NELFB_HUMAN
ID NELFB_HUMAN Reviewed; 580 AA.
AC Q8WX92; A0A0X1KG71; A2BFA3; Q96EW5; Q9H9R4; Q9ULN8; Q9Y3W0;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Negative elongation factor B;
DE Short=NELF-B;
DE AltName: Full=Cofactor of BRCA1 {ECO:0000303|PubMed:11739404};
GN Name=NELFB; Synonyms=COBRA1 {ECO:0000303|PubMed:11739404}, KIAA1182;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP BRCA1.
RC TISSUE=Ovary;
RX PubMed=11739404; DOI=10.1083/jcb.200108049;
RA Ye Q., Hu Y.-F., Zhong H., Nye A.C., Belmont A.S., Li R.;
RT "BRCA1-induced large-scale chromatin unfolding and allele-specific effects
RT of cancer-predisposing mutations.";
RL J. Cell Biol. 155:911-921(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 99-580 (ISOFORMS 1/2).
RC TISSUE=Brain, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-580 (ISOFORMS 1/2).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 182-580 (ISOFORMS 1/2).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 371-580 (ISOFORMS 1/2).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [7]
RP PROTEIN SEQUENCE OF 173-186; 399-412 AND 548-560, IDENTIFICATION IN A NELF
RP COMPLEX, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12612062; DOI=10.1128/mcb.23.6.1863-1873.2003;
RA Narita T., Yamaguchi Y., Yano K., Sugimoto S., Chanarat S., Wada T.,
RA Kim D.-K., Hasegawa J., Omori M., Inukai N., Endoh M., Yamada T., Handa H.;
RT "Human transcription elongation factor NELF: identification of novel
RT subunits and reconstitution of the functionally active complex.";
RL Mol. Cell. Biol. 23:1863-1873(2003).
RN [8]
RP FUNCTION OF THE NELF COMPLEX.
RX PubMed=10199401; DOI=10.1016/s0092-8674(00)80713-8;
RA Yamaguchi Y., Takagi T., Wada T., Yano K., Furuya A., Sugimoto S.,
RA Hasegawa J., Handa H.;
RT "NELF, a multisubunit complex containing RD, cooperates with DSIF to
RT repress RNA polymerase II elongation.";
RL Cell 97:41-51(1999).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-519, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP INTERACTION WITH KIAA1191.
RX PubMed=21153684; DOI=10.1007/s11010-010-0690-4;
RA Mishra M., Inoue N., Heese K.;
RT "Characterizing the novel protein p33MONOX.";
RL Mol. Cell. Biochem. 350:127-134(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP FUNCTION OF THE NELF COMPLEX IN HIV-1 LATENCY (MICROBIAL INFECTION).
RX PubMed=23884411; DOI=10.1074/jbc.m113.496489;
RA Natarajan M., Schiralli Lester G.M., Lee C., Missra A., Wasserman G.A.,
RA Steffen M., Gilmour D.S., Henderson A.J.;
RT "Negative elongation factor (NELF) coordinates RNA polymerase II pausing,
RT premature termination, and chromatin remodeling to regulate HIV
RT transcription.";
RL J. Biol. Chem. 288:25995-26003(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP ALTERNATIVE INITIATION (ISOFORM 2), AND CTG START CODON (ISOFORM 2).
RX PubMed=26010750; DOI=10.1371/journal.pone.0127422;
RA Pan H., Zhao X., Zhang X., Abouelsoud M., Sun J., April C., Amleh A.,
RA Fan J.B., Hu Y., Li R.;
RT "Translational initiation at a non-AUG start codon for human and mouse
RT negative elongation factor-B.";
RL PLoS ONE 10:E0127422-E0127422(2015).
RN [21]
RP RECONSTITUTION OF THE NELF COMPLEX, AND RNA BINDING.
RX PubMed=27282391; DOI=10.7554/elife.14981;
RA Vos S.M., Pollmann D., Caizzi L., Hofmann K.B., Rombaut P., Zimniak T.,
RA Herzog F., Cramer P.;
RT "Architecture and RNA binding of the human negative elongation factor.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Essential component of the NELF complex, a complex that
CC negatively regulates the elongation of transcription by RNA polymerase
CC II (PubMed:12612062). 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 (PubMed:10199401). May be
CC able to induce chromatin unfolding (PubMed:11739404). Essential for
CC early embryogenesis; plays an important role in maintaining the
CC undifferentiated state of embryonic stem cells (ESCs) by preventing
CC unscheduled expression of developmental genes (By similarity). Plays a
CC key role in establishing the responsiveness of stem cells to
CC developmental cues; facilitates plasticity and cell fate commitment in
CC ESCs by establishing the appropriate expression level of signaling
CC molecules (By similarity). Supports the transcription of genes involved
CC in energy metabolism in cardiomyocytes; facilitates the association of
CC transcription initiation factors with the promoters of the metabolism-
CC related genes (By similarity). {ECO:0000250|UniProtKB:Q8C4Y3,
CC ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:11739404,
CC ECO:0000269|PubMed:12612062}.
