|UniProtKB:Q571I4}.
uniprot
proteins