SARNP
entrez
84324
canonical
uniprot
P82979
canonical
ensembl
ENSG00000205323
resolver
ensp
ENSP00000337632
resolver
ensp
ENSP00000449409
resolver
enst
ENST00000336133
resolver
enst
ENST00000546604
resolver
genesymbol
SARNP
resolver
genesymbol_syn
HCC1
resolver
hgnc
HGNC:24432
resolver
uniprot
A8K393
resolver
uniprot
Q9P066
resolver
uniprot_entry
SARNP_HUMAN
resolver
uniprot_sec
A8K393
resolver
uniprot_sec
Q9P066
resolver
amino_acid_sequence
MATETVELHKLKLAELKQECLARGLETKGIKQDLIHRLQAYLEEHAEEEANEEDVLGDETEEEETKPIELPVKEEEPPEKTVDVAAEKKVVKITSEIPQTERMQKRAERFNVPVSLESKKAARAARFGISSVPTKGLSSDNKPMVNLDKLKERAQRFGLNVSSISRKSEDDEKLKKRKERFGIVTSSAGTGTTEDTEAKKRKRAERFGIA
uniprot
proteins
function
FUNCTION: Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single-stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15338056, PubMed:17196963, PubMed:20844015). The TREX complex is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15338056, PubMed:17196963, PubMed:20844015). Associates with DDX39B, which facilitates RNA binding of DDX39B and likely plays a role in mRNA export (PubMed:37578863). {ECO:0000269|PubMed:15338056, ECO:0000269|PubMed:17196963, ECO:0000269|PubMed:20844015, ECO:0000269|PubMed:37578863}.
uniprot
proteins
mass_dalton
23671
uniprot
proteins
mutagenesis
MUTAGEN 106..110; /note="RAERF->AAERA: Abolishes interaction with DDX39B; when associated with 123-A--A-127; 153-A--A-157; 177-A--A-181 and 203-A--A-207."; /evidence="ECO:0000269|PubMed:37578863"; MUTAGEN 107..210; /note="Missing: Impairs interaction with DDX39B."; /evidence="ECO:0000269|PubMed:37578863"; MUTAGEN 123..127; /note="RAARF->AAARA: Abolishes interaction with DDX39B; when associated with 106-A--A-110; 153-A--A-157; 177-A--A-181 and 203-A--A-207."; /evidence="ECO:0000269|PubMed:37578863"; MUTAGEN 153..157; /note="RAQRF->AAQRA: Impairs interaction with DDX39B; when associated with 177-A--A-181 and 203-A--A-207. Abolishes interaction with DDX39B; when associated with 106-A--A-110; 123-A--A-127; 177-A--A-181 and 203-A--A-207."; /evidence="ECO:0000269|PubMed:37578863"; MUTAGEN 177..181; /note="RKERF->AKERA: Impairs interaction with DDX39B; when associated with 153-A--A-157 and 203-A--A-207. Abolishes interaction with DDX39B; when associated with 106-A--A-110; 123-A--A-127; 153-A--A-157 and 203-A--A-207."; /evidence="ECO:0000269|PubMed:37578863"; MUTAGEN 203..207; /note="RAERF->AAERA: Impairs interaction with DDX39B; when associated with 153-A--A-157 and 177-A--A-181. Abolishes interaction with DDX39B; when associated with 106-A--A-110; 123-A--A-127; 153-A--A-157 and 177-A--A-181."; /evidence="ECO:0000269|PubMed:37578863
uniprot
proteins
protein_family
SAP domain-containing ribonucleoprotein family
uniprot
proteins
pubmed
11042152
uniprot
proteins
pubmed
11356193
uniprot
proteins
pubmed
11922608
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15338056
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17196963
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20844015
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
37578863
uniprot
proteins
sequence_length
210
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Nucleus speckle.
uniprot
proteins