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NELFD_PONAB
ID   NELFD_PONAB             Reviewed;         590 AA.
AC   Q5RFA0;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Negative elongation factor D;
DE            Short=NELF-D;
DE   AltName: Full=TH1-like protein;
GN   Name=NELFCD; Synonyms=NELFD, TH1L;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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).
CC       {ECO:0000250|UniProtKB:Q8IXH7}.
CC   -!- SUBUNIT: The NELF complex is composed of NELFA, NELFB, NELFCD and
CC       NELFE; NELFA and NELFCD form a stable subcomplex that binds primarily
CC       through NELFCD to the N-terminus of NELFB (By similarity). Binds RNA
CC       which may help to stabilize the NELF complex on nucleic acid (By
CC       similarity). In vitro, the NELFA:NELFCD subcomplex binds to ssDNA and
CC       ssRNA in a sequence- and structure-dependent manner (By similarity).
CC       Interacts with ARAF1 (By similarity). Interacts with PCF11 (By
CC       similarity). Interacts with NELFB (By similarity). Interacts with KAT8
CC       (By similarity). {ECO:0000250|UniProtKB:Q8IXH7,
CC       ECO:0000250|UniProtKB:Q922L6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IXH7}.
CC   -!- SIMILARITY: Belongs to the NELF-D family. {ECO:0000305}.
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DR   EMBL; CR857261; CAH89557.1; -; mRNA.
DR   RefSeq; NP_001124679.1; NM_001131207.1.
DR   AlphaFoldDB; Q5RFA0; -.
DR   SMR; Q5RFA0; -.
DR   GeneID; 100171526; -.
DR   KEGG; pon:100171526; -.
DR   CTD; 51497; -.
DR   eggNOG; ENOG502QPUE; Eukaryota.
DR   InParanoid; Q5RFA0; -.
DR   OrthoDB; 1288184at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR006942; TH1.
DR   PANTHER; PTHR12144; PTHR12144; 1.
DR   Pfam; PF04858; TH1; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Reference proteome; Repressor; RNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..590
FT                   /note="Negative elongation factor D"
FT                   /id="PRO_0000312640"
FT   REGION          15..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..41
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  66219 MW;  7B034E965E88B34C CRC64;
     MAGAAPGAIM DEDYYGSAAE WGDEADGGQQ EDDSGEGEDD AEVQQECLHK FSTRDYIMEP
     SIFNTLKRYF QAGGSPENVI QLLSENYTAV AQTVNLLAEW LIQTGVEPVQ VQETVENHLK
     SLLIKHFDPR KADSIFTEEG ETPAWLEQMI AHTTWRDLFY KLAEAHPDCL MLNFTVKLIS
     DAGYQGEITS VSTACQQLEV FSRVLRTSLA TILDGGEENL EKNLPEFAKM VCHGEHTYLF
     AQAMMSVLAQ EEQGGSAVRR IAQEVQRFAQ EKGHDASQIT LALGTAASYP RACQALGAML
     SKGALNPADI TVLFKMFTSM DPPPVELIRV PAFLDLFMQS LFKPGARINQ DHKHKYIHIL
     AYAASVVETW KKNKRVSINK DELKSTSKAV ETVHNLCCNE NKGASELVAE LSTLYQCIRF
     PVVAMGVLKW VDWTVSEPRY FQLQTDHTPV HLALLDEIST CHQLLHPQVL QLLVKLFETE
     HSQLDVMEQL ELKKTLLDRM VHLLSRGYVL PVVSYIRKCL EKLDTDISLI RYFVTEVLDV
     IAPPYTSDFV QLFLPILEND SIAGTIKTEG EHDPVTEFIA HCKSNFIMVN
 
 
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