GENTAUR Molecular Products.

 RTF1_HUMAN              Reviewed;         710 AA.
 Q92541; Q96BX6;
 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
 30-NOV-2010, sequence version 4.
 28-MAR-2018, entry version 143.
 RecName: Full=RNA polymerase-associated protein RTF1 homolog;
 Name=RTF1; Synonyms=KIAA0252;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=16572171; DOI=10.1038/nature04601;
 Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
 Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
 FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
 Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
 Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
 DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
 Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
 Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
 Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
 Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
 Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
 Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
 Nusbaum C.;
 "Analysis of the DNA sequence and duplication history of human
 chromosome 15.";
 Nature 440:671-675(2006).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-710.
 TISSUE=Brain;
 PubMed=9039502; DOI=10.1093/dnares/3.5.321;
 Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
 Tanaka A., Kotani H., Miyajima N., Nomura N.;
 "Prediction of the coding sequences of unidentified human genes. VI.
 The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
 analysis of cDNA clones from cell line KG-1 and brain.";
 DNA Res. 3:321-329(1996).
 [3]
 SEQUENCE REVISION.
 PubMed=12168954; DOI=10.1093/dnares/9.3.99;
 Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
 "Construction of expression-ready cDNA clones for KIAA genes: manual
 curation of 330 KIAA cDNA clones.";
 DNA Res. 9:99-106(2002).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-710.
 TISSUE=Uterus;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [5]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
 Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
 Mann M.;
 "Global, in vivo, and site-specific phosphorylation dynamics in
 signaling networks.";
 Cell 127:635-648(2006).
 [6]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, AND IDENTIFICATION
 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=18669648; DOI=10.1073/pnas.0805139105;
 Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
 Elledge S.J., Gygi S.P.;
 "A quantitative atlas of mitotic phosphorylation.";
 Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
 [7]
 FUNCTION.
 PubMed=19345177; DOI=10.1016/j.stem.2009.03.009;
 Ding L., Paszkowski-Rogacz M., Nitzsche A., Slabicki M.M.,
 Heninger A.K., de Vries I., Kittler R., Junqueira M., Shevchenko A.,
 Schulz H., Hubner N., Doss M.X., Sachinidis A., Hescheler J.,
 Iacone R., Anastassiadis K., Stewart A.F., Pisabarro M.T.,
 Caldarelli A., Poser I., Theis M., Buchholz F.;
 "A genome-scale RNAi screen for Oct4 modulators defines a role of the
 Paf1 complex for embryonic stem cell identity.";
 Cell Stem Cell 4:403-415(2009).
 [8]
 IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX,
 AND FUNCTION OF THE PAF1 COMPLEX.
 PubMed=20178742; DOI=10.1016/j.cell.2009.12.050;
 Kim J., Guermah M., Roeder R.G.;
 "The human PAF1 complex acts in chromatin transcription elongation
 both independently and cooperatively with SII/TFIIS.";
 Cell 140:491-503(2010).
 [9]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-650 AND SER-697,
 AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=20068231; DOI=10.1126/scisignal.2000475;
 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.;
 "Quantitative phosphoproteomics reveals widespread full
 phosphorylation site occupancy during mitosis.";
 Sci. Signal. 3:RA3-RA3(2010).
 [10]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=21269460; DOI=10.1186/1752-0509-5-17;
 Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
 Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
 "Initial characterization of the human central proteome.";
 BMC Syst. Biol. 5:17-17(2011).
 [11]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND THR-55, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=21406692; DOI=10.1126/scisignal.2001570;
 Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
 Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
 Blagoev B.;
 "System-wide temporal characterization of the proteome and
 phosphoproteome of human embryonic stem cell differentiation.";
 Sci. Signal. 4:RS3-RS3(2011).
 [12]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626; SER-650; SER-655
 AND SER-697, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
 ANALYSIS].
 TISSUE=Cervix carcinoma, and Erythroleukemia;
 PubMed=23186163; DOI=10.1021/pr300630k;
 Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
 Mohammed S.;
 "Toward a comprehensive characterization of a human cancer cell
 phosphoproteome.";
 J. Proteome Res. 12:260-271(2013).
 [13]
 STRUCTURE BY NMR OF 347-482.
 RIKEN structural genomics initiative (RSGI);
 "Solution structure of the plus-3 domain of human KIAA0252 protein.";
 Submitted (JUN-2006) to the PDB data bank.
 [14]
 STRUCTURE BY NMR OF 353-484, DOMAIN PLUS3, DNA-BINDING, AND
 MUTAGENESIS OF ARG-401; GLU-410; ARG-429; GLN-434 AND ARG-435.
 PubMed=18184592; DOI=10.1016/j.str.2007.10.018;
 de Jong R.N., Truffault V., Diercks T., Ab E., Daniels M.A.,
 Kaptein R., Folkers G.E.;
 "Structure and DNA binding of the human Rtf1 Plus3 domain.";
 Structure 16:149-159(2008).
 -!- FUNCTION: 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. Binds single-stranded DNA.
     Required for maximal induction of heat-shock genes. Required for
     the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes
     involved in stem cell pluripotency; this function is synergistic
     with CXXC1 indicative for an involvement of a SET1 complex (By
     similarity). {ECO:0000250, ECO:0000269|PubMed:19345177,
     ECO:0000269|PubMed:20178742}.
 -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73,
     PAF1, LEO1, CTR9, RTF1 and WDR61; the association of RTF1 appears
     to be less stable than that of other subunits. At least in HeLa
     cells a N-terminal shorter form of RTF1 is also found in the
     complex (PubMed:20178742). The PAF1 complex interacts with PHF5A
     (By similarity). {ECO:0000250|UniProtKB:A2AQ19,
     ECO:0000269|PubMed:20178742}.
 -!- INTERACTION:
     Q6P1J9:CDC73; NbExp=12; IntAct=EBI-1055239, EBI-930143;
     Q8N7H5:PAF1; NbExp=16; IntAct=EBI-1055239, EBI-2607770;
 -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
 -!- DOMAIN: The Plus3 domain mediates single-stranded DNA-binding.
     {ECO:0000269|PubMed:18184592}.
 -!- CAUTION: It is uncertain whether Met-1 or Met-41 is the initiator.
     {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=AAH15052.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
     Sequence=BAA13382.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
 -----------------------------------------------------------------------
 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
 Distributed under the Creative Commons Attribution-NoDerivs License
 -----------------------------------------------------------------------
 EMBL; AC087721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; D87440; BAA13382.2; ALT_INIT; mRNA.
 EMBL; BC015052; AAH15052.1; ALT_INIT; mRNA.
 CCDS; CCDS32200.2; -.
 RefSeq; NP_055953.3; NM_015138.4.
 UniGene; Hs.511096; -.
 PDB; 2BZE; NMR; -; A=353-484.
 PDB; 2DB9; NMR; -; A=347-482.
 PDB; 3U1U; X-ray; 1.80 A; A/B=347-482.
 PDB; 4L1P; X-ray; 2.12 A; A/B=353-484.
 PDB; 4L1U; X-ray; 2.42 A; A/B/C/D/E/F=353-484.
 PDBsum; 2BZE; -.
 PDBsum; 2DB9; -.
 PDBsum; 3U1U; -.
 PDBsum; 4L1P; -.
 PDBsum; 4L1U; -.
 ProteinModelPortal; Q92541; -.
 SMR; Q92541; -.
 BioGrid; 116780; 40.
 IntAct; Q92541; 15.
 MINT; Q92541; -.
 STRING; 9606.ENSP00000374280; -.
 iPTMnet; Q92541; -.
 PhosphoSitePlus; Q92541; -.
 BioMuta; RTF1; -.
 DMDM; 313104316; -.
 EPD; Q92541; -.
 MaxQB; Q92541; -.
 PaxDb; Q92541; -.
