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Q8N7H5

- PAF1_HUMAN

UniProt

Q8N7H5 - PAF1_HUMAN

Protein

RNA polymerase II-associated factor 1 homolog

Gene

PAF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (08 Apr 2008)
      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. Connects PAF1C with the RNF20/40 E3 ubiquitin-protein ligase complex. Involved in polyadenylation of mRNA precursors. Has oncogenic activity in vivo and in vitro.7 Publications

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. protein binding Source: IntAct
    3. RNA polymerase II core binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Biological processi

    Transcription, Transcription regulation, Wnt signaling pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA polymerase II-associated factor 1 homolog
    Short name:
    hPAF1
    Alternative name(s):
    Pancreatic differentiation protein 2
    Gene namesi
    Name:PAF1
    Synonyms:PD2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:25459. PAF1.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Punctuate distribution throughout the nucleus except in nucleoli and the perinuclear chromatin.

    GO - Cellular componenti

    1. Cdc73/Paf1 complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA142671206.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 531531RNA polymerase II-associated factor 1 homologPRO_0000326400Add
    BLAST

    Proteomic databases

    MaxQBiQ8N7H5.
    PaxDbiQ8N7H5.
    PRIDEiQ8N7H5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8N7H5.
    BgeeiQ8N7H5.
    CleanExiHS_PAF1.
    GenevestigatoriQ8N7H5.

    Organism-specific databases

    HPAiHPA041875.

    Interactioni

    Subunit structurei

    Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. Interacts with POLR2A, TCEA1, TTC37, KMT2A/MLL1, SUPT5H, RNF20 and RNF40. Interacts with UBE2E1. Interacts with influenza A strain H3N2 NS1 protein; the interaction interferes with host cell gene transcription, specifically with that of antiviral genes.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC73Q6P1J925EBI-2607770,EBI-930143
    CTR9Q6PD6222EBI-2607770,EBI-1019583
    KMT2AQ031644EBI-2607770,EBI-591370
    LEO1Q8WVC017EBI-2607770,EBI-932432
    NS1B2BUF16EBI-2607770,EBI-4291940From a different organism.
    POLR2AP249285EBI-2607770,EBI-295301
    RTF1Q9254116EBI-2607770,EBI-1055239
    TCEA1P231934EBI-2607770,EBI-2608271
    TTC37Q6PGP72EBI-2607770,EBI-6083436
    UBE2E1P519652EBI-2607770,EBI-348546

    Protein-protein interaction databases

    BioGridi120081. 43 interactions.
    DIPiDIP-48673N.
    IntActiQ8N7H5. 19 interactions.
    STRINGi9606.ENSP00000221265.

    Structurei

    Secondary structure

    1
    531
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi172 – 18716
    Beta strandi201 – 2066
    Beta strandi211 – 2155
    Beta strandi231 – 2344
    Beta strandi238 – 2414
    Helixi246 – 2494

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4M6TX-ray2.50A170-250[»]
    ProteinModelPortaliQ8N7H5.
    SMRiQ8N7H5. Positions 170-257.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili352 – 40049Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi358 – 45295Glu-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PAF1 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG297168.
    HOGENOMiHOG000115425.
    HOVERGENiHBG053131.
    InParanoidiQ8N7H5.
    KOiK15174.
    OMAiYEVLTEH.
    PhylomeDBiQ8N7H5.
    TreeFamiTF313642.

    Family and domain databases

    InterProiIPR007133. RNA_pol_II-assoc_Paf1.
    [Graphical view]
    PANTHERiPTHR23188. PTHR23188. 1 hit.
    PfamiPF03985. Paf1. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8N7H5-1) [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

    MAPTIQTQAQ REDGHRPNSH RTLPERSGVV CRVKYCNSLP DIPFDPKFIT    50
    YPFDQNRFVQ YKATSLEKQH KHDLLTEPDL GVTIDLINPD TYRIDPNVLL 100
    DPADEKLLEE EIQAPTSSKR SQQHAKVVPW MRKTEYISTE FNRYGISNEK 150
    PEVKIGVSVK QQFTEEEIYK DRDSQITAIE KTFEDAQKSI SQHYSKPRVT 200
    PVEVMPVFPD FKMWINPCAQ VIFDSDPAPK DTSGAAALEM MSQAMIRGMM 250
    DEEGNQFVAY FLPVEETLKK RKRDQEEEMD YAPDDVYDYK IAREYNWNVK 300
    NKASKGYEEN YFFIFREGDG VYYNELETRV RLSKRRAKAG VQSGTNALLV 350
    VKHRDMNEKE LEAQEARKAQ LENHEPEEEE EEEMETEEKE AGGSDEEQEK 400
    GSSSEKEGSE DEHSGSESER EEGDRDEASD KSGSGEDESS EDEARAARDK 450
    EEIFGSDADS EDDADSDDED RGQAQGGSDN DSDSGSNGGG QRSRSHSRSA 500
    SPFPSGSEHS AQEDGSEAAA SDSSEADSDS D 531
    Length:531
    Mass (Da):59,976
    Last modified:April 8, 2008 - v2
    Checksum:i756F800AA64255D6
    GO
    Isoform 2 (identifier: Q8N7H5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         17-26: Missing.
         190-212: Missing.
         395-508: DEEQEKGSSS...SASPFPSGSE → VMLILRTMPT...QQSTFLVVCL

