PAF1_HUMAN
ID PAF1_HUMAN Reviewed; 531 AA.
AC Q8N7H5; M0QX35; O75239; Q9H166; Q9NUU9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=RNA polymerase II-associated factor 1 homolog;
DE Short=hPAF1;
DE AltName: Full=Pancreatic differentiation protein 2;
GN Name=PAF1; Synonyms=PD2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION
RP WITH POLR2A, AND FUNCTION.
RC TISSUE=Fetal pancreas;
RX PubMed=16491129; DOI=10.1038/sj.onc.1209353;
RA Moniaux N., Nemos C., Schmied B.M., Chauhan S.C., Deb S., Morikane K.,
RA Choudhury A., Vanlith M., Sutherlin M., Sikela J.M., Hollingsworth M.A.,
RA Batra S.K.;
RT "The human homologue of the RNA polymerase II-associated factor 1 (hPaf1),
RT localized on the 19q13 amplicon, is associated with tumorigenesis.";
RL Oncogene 25:3247-3257(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH TTC37.
RX PubMed=16024656; DOI=10.1101/gad.1292105;
RA Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H., Batra S.K.,
RA Tempst P., Reinberg D.;
RT "The human PAF complex coordinates transcription with events downstream of
RT RNA synthesis.";
RL Genes Dev. 19:1668-1673(2005).
RN [7]
RP INTERACTION WITH UBE2E1.
RX PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
RA Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P.,
RA Reinberg D.;
RT "Monoubiquitination of human histone H2B: the factors involved and their
RT roles in HOX gene regulation.";
RL Mol. Cell 20:601-611(2005).
RN [8]
RP INTERACTION WITH CDC73 AND POLR2A.
RX PubMed=15923622; DOI=10.1128/mcb.25.12.5052-5060.2005;
RA Yart A., Gstaiger M., Wirbelauer C., Pecnik M., Anastasiou D., Hess D.,
RA Krek W.;
RT "The HRPT2 tumor suppressor gene product parafibromin associates with human
RT PAF1 and RNA polymerase II.";
RL Mol. Cell. Biol. 25:5052-5060(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP FUNCTION OF THE PAF1 COMPLEX, AND INTERACTION WITH RNF20 AND RNF40.
RX PubMed=19410543; DOI=10.1016/j.cell.2009.02.027;
RA Kim J., Guermah M., McGinty R.K., Lee J.S., Tang Z., Milne T.A.,
RA Shilatifard A., Muir T.W., Roeder R.G.;
RT "RAD6-mediated transcription-coupled H2B ubiquitylation directly stimulates
RT H3K4 methylation in human cells.";
RL Cell 137:459-471(2009).
RN [11]
RP IDENTIFICATION IN THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX, AND
RP INTERACTION WITH SUPT5H.
RX PubMed=19952111; DOI=10.1101/gad.1834709;
RA Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T., Nakamura M.,
RA Hisatake K., Handa H.;
RT "DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative roles
RT in RNA polymerase II elongation.";
RL Genes Dev. 23:2765-2777(2009).
RN [12]
RP FUNCTION OF THE PAF1 COMPLEX, AND INTERACTION WITH KMT2A.
RX PubMed=20541477; DOI=10.1016/j.ccr.2010.04.012;
RA Muntean A.G., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly J.A.,
RA Basrur V., Elenitoba-Johnson K.S., Hess J.L.;
RT "The PAF complex synergizes with MLL fusion proteins at HOX loci to promote
RT leukemogenesis.";
RL Cancer Cell 17:609-621(2010).
RN [13]
RP IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX,
RP FUNCTION OF THE PAF1 COMPLEX, AND INTERACTION WITH TCEA1.
RX PubMed=20178742; DOI=10.1016/j.cell.2009.12.050;
RA Kim J., Guermah M., Roeder R.G.;
RT "The human PAF1 complex acts in chromatin transcription elongation both
RT independently and cooperatively with SII/TFIIS.";
RL Cell 140:491-503(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP FUNCTION, AND FUNCTION OF THE PAF1 COMPLEX.
RX PubMed=21329879; DOI=10.1016/j.molcel.2011.01.022;
RA Nagaike T., Logan C., Hotta I., Rozenblatt-Rosen O., Meyerson M.,
RA Manley J.L.;
RT "Transcriptional activators enhance polyadenylation of mRNA precursors.";
RL Mol. Cell 41:409-418(2011).
