RBM7
entrez
10179
canonical
uniprot
Q9Y580
canonical
ensembl
ENSG00000076053
resolver
ensp
ENSP00000364639
resolver
ensp
ENSP00000439918
resolver
ensp
ENSP00000445848
resolver
enst
ENST00000375490
resolver
enst
ENST00000540163
resolver
enst
ENST00000545678
resolver
genesymbol
RBM7
resolver
hgnc
HGNC:9904
resolver
uniprot
B2R6K8
resolver
uniprot
G3V1T9
resolver
uniprot
J3KPD3
resolver
uniprot
Q9NUT4
resolver
uniprot_entry
G3V1T9_HUMAN
resolver
uniprot_entry
J3KPD3_HUMAN
resolver
uniprot_entry
RBM7_HUMAN
resolver
uniprot_sec
B2R6K8
resolver
uniprot_sec
Q9NUT4
resolver
amino_acid_sequence
MGAAAAEADRTLFVGNLETKVTEELLFELFHQAGPVIKVKIPKDKDGKPKQFAFVNFKHEVSVPYAMNLLNGIKLYGRPIKIQFRSGSSHAPQDVSLSYPQHHVGNSSPTSTSPSRYERTMDNMTSSAQIIQRSFSSPENFQRQAVMNSALRQMSYGGKFGSSPLDQSGFSPSVQSHSHSFNQSSSSQWRQGTPSSQRKVRMNSYPYLADRHYSREQRYTDHGSDHHYRGKRDDFFYEDRNHDDWSHDYDNRRDSSRDGKWRSSRH
uniprot
proteins
function
FUNCTION: RNA-binding subunit of the trimeric nuclear exosome targeting (NEXT) complex, a complex that functions as an RNA exosome cofactor that directs a subset of non-coding short-lived RNAs for exosomal degradation (PubMed:25189701, PubMed:25525152, PubMed:25578728, PubMed:25852104, PubMed:27871484). NEXT is involved in surveillance and turnover of aberrant transcripts and non-coding RNAs (PubMed:25189701, PubMed:25852104, PubMed:27871484). Binds preferentially polyuridine sequences and associates with newly synthesized RNAs, including pre-mRNAs and short-lived exosome substrates such as promoter upstream transcripts (PROMPTs), enhancer RNAs (eRNAs), and 3'-extended products from small nuclear RNAs (snRNAs) (PubMed:25189701, PubMed:25525152, PubMed:25578728, PubMed:25852104). Participates in several biological processes including DNA damage response (DDR) and stress response (PubMed:25525152, PubMed:30824372). During stress response, activation of the p38MAPK-MK2 pathway decreases RBM7-RNA-binding and subsequently the RNA exosome degradation activities, thereby modulating the turnover of non-coding transcriptome (PubMed:25525152). Participates in DNA damage response (DDR), through its interaction with MEPCE and LARP7, the core subunits of 7SK snRNP complex, that release the positive transcription elongation factor b (P-TEFb) complex from the 7SK snRNP. In turn, activation of P-TEFb complex induces the transcription of P-TEFb-dependent DDR genes to promote cell viability (PubMed:30824372). {ECO:0000269|PubMed:25189701, ECO:0000269|PubMed:25525152, ECO:0000269|PubMed:25578728, ECO:0000269|PubMed:25852104, ECO:0000269|PubMed:27871484, ECO:0000269|PubMed:30824372}.