    Note: No experimental confirmation available.

    Show »
    Length:485
    Mass (Da):55,039
    Checksum:i619FCF62CF34627D
    GO
    Isoform 3 (identifier: Q8N7H5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         17-26: Missing.
         395-495: DEEQEKGSSS...SNGGGQRSRS → VMLILRTMPT...QQSTFLVVCL
         496-531: Missing.

    Show »
    Length:485
    Mass (Da):55,473
    Checksum:iE92BFB28CB9D655E
    GO

    Sequence cautioni

    The sequence AAC25503.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAW56880.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAW56881.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 581F → I in BAA92020. (PubMed:15057824)Curated
    Sequence conflicti68 – 681K → R in BAC05305. (PubMed:15057824)Curated
    Sequence conflicti152 – 1521E → G in BAA92020. (PubMed:15057824)Curated
    Sequence conflicti378 – 3781E → G in BAA92020. (PubMed:15057824)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei17 – 2610Missing in isoform 2 and isoform 3. 1 PublicationVSP_032650
    Alternative sequencei190 – 21223Missing in isoform 2. CuratedVSP_032651Add
    BLAST
    Alternative sequencei395 – 508114DEEQE…PSGSE → VMLILRTMPTLMMRTEDRPK VAVTMIQTAAAMGVASGAGA TAAAPVPSPVAASTRPRRMA VKLQLLIPVKLIVTVTESQG IQGWFRHHYCEQQSTFLVVC L in isoform 2. CuratedVSP_032652Add
    BLAST
    Alternative sequencei395 – 495101DEEQE…QRSRS → VMLILRTMPTLMMRTEDRPK VAVTMIQTAAAMGVASGAGA TAAAPVPSPVAASTRPRRMA VKLQLLIPVKLIVTVTESQG IQGWFRHHYCEQQSTFLVVC L in isoform 3. 1 PublicationVSP_055740Add
    BLAST
    Alternative sequencei496 – 53136Missing in isoform 3. 1 PublicationVSP_055741Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ401156 mRNA. Translation: CAC20564.1.
    AK001985 mRNA. Translation: BAA92020.1.
    AK098423 mRNA. Translation: BAC05305.1.
    AC005239 Genomic DNA. Translation: AAC25503.1. Sequence problems.
    CH471126 Genomic DNA. Translation: EAW56880.1. Sequence problems.
    CH471126 Genomic DNA. Translation: EAW56881.1. Sequence problems.
    CH471126 Genomic DNA. Translation: EAW56883.1.
    BC000017 mRNA. Translation: AAH00017.1.
    BC013402 mRNA. Translation: AAH13402.1.
    CCDSiCCDS12533.1. [Q8N7H5-1]
    RefSeqiNP_001243755.1. NM_001256826.1.
    NP_061961.2. NM_019088.3. [Q8N7H5-1]
    UniGeneiHs.466714.

    Genome annotation databases

    EnsembliENST00000221265; ENSP00000221265; ENSG00000006712. [Q8N7H5-1]
    ENST00000595564; ENSP00000468874; ENSG00000006712. [Q8N7H5-3]
    GeneIDi54623.
    KEGGihsa:54623.
    UCSCiuc002old.4. human. [Q8N7H5-1]

    Polymorphism databases

    DMDMi182670295.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ401156 mRNA. Translation: CAC20564.1 .
    AK001985 mRNA. Translation: BAA92020.1 .
    AK098423 mRNA. Translation: BAC05305.1 .
    AC005239 Genomic DNA. Translation: AAC25503.1 . Sequence problems.
    CH471126 Genomic DNA. Translation: EAW56880.1 . Sequence problems.
    CH471126 Genomic DNA. Translation: EAW56881.1 . Sequence problems.
    CH471126 Genomic DNA. Translation: EAW56883.1 .
    BC000017 mRNA. Translation: AAH00017.1 .
    BC013402 mRNA. Translation: AAH13402.1 .
    CCDSi CCDS12533.1. [Q8N7H5-1 ]
    RefSeqi NP_001243755.1. NM_001256826.1.
    NP_061961.2. NM_019088.3. [Q8N7H5-1 ]
    UniGenei Hs.466714.