CC -!- FUNCTION: (Microbial infection) The NELF complex is involved in HIV-1
CC latency possibly involving recruitment of PCF11 to paused RNA
CC polymerase II (PubMed:23884411). In vitro, binds weakly to the HIV-1
CC TAR RNA which is located in the long terminal repeat (LTR) of HIV-1
CC (PubMed:23884411). {ECO:0000269|PubMed:23884411}.
CC -!- SUBUNIT: The NELF complex is composed of NELFA, NELFB, NELFCD (isoform
CC NELF-C or isoform NELF-D) and NELFE; the N-terminus of NELFB binds to
CC the NELFA:NELFCD subcomplex (PubMed:12612062). Binds RNA which may help
CC to stabilize the NELF complex on nucleic acid (PubMed:27282391).
CC Interacts with the first BRCT repeat of BRCA1 (PubMed:11739404).
CC Interacts with KIAA1191 (PubMed:21153684). Interacts with NELFE (By
CC similarity). {ECO:0000250|UniProtKB:Q8C4Y3,
CC ECO:0000269|PubMed:11739404, ECO:0000269|PubMed:12612062,
CC ECO:0000269|PubMed:21153684, ECO:0000269|PubMed:27282391}.
CC -!- INTERACTION:
CC Q8WX92; P38398: BRCA1; NbExp=5; IntAct=EBI-347721, EBI-349905;
CC Q8WX92; O43583: DENR; NbExp=2; IntAct=EBI-347721, EBI-716083;
CC Q8WX92; P06241: FYN; NbExp=2; IntAct=EBI-347721, EBI-515315;
CC Q8WX92; P62993: GRB2; NbExp=2; IntAct=EBI-347721, EBI-401755;
CC Q8WX92; P38646: HSPA9; NbExp=2; IntAct=EBI-347721, EBI-354932;
CC Q8WX92; O75525: KHDRBS3; NbExp=2; IntAct=EBI-347721, EBI-722504;
CC Q8WX92; P10620: MGST1; NbExp=2; IntAct=EBI-347721, EBI-2691601;
CC Q8WX92; P16333: NCK1; NbExp=6; IntAct=EBI-347721, EBI-389883;
CC Q8WX92; P18615: NELFE; NbExp=7; IntAct=EBI-347721, EBI-348444;
CC Q8WX92; P27986: PIK3R1; NbExp=2; IntAct=EBI-347721, EBI-79464;
CC Q8WX92-2; Q8IXH7: NELFCD; NbExp=3; IntAct=EBI-22734860, EBI-536725;
CC Q8WX92-2; P18615: NELFE; NbExp=7; IntAct=EBI-22734860, EBI-348444;
CC Q8WX92-2; Q8N7U7-2: TPRX1; NbExp=3; IntAct=EBI-22734860, EBI-14115717;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11739404}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WX92-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WX92-2; Sequence=VSP_059998;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, lung,
CC placenta, liver, skeletal muscle, kidney and pancreas.
CC {ECO:0000269|PubMed:12612062}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at a CTG
CC start codon. {ECO:0000305|PubMed:26010750}.
CC -!- SIMILARITY: Belongs to the NELF-B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11892.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14157.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG52272.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB43381.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF464935; AAL69965.1; -; mRNA.
DR EMBL; AK022651; BAB14157.1; ALT_INIT; mRNA.
DR EMBL; AK091056; BAG52272.1; ALT_INIT; mRNA.
DR EMBL; BX255925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011892; AAH11892.1; ALT_INIT; mRNA.
DR EMBL; AL050280; CAB43381.3; ALT_INIT; mRNA.
DR EMBL; AB033008; BAA86496.1; -; mRNA.
DR CCDS; CCDS7040.2; -. [Q8WX92-2]
DR PIR; T08747; T08747.
DR RefSeq; NP_056271.3; NM_015456.4. [Q8WX92-2]
DR PDB; 6GML; EM; 3.20 A; V=42-580.
DR PDB; 7PKS; EM; 3.60 A; V=1-580.
DR PDBsum; 6GML; -.
DR PDBsum; 7PKS; -.
DR AlphaFoldDB; Q8WX92; -.
DR SMR; Q8WX92; -.
DR BioGRID; 117421; 89.
DR ComplexPortal; CPX-6267; NELF negative elongation factor complex.
DR CORUM; Q8WX92; -.
DR DIP; DIP-32670N; -.
DR IntAct; Q8WX92; 42.
DR MINT; Q8WX92; -.
DR STRING; 9606.ENSP00000339495; -.
DR iPTMnet; Q8WX92; -.
DR PhosphoSitePlus; Q8WX92; -.
DR SwissPalm; Q8WX92; -.
DR BioMuta; NELFB; -.
DR DMDM; 38372378; -.
DR EPD; Q8WX92; -.
DR jPOST; Q8WX92; -.
DR MassIVE; Q8WX92; -.
