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Q15369

- ELOC_HUMAN

UniProt

Q15369 - ELOC_HUMAN

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
  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).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 - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to hypoxia Source: Reactome
    2. gene expression Source: Reactome
    3. positive regulation of transcription elongation from RNA polymerase II promoter Source: Ensembl
    4. positive regulation of viral transcription Source: Reactome
    5. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    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. ubiquitin-dependent protein catabolic process Source: InterPro
    10. viral process Source: Reactome

    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. elongin complex Source: Ensembl
    3. nucleoplasm Source: Reactome
    4. VCB complex Source: Ensembl

    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

    ArrayExpressiQ15369.
    BgeeiQ15369.
    CleanExiHS_TCEB1.
    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. 113 interactions.
    DIPiDIP-29571N.
    IntActiQ15369. 51 interactions.
    MINTiMINT-1323870.
    STRINGi9606.ENSP00000284811.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    ProteinModelPortaliQ15369.
    SMRiQ15369. Positions 17-112.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15369.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SKP1 family.Curated

    Phylogenomic databases

    eggNOGiNOG298860.
    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

    MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG    50
    QFAENETNEV NFREIPSHVL SKVCMYFTYK VRYTNSSTEI PEFPIAPEIA 100
    LELLMAANFL DC 112
    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:
    EMBL
    GenBank
    DDBJ
    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]
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 [» ]
    ProteinModelPortali Q15369.
    SMRi Q15369. Positions 17-112.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112783. 113 interactions.
    DIPi DIP-29571N.
    IntActi Q15369. 51 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 ]
    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.
    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

    ArrayExpressi Q15369.
    Bgeei Q15369.
    CleanExi HS_TCEB1.
    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

    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: October 1, 2014
    This is version 142 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