 PeptideAtlas; Q92541; -.
 PRIDE; Q92541; -.
 Ensembl; ENST00000389629; ENSP00000374280; ENSG00000137815.
 GeneID; 23168; -.
 KEGG; hsa:23168; -.
 UCSC; uc001zny.3; human.
 CTD; 23168; -.
 DisGeNET; 23168; -.
 EuPathDB; HostDB:ENSG00000137815.14; -.
 GeneCards; RTF1; -.
 H-InvDB; HIX0012153; -.
 HGNC; HGNC:28996; RTF1.
 HPA; HPA006714; -.
 MIM; 611633; gene.
 neXtProt; NX_Q92541; -.
 OpenTargets; ENSG00000137815; -.
 PharmGKB; PA134961778; -.
 eggNOG; KOG2402; Eukaryota.
 eggNOG; COG5296; LUCA.
 GeneTree; ENSGT00390000012493; -.
 HOGENOM; HOG000231764; -.
 HOVERGEN; HBG057331; -.
 InParanoid; Q92541; -.
 KO; K15178; -.
 OMA; SGCKSAV; -.
 OrthoDB; EOG091G1817; -.
 PhylomeDB; Q92541; -.
 TreeFam; TF321360; -.
 Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
 Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
 Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
 Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
 ChiTaRS; RTF1; human.
 EvolutionaryTrace; Q92541; -.
 GeneWiki; RTF1; -.
 GenomeRNAi; 23168; -.
 PMAP-CutDB; Q92541; -.
 PRO; PR:Q92541; -.
 Proteomes; UP000005640; Chromosome 15.
 Bgee; ENSG00000137815; -.
 CleanEx; HS_RTF1; -.
 ExpressionAtlas; Q92541; baseline and differential.
 Genevisible; Q92541; HS.
 GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
 GO; GO:0005730; C:nucleolus; IEA:Ensembl.
 GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
 GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IBA:GO_Central.
 GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
 GO; GO:0001076; F:transcription factor activity, RNA polymerase II transcription factor binding; IBA:GO_Central.
 GO; GO:0001832; P:blastocyst growth; IEA:Ensembl.
 GO; GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
 GO; GO:0080182; P:histone H3-K4 trimethylation; IEA:Ensembl.
 GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
 GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IEA:Ensembl.
 GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
 GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
 GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
 GO; GO:0019827; P:stem cell population maintenance; IDA:UniProtKB.
 GO; GO:0006366; P:transcription by RNA polymerase II; TAS:Reactome.
 GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
 GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
 Gene3D; 2.170.260.30; -; 1.
 InterPro; IPR004343; Plus-3_dom.
 InterPro; IPR036128; Plus3-like_sf.
 InterPro; IPR031102; Rtf1.
 PANTHER; PTHR13115; PTHR13115; 1.
 Pfam; PF03126; Plus-3; 1.
 SMART; SM00719; Plus3; 1.
 SUPFAM; SSF159042; SSF159042; 1.
 PROSITE; PS51360; PLUS3; 1.
 1: Evidence at protein level;
 3D-structure; Activator; Coiled coil; Complete proteome; DNA-binding;
 Nucleus; Phosphoprotein; Reference proteome; Transcription;
 Transcription regulation; Wnt signaling pathway.
 CHAIN         1    710       RNA polymerase-associated protein RTF1
                              homolog.
                              /FTId=PRO_0000255936.
 DOMAIN      353    484       Plus3. {ECO:0000255|PROSITE-
                              ProRule:PRU00693}.
 COILED      526    560       {ECO:0000255}.
 COMPBIAS     10     18       Poly-Ala.
 COMPBIAS    135    173       Ser-rich.
 COMPBIAS    174    345       Glu-rich.
 COMPBIAS    214    307       Lys-rich.
 MOD_RES      53     53       Phosphoserine.
                              {ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:21406692}.
 MOD_RES      55     55       Phosphothreonine.
