NELFE
entrez
7936
canonical
uniprot
P18615
canonical
ensembl
ENSG00000204356
resolver
ensembl
ENSG00000206268
resolver
ensembl
ENSG00000206357
resolver
ensembl
ENSG00000229363
resolver
ensembl
ENSG00000231044
resolver
ensembl
ENSG00000233801
resolver
ensp
ENSP00000364574
resolver
ensp
ENSP00000364578
resolver
ensp
ENSP00000552661
resolver
ensp
ENSP00000618368
resolver
genesymbol
NELFE
resolver
genesymbol_syn
RD
resolver
genesymbol_syn
RDBP
resolver
hgnc
HGNC:13974
resolver
uniprot
A2BE08
resolver
uniprot
B4DUN1
resolver
uniprot
B4DYX9
resolver
uniprot
Q5JP74
resolver
uniprot
Q5JP75
resolver
uniprot
Q96F56
resolver
uniprot
Q9NPK2
resolver
uniprot_entry
NELFE_HUMAN
resolver
uniprot_sec
A2BE08
resolver
uniprot_sec
B4DUN1
resolver
uniprot_sec
B4DYX9
resolver
uniprot_sec
Q5JP74
resolver
uniprot_sec
Q5JP75
resolver
uniprot_sec
Q96F56
resolver
uniprot_sec
Q9NPK2
resolver
amino_acid_sequence
MLVIPPGLSEEEEALQKKFNKLKKKKKALLALKKQSSSSTTSQGGVKRSLSEQPVMDTATATEQAKQLVKSGAISAIKAETKNSGFKRSRTLEGKLKDPEKGPVPTFQPFQRSISADDDLQESSRRPQRKSLYESFVSSSDRLRELGPDGEEAEGPGAGDGPPRSFDWGYEERSGAHSSASPPRSRSRDRSHERNRDRDRDRERDRDRDRDRDRERDRDRDRDRDRDRERDRDRERDRDRDREGPFRRSDSFPERRAPRKGNTLYVYGEDMTPTLLRGAFSPFGNIIDLSMDPPRNCAFVTYEKMESADQAVAELNGTQVESVQLKVNIARKQPMLDAATGKSVWGSLAVQNSPKGCHRDKRTQIVYSDDVYKENLVDGF
uniprot
proteins
function
FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II (PubMed:10199401, PubMed:27256882). The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex (PubMed:11940650, PubMed:12612062, PubMed:27256882). Provides the strongest RNA binding activity of the NELF complex and may initially recruit the NELF complex to RNA (PubMed:18303858, PubMed:27256882, PubMed:27282391). {ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:11940650, ECO:0000269|PubMed:12612062, ECO:0000269|PubMed:18303858, ECO:0000269|PubMed:27256882, ECO:0000269|PubMed:27282391}.; FUNCTION: (Microbial infection) The NELF complex is involved in HIV-1 latency possibly involving recruitment of PCF11 to paused RNA polymerase II. {ECO:0000269|PubMed:23884411}.
uniprot
proteins
mass_dalton
43240
uniprot
proteins
mutagenesis
MUTAGEN 122; /note="E->Q: Abolished poly-ADP-ribosylation by PARP1; when associated with Q-151; Q-172 and Q-374."; /evidence="ECO:0000269|PubMed:27256882"; MUTAGEN 151; /note="E->Q: Abolished poly-ADP-ribosylation by PARP1; when associated with Q-122; Q-172 and Q-374."; /evidence="ECO:0000269|PubMed:27256882"; MUTAGEN 171; /note="E->Q: Abolished poly-ADP-ribosylation by PARP1; when associated with Q-122; Q-151 and Q-374."; /evidence="ECO:0000269|PubMed:27256882"; MUTAGEN 181..191; /note="SPPRSRSRDRS->APPRARARDRA: Decreased phosphorylation."; /evidence="ECO:0000269|PubMed:14701750"; MUTAGEN 181..191; /note="SPPRSRSRDRS->EPPRERERDRE: Mimics phosphorylation, promoting its release from chromatin."; /evidence="ECO:0000269|PubMed:14701750"; MUTAGEN 295..299; /note="RNCAF->EQMAT: Abolishes interaction with RNA but not the interaction with other proteins of the NELF complex."; /evidence="ECO:0000269|PubMed:11940650"; MUTAGEN 374; /note="E->Q: Abolished poly-ADP-ribosylation by PARP1; when associated with Q-122; Q-151 and Q-172."; /evidence="ECO:0000269|PubMed:27256882
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by the P-TEFb complex at sites next to its RNA recognition motif, promoting its release from chromatin. {ECO:0000269|PubMed:14701750}.; PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.; PTM: Poly-ADP-ribosylated by PARP1, thereby preventing RNA-binding and relieving transcription pausing. {ECO:0000269|PubMed:27256882}.
uniprot
proteins
protein_family
RRM NELF-E family
uniprot
proteins
pubmed
10199401
uniprot
proteins
pubmed
11940650
uniprot
proteins
pubmed
12612062
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14656967
uniprot
proteins
pubmed
14701750
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15561718
uniprot
proteins
pubmed
16898873
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18303858
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
2119325
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23884411
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
2612324
uniprot
proteins
pubmed
27256882
uniprot
proteins
pubmed
27282391
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
8373374
uniprot
proteins
sequence_length
380
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14701750}. Chromosome {ECO:0000269|PubMed:14701750}. Note=Localizes to chromatin (PubMed:14701750). Phosphorylation by the P-TEFb complex promotes its release from chromatin (PubMed:14701750). {ECO:0000269|PubMed:14701750}.
uniprot
proteins