RN [17]
RP FUNCTION OF THE PAF1 COMPLEX, AND INTERACTION WITH INFLUENZA A NS1 PROTEIN.
RX PubMed=22419161; DOI=10.1038/nature10892;
RA Marazzi I., Ho J.S., Kim J., Manicassamy B., Dewell S., Albrecht R.A.,
RA Seibert C.W., Schaefer U., Jeffrey K.L., Prinjha R.K., Lee K.,
RA Garcia-Sastre A., Roeder R.G., Tarakhovsky A.;
RT "Suppression of the antiviral response by an influenza histone mimic.";
RL Nature 483:428-433(2012).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-133 AND LYS-154, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP INTERACTION WITH ZIKA VIRUS FRENCH POLYNESIA 10087PF/2013 NS5; DENGUE VIRUS
RP DENV2 16681 NS5 AND DENGUE VIRUS DENV4 DOMINICA/814669/1981 NS5.
RX PubMed=30550790; DOI=10.1016/j.cell.2018.11.028;
RA Shah P.S., Link N., Jang G.M., Sharp P.P., Zhu T., Swaney D.L.,
RA Johnson J.R., Von Dollen J., Ramage H.R., Satkamp L., Newton B.,
RA Huettenhain R., Petit M.J., Baum T., Everitt A., Laufman O., Tassetto M.,
RA Shales M., Stevenson E., Iglesias G.N., Shokat L., Tripathi S.,
RA Balasubramaniam V., Webb L.G., Aguirre S., Willsey A.J., Garcia-Sastre A.,
RA Pollard K.S., Cherry S., Gamarnik A.V., Marazzi I., Taunton J.,
RA Fernandez-Sesma A., Bellen H.J., Andino R., Krogan N.J.;
RT "Comparative Flavivirus-Host Protein Interaction Mapping Reveals Mechanisms
RT of Dengue and Zika Virus Pathogenesis.";
RL Cell 175:1931-1945(2018).
RN [22]
RP INTERACTION WITH PINT87AA, AND SUBCELLULAR LOCATION.
RX PubMed=30367041; DOI=10.1038/s41467-018-06862-2;
RA Zhang M., Zhao K., Xu X., Yang Y., Yan S., Wei P., Liu H., Xu J., Xiao F.,
RA Zhou H., Yang X., Huang N., Liu J., He K., Xie K., Zhang G., Huang S.,
RA Zhang N.;
RT "A peptide encoded by circular form of LINC-PINT suppresses oncogenic
RT transcriptional elongation in glioblastoma.";
RL Nat. Commun. 9:4475-4475(2018).
CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
CC functions during transcription by RNA polymerase II and is implicated
CC in regulation of development and maintenance of embryonic stem cell
CC pluripotency. PAF1C associates with RNA polymerase II through
CC interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-
CC 5'-phosphorylated forms and is involved in transcriptional elongation,
CC acting both independently and synergistically with TCEA1 and in
CC cooperation with the DSIF complex and HTATSF1. PAF1C is required for
CC transcription of Hox and Wnt target genes. PAF1C is involved in
CC hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it
CC promotes leukemogenesis through association with KMT2A/MLL1-rearranged
CC oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL.
CC PAF1C is involved in histone modifications such as ubiquitination of
CC histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C
CC recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2
CC enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of
CC 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B
CC ubiquitination is proposed to be coupled to transcription. PAF1C is
CC involved in mRNA 3' end formation probably through association with
CC cleavage and poly(A) factors. In case of infection by influenza A
CC strain H3N2, PAF1C associates with viral NS1 protein, thereby
CC regulating gene transcription. Connects PAF1C with the RNF20/40 E3
CC ubiquitin-protein ligase complex. Involved in polyadenylation of mRNA
CC precursors. Has oncogenic activity in vivo and in vitro.
CC {ECO:0000269|PubMed:16491129, ECO:0000269|PubMed:19410543,
CC ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742,
CC ECO:0000269|PubMed:20541477, ECO:0000269|PubMed:21329879,
CC ECO:0000269|PubMed:22419161}.
CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1,
CC LEO1, CTR9, RTF1 and WDR61 (PubMed:19952111, PubMed:20178742). The PAF1
CC complex interacts with PHF5A (By similarity). Interacts with POLR2A,
CC TCEA1, TTC37, KMT2A/MLL1, SUPT5H, RNF20 and RNF40 (PubMed:15923622,
CC PubMed:16024656, PubMed:19952111, PubMed:20178742, PubMed:20541477,
CC PubMed:16491129, PubMed:19410543). Interacts with UBE2E1
CC (PubMed:16307923). Interacts with PINT87aa which is encoded by the
CC circular form of the long non-coding RNA LINC-PINT; the interaction
CC enhances the binding of the PAF1 complex to target gene promoters and
CC may anchor the complex on target gene promoters, sequentially pausing
CC RNA polymerase II-induced mRNA elongation (PubMed:30367041).
