KHDRBS1
entrez
10657
canonical
uniprot
Q07666
canonical
ensembl
ENSG00000121774
resolver
ensp
ENSP00000313829
resolver
ensp
ENSP00000417731
resolver
genesymbol
KHDRBS1
resolver
genesymbol_syn
SAM68
resolver
hgnc
HGNC:18116
resolver
uniprot
D3DPP3
resolver
uniprot
Q6PJX7
resolver
uniprot
Q8NB97
resolver
uniprot
Q99760
resolver
uniprot_entry
KHDR1_HUMAN
resolver
uniprot_sec
D3DPP3
resolver
uniprot_sec
Q6PJX7
resolver
uniprot_sec
Q8NB97
resolver
uniprot_sec
Q99760
resolver
amino_acid_sequence
MQRRDDPAARMSRSSGRSGSMDPSGAHPSVRQTPSRQPPLPHRSRGGGGGSRGGARASPATQPPPLLPPSATGPDATVGGPAPTPLLPPSATASVKMEPENKYLPELMAEKDSLDPSFTHAMQLLTAEIEKIQKGDSKKDDEENYLDLFSHKNMKLKERVLIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKAKEEELRKGGDPKYAHLNMDLHVFIEVFGPPCEAYALMAHAMEEVKKFLVPDMMDDICQEQFLELSYLNGVPEPSRGRGVPVRGRGAAPPPPPVPRGRGVGPPRGALVRGTPVRGAITRGATVTRGVPPPPTVRGAPAPRARTAGIQRIPLPPPPAPETYEEYGYDDTYAEQSYEGYEGYYSQSQGDSEYYDYGHGEVQDSYEAYGQDDWNGTRPSLKAPPARPVKGAYREHPYGRY
uniprot
proteins
function
FUNCTION: Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824). RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner (PubMed:26080397). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (PubMed:17371836, PubMed:20186123). Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (By similarity). {ECO:0000250|UniProtKB:Q60749, ECO:0000269|PubMed:15021911, ECO:0000269|PubMed:17371836, ECO:0000269|PubMed:20186123, ECO:0000269|PubMed:20610388, ECO:0000269|PubMed:22253824, ECO:0000269|PubMed:26080397, ECO:0000269|PubMed:26758068}.; FUNCTION: Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase. {ECO:0000269|PubMed:9013542}.
uniprot
proteins
mass_dalton
48227
uniprot
proteins
mutagenesis
MUTAGEN 103; /note="Y->S: Impairs homodimerization."; /evidence="ECO:0000269|PubMed:20610388"; MUTAGEN 110; /note="E->A: Impairs homodimerization."; /evidence="ECO:0000269|PubMed:20610388"; MUTAGEN 118; /note="F->S: Disrupts homodimerization, impairs influence on alternative splicing."; /evidence="ECO:0000269|PubMed:20610388"; MUTAGEN 229; /note="V->F: Disrupts binding to poly(A). Decreased binding to the BCL2L1 mRNA. Loss of function in BCL2L1 splicing. Changed nuclear localization."; /evidence="ECO:0000269|PubMed:17371836"; MUTAGEN 241; /note="Y->E: Fails to influence alternative splicing of CD44, NRXN2 and NRXN3."; /evidence="ECO:0000269|PubMed:26758068"; MUTAGEN 381; /note="E->K: Disrupts interaction with APC."; /evidence="ECO:0000269|PubMed:22000517"; MUTAGEN 383; /note="Y->K: Impairs interaction with APC."; /evidence="ECO:0000269|PubMed:22000517"; MUTAGEN 384; /note="E->K: Disrupts interaction with APC."; /evidence="ECO:0000269|PubMed:22000517"; MUTAGEN 435; /note="Y->F: No effect on the nuclear localization."; /evidence="ECO:0000269|PubMed:16179349"; MUTAGEN 440; /note="Y->F: Completely blocks nuclear localization."; /evidence="ECO:0000269|PubMed:16179349"; MUTAGEN 443; /note="Y->F: No effect on the nuclear localization."; /evidence="ECO:0000269|PubMed:16179349
uniprot
proteins
post_translational_modification
PTM: Tyrosine phosphorylated by several non-receptor tyrosine kinases including LCK, FYN and JAK3. Also tyrosine phosphorylated by the non-receptor tyrosine kinase SRMS in an EGF-dependent manner (PubMed:29496907). Negatively correlates with ability to bind RNA but required for many interactions with proteins. Phosphorylation by PTK6 negatively regulates its RNA binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the nuclear localization of KHDRBS1. Phosphorylation at Tyr-387 disrupts interaction with APC. Phosphorylation at tyrosine residues by FYN inverts activity on modulation of BCL2L1 alternative splicing. {ECO:0000269|PubMed:11585385, ECO:0000269|PubMed:16179349, ECO:0000269|PubMed:17371836, ECO:0000269|PubMed:22000517, ECO:0000269|PubMed:29496907, ECO:0000269|PubMed:9045636}.; PTM: Acetylated (PubMed:15021911, PubMed:26080397). Positively correlates with ability to bind RNA (PubMed:15021911). Deacetylated by HDAC6; this regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons (PubMed:26080397). {ECO:0000269|PubMed:15021911, ECO:0000269|PubMed:26080397}.; PTM: Arginine methylation is required for nuclear localization. Also can affect interaction with other proteins. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 and FNBP4/FBP30. {ECO:0000269|PubMed:12529443, ECO:0000269|PubMed:1374686, ECO:0000269|Ref.7}.
uniprot
proteins
protein_family
KHDRBS family
uniprot
proteins
pubmed
10332027
uniprot
proteins
pubmed
10913193
uniprot
proteins
pubmed
11585385
uniprot
proteins
pubmed
12529443
uniprot
proteins
pubmed
1374686
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15021911
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15782174
uniprot
proteins
pubmed
16179349
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17371836
uniprot
proteins
pubmed
17890166
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20186123
uniprot
proteins
pubmed
20610388
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21613532
uniprot
proteins
pubmed
22000517
uniprot
proteins
pubmed
22253824
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24514149
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26080397
uniprot
proteins
pubmed
26758068
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29496907
uniprot
proteins
pubmed
9013542
uniprot
proteins
pubmed
9045636
uniprot
proteins
sequence_length
443
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1374686, ECO:0000269|PubMed:26080397, ECO:0000269|PubMed:29496907}. Cytoplasm {ECO:0000269|PubMed:29496907}. Membrane {ECO:0000269|PubMed:1374686}. Note=Predominantly located in the nucleus but also located partially in the cytoplasm. {ECO:0000269|PubMed:29496907}.
uniprot
proteins