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Q15370

- ELOB_HUMAN

UniProt

Q15370 - ELOB_HUMAN

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
  1. 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. protein binding Source: UniProtKB
    2. 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

    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

    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

    ArrayExpressiQ15370.
    BgeeiQ15370.
    CleanExiHS_TCEB2.
    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. 99 interactions.
    DIPiDIP-29570N.
    IntActiQ15370. 32 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[»]
    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.
    HOGENOMiHOG000293425.
    HOVERGENiHBG008581.
    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: Q15370-1) [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

    MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL    50
    LDDGKTLGEC GFTSQTARPQ APATVGLAFR ADDTFEALCI EPFSSPPELP 100
    DVMKPQDSGS SANEQAVQ 118
    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 [» ]
    ProteinModelPortali Q15370.
    SMRi Q15370. Positions 1-118.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112785. 99 interactions.
    DIPi DIP-29570N.
    IntActi Q15370. 32 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.
    HOGENOMi HOG000293425.
    HOVERGENi HBG008581.
    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

    ArrayExpressi Q15370.
    Bgeei Q15370.
    CleanExi HS_TCEB2.
    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

    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 1, 2014
    This is version 149 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