CC {ECO:0000250|UniProtKB:Q8K2T8, ECO:0000269|PubMed:15923622,
CC ECO:0000269|PubMed:16024656, ECO:0000269|PubMed:16307923,
CC ECO:0000269|PubMed:16491129, ECO:0000269|PubMed:19410543,
CC ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742,
CC ECO:0000269|PubMed:20541477, ECO:0000269|PubMed:30367041}.
CC -!- SUBUNIT: (Microbial infection) Interacts with influenza A strain H3N2
CC NS1 protein; the interaction interferes with host cell gene
CC transcription, specifically with that of antiviral genes.
CC {ECO:0000269|PubMed:22419161}.
CC -!- SUBUNIT: (Microbial infection) The PAF1 complex interacts with Zika
CC virus French Polynesia 10087PF/2013 non-structural protein 5/NS5
CC (PubMed:30550790). The interaction with viral NS5 proteins may reduce
CC the antiviral immune response by inhibiting the recruitment of the PAF1
CC complex to interferon-stimulated genes, thus preventing their
CC transcription (PubMed:30550790). {ECO:0000269|PubMed:30550790}.
CC -!- SUBUNIT: (Microbial infection) The PAF1 complex interacts with Dengue
CC virus DENV2 16681 non-structural protein 5/NS5 (PubMed:30550790). The
CC PAF1 complex interacts with Dengue virus DENV4 Dominica/814669/1981
CC non-structural protein 5/NS5 (PubMed:30550790). The interaction with
CC viral NS5 proteins may reduce the antiviral immune response by
CC inhibiting the recruitment of the PAF1 complex to interferon-stimulated
CC genes, thus preventing their transcription (PubMed:30550790).
CC {ECO:0000269|PubMed:30550790}.
CC -!- INTERACTION:
CC Q8N7H5; Q6P1J9: CDC73; NbExp=31; IntAct=EBI-2607770, EBI-930143;
CC Q8N7H5; A0A455ZAR2: circPINTexon2; NbExp=5; IntAct=EBI-2607770, EBI-27121529;
CC Q8N7H5; Q6PD62: CTR9; NbExp=26; IntAct=EBI-2607770, EBI-1019583;
CC Q8N7H5; P51116: FXR2; NbExp=4; IntAct=EBI-2607770, EBI-740459;
CC Q8N7H5; P04792: HSPB1; NbExp=2; IntAct=EBI-2607770, EBI-352682;
CC Q8N7H5; Q03164: KMT2A; NbExp=4; IntAct=EBI-2607770, EBI-591370;
CC Q8N7H5; Q8WVC0: LEO1; NbExp=28; IntAct=EBI-2607770, EBI-932432;
CC Q8N7H5; P24928: POLR2A; NbExp=5; IntAct=EBI-2607770, EBI-295301;
CC Q8N7H5; Q92541: RTF1; NbExp=17; IntAct=EBI-2607770, EBI-1055239;
CC Q8N7H5; P23193: TCEA1; NbExp=4; IntAct=EBI-2607770, EBI-2608271;
CC Q8N7H5; Q6PGP7: TTC37; NbExp=2; IntAct=EBI-2607770, EBI-6083436;
CC Q8N7H5; P51965: UBE2E1; NbExp=2; IntAct=EBI-2607770, EBI-348546;
CC Q8N7H5; B2BUF1: NS1; Xeno; NbExp=6; IntAct=EBI-2607770, EBI-4291940;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16491129,
CC ECO:0000269|PubMed:30367041}. Note=Punctuate distribution throughout
CC the nucleus except in nucleoli and the perinuclear chromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N7H5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N7H5-2; Sequence=VSP_032650, VSP_032651, VSP_032652;
CC Name=3;
CC IsoId=Q8N7H5-3; Sequence=VSP_032650, VSP_055740, VSP_055741;
CC -!- SIMILARITY: Belongs to the PAF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC25503.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAW56880.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAW56881.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PAF1ID44202ch19q13.html";
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DR EMBL; AJ401156; CAC20564.1; -; mRNA.
DR EMBL; AK001985; BAA92020.1; -; mRNA.
DR EMBL; AK098423; BAC05305.1; -; mRNA.
DR EMBL; AC005239; AAC25503.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471126; EAW56880.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471126; EAW56881.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471126; EAW56883.1; -; Genomic_DNA.
DR EMBL; BC000017; AAH00017.1; -; mRNA.
DR EMBL; BC013402; AAH13402.1; -; mRNA.
DR CCDS; CCDS12533.1; -. [Q8N7H5-1]
DR CCDS; CCDS59387.1; -. [Q8N7H5-3]
DR RefSeq; NP_001243755.1; NM_001256826.1. [Q8N7H5-3]
DR RefSeq; NP_061961.2; NM_019088.3. [Q8N7H5-1]
DR PDB; 4M6T; X-ray; 2.50 A; A=170-250.
DR PDB; 5ZYQ; X-ray; 2.53 A; A=57-116.
DR PDB; 6GMH; EM; 3.10 A; V=1-531.
DR PDB; 6TED; EM; 3.10 A; V=1-531.
DR PDB; 7OOP; EM; 2.90 A; V=1-531.
DR PDB; 7OPC; EM; 3.00 A; V=1-531.
DR PDB; 7OPD; EM; 3.00 A; V=1-531.
DR PDBsum; 4M6T; -.
DR PDBsum; 5ZYQ; -.
DR PDBsum; 6GMH; -.
DR PDBsum; 6TED; -.
DR PDBsum; 7OOP; -.
DR PDBsum; 7OPC; -.
DR PDBsum; 7OPD; -.
DR AlphaFoldDB; Q8N7H5; -.
DR SMR; Q8N7H5; -.
DR BioGRID; 120081; 214.
DR CORUM; Q8N7H5; -.
DR DIP; DIP-48673N; -.
DR IntAct; Q8N7H5; 69.
DR MINT; Q8N7H5; -.
DR STRING; 9606.ENSP00000221265; -.
DR GlyGen; Q8N7H5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N7H5; -.
DR PhosphoSitePlus; Q8N7H5; -.
DR BioMuta; PAF1; -.
DR DMDM; 182670295; -.
DR EPD; Q8N7H5; -.
DR jPOST; Q8N7H5; -.
DR MassIVE; Q8N7H5; -.
DR MaxQB; Q8N7H5; -.
DR PaxDb; Q8N7H5; -.
DR PeptideAtlas; Q8N7H5; -.
DR PRIDE; Q8N7H5; -.
DR ProteomicsDB; 72295; -. [Q8N7H5-1]
DR ProteomicsDB; 72296; -. [Q8N7H5-2]
DR Antibodypedia; 30305; 231 antibodies from 27 providers.
DR DNASU; 54623; -.
DR Ensembl; ENST00000221265.8; ENSP00000221265.2; ENSG00000006712.15. [Q8N7H5-1]
DR Ensembl; ENST00000595564.5; ENSP00000468874.1; ENSG00000006712.15. [Q8N7H5-3]
DR GeneID; 54623; -.
DR KEGG; hsa:54623; -.
DR MANE-Select; ENST00000221265.8; ENSP00000221265.2; NM_019088.4; NP_061961.2.
DR UCSC; uc002old.5; human. [Q8N7H5-1]
DR CTD; 54623; -.
DR DisGeNET; 54623; -.
DR GeneCards; PAF1; -.
DR HGNC; HGNC:25459; PAF1.
DR HPA; ENSG00000006712; Low tissue specificity.
DR MIM; 610506; gene.
DR neXtProt; NX_Q8N7H5; -.
DR OpenTargets; ENSG00000006712; -.
DR PharmGKB; PA142671206; -.
DR VEuPathDB; HostDB:ENSG00000006712; -.
DR eggNOG; KOG2478; Eukaryota.
DR GeneTree; ENSGT00390000001474; -.
DR HOGENOM; CLU_021991_2_0_1; -.
DR InParanoid; Q8N7H5; -.
DR OMA; MRPDGIY; -.
DR PhylomeDB; Q8N7H5; -.
DR TreeFam; TF313642; -.
DR PathwayCommons; Q8N7H5; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR SignaLink; Q8N7H5; -.
DR BioGRID-ORCS; 54623; 552 hits in 1095 CRISPR screens.
DR ChiTaRS; PAF1; human.
DR GenomeRNAi; 54623; -.
DR Pharos; Q8N7H5; Tbio.
