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Q8WVC0

- LEO1_HUMAN

UniProt

Q8WVC0 - LEO1_HUMAN

Protein

RNA polymerase-associated protein LEO1

Gene

LEO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Involved in polyadenylation of mRNA precursors. Connects PAF1C to Wnt signaling.5 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. endodermal cell fate commitment Source: UniProtKB
    2. histone H2B ubiquitination Source: UniProtKB
    3. histone monoubiquitination Source: UniProtKB
    4. mRNA polyadenylation Source: UniProtKB
    5. negative regulation of myeloid cell differentiation Source: UniProtKB
    6. positive regulation of mRNA 3'-end processing Source: UniProtKB
    7. positive regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
    8. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    9. stem cell maintenance Source: UniProtKB
    10. transcription, DNA-templated Source: UniProtKB-KW
    11. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation, Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_200753. formation of the beta-catenin:TCF transactivating complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA polymerase-associated protein LEO1
    Alternative name(s):
    Replicative senescence down-regulated leo1-like protein
    Gene namesi
    Name:LEO1
    Synonyms:RDL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:30401. LEO1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. Cdc73/Paf1 complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671558.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 666665RNA polymerase-associated protein LEO1PRO_0000247819Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei10 – 101Phosphoserine2 Publications
    Modified residuei14 – 141Phosphoserine3 Publications
    Modified residuei151 – 1511Phosphoserine3 Publications
    Modified residuei154 – 1541Phosphoserine3 Publications
    Modified residuei162 – 1621Phosphoserine2 Publications
    Modified residuei171 – 1711Phosphoserine2 Publications
    Modified residuei179 – 1791Phosphoserine2 Publications
    Modified residuei188 – 1881Phosphothreonine3 Publications
    Modified residuei197 – 1971Phosphoserine3 Publications
    Modified residuei205 – 2051Phosphoserine1 Publication
    Modified residuei212 – 2121Phosphoserine3 Publications
    Modified residuei220 – 2201Phosphoserine3 Publications
    Modified residuei229 – 2291Phosphoserine3 Publications
    Modified residuei238 – 2381Phosphoserine3 Publications
    Modified residuei277 – 2771PhosphoserineBy similarity
    Modified residuei279 – 2791Phosphoserine3 Publications
    Modified residuei294 – 2941Phosphoserine2 Publications
    Modified residuei296 – 2961Phosphoserine1 Publication
    Modified residuei300 – 3001Phosphoserine2 Publications
    Modified residuei607 – 6071Phosphoserine2 Publications
    Modified residuei608 – 6081Phosphoserine2 Publications
    Modified residuei610 – 6101Phosphoserine2 Publications
    Modified residuei614 – 6141Phosphoserine1 Publication
    Modified residuei629 – 6291Phosphothreonine2 Publications
    Modified residuei630 – 6301Phosphoserine5 Publications
    Modified residuei658 – 6581Phosphoserine7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8WVC0.
    PaxDbiQ8WVC0.
    PeptideAtlasiQ8WVC0.
    PRIDEiQ8WVC0.

    PTM databases

    PhosphoSiteiQ8WVC0.

    Expressioni

    Tissue specificityi

    Highly expressed in skeletal muscle and heart. Weakly expressed in placenta and liver.1 Publication

    Gene expression databases

    BgeeiQ8WVC0.
    CleanExiHS_LEO1.
    GenevestigatoriQ8WVC0.

    Organism-specific databases

    HPAiHPA040741.
    HPA040941.

    Interactioni

    Subunit structurei

    Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. Interacts with TCEA1, SUPT5H and CTNNB1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC73Q6P1J911EBI-932432,EBI-930143
    CTNNB1P352222EBI-932432,EBI-491549
    PAF1Q8N7H517EBI-932432,EBI-2607770
    TCEA1P231934EBI-932432,EBI-2608271

    Protein-protein interaction databases

    BioGridi125817. 31 interactions.
    DIPiDIP-37885N.
    IntActiQ8WVC0. 25 interactions.
    STRINGi9606.ENSP00000299601.

