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Protein

Negative elongation factor E

Gene

NELFE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.3 Publications

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-75955. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Negative elongation factor E
Short name:
NELF-E
Alternative name(s):
RNA-binding protein RD
Gene namesi
Name:NELFE
Synonyms:RD, RDBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:13974. NELFE.

Subcellular locationi

GO - Cellular componenti

  • NELF complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi295 – 2995RNCAF → EQMAT: Abolishes interaction with RNA but not the interaction with other proteins of the NELF complex. 1 Publication

Organism-specific databases

PharmGKBiPA134974984.

Polymorphism and mutation databases

BioMutaiNELFE.
DMDMi1350554.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380Negative elongation factor EPRO_0000081802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511PhosphoserineCombined sources
Cross-linki78 – 78Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei115 – 1151PhosphoserineCombined sources
Modified residuei131 – 1311PhosphoserineCombined sources
Modified residuei139 – 1391PhosphoserineCombined sources
Modified residuei165 – 1651PhosphoserineCombined sources
Modified residuei179 – 1791PhosphoserineCombined sources
Modified residuei181 – 1811PhosphoserineCombined sources
Modified residuei185 – 1851PhosphoserineCombined sources
Modified residuei249 – 2491PhosphoserineCombined sources
Modified residuei251 – 2511PhosphoserineCombined sources
Modified residuei272 – 2721PhosphothreonineCombined sources
Modified residuei274 – 2741PhosphothreonineCombined sources
Modified residuei281 – 2811PhosphoserineCombined sources
Modified residuei353 – 3531PhosphoserineCombined sources

Post-translational modificationi

Sumoylated.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP18615.
MaxQBiP18615.
PaxDbiP18615.
PeptideAtlasiP18615.
PRIDEiP18615.

PTM databases

iPTMnetiP18615.
PhosphoSiteiP18615.

Expressioni

Tissue specificityi

Widely expressed. Expressed in heart, brain, lung, placenta, liver, skeletal muscle, kidney and pancreas.1 Publication

Gene expression databases

BgeeiP18615.
CleanExiHS_RDBP.
ExpressionAtlasiP18615. baseline and differential.
GenevisibleiP18615. HS.

Organism-specific databases

HPAiHPA007187.
HPA046502.

Interactioni

Subunit structurei

The NELF complex is composed of NELFA, NELFB, NELFCD (isoform NELF-C or isoform NELF-D) and NELFE.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC57Q2TAC23EBI-348444,EBI-2808286
MTUS2Q5JR593EBI-348444,EBI-742948
NELFBQ8WX924EBI-348444,EBI-347721
TRIM27P143733EBI-348444,EBI-719493

Protein-protein interaction databases

BioGridi113662. 36 interactions.
DIPiDIP-32669N.
IntActiP18615. 18 interactions.
MINTiMINT-1033320.
STRINGi9606.ENSP00000364578.

Structurei

Secondary structure

1
380
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi262 – 2676Combined sources
Helixi273 – 2808Combined sources
Turni281 – 2833Combined sources
Beta strandi286 – 2927Combined sources
Turni293 – 2964Combined sources
Beta strandi297 – 3048Combined sources
Helixi305 – 31410Combined sources
Turni315 – 3173Combined sources
Beta strandi318 – 3203Combined sources
Beta strandi323 – 3286Combined sources
Turni334 – 3374Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X5PNMR-A254-337[»]
2BZ2NMR-A244-343[»]
2JX2NMR-A244-343[»]
ProteinModelPortaliP18615.
SMRiP18615. Positions 257-343.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18615.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati184 – 18521
Repeati186 – 18722
Repeati188 – 18923
Repeati190 – 19124
Repeati192 – 19325; approximate
Repeati194 – 19526
Repeati196 – 19727
Repeati198 – 19928
Repeati200 – 20129
Repeati202 – 203210
Repeati204 – 205211
Repeati206 – 207212
Repeati208 – 209213
Repeati210 – 211214
Repeati212 – 213215
Repeati214 – 215216
Repeati216 – 217217
Repeati218 – 219218
Repeati220 – 221219
Repeati222 – 223220
Repeati224 – 225221
Repeati226 – 227222
Repeati228 – 229223
Repeati230 – 231224
Repeati232 – 233225
Repeati234 – 235226
Repeati236 – 237227
Repeati238 – 239228
Repeati240 – 241229
Repeati242 – 243230
Domaini262 – 33271RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 2436030 X 2 AA approximate tandem repeats of R-[DSNE]Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili7 – 3630Sequence analysisAdd
BLAST

Domaini

The RRM domain interacts with RNA, and is essential for NELF complex function. It is however not required for the NELF complex formation.1 Publication

Sequence similaritiesi

Belongs to the RRM NELF-E family.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410IK4K. Eukaryota.
ENOG41101UX. LUCA.
GeneTreeiENSGT00630000089917.
HOGENOMiHOG000232089.
HOVERGENiHBG052598.
InParanoidiP18615.
KOiK15182.
OMAiVYIHFPS.
PhylomeDBiP18615.
TreeFamiTF324087.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR033102. NELFE.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR17250:SF0. PTHR17250:SF0. 1 hit.
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P18615-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLVIPPGLSE EEEALQKKFN KLKKKKKALL ALKKQSSSST TSQGGVKRSL
60 70 80 90 100
SEQPVMDTAT ATEQAKQLVK SGAISAIKAE TKNSGFKRSR TLEGKLKDPE
110 120 130 140 150
KGPVPTFQPF QRSISADDDL QESSRRPQRK SLYESFVSSS DRLRELGPDG
160 170 180 190 200
EEAEGPGAGD GPPRSFDWGY EERSGAHSSA SPPRSRSRDR SHERNRDRDR
210 220 230 240 250
DRERDRDRDR DRDRERDRDR DRDRDRDRER DRDRERDRDR DREGPFRRSD
260 270 280 290 300
SFPERRAPRK GNTLYVYGED MTPTLLRGAF SPFGNIIDLS MDPPRNCAFV
310 320 330 340 350
TYEKMESADQ AVAELNGTQV ESVQLKVNIA RKQPMLDAAT GKSVWGSLAV
360 370 380
QNSPKGCHRD KRTQIVYSDD VYKENLVDGF
Length:380
Mass (Da):43,240
Last modified:February 1, 1996 - v3
Checksum:i95EB422B5E07410B
GO
Isoform 2 (identifier: P18615-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVPKGATM

Note: No experimental confirmation available.
Show »
Length:387
Mass (Da):43,925
Checksum:iCF6DCF317D74A6ED
GO
Isoform 3 (identifier: P18615-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     135-164: Missing.

Note: No experimental confirmation available.
Show »
Length:350
Mass (Da):40,216
Checksum:iD3066C12B041493F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191D → DD in AAA36308 (PubMed:2612324).Curated
Sequence conflicti174 – 1741S → M in CAA34231 (PubMed:2119325).Curated
Sequence conflicti265 – 2651Y → YD in AAA36308 (PubMed:2612324).Curated
Sequence conflicti312 – 3121V → A in AAA36308 (PubMed:2612324).Curated
Sequence conflicti327 – 3271V → D in AAA36308 (PubMed:2612324).Curated
Sequence conflicti347 – 3471S → A in AAA36308 (PubMed:2612324).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MVPKGATM in isoform 2. 1 PublicationVSP_056151
Alternative sequencei135 – 16430Missing in isoform 3. 1 PublicationVSP_056152Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33231
, M32274, M32275, M32276, M33230 Genomic DNA. Translation: AAA36308.1.
L03411 mRNA. Translation: AAC37523.1.
AF019413 Genomic DNA. Translation: AAB67979.1.
AK300717 mRNA. Translation: BAG62393.1.
AK302652 mRNA. Translation: BAG63891.1.
AL049547 Genomic DNA. Translation: CAB89308.1.
AL662849 Genomic DNA. Translation: CAI17457.1.
AL844853 Genomic DNA. Translation: CAI41861.1.
BX005143 Genomic DNA. Translation: CAM25865.1.
CR759782 Genomic DNA. Translation: CAQ07114.1.
CR388219, CR753845 Genomic DNA. Translation: CAQ07466.1.
AL645922 Genomic DNA. Translation: CAQ09275.1.
CR753845, CR388219 Genomic DNA. Translation: CAQ10906.1.
CH471081 Genomic DNA. Translation: EAX03553.1.
BC025235 mRNA. Translation: AAH25235.1.
BC050617 mRNA. Translation: AAH50617.1.
X16105 mRNA. Translation: CAA34231.1.
CCDSiCCDS4730.1. [P18615-1]
PIRiS36789.
RefSeqiNP_002895.3. NM_002904.5. [P18615-1]
UniGeneiHs.423935.

Genome annotation databases

EnsembliENST00000375425; ENSP00000364574; ENSG00000204356. [P18615-3]
ENST00000375429; ENSP00000364578; ENSG00000204356. [P18615-1]
ENST00000383174; ENSP00000372660; ENSG00000206268. [P18615-1]
ENST00000383343; ENSP00000372834; ENSG00000206357. [P18615-1]
ENST00000429857; ENSP00000403623; ENSG00000231044. [P18615-1]
ENST00000444811; ENSP00000388400; ENSG00000204356. [P18615-4]
ENST00000448628; ENSP00000394879; ENSG00000229363. [P18615-1]
ENST00000457397; ENSP00000393005; ENSG00000233801. [P18615-1]
GeneIDi7936.
KEGGihsa:7936.
UCSCiuc003nyk.4. human. [P18615-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33231
, M32274, M32275, M32276, M33230 Genomic DNA. Translation: AAA36308.1.
L03411 mRNA. Translation: AAC37523.1.
AF019413 Genomic DNA. Translation: AAB67979.1.
AK300717 mRNA. Translation: BAG62393.1.
AK302652 mRNA. Translation: BAG63891.1.
AL049547 Genomic DNA. Translation: CAB89308.1.
AL662849 Genomic DNA. Translation: CAI17457.1.
AL844853 Genomic DNA. Translation: CAI41861.1.
BX005143 Genomic DNA. Translation: CAM25865.1.
CR759782 Genomic DNA. Translation: CAQ07114.1.
CR388219, CR753845 Genomic DNA. Translation: CAQ07466.1.
AL645922 Genomic DNA. Translation: CAQ09275.1.
CR753845, CR388219 Genomic DNA. Translation: CAQ10906.1.
CH471081 Genomic DNA. Translation: EAX03553.1.
BC025235 mRNA. Translation: AAH25235.1.
BC050617 mRNA. Translation: AAH50617.1.
X16105 mRNA. Translation: CAA34231.1.
CCDSiCCDS4730.1. [P18615-1]
PIRiS36789.
RefSeqiNP_002895.3. NM_002904.5. [P18615-1]
UniGeneiHs.423935.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X5PNMR-A254-337[»]
2BZ2NMR-A244-343[»]
2JX2NMR-A244-343[»]
ProteinModelPortaliP18615.
SMRiP18615. Positions 257-343.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113662. 36 interactions.
DIPiDIP-32669N.
IntActiP18615. 18 interactions.
MINTiMINT-1033320.
STRINGi9606.ENSP00000364578.

PTM databases

iPTMnetiP18615.
PhosphoSiteiP18615.

Polymorphism and mutation databases

BioMutaiNELFE.
DMDMi1350554.

Proteomic databases

EPDiP18615.
MaxQBiP18615.
PaxDbiP18615.
PeptideAtlasiP18615.
PRIDEiP18615.