DR MaxQB; Q8WX92; -.
DR PaxDb; Q8WX92; -.
DR PeptideAtlas; Q8WX92; -.
DR PRIDE; Q8WX92; -.
DR ProteomicsDB; 74978; -.
DR DNASU; 25920; -.
DR Ensembl; ENST00000343053.6; ENSP00000339495.6; ENSG00000188986.9. [Q8WX92-2]
DR GeneID; 25920; -.
DR KEGG; hsa:25920; -.
DR MANE-Select; ENST00000343053.6; ENSP00000339495.6; NM_015456.5; NP_056271.3. [Q8WX92-2]
DR UCSC; uc004cmm.5; human. [Q8WX92-1]
DR CTD; 25920; -.
DR DisGeNET; 25920; -.
DR GeneCards; NELFB; -.
DR HGNC; HGNC:24324; NELFB.
DR MIM; 611180; gene.
DR neXtProt; NX_Q8WX92; -.
DR OpenTargets; ENSG00000188986; -.
DR PharmGKB; PA162382703; -.
DR eggNOG; ENOG502QTMJ; Eukaryota.
DR GeneTree; ENSGT00390000012665; -.
DR HOGENOM; CLU_037919_0_0_1; -.
DR InParanoid; Q8WX92; -.
DR OMA; HINEMGQ; -.
DR OrthoDB; 1095614at2759; -.
DR PhylomeDB; Q8WX92; -.
DR TreeFam; TF324620; -.
DR PathwayCommons; Q8WX92; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
DR Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-9603505; NTRK3 as a dependence receptor.
DR SignaLink; Q8WX92; -.
DR BioGRID-ORCS; 25920; 655 hits in 1086 CRISPR screens.
DR ChiTaRS; NELFB; human.
DR GeneWiki; Cofactor_of_BRCA1; -.
DR GenomeRNAi; 25920; -.
DR Pharos; Q8WX92; Tbio.
DR PRO; PR:Q8WX92; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8WX92; protein.
DR Bgee; ENSG00000188986; Expressed in apex of heart and 198 other tissues.
DR Genevisible; Q8WX92; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0032021; C:NELF complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR InterPro; IPR010405; COBRA1.
DR PANTHER; PTHR13503; PTHR13503; 1.
DR Pfam; PF06209; COBRA1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..580
FT /note="Negative elongation factor B"
FT /id="PRO_0000219129"
FT REGION 548..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 519
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1
FT /note="M -> MAELEGAGERGSGGPRGPAERASGVSAAAPGERAGDGAPSRAVAGAS
FT AM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_059998"
FT CONFLICT 156
FT /note="L -> F (in Ref. 2; BAB14157)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> A (in Ref. 5; CAB43381)"
FT /evidence="ECO:0000305"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 58..79
FT /evidence="ECO:0007829|PDB:6GML"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 86..102
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:6GML"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:6GML"
FT TURN 144..151
FT /evidence="ECO:0007829|PDB:6GML"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 156..175
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 212..229
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 234..242
FT /evidence="ECO:0007829|PDB:6GML"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 260..272
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 308..328
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:6GML"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 368..386
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 409..416
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 421..428
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 439..452
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 460..474
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 477..488
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 496..507
FT /evidence="ECO:0007829|PDB:6GML"
FT TURN 513..515
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 516..524
FT /evidence="ECO:0007829|PDB:6GML"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 533..546
FT /evidence="ECO:0007829|PDB:6GML"
SQ SEQUENCE 580 AA; 65697 MW; C0A4F7F2BEE52CBD CRC64;
MFAGLQDLGV ANGEDLKETL TNCTEPLKAI EQFQTENGVL LPSLQSALPF LDLHGTPRLE
FHQSVFDELR DKLLERVSAI ASEGKAEERY KKLEDLLEKS FSLVKMPSLQ PVVMCVMKHL
PKVPEKKLKL VMADKELYRA CAVEVKRQIW QDNQALFGDE VSPLLKQYIL EKESALFSTE
LSVLHNFFSP SPKTRRQGEV VQRLTRMVGK NVKLYDMVLQ FLRTLFLRTR NVHYCTLRAE
LLMSLHDLDV GEICTVDPCH KFTWCLDACI RERFVDSKRA RELQGFLDGV KKGQEQVLGD
LSMILCDPFA INTLALSTVR HLQELVGQET LPRDSPDLLL LLRLLALGQG AWDMIDSQVF
KEPKMEVELI TRFLPMLMSF LVDDYTFNVD QKLPAEEKAP VSYPNTLPES FTKFLQEQRM
ACEVGLYYVL HITKQRNKNA LLRLLPGLVE TFGDLAFGDI FLHLLTGNLA LLADEFALED
FCSSLFDGFF LTASPRKENV HRHALRLLIH LHPRVAPSKL EALQKALEPT GQSGEAVKEL
YSQLGEKLEQ LDHRKPSPAQ AAETPALELP LPSVPAPAPL
