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Reviewed, UniProtKB/Swiss-Prot Q8WX92 (NELFB_HUMAN)

Last modified January 19, 2010. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Negative elongation factor B
      Short name=NELF-B
Alternative name(s):
    Cofactor of BRCA1
Gene names
Name: COBRA1
Synonyms: KIAA1182, NELFB
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length580 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Nucleus Ref.1.

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 processTranscription
Transcription regulation
   Cellular componentNucleus
   Molecular functionRepressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processnegative regulation of transcription

Inferred from electronic annotation. Source: InterPro

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from direct assay. Source: LIFEdb

nucleoplasm

Inferred from Experiment. Source: Reactome

   Molecular functionprotein binding Ref.1

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 580580Negative elongation factor B
PRO_0000219129

Amino acid modifications

Modified residue5191N6-acetyllysine Ref.15
Modified residue5571Phosphoserine Ref.9 Ref.10 Ref.11 Ref.13 Ref.14

Experimental info

Sequence conflict1561L → F in BAB14157. Ref.2
Sequence conflict1821S → A Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q8WX92-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: C0A4F7F2BEE52CBD

FASTA58065,697
        10         20         30         40         50         60 
MFAGLQDLGV ANGEDLKETL TNCTEPLKAI EQFQTENGVL LPSLQSALPF LDLHGTPRLE 

        70         80         90        100        110        120 
FHQSVFDELR DKLLERVSAI ASEGKAEERY KKLEDLLEKS FSLVKMPSLQ PVVMCVMKHL 

       130        140        150        160        170        180 
PKVPEKKLKL VMADKELYRA CAVEVKRQIW QDNQALFGDE VSPLLKQYIL EKESALFSTE 

       190        200        210        220        230        240 
LSVLHNFFSP SPKTRRQGEV VQRLTRMVGK NVKLYDMVLQ FLRTLFLRTR NVHYCTLRAE 

       250        260        270        280        290        300 
LLMSLHDLDV GEICTVDPCH KFTWCLDACI RERFVDSKRA RELQGFLDGV KKGQEQVLGD 

       310        320        330        340        350        360 
LSMILCDPFA INTLALSTVR HLQELVGQET LPRDSPDLLL LLRLLALGQG AWDMIDSQVF 

       370        380        390        400        410        420 
KEPKMEVELI TRFLPMLMSF LVDDYTFNVD QKLPAEEKAP VSYPNTLPES FTKFLQEQRM 

       430        440        450        460        470        480 
ACEVGLYYVL HITKQRNKNA LLRLLPGLVE TFGDLAFGDI FLHLLTGNLA LLADEFALED 

       490        500        510        520        530        540 
FCSSLFDGFF LTASPRKENV HRHALRLLIH LHPRVAPSKL EALQKALEPT GQSGEAVKEL 

       550        560        570        580 
YSQLGEKLEQ LDHRKPSPAQ AAETPALELP LPSVPAPAPL 

« Hide

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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., 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. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., 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. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., 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.
IPIIPI00103483.
PIRT08747.
RefSeqNP_056271.2.
UniGeneHs.655043

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ8WX92. 9 interactions.
STRINGQ8WX92.

PTM databases

PhosphoSiteQ8WX92.

Proteomic databases

PeptideAtlasQ8WX92.
PRIDEQ8WX92.

Genome annotation databases

EnsemblENST00000343053; ENSP00000339495; ENSG00000188986; Homo sapiens. [Genome view]
GeneID25920.
KEGGhsa:25920.
UCSCuc004cmm.2. human.

Organism-specific databases

CTD25920.
GeneCardsGC09P139269.
H-InvDBHIX0021915.
HGNCHGNC:24324. COBRA1.
HPAHPA020259.
MIM611180. gene.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG716510.
HOVERGENQ8WX92.
InParanoidQ8WX92.
OMATKQRNKN.
OrthoDBEOG94XN3D.
PhylomeDBQ8WX92.

Enzyme and pathway databases

ReactomeREACT_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

ArrayExpressQ8WX92.
BgeeQ8WX92.
CleanExHS_COBRA1.
GenevestigatorQ8WX92.
GermOnlineENSG00000188986. Homo sapiens.

Family and domain databases

InterProIPR010405. COBRA1.
[Graphical view]
PANTHERPTHR13503. COBRA1. 1 hit.
PTHR13503:SF2. COBRA1. 1 hit.
PfamPF06209. COBRA1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio47437.
SOURCESearch...

Entry information

Entry nameNELFB_HUMAN
AccessionPrimary (citable) accession number: Q8WX92
Secondary accession number(s): A2BFA3 expand/collapse secondary AC list , Q96EW5, Q9H9R4, Q9ULN8, Q9Y3W0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: March 1, 2002
Last modified: January 19, 2010
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents