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Q15370

- ELOB_HUMAN

UniProt

Q15370 - ELOB_HUMAN

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Protein

Transcription elongation factor B polypeptide 2

Gene

TCEB2

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).
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.

Pathwayi

GO - Molecular functioni

  1. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

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

Keywords - Biological processi

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.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor B polypeptide 2
Alternative name(s):
Elongin 18 kDa subunit
Elongin-B
Short name:
EloB
RNA polymerase II transcription factor SIII subunit B
SIII p18
Gene namesi
Name:TCEB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:11619. TCEB2.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. Cul2-RING ubiquitin ligase complex Source: UniProtKB
  2. Cul5-RING ubiquitin ligase complex Source: UniProtKB
  3. cytosol Source: Reactome
  4. elongin complex Source: Ensembl
  5. extracellular vesicular exosome Source: UniProt
  6. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36378.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 118118Transcription elongation factor B polypeptide 2PRO_0000114914Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ15370.
PaxDbiQ15370.
PeptideAtlasiQ15370.
PRIDEiQ15370.

PTM databases

PhosphoSiteiQ15370.

Expressioni

Gene expression databases

BgeeiQ15370.
CleanExiHS_TCEB2.
ExpressionAtlasiQ15370. baseline and differential.
GenevestigatoriQ15370.

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. Substrate adapter protein can be a viral protein such as HIV Vif. Interacts with VHL. Found in a complex composed 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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MED8Q96G255EBI-301238,EBI-394405
TCEB1Q153698EBI-301238,EBI-301231
vifP125045EBI-301238,EBI-779991From a different organism.

Protein-protein interaction databases

BioGridi112785. 100 interactions.
DIPiDIP-29570N.
IntActiQ15370. 33 interactions.
MINTiMINT-1323839.
STRINGi9606.ENSP00000262306.

Structurei

Secondary structure

1
118
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109
Beta strandi12 – 198
Helixi24 – 3512
Helixi39 – 413
Beta strandi42 – 465
Beta strandi49 – 513
Turni57 – 615
Helixi64 – 663
Beta strandi69 – 713
Beta strandi73 – 797
Beta strandi82 – 843
Helixi86 – 894
Turni92 – 943
Beta strandi96 – 983
Helixi101 – 1033
Beta strandi110 – 1123

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LM8X-ray1.85B1-118[»]
1LQBX-ray2.00A1-118[»]
1VCBX-ray2.70A/D/G/J1-118[»]
2C9WX-ray1.90B1-118[»]
2IZVX-ray2.55B1-118[»]
2JZ3NMR-B1-118[»]
2MA9NMR-B1-118[»]
3DCGX-ray2.40A/C1-118[»]
3ZKJX-ray2.58C/F1-118[»]
3ZNGX-ray2.85C/F1-118[»]
3ZRCX-ray2.90A/D/G/J1-118[»]
3ZRFX-ray2.80A/D/G/J1-118[»]
3ZTCX-ray2.65A/D/G/J1-118[»]
3ZTDX-ray2.79A/D/G/J1-118[»]
3ZUNX-ray2.50A/D/G/J1-118[»]
4AJYX-ray1.73B1-118[»]
4AWJX-ray2.50A/D/G/J1-104[»]
4B95X-ray2.80A/D/G/J1-118[»]
4B9KX-ray2.00A/D/G/J1-104[»]
4BKSX-ray2.20A/D/G/J1-104[»]
4BKTX-ray2.35A/D/G/J1-104[»]
4N9FX-ray3.304/D/H/J/P/W/X/e/g/m/s/y1-102[»]
4W9CX-ray2.20A/D/G/J1-104[»]
4W9DX-ray2.20A/D/G/J1-104[»]
4W9EX-ray2.60A/D/G/J1-104[»]
4W9FX-ray2.10A/D/G/J1-104[»]
4W9GX-ray2.70A/D/G/J1-104[»]
4W9HX-ray2.10A/D/G/J1-104[»]
4W9IX-ray2.40A/D/G/J1-104[»]
4W9JX-ray2.20A/D/G/J1-104[»]
4W9KX-ray2.10A/D/G/J1-104[»]
4W9LX-ray2.20A/D/G/J1-104[»]
ProteinModelPortaliQ15370.
SMRiQ15370. Positions 1-118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15370.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6666Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG316144.
GeneTreeiENSGT00390000018316.
HOGENOMiHOG000293425.
HOVERGENiHBG008581.
InParanoidiQ15370.
KOiK03873.
OMAiNEMQTSE.
OrthoDBiEOG7GQXX6.
PhylomeDBiQ15370.
TreeFamiTF325964.