Protocols and materials databases

DNASUi7936.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375425; ENSP00000364574; ENSG00000204356. [P18615-3]
ENST00000375429; ENSP00000364578; ENSG00000204356. [P18615-1]
ENST00000383174; ENSP00000372660; ENSG00000206268. [P18615-1]
ENST00000383343; ENSP00000372834; ENSG00000206357. [P18615-1]
ENST00000429857; ENSP00000403623; ENSG00000231044. [P18615-1]
ENST00000444811; ENSP00000388400; ENSG00000204356. [P18615-4]
ENST00000448628; ENSP00000394879; ENSG00000229363. [P18615-1]
ENST00000457397; ENSP00000393005; ENSG00000233801. [P18615-1]
GeneIDi7936.
KEGGihsa:7936.
UCSCiuc003nyk.4. human. [P18615-1]

Organism-specific databases

CTDi7936.
GeneCardsiNELFE.
HGNCiHGNC:13974. NELFE.
HPAiHPA007187.
HPA046502.
MIMi154040. gene.
neXtProtiNX_P18615.
PharmGKBiPA134974984.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IK4K. Eukaryota.
ENOG41101UX. LUCA.
GeneTreeiENSGT00630000089917.
HOGENOMiHOG000232089.
HOVERGENiHBG052598.
InParanoidiP18615.
KOiK15182.
OMAiVYIHFPS.
PhylomeDBiP18615.
TreeFamiTF324087.

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-75955. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

EvolutionaryTraceiP18615.
GeneWikiiRDBP.
GenomeRNAii7936.
PROiP18615.
SOURCEiSearch...

Gene expression databases

BgeeiP18615.
CleanExiHS_RDBP.
ExpressionAtlasiP18615. baseline and differential.
GenevisibleiP18615. HS.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR033102. NELFE.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR17250:SF0. PTHR17250:SF0. 1 hit.
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the human RD gene: a highly conserved gene in the class III region of the major histocompatibility complex."
    Speiser P.W., White P.C.
    DNA 8:745-751(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "cDNA cloning and characterization of the protein encoded by RD, a gene located in the class III region of the human major histocompatibility complex."
    Cheng J., Macon K.J., Volanakis J.E.
    Biochem. J. 294:589-593(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: T-cell.
  3. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
    Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
    Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Testis.
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Retinal pigment epithelium and Skin.
  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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 48-65 AND 362-373, IDENTIFICATION IN THE NELF COMPLEX, FUNCTION OF THE NELF COMPLEX.
  9. "The human RD protein is closely related to nuclear RNA-binding proteins and has been highly conserved."
    Surowy C.S., Hoganson G., Gosink J., Strunk K., Spritz R.A.
    Gene 90:299-302(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 56-380 (ISOFORM 1).
    Tissue: Liver.
  10. "Evidence that negative elongation factor represses transcription elongation through binding to a DRB sensitivity-inducing factor/RNA polymerase II complex and RNA."
    Yamaguchi Y., Inukai N., Narita T., Wada T., Handa H.
    Mol. Cell. Biol. 22:2918-2927(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, DOMAIN, MUTAGENESIS OF 295-ARG--PHE-299.
  11. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  12. "Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
    Gocke C.B., Yu H., Kang J.
    J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION.
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-131; SER-251; THR-272; THR-274; SER-281 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-131; SER-281 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-181; SER-185 AND SER-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-115; SER-131; SER-139; SER-165; SER-249; SER-251 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  25. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  26. "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli."
    Impens F., Radoshevich L., Cossart P., Ribet D.
    Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Structural studies on the RNA-recognition motif of NELF E, a cellular negative transcription elongation factor involved in the regulation of HIV transcription."
    Rao J.N., Neumann L., Wenzel S., Schweimer K., Rosch P., Wohrl B.M.
    Biochem. J. 400:449-456(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 244-343.
  28. "Solution structure of RRM domain in PARP14."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 254-337.

Entry informationi

Entry nameiNELFE_HUMAN
AccessioniPrimary (citable) accession number: P18615
Secondary accession number(s): A2BE08
, B4DUN1, B4DYX9, Q5JP74, Q5JP75, Q96F56, Q9NPK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 1, 1996
Last modified: July 6, 2016
This is version 188 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.