    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 170-250 [» ]
    ProteinModelPortali Q8N7H5.
    SMRi Q8N7H5. Positions 170-257.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120081. 43 interactions.
    DIPi DIP-48673N.
    IntActi Q8N7H5. 19 interactions.
    STRINGi 9606.ENSP00000221265.

    Polymorphism databases

    DMDMi 182670295.

    Proteomic databases

    MaxQBi Q8N7H5.
    PaxDbi Q8N7H5.
    PRIDEi Q8N7H5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221265 ; ENSP00000221265 ; ENSG00000006712 . [Q8N7H5-1 ]
    ENST00000595564 ; ENSP00000468874 ; ENSG00000006712 . [Q8N7H5-3 ]
    GeneIDi 54623.
    KEGGi hsa:54623.
    UCSCi uc002old.4. human. [Q8N7H5-1 ]

    Organism-specific databases

    CTDi 54623.
    GeneCardsi GC19M039876.
    HGNCi HGNC:25459. PAF1.
    HPAi HPA041875.
    MIMi 610506. gene.
    neXtProti NX_Q8N7H5.
    PharmGKBi PA142671206.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG297168.
    HOGENOMi HOG000115425.
    HOVERGENi HBG053131.
    InParanoidi Q8N7H5.
    KOi K15174.
    OMAi YEVLTEH.
    PhylomeDBi Q8N7H5.
    TreeFami TF313642.

    Miscellaneous databases

    ChiTaRSi PAF1. human.
    GenomeRNAii 54623.
    NextBioi 57158.
    PROi Q8N7H5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8N7H5.
    Bgeei Q8N7H5.
    CleanExi HS_PAF1.
    Genevestigatori Q8N7H5.

    Family and domain databases

    InterProi IPR007133. RNA_pol_II-assoc_Paf1.
    [Graphical view ]
    PANTHERi PTHR23188. PTHR23188. 1 hit.
    Pfami PF03985. Paf1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human homologue of the RNA polymerase II-associated factor 1 (hPaf1), localized on the 19q13 amplicon, is associated with tumorigenesis."
      Moniaux N., Nemos C., Schmied B.M., Chauhan S.C., Deb S., Morikane K., Choudhury A., Vanlith M., Sutherlin M., Sikela J.M., Hollingsworth M.A., Batra S.K.
      Oncogene 25:3247-3257(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH POLR2A, FUNCTION.
      Tissue: Fetal pancreas.
    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 3).
      Tissue: Placenta.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(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: Muscle and Placenta.
    6. "The human PAF complex coordinates transcription with events downstream of RNA synthesis."
      Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H., Batra S.K., Tempst P., Reinberg D.
      Genes Dev. 19:1668-1673(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TTC37.
    7. "Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation."
      Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D.
      Mol. Cell 20:601-611(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2E1.
    8. "The HRPT2 tumor suppressor gene product parafibromin associates with human PAF1 and RNA polymerase II."
      Yart A., Gstaiger M., Wirbelauer C., Pecnik M., Anastasiou D., Hess D., Krek W.
      Mol. Cell. Biol. 25:5052-5060(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC73 AND POLR2A.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "RAD6-mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells."
      Kim J., Guermah M., McGinty R.K., Lee J.S., Tang Z., Milne T.A., Shilatifard A., Muir T.W., Roeder R.G.
      Cell 137:459-471(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH RNF20 AND RNF40.
    11. "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.
    12. "The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis."
      Muntean A.G., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly J.A., Basrur V., Elenitoba-Johnson K.S., Hess J.L.
      Cancer Cell 17:609-621(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH KMT2A.
    13. "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.
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Transcriptional activators enhance polyadenylation of mRNA precursors."
      Nagaike T., Logan C., Hotta I., Rozenblatt-Rosen O., Meyerson M., Manley J.L.
      Mol. Cell 41:409-418(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, FUNCTION OF THE PAF1 COMPLEX.
    17. Cited for: FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH INFLUENZA A NS1 PROTEIN.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPAF1_HUMAN
    AccessioniPrimary (citable) accession number: Q8N7H5
    Secondary accession number(s): M0QX35
    , O75239, Q9H166, Q9NUU9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 85 of the entry and version 2 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 19
      Human chromosome 19: 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