Family and domain databases

InterProiIPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15370) [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
MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL
60 70 80 90 100
LDDGKTLGEC GFTSQTARPQ APATVGLAFR ADDTFEALCI EPFSSPPELP
110
DVMKPQDSGS SANEQAVQ
Length:118
Mass (Da):13,133
Last modified:November 1, 1996 - v1
Checksum:iC045F58FBED0EC47
GO
Isoform 2 (identifier: Q15370-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     118-118: Q → HLHVHSQTMAKSRNTSWSQCPGLTACSTREPQDGPTQVHPRWGL

Note: No experimental confirmation available.

Show »
Length:161
Mass (Da):17,911
Checksum:i72277A4ACF21429F
GO

Sequence cautioni

The sequence AAC08452.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei118 – 1181Q → HLHVHSQTMAKSRNTSWSQC PGLTACSTREPQDGPTQVHP RWGL in isoform 2. 1 PublicationVSP_045784

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42856 mRNA. Translation: AAA75522.1.
BM700019 mRNA. No translation available.
AC004493 Genomic DNA. Translation: AAC08452.1. Sequence problems.
AC092117 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85472.1.
CH471112 Genomic DNA. Translation: EAW85474.1.
BC013306 mRNA. Translation: AAH13306.1.
BC065000 mRNA. Translation: AAH65000.1.
CCDSiCCDS32374.1. [Q15370-2]
CCDS45387.1. [Q15370-1]
PIRiI59405.
RefSeqiNP_009039.1. NM_007108.3. [Q15370-1]
NP_996896.1. NM_207013.2. [Q15370-2]
UniGeneiHs.172772.

Genome annotation databases

EnsembliENST00000262306; ENSP00000262306; ENSG00000103363. [Q15370-2]
ENST00000409906; ENSP00000386652; ENSG00000103363. [Q15370-1]
GeneIDi6923.
KEGGihsa:6923.
UCSCiuc002crm.3. human.
uc002crn.3. human. [Q15370-1]

Polymorphism databases

DMDMi32699512.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42856 mRNA. Translation: AAA75522.1 .
BM700019 mRNA. No translation available.
AC004493 Genomic DNA. Translation: AAC08452.1 . Sequence problems.
AC092117 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85472.1 .
CH471112 Genomic DNA. Translation: EAW85474.1 .
BC013306 mRNA. Translation: AAH13306.1 .
BC065000 mRNA. Translation: AAH65000.1 .
CCDSi CCDS32374.1. [Q15370-2 ]
CCDS45387.1. [Q15370-1 ]
PIRi I59405.
RefSeqi NP_009039.1. NM_007108.3. [Q15370-1 ]
NP_996896.1. NM_207013.2. [Q15370-2 ]
UniGenei Hs.172772.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LM8 X-ray 1.85 B 1-118 [» ]
1LQB X-ray 2.00 A 1-118 [» ]
1VCB X-ray 2.70 A/D/G/J 1-118 [» ]
2C9W X-ray 1.90 B 1-118 [» ]
2IZV X-ray 2.55 B 1-118 [» ]
2JZ3 NMR - B 1-118 [» ]
2MA9 NMR - B 1-118 [» ]
3DCG X-ray 2.40 A/C 1-118 [» ]
3ZKJ X-ray 2.58 C/F 1-118 [» ]
3ZNG X-ray 2.85 C/F 1-118 [» ]
3ZRC X-ray 2.90 A/D/G/J 1-118 [» ]
3ZRF X-ray 2.80 A/D/G/J 1-118 [» ]
3ZTC X-ray 2.65 A/D/G/J 1-118 [» ]
3ZTD X-ray 2.79 A/D/G/J 1-118 [» ]
3ZUN X-ray 2.50 A/D/G/J 1-118 [» ]
4AJY X-ray 1.73 B 1-118 [» ]
4AWJ X-ray 2.50 A/D/G/J 1-104 [» ]
4B95 X-ray 2.80 A/D/G/J 1-118 [» ]
4B9K X-ray 2.00 A/D/G/J 1-104 [» ]
4BKS X-ray 2.20 A/D/G/J 1-104 [» ]
4BKT X-ray 2.35 A/D/G/J 1-104 [» ]
4N9F X-ray 3.30 4/D/H/J/P/W/X/e/g/m/s/y 1-102 [» ]
4W9C X-ray 2.20 A/D/G/J 1-104 [» ]
4W9D X-ray 2.20 A/D/G/J 1-104 [» ]
4W9E X-ray 2.60 A/D/G/J 1-104 [» ]
4W9F X-ray 2.10 A/D/G/J 1-104 [» ]
4W9G X-ray 2.70 A/D/G/J 1-104 [» ]
4W9H X-ray 2.10 A/D/G/J 1-104 [» ]
4W9I X-ray 2.40 A/D/G/J 1-104 [» ]
4W9J X-ray 2.20 A/D/G/J 1-104 [» ]
4W9K X-ray 2.10 A/D/G/J 1-104 [» ]
4W9L X-ray 2.20 A/D/G/J 1-104 [» ]
ProteinModelPortali Q15370.
SMRi Q15370. Positions 1-118.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112785. 100 interactions.
DIPi DIP-29570N.
IntActi Q15370. 33 interactions.
MINTi MINT-1323839.
STRINGi 9606.ENSP00000262306.

