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Q15369

- ELOC_HUMAN

UniProt

Q15369 - ELOC_HUMAN

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Protein

Transcription elongation factor B polypeptide 1

Gene

TCEB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).1 Publication
The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes.1 Publication

GO - Biological processi

  1. cellular response to hypoxia Source: Reactome
  2. gene expression Source: Reactome
  3. positive regulation of viral transcription Source: Reactome
  4. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  5. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  6. transcription elongation from RNA polymerase II promoter Source: Reactome
  7. transcription from RNA polymerase II promoter Source: Reactome
  8. ubiquitin-dependent protein catabolic process Source: InterPro
  9. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6259. HIV elongation arrest and recovery.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor B polypeptide 1
Alternative name(s):
Elongin 15 kDa subunit
Elongin-C
Short name:
EloC
RNA polymerase II transcription factor SIII subunit C
SIII p15
Gene namesi
Name:TCEB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:11617. TCEB1.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36376.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 112112Transcription elongation factor B polypeptide 1PRO_0000187258Add
BLAST

Proteomic databases

MaxQBiQ15369.
PaxDbiQ15369.
PRIDEiQ15369.

PTM databases

PhosphoSiteiQ15369.

Expressioni

Tissue specificityi

Overexpressed in prostate cancer cell line PC-3 and breast cancer cell line SK-BR-3.1 Publication

Gene expression databases

BgeeiQ15369.
CleanExiHS_TCEB1.
ExpressionAtlasiQ15369. baseline and differential.
GenevestigatoriQ15369.

Interactioni

Subunit structurei

Heterotrimer of an A (A1, A2 or A3), B and C subunit. Part of E3 ubiquitin ligase complexes with CUL5 or CUL2, RBX1 and a substrate adapter protein that can be either SOCS1, SOCS5, TCEB3, VHL or WSB1. The elongin BC complex is part of a complex with hydroxylated HIF1A. Substrate adapter protein can be a viral protein such as HIV Vif. Interacts with VHL. Interacts with TMF1. Interacts with human respiratory syncytial virus (HRSV) protein NS1. Interacts with SPSB1. posed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Interacts with SPSB1. Interacts with KLHDC10; which may be an E3 ubiquitin ligase complex substrate recognition component.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CUL2Q136175EBI-301231,EBI-456179
GAMMAHV.ORF73O419742EBI-301231,EBI-6933128From a different organism.
MED8Q96G253EBI-301231,EBI-394405
SOCS1O155242EBI-301231,EBI-968198
SOCS2O145082EBI-301231,EBI-617737
SPSB2Q996193EBI-301231,EBI-2323209
SPSB4Q96A442EBI-301231,EBI-2323233
TCEB2Q153708EBI-301231,EBI-301238
vifP125045EBI-301231,EBI-779991From a different organism.

Protein-protein interaction databases

BioGridi112783. 117 interactions.
DIPiDIP-29571N.
IntActiQ15369. 52 interactions.
MINTiMINT-1323870.
STRINGi9606.ENSP00000284811.

Structurei

Secondary structure

1
112
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 225Combined sources
Beta strandi24 – 263Combined sources
Beta strandi28 – 325Combined sources
Helixi33 – 364Combined sources
Helixi40 – 467Combined sources
Beta strandi47 – 504Combined sources
Helixi54 – 585Combined sources
Beta strandi59 – 613Combined sources
Helixi67 – 8317Combined sources
Turni84 – 863Combined sources
Helixi97 – 993Combined sources
Helixi100 – 11011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LM8X-ray1.85C17-112[»]
1LQBX-ray2.00B17-112[»]
1VCBX-ray2.70B/E/H/K1-112[»]
2C9WX-ray1.90C17-112[»]
2IZVX-ray2.55C17-112[»]
2MA9NMR-C19-109[»]
3DCGX-ray2.40B/D17-112[»]
3ZKJX-ray2.58B/E17-112[»]
3ZNGX-ray2.85B/E17-112[»]
3ZRCX-ray2.90B/E/H/K17-112[»]
3ZRFX-ray2.80B/E/H/K17-112[»]
3ZTCX-ray2.65B/E/H/K17-112[»]
3ZTDX-ray2.79B/E/H/K17-112[»]
3ZUNX-ray2.50B/E/H/K17-112[»]
4AJYX-ray1.73C17-112[»]
4AWJX-ray2.50B/E/H/K17-112[»]
4B95X-ray2.80B/E/H/K18-112[»]
4B9KX-ray2.00B/E/H/K17-112[»]
4BKSX-ray2.20B/E/H/K17-112[»]
4BKTX-ray2.35B/E/H/K17-112[»]
4N9FX-ray3.305/B/E/K/Q/T/Y/Z/h/n/t/z17-112[»]
4W9CX-ray2.20B/E/H/K17-112[»]
4W9DX-ray2.20B/E/H/K17-112[»]
4W9EX-ray2.60B/E/H/K17-112[»]
4W9FX-ray2.10B/E/H/K17-112[»]
4W9GX-ray2.70B/E/H/K17-112[»]
4W9HX-ray2.10B/E/H/K17-112[»]
4W9IX-ray2.40B/E/H/K17-112[»]
4W9JX-ray2.20B/E/H/K17-112[»]
4W9KX-ray2.10B/E/H/K17-112[»]
4W9LX-ray2.20B/E/H/K17-112[»]
ProteinModelPortaliQ15369.
SMRiQ15369. Positions 17-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15369.