    Structurei

    Secondary structure

    1
    666
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi372 – 3776
    Helixi391 – 3933
    Helixi409 – 4168
    Beta strandi418 – 4203
    Beta strandi422 – 4265
    Beta strandi432 – 44312
    Beta strandi448 – 4525
    Beta strandi455 – 4595

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4M6TX-ray2.50A370-462[»]
    ProteinModelPortaliQ8WVC0.
    SMRiQ8WVC0. Positions 370-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi3 – 329327Asp-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the LEO1 family.Curated

    Phylogenomic databases

    eggNOGiNOG130430.
    HOGENOMiHOG000253934.
    HOVERGENiHBG081913.
    InParanoidiQ8WVC0.
    KOiK15177.
    OMAiEERPQMS.
    OrthoDBiEOG7W41BG.
    PhylomeDBiQ8WVC0.
    TreeFamiTF321961.

    Family and domain databases

    InterProiIPR007149. Leo1.
    [Graphical view]
    PfamiPF04004. Leo1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8WVC0-1) [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

    MADMEDLFGS DADSEAERKD SDSGSDSDSD QENAASGSNA SGSESDQDER    50
    GDSGQPSNKE LFGDDSEDEG ASHHSGSDNH SERSDNRSEA SERSDHEDND 100
    PSDVDQHSGS EAPNDDEDEG HRSDGGSHHS EAEGSEKAHS DDEKWGREDK 150
    SDQSDDEKIQ NSDDEERAQG SDEDKLQNSD DDEKMQNTDD EERPQLSDDE 200
    RQQLSEEEKA NSDDERPVAS DNDDEKQNSD DEEQPQLSDE EKMQNSDDER 250
    PQASDEEHRH SDDEEEQDHK SESARGSDSE DEVLRMKRKN AIASDSEADS 300
    DTEVPKDNSG TMDLFGGADD ISSGSDGEDK PPTPGQPVDE NGLPQDQQEE 350
    EPIPETRIEV EIPKVNTDLG NDLYFVKLPN FLSVEPRPFD PQYYEDEFED 400
    EEMLDEEGRT RLKLKVENTI RWRIRRDEEG NEIKESNARI VKWSDGSMSL 450
    HLGNEVFDVY KAPLQGDHNH LFIRQGTGLQ GQAVFKTKLT FRPHSTDSAT 500
    HRKMTLSLAD RCSKTQKIRI LPMAGRDPEC QRTEMIKKEE ERLRASIRRE 550
    SQQRRMREKQ HQRGLSASYL EPDRYDEEEE GEESISLAAI KNRYKGGIRE 600
    ERARIYSSDS DEGSEEDKAQ RLLKAKKLTS DEEGEPSGKR KAEDDDKANK 650
    KHKKYVISDE EEEDDD 666
    Length:666
    Mass (Da):75,404
    Last modified:March 1, 2002 - v1
    Checksum:iEB405BE0EDA7E0B0
    GO
    Isoform 2 (identifier: Q8WVC0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         387-446: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:606
    Mass (Da):68,004
    Checksum:iAF31C9793F9545D5
    GO

    Sequence cautioni

    The sequence BAB71006.1 differs from that shown. Reason: Frameshift at position 473.
    Isoform 2 : The sequence BAB71006.1 differs from that shown. Reason: Frameshift at position 471.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei387 – 44660Missing in isoform 2. 1 PublicationVSP_020051Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY302186 mRNA. Translation: AAP68819.1.
    AK055762 mRNA. Translation: BAB71006.1. Frameshift.
    BC018147 mRNA. Translation: AAH18147.1.
    CCDSiCCDS10146.1. [Q8WVC0-1]
    CCDS66767.1. [Q8WVC0-2]
    RefSeqiNP_001273359.1. NM_001286430.1. [Q8WVC0-2]
    NP_620147.1. NM_138792.3. [Q8WVC0-1]
    UniGeneiHs.567662.

    Genome annotation databases

    EnsembliENST00000299601; ENSP00000299601; ENSG00000166477. [Q8WVC0-1]
    ENST00000315141; ENSP00000314610; ENSG00000166477. [Q8WVC0-2]
    GeneIDi123169.
    KEGGihsa:123169.
    UCSCiuc002abo.3. human. [Q8WVC0-1]
    uc010bfd.3. human. [Q8WVC0-2]

    Polymorphism databases

    DMDMi74751545.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY302186 mRNA. Translation: AAP68819.1 .
    AK055762 mRNA. Translation: BAB71006.1 . Frameshift.
    BC018147 mRNA. Translation: AAH18147.1 .
    CCDSi CCDS10146.1. [Q8WVC0-1 ]
    CCDS66767.1. [Q8WVC0-2 ]
    RefSeqi NP_001273359.1. NM_001286430.1. [Q8WVC0-2 ]
    NP_620147.1. NM_138792.3. [Q8WVC0-1 ]
    UniGenei Hs.567662.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4M6T X-ray 2.50 A 370-462 [» ]
    ProteinModelPortali Q8WVC0.
    SMRi Q8WVC0. Positions 370-462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125817. 31 interactions.
    DIPi DIP-37885N.
    IntActi Q8WVC0. 25 interactions.
    STRINGi 9606.ENSP00000299601.

