Reviewed,
UniProtKB/Swiss-Prot Q8WX92 (NELFB_HUMAN)
Last modified
January 19, 2010.
Version 78.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Negative elongation factor B Short name=NELF-B Alternative name(s): Cofactor of BRCA1 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 580 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. May be able to induce chromatin unfolding. Ref.7 Ref.8 |
| Subunit structure | The NELF complex is composed of 4 subunits: WHSC2/NELF-A, COBRA1/NELF-B, TH1L (isoform NELF-C or isoform NELF-D) and RDBP/NELF-E. Interacts with the first BRCT repeat of BRCA1. Ref.1 |
| Subcellular location | |
| Tissue specificity | Widely expressed. Expressed in heart, brain, lung, placenta, liver, skeletal muscle, kidney and pancreas. Ref.7 |
| Sequence similarities | Belongs to the NELF-B family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Nucleus |
| Molecular function | Repressor |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | negative regulation of transcription Inferred from electronic annotation. Source: InterPro transcriptionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from direct assay. Source: LIFEdb nucleoplasmInferred from Experiment. Source: Reactome |
| Molecular function | protein binding Ref.1 Inferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ABL1 | P00519 | 1 | EBI-347721,EBI-375543 | |
| BRCA1 | P38398 | 3 | EBI-347721,EBI-349905 | |
| FYN | P06241 | 1 | EBI-347721,EBI-515315 | |
| GRB2 | P62993 | 1 | EBI-347721,EBI-401755 | |
| NCK1 | P16333 | 1 | EBI-347721,EBI-389883 | |
| PIK3R1 | P27986 | 1 | EBI-347721,EBI-79464 | |
| PLCG1 | P19174 | 1 | EBI-347721,EBI-79387 | |
| RDBP | P18615 | 1 | EBI-347721,EBI-348444 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 580 | 580 | Negative elongation factor B | PRO_0000219129 | |||||
Amino acid modifications | |||||||||
| Modified residue | 519 | 1 | N6-acetyllysine Ref.15 | ||||||
| Modified residue | 557 | 1 | Phosphoserine Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 | ||||||
Experimental info | |||||||||
| Sequence conflict | 156 | 1 | L → F in BAB14157. Ref.2 | ||||||
| Sequence conflict | 182 | 1 | S → A Ref.5 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "BRCA1-induced large-scale chromatin unfolding and allele-specific effects of cancer-predisposing mutations." Ye Q., Hu Y.-F., Zhong H., Nye A.C., Belmont A.S., Li R. J. Cell Biol. 155:911-921(2001) [PubMed: 11739404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH BRCA1. Tissue: Ovary. |
| [2] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [3] | "DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. Dunham I.Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-580. Tissue: Lung. |
| [5] | "Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. Poustka A.Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 182-580. Tissue: Uterus. |
| [6] | "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain." Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O. DNA Res. 6:329-336(1999) [PubMed: 10574461] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 371-580. Tissue: Brain. |
| [7] | "Human transcription elongation factor NELF: identification of novel subunits and reconstitution of the functionally active complex." Narita T., Yamaguchi Y., Yano K., Sugimoto S., Chanarat S., Wada T., Kim D.-K., Hasegawa J., Omori M., Inukai N., Endoh M., Yamada T., Handa H. Mol. Cell. Biol. 23:1863-1873(2003) [PubMed: 12612062] [Abstract] Cited for: PROTEIN SEQUENCE OF 173-186; 399-412 AND 548-560, IDENTIFICATION IN A NELF COMPLEX, FUNCTION, TISSUE SPECIFICITY. |
| [8] | "NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation." Yamaguchi Y., Takagi T., Wada T., Yano K., Furuya A., Sugimoto S., Hasegawa J., Handa H. Cell 97:41-51(1999) [PubMed: 10199401] [Abstract] Cited for: FUNCTION OF THE NELF COMPLEX. |
| [9] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, MASS SPECTROMETRY. Tissue: Epithelium. |
| [10] | "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, MASS SPECTROMETRY. Tissue: Epithelium. |
| [11] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, MASS SPECTROMETRY. |
| [12] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [13] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, MASS SPECTROMETRY. |
| [14] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, MASS SPECTROMETRY. Tissue: T-cell. |
| [15] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-519, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF464935 mRNA. Translation: AAL69965.1. AK022651 mRNA. Translation: BAB14157.1. Different initiation. AK091056 mRNA. Translation: BAG52272.1. BX255925 Genomic DNA. Translation: CAM24149.1. BC011892 mRNA. Translation: AAH11892.1. Different initiation. AL050280 mRNA. Translation: CAB43381.3. Different initiation. AB033008 mRNA. Translation: BAA86496.1. |
| IPI | IPI00103483. |
| PIR | T08747. |
| RefSeq | NP_056271.2. |
| UniGene | Hs.655043 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q8WX92. 9 interactions. |
| STRING | Q8WX92. |
PTM databases | |
| PhosphoSite | Q8WX92. |
Proteomic databases | |
| PeptideAtlas | Q8WX92. |
| PRIDE | Q8WX92. |
Genome annotation databases | |
| Ensembl | ENST00000343053; ENSP00000339495; ENSG00000188986; Homo sapiens. [Genome view] |
| GeneID | 25920. |
| KEGG | hsa:25920. |
| UCSC | uc004cmm.2. human. |
Organism-specific databases | |
| CTD | 25920. |
| GeneCards | GC09P139269. |
| H-InvDB | HIX0021915. |
| HGNC | HGNC:24324. COBRA1. |
| HPA | HPA020259. |
| MIM | 611180. gene. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | HBG716510. |
| HOVERGEN | Q8WX92. |
| InParanoid | Q8WX92. |
| OMA | TKQRNKN. |
| OrthoDB | EOG94XN3D. |
| PhylomeDB | Q8WX92. |
Enzyme and pathway databases | |
| Reactome | REACT_1788. Transcription. REACT_1892. Elongation arrest and recovery. REACT_6143. Pausing and recovery of Tat-mediated HIV-1 elongation. REACT_6185. HIV Infection. REACT_6244. Pausing and recovery of HIV-1 elongation. REACT_6259. HIV-1 elongation arrest and recovery. REACT_6344. Tat-mediated HIV-1 elongation arrest and recovery. REACT_71. Gene Expression. REACT_769. Pausing and recovery of elongation. |
Gene expression databases | |
| ArrayExpress | Q8WX92. |
| Bgee | Q8WX92. |
| CleanEx | HS_COBRA1. |
| Genevestigator | Q8WX92. |
| GermOnline | ENSG00000188986. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR010405. COBRA1. [Graphical view] |
| PANTHER | PTHR13503. COBRA1. 1 hit. PTHR13503:SF2. COBRA1. 1 hit. |
| Pfam | PF06209. COBRA1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 47437. |
| SOURCE | Search... |
Entry information
| Entry name | NELFB_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q8WX92 Secondary accession number(s): A2BFA3 Q9Y3W0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 9 Human chromosome 9: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