Family & Domainsi

Sequence similaritiesi

Belongs to the SKP1 family.Curated

Phylogenomic databases

eggNOGiNOG298860.
GeneTreeiENSGT00390000011717.
HOGENOMiHOG000216525.
HOVERGENiHBG007440.
InParanoidiQ15369.
KOiK03872.
OMAiYFHYWYR.
OrthoDBiEOG77M8QN.
PhylomeDBiQ15369.
TreeFamiTF300233.

Family and domain databases

Gene3Di3.30.710.10. 1 hit.
InterProiIPR011333. BTB/POZ_fold.
IPR001232. Skp1_comp.
IPR016073. Skp1_comp_POZ.
[Graphical view]
PfamiPF03931. Skp1_POZ. 1 hit.
[Graphical view]
SMARTiSM00512. Skp1. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15369-1) [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
MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG
60 70 80 90 100
QFAENETNEV NFREIPSHVL SKVCMYFTYK VRYTNSSTEI PEFPIAPEIA
110
LELLMAANFL DC
Length:112
Mass (Da):12,473
Last modified:November 1, 1996 - v1
Checksum:i98D88696E883538B
GO
Isoform 2 (identifier: Q15369-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.

Note: No experimental confirmation available.

Show »
Length:96
Mass (Da):10,832
Checksum:i749EC1F8EC3DB62E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1616Missing in isoform 2. 1 PublicationVSP_045955Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34587 mRNA. Translation: AAA67650.1.
BX649138 mRNA. No translation available.
AC022868 Genomic DNA. No translation available.
BC013809 mRNA. Translation: AAH13809.1.
BC093065 mRNA. Translation: AAH93065.1.
BC100028 mRNA. Translation: AAI00029.1.
BC100283 mRNA. Translation: AAI00284.1.
CCDSiCCDS34910.1. [Q15369-1]
CCDS56539.1. [Q15369-2]
RefSeqiNP_001191786.1. NM_001204857.1. [Q15369-1]
NP_001191787.1. NM_001204858.1. [Q15369-1]
NP_001191788.1. NM_001204859.1. [Q15369-1]
NP_001191789.1. NM_001204860.1. [Q15369-1]
NP_001191790.1. NM_001204861.1. [Q15369-1]
NP_001191791.1. NM_001204862.1. [Q15369-1]
NP_001191792.1. NM_001204863.1. [Q15369-2]
NP_001191793.1. NM_001204864.1. [Q15369-2]
NP_005639.1. NM_005648.3. [Q15369-1]
XP_005251347.1. XM_005251290.2. [Q15369-1]
UniGeneiHs.533437.
Hs.554594.
Hs.731928.

Genome annotation databases

EnsembliENST00000284811; ENSP00000284811; ENSG00000154582. [Q15369-1]
ENST00000518127; ENSP00000428334; ENSG00000154582. [Q15369-1]
ENST00000519487; ENSP00000429596; ENSG00000154582. [Q15369-1]
ENST00000520210; ENSP00000430224; ENSG00000154582. [Q15369-2]
ENST00000520242; ENSP00000428171; ENSG00000154582. [Q15369-1]
ENST00000522337; ENSP00000429906; ENSG00000154582. [Q15369-1]
ENST00000523815; ENSP00000428074; ENSG00000154582. [Q15369-1]
ENST00000622804; ENSP00000478121; ENSG00000154582. [Q15369-1]
GeneIDi6921.
KEGGihsa:6921.
UCSCiuc003xzx.2. human. [Q15369-1]