PTM databases

PhosphoSitei Q15370.

Polymorphism databases

DMDMi 32699512.

Proteomic databases

MaxQBi Q15370.
PaxDbi Q15370.
PeptideAtlasi Q15370.
PRIDEi Q15370.

Protocols and materials databases

DNASUi 6923.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262306 ; ENSP00000262306 ; ENSG00000103363 . [Q15370-2 ]
ENST00000409906 ; ENSP00000386652 ; ENSG00000103363 . [Q15370-1 ]
GeneIDi 6923.
KEGGi hsa:6923.
UCSCi uc002crm.3. human.
uc002crn.3. human. [Q15370-1 ]

Organism-specific databases

CTDi 6923.
GeneCardsi GC16M002824.
HGNCi HGNC:11619. TCEB2.
MIMi 600787. gene.
neXtProti NX_Q15370.
PharmGKBi PA36378.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG316144.
GeneTreei ENSGT00390000018316.
HOGENOMi HOG000293425.
HOVERGENi HBG008581.
InParanoidi Q15370.
KOi K03873.
OMAi NEMQTSE.
OrthoDBi EOG7GQXX6.
PhylomeDBi Q15370.
TreeFami TF325964.

Enzyme and pathway databases

UniPathwayi UPA00143 .
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

EvolutionaryTracei Q15370.
GeneWikii TCEB2.
GenomeRNAii 6923.
NextBioi 27083.
PROi Q15370.
SOURCEi Search...

Gene expression databases

Bgeei Q15370.
CleanExi HS_TCEB2.
ExpressionAtlasi Q15370. baseline and differential.
Genevestigatori Q15370.

Family and domain databases

InterProi IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF00240. ubiquitin. 1 hit.
[Graphical view ]
SMARTi SM00213. UBQ. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
PROSITEi PS50053. UBIQUITIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog."
    Garrett K.P., Aso T., Bradsher J.N., Foundling S.I., Lane W.S., Conaway R.C., Conaway J.W.
    Proc. Natl. Acad. Sci. U.S.A. 92:7172-7176(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
  2. Bonaldo M.F., Lennon G., Soares M.B.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Pancreas and Placenta.
  6. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-8 AND 44-80, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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. Cited for: IDENTIFICATION IN A COMPLEX WITH LIMD1; EGLN1/PHD2; VHL AND CUL2.
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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) IN COMPLEX WITH TCEB1 AND VHL.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) COMPLEX WITH TCEB1; VHL AND HIF1A.
  18. "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 TCEB1; VHL AND HIF1A.
  19. "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) IN COMPLEX WITH TCEB1 ANS SOX4, SUBUNIT.

Entry informationi

Entry nameiELOB_HUMAN
AccessioniPrimary (citable) accession number: Q15370
Secondary accession number(s): B7WPD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 150 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3