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Protein

Negative elongation factor B

Gene

Nelfb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-113418. Formation of the Early Elongation Complex.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-MMU-75955. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Negative elongation factor B
Short name:
NELF-B
Alternative name(s):
Cofactor of BRCA1
Gene namesi
Name:Nelfb
Synonyms:Cobra1
ORF Names:MNCb-5210
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1931035. Nelfb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 580580Negative elongation factor BPRO_0000219130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei519 – 5191N6-acetyllysineBy similarity
Modified residuei557 – 5571PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8C4Y3.
MaxQBiQ8C4Y3.
PaxDbiQ8C4Y3.
PeptideAtlasiQ8C4Y3.
PRIDEiQ8C4Y3.

PTM databases

iPTMnetiQ8C4Y3.
PhosphoSiteiQ8C4Y3.

Expressioni

Gene expression databases

BgeeiQ8C4Y3.
CleanExiMM_COBRA1.
ExpressionAtlasiQ8C4Y3. baseline and differential.
GenevisibleiQ8C4Y3. MM.

Interactioni

Subunit structurei

The NELF complex is composed of NELFA, NELFB, NELFCD and NELFE. Interacts with the first BRCT repeat of BRCA1 (By similarity). Interacts with KIAA1191 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000057731.

Family & Domainsi

Sequence similaritiesi

Belongs to the NELF-B family.Curated

Phylogenomic databases

eggNOGiENOG410IEBF. Eukaryota.
ENOG410YK9P. LUCA.
GeneTreeiENSGT00390000012665.
HOGENOMiHOG000231489.
HOVERGENiHBG052596.
InParanoidiQ8C4Y3.
KOiK15180.
OMAiSRKENVH.
OrthoDBiEOG7Z69BV.
PhylomeDBiQ8C4Y3.
TreeFamiTF324620.

Family and domain databases

InterProiIPR010405. COBRA1.
[Graphical view]
PANTHERiPTHR13503. PTHR13503. 1 hit.
PfamiPF06209. COBRA1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8C4Y3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFAGLQDLGV ANGEDLKETL TNCTEPLKAI EQFQTENGVL LPSLQSALPF
60 70 80 90 100
LDLHGTPRLE FHQSVFDELR DKLLERVSAI ASEGKAEERY KKLEDLLEKS
110 120 130 140 150
FSLVKMPSLQ PVVMCVMKHL PKVPEKKLKL VMADKELYRA CAVEVKRQIW
160 170 180 190 200
QDNQALFGDE VSPLLKQYIL EKESALFSTE LSVLHNFFSP SPKTRRQGEV
210 220 230 240 250
VQKLTQMVGK NVKLYDMVLQ FLRTLFLRTR NVHYCTLRAE LLMSLHDLDV
260 270 280 290 300
SDICTVDPCH KFTWCLDACI RERFVDSKRA RELQGFLDGV KKGQEQVLGD
310 320 330 340 350
LSMILCDPFA INTLSLSTIR HLQELVSQET LPRDSPDLLL LLRLLALGQG
360 370 380 390 400
AWDLIDSQVF KEPKMEAELI TKFLPMLMSL VVDDFTFNVD QKLPAEEKAS
410 420 430 440 450
VTYPNTLPES FTKFLQEQRM ACEVGLYYVL HITKQRNKNA LLRLLPGLVE
460 470 480 490 500
TFGDLAFSDI FLHLLTGSLV LLADEFALED FCSSLFDGFF LTASPRKENV
510 520 530 540 550
HRHVLRLLLH LHARVAPSKL EALQKALEPT GQSGEAVKEL YSQLGEKLEQ
560 570 580
LDHRKPSPTQ AAETPALDLP LPSVPAPATL
Length:580
Mass (Da):65,636
Last modified:November 14, 2003 - v2
Checksum:i716FCC01C59D3F8A
GO

Sequence cautioni

The sequence AAH04762.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AK080419 differs from that shown. Reason: Frameshift at position 46. Curated
The sequence BAA95090.1 differs from that shown. Reason: Frameshift at position 35. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti470 – 4701V → A in BAA95090 (Ref. 1) Curated
Sequence conflicti547 – 5471K → R in BAA95090 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041607 mRNA. Translation: BAA95090.1. Frameshift.
BC004762 mRNA. Translation: AAH04762.1. Different initiation.
AK080419 mRNA. No translation available.
RefSeqiNP_001297086.1. NM_001310157.1.
UniGeneiMm.116418.

Genome annotation databases

EnsembliENSMUST00000205741; ENSMUSP00000145869; ENSMUSG00000013465.
GeneIDi58202.
KEGGimmu:58202.
UCSCiuc008iqm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041607 mRNA. Translation: BAA95090.1. Frameshift.
BC004762 mRNA. Translation: AAH04762.1. Different initiation.
AK080419 mRNA. No translation available.
RefSeqiNP_001297086.1. NM_001310157.1.
UniGeneiMm.116418.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000057731.

PTM databases

iPTMnetiQ8C4Y3.
PhosphoSiteiQ8C4Y3.

Proteomic databases

EPDiQ8C4Y3.
MaxQBiQ8C4Y3.
PaxDbiQ8C4Y3.
PeptideAtlasiQ8C4Y3.
PRIDEiQ8C4Y3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000205741; ENSMUSP00000145869; ENSMUSG00000013465.
GeneIDi58202.
KEGGimmu:58202.
UCSCiuc008iqm.2. mouse.

Organism-specific databases

CTDi25920.
MGIiMGI:1931035. Nelfb.

Phylogenomic databases

eggNOGiENOG410IEBF. Eukaryota.
ENOG410YK9P. LUCA.
GeneTreeiENSGT00390000012665.
HOGENOMiHOG000231489.
HOVERGENiHBG052596.
InParanoidiQ8C4Y3.
KOiK15180.
OMAiSRKENVH.
OrthoDBiEOG7Z69BV.
PhylomeDBiQ8C4Y3.
TreeFamiTF324620.

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-113418. Formation of the Early Elongation Complex.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-MMU-75955. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

PROiQ8C4Y3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C4Y3.
CleanExiMM_COBRA1.
ExpressionAtlasiQ8C4Y3. baseline and differential.
GenevisibleiQ8C4Y3. MM.

Family and domain databases

InterProiIPR010405. COBRA1.
[Graphical view]
PANTHERiPTHR13503. PTHR13503. 1 hit.
PfamiPF06209. COBRA1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
    Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-580.
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Spleen and Testis.

Entry informationi

Entry nameiNELFB_MOUSE
AccessioniPrimary (citable) accession number: Q8C4Y3
Secondary accession number(s): Q99J41, Q9JJA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: November 14, 2003
Last modified: July 6, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.