Polymorphism databases

DMDMi32699511.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34587 mRNA. Translation: AAA67650.1 .
BX649138 mRNA. No translation available.
AC022868 Genomic DNA. No translation available.
BC013809 mRNA. Translation: AAH13809.1 .
BC093065 mRNA. Translation: AAH93065.1 .
BC100028 mRNA. Translation: AAI00029.1 .
BC100283 mRNA. Translation: AAI00284.1 .
CCDSi CCDS34910.1. [Q15369-1 ]
CCDS56539.1. [Q15369-2 ]
RefSeqi NP_001191786.1. NM_001204857.1. [Q15369-1 ]
NP_001191787.1. NM_001204858.1. [Q15369-1 ]
NP_001191788.1. NM_001204859.1. [Q15369-1 ]
NP_001191789.1. NM_001204860.1. [Q15369-1 ]
NP_001191790.1. NM_001204861.1. [Q15369-1 ]
NP_001191791.1. NM_001204862.1. [Q15369-1 ]
NP_001191792.1. NM_001204863.1. [Q15369-2 ]
NP_001191793.1. NM_001204864.1. [Q15369-2 ]
NP_005639.1. NM_005648.3. [Q15369-1 ]
XP_005251347.1. XM_005251290.2. [Q15369-1 ]
UniGenei Hs.533437.
Hs.554594.
Hs.731928.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LM8 X-ray 1.85 C 17-112 [» ]
1LQB X-ray 2.00 B 17-112 [» ]
1VCB X-ray 2.70 B/E/H/K 1-112 [» ]
2C9W X-ray 1.90 C 17-112 [» ]
2IZV X-ray 2.55 C 17-112 [» ]
2MA9 NMR - C 19-109 [» ]
3DCG X-ray 2.40 B/D 17-112 [» ]
3ZKJ X-ray 2.58 B/E 17-112 [» ]
3ZNG X-ray 2.85 B/E 17-112 [» ]
3ZRC X-ray 2.90 B/E/H/K 17-112 [» ]
3ZRF X-ray 2.80 B/E/H/K 17-112 [» ]
3ZTC X-ray 2.65 B/E/H/K 17-112 [» ]
3ZTD X-ray 2.79 B/E/H/K 17-112 [» ]
3ZUN X-ray 2.50 B/E/H/K 17-112 [» ]
4AJY X-ray 1.73 C 17-112 [» ]
4AWJ X-ray 2.50 B/E/H/K 17-112 [» ]
4B95 X-ray 2.80 B/E/H/K 18-112 [» ]
4B9K X-ray 2.00 B/E/H/K 17-112 [» ]
4BKS X-ray 2.20 B/E/H/K 17-112 [» ]
4BKT X-ray 2.35 B/E/H/K 17-112 [» ]
4N9F X-ray 3.30 5/B/E/K/Q/T/Y/Z/h/n/t/z 17-112 [» ]
4W9C X-ray 2.20 B/E/H/K 17-112 [» ]
4W9D X-ray 2.20 B/E/H/K 17-112 [» ]
4W9E X-ray 2.60 B/E/H/K 17-112 [» ]
4W9F X-ray 2.10 B/E/H/K 17-112 [» ]
4W9G X-ray 2.70 B/E/H/K 17-112 [» ]
4W9H X-ray 2.10 B/E/H/K 17-112 [» ]
4W9I X-ray 2.40 B/E/H/K 17-112 [» ]
4W9J X-ray 2.20 B/E/H/K 17-112 [» ]
4W9K X-ray 2.10 B/E/H/K 17-112 [» ]
4W9L X-ray 2.20 B/E/H/K 17-112 [» ]
ProteinModelPortali Q15369.
SMRi Q15369. Positions 17-112.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112783. 117 interactions.
DIPi DIP-29571N.
IntActi Q15369. 52 interactions.
MINTi MINT-1323870.
STRINGi 9606.ENSP00000284811.

PTM databases

PhosphoSitei Q15369.

Polymorphism databases

DMDMi 32699511.

Proteomic databases

MaxQBi Q15369.
PaxDbi Q15369.
PRIDEi Q15369.

Protocols and materials databases

DNASUi 6921.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000284811 ; ENSP00000284811 ; ENSG00000154582 . [Q15369-1 ]
ENST00000518127 ; ENSP00000428334 ; ENSG00000154582 . [Q15369-1 ]
ENST00000519487 ; ENSP00000429596 ; ENSG00000154582 . [Q15369-1 ]
ENST00000520210 ; ENSP00000430224 ; ENSG00000154582 . [Q15369-2 ]
ENST00000520242 ; ENSP00000428171 ; ENSG00000154582 . [Q15369-1 ]
ENST00000522337 ; ENSP00000429906 ; ENSG00000154582 . [Q15369-1 ]
ENST00000523815 ; ENSP00000428074 ; ENSG00000154582 . [Q15369-1 ]
ENST00000622804 ; ENSP00000478121 ; ENSG00000154582 . [Q15369-1 ]
GeneIDi 6921.
KEGGi hsa:6921.
UCSCi uc003xzx.2. human. [Q15369-1 ]

Organism-specific databases

CTDi 6921.
GeneCardsi GC08M074858.
HGNCi HGNC:11617. TCEB1.
MIMi 600788. gene.
neXtProti NX_Q15369.
PharmGKBi PA36376.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG298860.
GeneTreei ENSGT00390000011717.
HOGENOMi HOG000216525.
HOVERGENi HBG007440.
InParanoidi Q15369.
KOi K03872.
OMAi YFHYWYR.
OrthoDBi EOG77M8QN.
PhylomeDBi Q15369.
TreeFami TF300233.

