PAF1_MOUSE
ID PAF1_MOUSE Reviewed; 535 AA.
AC Q8K2T8; Q3UY97; Q9CS63; Q9JJ99;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=RNA polymerase II-associated factor 1 homolog;
GN Name=Paf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
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 [4]
RP FUNCTION.
RX PubMed=19345177; DOI=10.1016/j.stem.2009.03.009;
RA Ding L., Paszkowski-Rogacz M., Nitzsche A., Slabicki M.M., Heninger A.K.,
RA de Vries I., Kittler R., Junqueira M., Shevchenko A., Schulz H., Hubner N.,
RA Doss M.X., Sachinidis A., Hescheler J., Iacone R., Anastassiadis K.,
RA Stewart A.F., Pisabarro M.T., Caldarelli A., Poser I., Theis M.,
RA Buchholz F.;
RT "A genome-scale RNAi screen for Oct4 modulators defines a role of the Paf1
RT complex for embryonic stem cell identity.";
RL Cell Stem Cell 4:403-415(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=27749823; DOI=10.1038/ncb3424;
RA Strikoudis A., Lazaris C., Trimarchi T., Galvao Neto A.L., Yang Y.,
RA Ntziachristos P., Rothbart S., Buckley S., Dolgalev I., Stadtfeld M.,
RA Strahl B.D., Dynlacht B.D., Tsirigos A., Aifantis I.;
RT "Regulation of transcriptional elongation in pluripotency and cell
RT differentiation by the PHD-finger protein Phf5a.";
RL Nat. Cell Biol. 18:1127-1138(2016).
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.
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. Connects PAF1C with the RNF20/40 E3
CC ubiquitin-protein ligase complex. Involved in polyadenylation of mRNA
CC precursors (By similarity). {ECO:0000250, ECO:0000269|PubMed:19345177}.
CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1,
CC LEO1, CTR9, RTF1 and WDR61. The PAF1 complex interacts with PHF5A
CC (PubMed:27749823). Interacts with POLR2A, TCEA1, TTC37, KMT2A/MLL1,
CC SUPT5H, RNF20 and RNF40. Interacts with UBE2E1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8N7H5, ECO:0000269|PubMed:27749823}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Punctuate distribution throughout
CC the nucleus except in nucleoli and the perinuclear chromatin.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PAF1 family. {ECO:0000305}.
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DR EMBL; AB041615; BAA95098.1; -; mRNA.
DR EMBL; AK017762; BAB30913.1; -; mRNA.
DR EMBL; AK134857; BAE22315.1; -; mRNA.
DR EMBL; AK148538; BAE28608.1; -; mRNA.
DR EMBL; BC029843; AAH29843.1; -; mRNA.
DR EMBL; BC083337; AAH83337.1; -; mRNA.
DR CCDS; CCDS21043.1; -.
DR RefSeq; NP_062331.2; NM_019458.3.
DR AlphaFoldDB; Q8K2T8; -.
DR SMR; Q8K2T8; -.
DR BioGRID; 207692; 12.
DR IntAct; Q8K2T8; 9.
DR MINT; Q8K2T8; -.
DR STRING; 10090.ENSMUSP00000003529; -.
DR iPTMnet; Q8K2T8; -.
DR PhosphoSitePlus; Q8K2T8; -.
DR EPD; Q8K2T8; -.
DR MaxQB; Q8K2T8; -.
DR PaxDb; Q8K2T8; -.
DR PeptideAtlas; Q8K2T8; -.
DR PRIDE; Q8K2T8; -.
DR ProteomicsDB; 294149; -.
DR Antibodypedia; 30305; 231 antibodies from 27 providers.
DR DNASU; 54624; -.
DR Ensembl; ENSMUST00000003529; ENSMUSP00000003529; ENSMUSG00000003437.
DR GeneID; 54624; -.
DR KEGG; mmu:54624; -.
DR UCSC; uc009fyu.1; mouse.
DR CTD; 54623; -.
DR MGI; MGI:1923988; Paf1.
DR VEuPathDB; HostDB:ENSMUSG00000003437; -.
DR eggNOG; KOG2478; Eukaryota.
DR GeneTree; ENSGT00390000001474; -.
DR HOGENOM; CLU_021991_2_0_1; -.
DR InParanoid; Q8K2T8; -.
DR OMA; MRPDGIY; -.
DR OrthoDB; 599989at2759; -.
DR PhylomeDB; Q8K2T8; -.
DR TreeFam; TF313642; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR BioGRID-ORCS; 54624; 25 hits in 75 CRISPR screens.
DR PRO; PR:Q8K2T8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K2T8; protein.
DR Bgee; ENSMUSG00000003437; Expressed in ear vesicle and 259 other tissues.
DR Genevisible; Q8K2T8; MM.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IPI:UniProtKB.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0001711; P:endodermal cell fate commitment; IMP:UniProtKB.
DR GO; GO:0033523; P:histone H2B ubiquitination; ISO:MGI.
DR GO; GO:0010390; P:histone monoubiquitination; ISO:MGI.
DR GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR GO; GO:0031062; P:positive regulation of histone methylation; ISO:MGI.
DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; ISO:MGI.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
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 Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation;
KW Wnt signaling pathway.
FT CHAIN 1..535
FT /note="RNA polymerase II-associated factor 1 homolog"
FT /id="PRO_0000326401"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..535
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 483..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N7H5"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N7H5"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N7H5"
FT CONFLICT 227
FT /note="P -> L (in Ref. 1; BAA95098)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="R -> Q (in Ref. 1; BAE22315)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="Missing (in Ref. 1; BAE22315)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 60518 MW; 7A5EAB1284988070 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 EEEMEAEEKE AGGSDEEQEK GSSSEKEGSE DEHSGSESDR
EEGDRDEASD KSGSGEDESS EDEARAARDK EEIFGSDADS EDDADSDDED RGQAHRGSDN
DSDSGSDGGG QRSRSQSRSR SRSASPFPSG SEHSAQEDGS EAAASDSSEA DSDSD
