NELFE_BOVIN
ID NELFE_BOVIN Reviewed; 374 AA.
AC Q0V898;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Negative elongation factor E;
DE Short=NELF-E;
DE AltName: Full=RNA-binding protein RD;
GN Name=NELFE; Synonyms=RDBP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential component of the NELF complex, a complex that
CC negatively regulates the elongation of transcription by RNA polymerase
CC II (By similarity). The NELF complex, which acts via an association
CC with the DSIF complex and causes transcriptional pausing, is
CC counteracted by the P-TEFb kinase complex (By similarity). Provides the
CC strongest RNA binding activity of the NELF complex and may initially
CC recruit the NELF complex to RNA (By similarity).
CC {ECO:0000250|UniProtKB:P18615}.
CC -!- SUBUNIT: The NELF complex is composed of NELFA, NELFB, NELFCD and NELFE
CC (By similarity). Interacts with NELFB (By similarity).
CC {ECO:0000250|UniProtKB:P18615, ECO:0000250|UniProtKB:P19426}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18615}.
CC Chromosome {ECO:0000250|UniProtKB:P18615}. Note=Localizes to chromatin.
CC Phosphorylation by the P-TEFb complex promotes its release from
CC chromatin. {ECO:0000250|UniProtKB:P18615}.
CC -!- DOMAIN: The RRM domain interacts with RNA, and is essential for NELF
CC complex function. It is however not required for the NELF complex
CC formation. {ECO:0000250|UniProtKB:P18615}.
CC -!- PTM: Phosphorylated by the P-TEFb complex at sites next to its RNA
CC recognition motif, promoting its release from chromatin.
CC {ECO:0000250|UniProtKB:P18615}.
CC -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:P18615}.
CC -!- SIMILARITY: Belongs to the RRM NELF-E family. {ECO:0000305}.
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DR EMBL; BT026321; ABG81477.1; -; mRNA.
DR EMBL; BC120072; AAI20073.1; -; mRNA.
DR RefSeq; NP_001069672.1; NM_001076204.2.
DR AlphaFoldDB; Q0V898; -.
DR BMRB; Q0V898; -.
DR SMR; Q0V898; -.
DR STRING; 9913.ENSBTAP00000009802; -.
DR iPTMnet; Q0V898; -.
DR PaxDb; Q0V898; -.
DR PeptideAtlas; Q0V898; -.
DR PRIDE; Q0V898; -.
DR Ensembl; ENSBTAT00000009802; ENSBTAP00000009802; ENSBTAG00000007453.
DR GeneID; 540158; -.
DR KEGG; bta:540158; -.
DR CTD; 7936; -.
DR VEuPathDB; HostDB:ENSBTAG00000007453; -.
DR VGNC; VGNC:32002; NELFE.
DR eggNOG; ENOG502QQQ4; Eukaryota.
DR GeneTree; ENSGT00630000089917; -.
DR HOGENOM; CLU_055643_0_0_1; -.
DR InParanoid; Q0V898; -.
DR OMA; SQKSAHK; -.
DR OrthoDB; 1377312at2759; -.
DR TreeFam; TF324087; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000007453; Expressed in isthmus of fallopian tube and 106 other tissues.
DR ExpressionAtlas; Q0V898; baseline.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032021; C:NELF complex; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd12305; RRM_NELFE; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR033102; NELFE.
DR InterPro; IPR034637; NELFE_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR17250; PTHR17250; 2.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..374
FT /note="Negative elongation factor E"
FT /id="PRO_0000283704"
FT REPEAT 184..185
FT /note="1"
FT REPEAT 186..187
FT /note="2"
FT REPEAT 188..189
FT /note="3"
FT REPEAT 190..191
FT /note="4"
FT REPEAT 192..193
FT /note="5"
FT REPEAT 194..195
FT /note="6"
FT REPEAT 196..197
FT /note="7"
FT REPEAT 198..199
FT /note="8"
FT REPEAT 200..201
FT /note="9"
FT REPEAT 202..203
FT /note="10"
FT REPEAT 204..205
FT /note="11"
FT REPEAT 206..207
FT /note="12"
FT REPEAT 208..209
FT /note="13"
FT REPEAT 210..211
FT /note="14"
FT REPEAT 212..213
FT /note="15"
FT REPEAT 214..215
FT /note="16"
FT REPEAT 216..217
FT /note="17"
FT REPEAT 218..219
FT /note="18"
FT REPEAT 220..221
FT /note="19"
FT REPEAT 222..223
FT /note="20"
FT REPEAT 224..225
FT /note="21"
FT REPEAT 226..227
FT /note="22"
FT REPEAT 228..229
FT /note="23"
FT REPEAT 230..231
FT /note="24"
FT REPEAT 232..233
FT /note="25"
FT REPEAT 234..235
FT /note="26"
FT REPEAT 236..237
FT /note="27"
FT DOMAIN 256..326
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 30..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..237
FT /note="27 X 2 AA approximate tandem repeats of R-[DSNE]"
FT COILED 7..36
FT /evidence="ECO:0000255"
FT COMPBIAS 32..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 266
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 268
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P18615"
SQ SEQUENCE 374 AA; 42331 MW; B9FEDD9B78AB2DBC CRC64;
MLVIPPGLSE EEEALQKKFN KLKKKKKALL ALKKQSSSST ASQGGVKRSL SEQPVVDTAT
ATEQAKQLVK SGAISAIKAE TKNSGFKRSR TLEGKLKDPE KGPVPTFQPF QRSVSADDDL
QESSRRPQRK SLYESFVSSS DRLRELGPDG EEAEGPGAGD GPPRSFDWGY EERGGARSSA
SPPRSRSRDR SRERNRDRDR DRDRERDRER DRDRDRDRER DRDRDRDRDR DRERDREGPF
RRSDSFPERR APRKGNTLYV YGEDMTPTLL RGAFSPFGNI IDLSMDPPRN CAFVTYEKME
SADQAVAELN GTQVESVQLK VSIARKQPML DAATGKSVWG SLAVQNSPKG CHRDKRTQIV
YSDDVYKENL VDGF