Enzyme and pathway databases

Reactomei REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6259. HIV elongation arrest and recovery.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

ChiTaRSi TCEB1. human.
EvolutionaryTracei Q15369.
GeneWikii TCEB1.
GenomeRNAii 6921.
NextBioi 27077.
PROi Q15369.
SOURCEi Search...

Gene expression databases

Bgeei Q15369.
CleanExi HS_TCEB1.
ExpressionAtlasi Q15369. baseline and differential.
Genevestigatori Q15369.

Family and domain databases

Gene3Di 3.30.710.10. 1 hit.
InterProi IPR011333. BTB/POZ_fold.
IPR001232. Skp1_comp.
IPR016073. Skp1_comp_POZ.
[Graphical view ]
Pfami PF03931. Skp1_POZ. 1 hit.
[Graphical view ]
SMARTi SM00512. Skp1. 1 hit.
[Graphical view ]
SUPFAMi SSF54695. SSF54695. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A human cDNA encoding the small subunit of RNA polymerase II transcription factor SIII."
    Garrett K.P., Haque D., Conaway R.C., Conaway J.W.
    Gene 150:413-414(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Peripheral blood.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Colon.
  3. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skin.
  5. "Drosophila von Hippel-Lindau tumor suppressor complex possesses E3 ubiquitin ligase activity."
    Aso T., Yamazaki K., Aigaki T., Kitajima S.
    Biochem. Biophys. Res. Commun. 276:355-361(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VHL.
  6. "Amplification and overexpression of Elongin C gene discovered in prostate cancer by cDNA microarrays."
    Porkka K., Saramaeki O., Tanner M., Visakorpi T.
    Lab. Invest. 82:629-637(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation."
    Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.
    Genes Dev. 18:2861-2866(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV VIF.
  8. "TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3."
    Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S., Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.
    Oncogene 23:8908-8919(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMF1.
  9. "Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling."
    Kario E., Marmor M.D., Adamsky K., Citri A., Amit I., Amariglio N., Rechavi G., Yarden Y.
    J. Biol. Chem. 280:7038-7048(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EGFR DEGRADATION, INTERACTION WITH SOCS5.
  10. "Structural basis for protein recognition by B30.2/SPRY domains."
    Woo J.S., Suh H.Y., Park S.Y., Oh B.H.
    Mol. Cell 24:967-976(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPSB1.
  11. "Respiratory syncytial virus NS1 protein degrades STAT2 by using the Elongin-Cullin E3 ligase."
    Elliott J., Lynch O.T., Suessmuth Y., Qian P., Boyd C.R., Burrows J.F., Buick R., Stevenson N.J., Touzelet O., Gadina M., Power U.F., Johnston J.A.
    J. Virol. 81:3428-3436(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HRSV PROTEIN NS1.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "The Kelch repeat protein KLHDC10 regulates oxidative stress-induced ASK1 activation by suppressing PP5."
    Sekine Y., Hatanaka R., Watanabe T., Sono N., Iemura S., Natsume T., Kuranaga E., Miura M., Takeda K., Ichijo H.
    Mol. Cell 48:692-704(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KLHDC10.
  14. "Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function."
    Stebbins C.E., Kaelin W.G. Jr., Pavletich N.P.
    Science 284:455-461(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 17-112 IN COMPLEX WITH 1-120 OF TCEB2 AND 54-213 OF VHL.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-112 IN COMPLEX WITH TCEB2; 52-113 OF VHL AND 549-582 OF HIF1A.
  16. "Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition in signaling."
    Min J.-H., Yang H., Ivan M., Gertler F., Kaelin W.G. Jr., Pavletich N.P.
    Science 296:1886-1889(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) COMPLEX WITH TCEB2; 54-113 OF VHL AND 556-575 OF HIF1A.
  17. "Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation."
    Bullock A.N., Rodriguez M.C., Debreczeni J.E., Songyang Z., Knapp S.
    Structure 15:1493-1504(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 17-112 IN COMPLEX WITH TCEB2 ANS SOX4, SUBUNIT.

Entry informationi

Entry nameiELOC_HUMAN
AccessioniPrimary (citable) accession number: Q15369
Secondary accession number(s): E5RGD9, Q567Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 144 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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

External Data

Dasty 3