    PTM databases

    PhosphoSitei Q8WVC0.

    Polymorphism databases

    DMDMi 74751545.

    Proteomic databases

    MaxQBi Q8WVC0.
    PaxDbi Q8WVC0.
    PeptideAtlasi Q8WVC0.
    PRIDEi Q8WVC0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000299601 ; ENSP00000299601 ; ENSG00000166477 . [Q8WVC0-1 ]
    ENST00000315141 ; ENSP00000314610 ; ENSG00000166477 . [Q8WVC0-2 ]
    GeneIDi 123169.
    KEGGi hsa:123169.
    UCSCi uc002abo.3. human. [Q8WVC0-1 ]
    uc010bfd.3. human. [Q8WVC0-2 ]

    Organism-specific databases

    CTDi 123169.
    GeneCardsi GC15M052230.
    HGNCi HGNC:30401. LEO1.
    HPAi HPA040741.
    HPA040941.
    MIMi 610507. gene.
    neXtProti NX_Q8WVC0.
    PharmGKBi PA142671558.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG130430.
    HOGENOMi HOG000253934.
    HOVERGENi HBG081913.
    InParanoidi Q8WVC0.
    KOi K15177.
    OMAi EERPQMS.
    OrthoDBi EOG7W41BG.
    PhylomeDBi Q8WVC0.
    TreeFami TF321961.

    Enzyme and pathway databases

    Reactomei REACT_200753. formation of the beta-catenin:TCF transactivating complex.

    Miscellaneous databases

    ChiTaRSi LEO1. human.
    GeneWikii LEO1.
    GenomeRNAii 123169.
    NextBioi 81081.
    PROi Q8WVC0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8WVC0.
    CleanExi HS_LEO1.
    Genevestigatori Q8WVC0.

    Family and domain databases

    InterProi IPR007149. Leo1.
    [Graphical view ]
    Pfami PF04004. Leo1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of the Leo1-like domain of replicative senescence down-regulated Leo1-like (RDL) protein promotes senescence of 2BS fibroblasts."
      Zhao L., Tong T., Zhang Z.
      FASEB J. 19:521-532(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "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] (ISOFORM 2).
      Tissue: Kidney.
    3. "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: Colon.
    4. Cited for: COMPONENT OF PAF1 COMPLEX, FUNCTION, INTERACTION WITH CDC73.
    5. "Parafibromin/Hyrax activates Wnt/Wg target gene transcription by direct association with beta-catenin/Armadillo."
      Mosimann C., Hausmann G., Basler K.
      Cell 125:327-341(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTNNB1.
    6. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-14; SER-151; SER-154; THR-188; SER-197; SER-205; SER-212; SER-220; SER-229; SER-238 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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-279; SER-630 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294; SER-296; SER-607; SER-608; SER-610; SER-614; THR-629; SER-630 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "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].
    11. Cited for: FUNCTION.
    12. "DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative roles in RNA polymerase II elongation."
      Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T., Nakamura M., Hisatake K., Handa H.
      Genes Dev. 23:2765-2777(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH SUPT5H.
    13. "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 THR-629; SER-630 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "The human PAF1 complex acts in chromatin transcription elongation both independently and cooperatively with SII/TFIIS."
      Kim J., Guermah M., Roeder R.G.
      Cell 140:491-503(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH TCEA1.
    15. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-14; SER-151; SER-154; SER-162; SER-171; SER-179; THR-188; SER-197; SER-212; SER-220; SER-229; SER-238; SER-279; SER-300; SER-630 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-151; SER-154; SER-162; SER-171; SER-179; THR-188; SER-197; SER-212; SER-220; SER-229; SER-238; SER-279; SER-294; SER-300; SER-607; SER-608; SER-610; SER-630 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLEO1_HUMAN
    AccessioniPrimary (citable) accession number: Q8WVC0
    Secondary accession number(s): Q96N99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 104 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 15
      Human chromosome 15: 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