DR PRO; PR:Q8N7H5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8N7H5; protein.
DR Bgee; ENSG00000006712; Expressed in tendon of biceps brachii and 200 other tissues.
DR ExpressionAtlas; Q8N7H5; baseline and differential.
DR Genevisible; Q8N7H5; HS.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:CACAO.
DR GO; GO:0016020; C:membrane; IDA:CACAO.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
DR GO; GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
DR GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IMP:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
DR GO; GO:0031062; P:positive regulation of histone methylation; IMP:CACAO.
DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; IMP:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:CACAO.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR007133; RNA_pol_II-assoc_Paf1.
DR PANTHER; PTHR23188; PTHR23188; 1.
DR Pfam; PF03985; Paf1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation;
KW Wnt signaling pathway.
FT CHAIN 1..531
FT /note="RNA polymerase II-associated factor 1 homolog"
FT /id="PRO_0000326400"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..300
FT /note="Interaction with PINT87aa"
FT /evidence="ECO:0000269|PubMed:30367041"
FT REGION 361..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 352..400
FT /evidence="ECO:0000255"
FT COMPBIAS 375..392
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2T8"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 17..26
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032650"
FT VAR_SEQ 190..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032651"
FT VAR_SEQ 395..508
FT /note="DEEQEKGSSSEKEGSEDEHSGSESEREEGDRDEASDKSGSGEDESSEDEARA
FT ARDKEEIFGSDADSEDDADSDDEDRGQAQGGSDNDSDSGSNGGGQRSRSHSRSASPFPS
FT GSE -> VMLILRTMPTLMMRTEDRPKVAVTMIQTAAAMGVASGAGATAAAPVPSPVAA
FT STRPRRMAVKLQLLIPVKLIVTVTESQGIQGWFRHHYCEQQSTFLVVCL (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032652"
FT VAR_SEQ 395..495
FT /note="DEEQEKGSSSEKEGSEDEHSGSESEREEGDRDEASDKSGSGEDESSEDEARA
FT ARDKEEIFGSDADSEDDADSDDEDRGQAQGGSDNDSDSGSNGGGQRSRS -> VMLILR
FT TMPTLMMRTEDRPKVAVTMIQTAAAMGVASGAGATAAAPVPSPVAASTRPRRMAVKLQL
FT LIPVKLIVTVTESQGIQGWFRHHYCEQQSTFLVVCL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055740"
FT VAR_SEQ 496..531
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055741"
FT CONFLICT 58
FT /note="F -> I (in Ref. 3; BAA92020)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="K -> R (in Ref. 3; BAC05305)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="E -> G (in Ref. 3; BAA92020)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="E -> G (in Ref. 3; BAA92020)"
FT /evidence="ECO:0000305"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:6TED"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:7OOP"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6TED"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6TED"
FT HELIX 172..187
FT /evidence="ECO:0007829|PDB:4M6T"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:7OOP"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:4M6T"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:4M6T"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:4M6T"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:4M6T"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:4M6T"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:4M6T"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:4M6T"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:7OOP"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:7OOP"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:7OOP"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:6TED"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:7OOP"
SQ SEQUENCE 531 AA; 59976 MW; 756F800AA64255D6 CRC64;
MAPTIQTQAQ REDGHRPNSH RTLPERSGVV CRVKYCNSLP DIPFDPKFIT YPFDQNRFVQ
YKATSLEKQH KHDLLTEPDL GVTIDLINPD TYRIDPNVLL DPADEKLLEE EIQAPTSSKR
SQQHAKVVPW MRKTEYISTE FNRYGISNEK PEVKIGVSVK QQFTEEEIYK DRDSQITAIE
KTFEDAQKSI SQHYSKPRVT PVEVMPVFPD FKMWINPCAQ VIFDSDPAPK DTSGAAALEM
MSQAMIRGMM DEEGNQFVAY FLPVEETLKK RKRDQEEEMD YAPDDVYDYK IAREYNWNVK
NKASKGYEEN YFFIFREGDG VYYNELETRV RLSKRRAKAG VQSGTNALLV VKHRDMNEKE
LEAQEARKAQ LENHEPEEEE EEEMETEEKE AGGSDEEQEK GSSSEKEGSE DEHSGSESER
EEGDRDEASD KSGSGEDESS EDEARAARDK EEIFGSDADS EDDADSDDED RGQAQGGSDN
DSDSGSNGGG QRSRSHSRSA SPFPSGSEHS AQEDGSEAAA SDSSEADSDS D