                              {ECO:0000244|PubMed:21406692}.
 MOD_RES     626    626       Phosphoserine.
                              {ECO:0000244|PubMed:23186163}.
 MOD_RES     650    650       Phosphoserine.
                              {ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     655    655       Phosphoserine.
                              {ECO:0000244|PubMed:23186163}.
 MOD_RES     697    697       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:23186163}.
 MUTAGEN     401    401       R->E: Loss of binding to single-stranded
                              DNA. {ECO:0000269|PubMed:18184592}.
 MUTAGEN     410    410       E->K: Reduced binding to single-stranded
                              DNA. {ECO:0000269|PubMed:18184592}.
 MUTAGEN     429    429       R->E: Loss of binding to single-stranded
                              DNA. {ECO:0000269|PubMed:18184592}.
 MUTAGEN     434    434       Q->A: Reduced binding to single-stranded
                              DNA. {ECO:0000269|PubMed:18184592}.
 MUTAGEN     435    435       R->E: Loss of binding to single-stranded
                              DNA. {ECO:0000269|PubMed:18184592}.
 HELIX       356    360       {ECO:0000244|PDB:3U1U}.
 STRAND      362    364       {ECO:0000244|PDB:2BZE}.
 HELIX       366    372       {ECO:0000244|PDB:3U1U}.
 STRAND      373    377       {ECO:0000244|PDB:2BZE}.
 HELIX       378    382       {ECO:0000244|PDB:3U1U}.
 STRAND      386    392       {ECO:0000244|PDB:3U1U}.
 STRAND      395    397       {ECO:0000244|PDB:2BZE}.
 STRAND      399    417       {ECO:0000244|PDB:3U1U}.
 STRAND      420    430       {ECO:0000244|PDB:3U1U}.
 STRAND      433    438       {ECO:0000244|PDB:3U1U}.
 HELIX       439    441       {ECO:0000244|PDB:3U1U}.
 HELIX       449    462       {ECO:0000244|PDB:3U1U}.
 HELIX       469    478       {ECO:0000244|PDB:3U1U}.
 SEQUENCE   710 AA;  80313 MW;  54CC014655AA22B8 CRC64;
 MRGRLCVGRA AAAAAAVAVP LAGGQEGSPG GGRRGSRGTT MVKKRKGRVV IDSDTEDSGS
 DENLDQELLS LAKRKRSDSE EKEPPVSQPA ASSDSETSDS DDEWTFGSNK NKKKGKARKI
 EKKGTMKKQA NKTASSGSSD KDSSAESSAP EEGEVSDSDS NSSSSSSDSD SSSEDEEFHD
 GYGEDLMGDE EDRARLEQMT EKEREQELFN RIEKREVLKR RFEIKKKLKT AKKKEKKEKK
 KKQEEEQEKK KLTQIQESQV TSHNKERRSK RDEKLDKKSQ AMEELKAERE KRKNRTAELL
 AKKQPLKTSE VYSDDEEEEE DDKSSEKSDR SSRTSSSDEE EEKEEIPPKS QPVSLPEELN
 RVRLSRHKLE RWCHMPFFAK TVTGCFVRIG IGNHNSKPVY RVAEITGVVE TAKVYQLGGT
 RTNKGLQLRH GNDQRVFRLE FVSNQEFTES EFMKWKEAMF SAGMQLPTLD EINKKELSIK
 EALNYKFNDQ DIEEIVKEKE RFRKAPPNYA MKKTQLLKEK AMAEDLGDQD KAKQIQDQLN
 ELEERAEALD RQRTKNISAI SYINQRNREW NIVESEKALV AESHNMKNQQ MDPFTRRQCK
 PTIVSNSRDP AVQAAILAQL NAKYGSGVLP DAPKEMSKGQ GKDKDLNSKS ASDLSEDLFK
 VHDFDVKIDL QVPSSESKAL AITSKAPPAK DGAPRRSLNL EDYKKRRGLI

Related products :