uniprot
proteins
mass_dalton
30504
uniprot
proteins
mutagenesis
MUTAGEN 13; /note="F->A: Decreases affinity for RNA binding. Does not affect The NEXT complex assembly. Impairs snRNA binding."; /evidence="ECO:0000269|PubMed:25852104"; MUTAGEN 25; /note="L->E: Impaired interaction with ZCCHC8; when associated with E-29."; /evidence="ECO:0000269|PubMed:27905398"; MUTAGEN 29; /note="L->E: Impaired interaction with ZCCHC8; when associated with E-25."; /evidence="ECO:0000269|PubMed:27905398"; MUTAGEN 50; /note="K->A: Abrogates the interaction with 7SK small nuclear RNA (7SK); when associated with A-52 and A-54. Does not affect interaction between HEXIM1, CDK9 and 7SK small nuclear RNA (7SK); when associated with A-52 and A-54. Does not affect interaction with MEPCE and LARP7; when associated with A-52 and A-54. Decreases induction of P-TEFb-dependent DNA damage response (DDR); when associated with A-52 and A-54."; /evidence="ECO:0000269|PubMed:30824372"; MUTAGEN 52; /note="F->A: Decreases affinity for RNA binding. Abrogates the interaction with 7SK small nuclear RNA (7SK); when associated with A-50 and A-54. Does not affect interaction between HEXIM1, CDK9 and 7SK small nuclear RNA (7SK); when associated with A-50 and A-54. Does not affect interaction with MEPCE and LARP7; when associated with A-50 and A-54. Decreases induction of P-TEFb-dependent DNA damage response (DDR); when associated with A-50 and A-54."; /evidence="ECO:0000269|PubMed:25852104, ECO:0000269|PubMed:30824372"; MUTAGEN 54; /note="F->A: Abrogates the interaction with 7SK small nuclear RNA (7SK); when associated with A-50 and A-52. Does not affect interaction between HEXIM1, CDK9 and 7SK small nuclear RNA (7SK); when associated with A-50 and A-52. Does not affect interaction with MEPCE and LARP7; when associated with A-50 and A-52. Decreases induction of P-TEFb-dependent DNA damage response (DDR); when associated with A-50 and A-52."; /evidence="ECO:0000269|PubMed:30824372"; MUTAGEN 65; /note="Y->A: Reduced interaction with ZCCHC8, and impaired interaction with SF3B2/SAP145; when associated with E-69."; /evidence="ECO:0000269|PubMed:27905398"; MUTAGEN 69; /note="L->E: Reduced interaction with ZCCHC8, and impaired interaction with SF3B2/SAP145; when associated with A-65."; /evidence="ECO:0000269|PubMed:27905398"; MUTAGEN 136; /note="S->A: Impairs phosphorylation. Impairs phosphorylation; when associated with S-204. Prevents PROMPTs accumulation to >50%."; /evidence="ECO:0000269|PubMed:25189701, ECO:0000269|PubMed:25525152"; MUTAGEN 204; /note="S->A: Impairs phosphorylation. Impairs phosphorylation; when associated with S-136."; /evidence="ECO:0000269|PubMed:25189701
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-136 by MAPK14/p38-alpha-activated MAPKAPK2/MK2; this phosphorylation is stress-dependent; this phosphorylation decreases its RNA-binding capacity therefore affecting RNA nuclear exosome-mediated degradation (PubMed:25189701, PubMed:25525152). This phosphorylation mediates YWHAE and YWHAZ interactions (PubMed:25189701). {ECO:0000269|PubMed:25189701, ECO:0000269|PubMed:25525152}.
uniprot
proteins
pubmed
12634307
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16263084
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21855801
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25189701
uniprot
proteins
pubmed
25489052
uniprot
proteins
pubmed
25525152
uniprot
proteins
pubmed
25578728
uniprot
proteins
pubmed
25852104
uniprot
proteins
pubmed
27139832
uniprot
proteins
pubmed
27193168
uniprot
proteins
pubmed
27871484
uniprot
proteins
pubmed
27905398
uniprot
proteins
pubmed
30824372
uniprot
proteins
sequence_length
266
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:21855801, ECO:0000269|PubMed:25852104}. Nucleus {ECO:0000250|UniProtKB:Q9CQT2}. Note=Excluded from the nucleolus. {ECO:0000269|PubMed:21855801}.
uniprot
proteins