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RNA polymerase II-associated factor 1 homolog (hPAF1) (Pancreatic differentiation protein 2)

 PAF1_HUMAN              Reviewed;         531 AA.
Q8N7H5; M0QX35; O75239; Q9H166; Q9NUU9;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
08-APR-2008, sequence version 2.
20-JUN-2018, entry version 119.
RecName: Full=RNA polymerase II-associated factor 1 homolog;
Short=hPAF1;
AltName: Full=Pancreatic differentiation protein 2;
Name=PAF1; Synonyms=PD2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
INTERACTION WITH POLR2A, AND FUNCTION.
TISSUE=Fetal pancreas;
PubMed=16491129; DOI=10.1038/sj.onc.1209353;
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.;
"The human homologue of the RNA polymerase II-associated factor 1
(hPaf1), localized on the 19q13 amplicon, is associated with
tumorigenesis.";
Oncogene 25:3247-3257(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle, and Placenta;
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).
[6]
INTERACTION WITH TTC37.
PubMed=16024656; DOI=10.1101/gad.1292105;
Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H.,
Batra S.K., Tempst P., Reinberg D.;
"The human PAF complex coordinates transcription with events
downstream of RNA synthesis.";
Genes Dev. 19:1668-1673(2005).
[7]
INTERACTION WITH UBE2E1.
PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H.,
Tempst P., Reinberg D.;
"Monoubiquitination of human histone H2B: the factors involved and
their roles in HOX gene regulation.";
Mol. Cell 20:601-611(2005).
[8]
INTERACTION WITH CDC73 AND POLR2A.
PubMed=15923622; DOI=10.1128/MCB.25.12.5052-5060.2005;
Yart A., Gstaiger M., Wirbelauer C., Pecnik M., Anastasiou D.,
Hess D., Krek W.;
"The HRPT2 tumor suppressor gene product parafibromin associates with
human PAF1 and RNA polymerase II.";
Mol. Cell. Biol. 25:5052-5060(2005).
[9]
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).
[10]
FUNCTION OF THE PAF1 COMPLEX, AND INTERACTION WITH RNF20 AND RNF40.
PubMed=19410543; DOI=10.1016/j.cell.2009.02.027;
Kim J., Guermah M., McGinty R.K., Lee J.S., Tang Z., Milne T.A.,
Shilatifard A., Muir T.W., Roeder R.G.;
"RAD6-mediated transcription-coupled H2B ubiquitylation directly
stimulates H3K4 methylation in human cells.";
Cell 137:459-471(2009).
[11]
IDENTIFICATION IN THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX, AND
INTERACTION WITH SUPT5H.
PubMed=19952111; DOI=10.1101/gad.1834709;
Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T.,
Nakamura M., Hisatake K., Handa H.;
"DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative
roles in RNA polymerase II elongation.";
Genes Dev. 23:2765-2777(2009).
[12]
FUNCTION OF THE PAF1 COMPLEX, AND INTERACTION WITH KMT2A.
PubMed=20541477; DOI=10.1016/j.ccr.2010.04.012;
Muntean A.G., Tan J., Sitwala K., Huang Y., Bronstein J.,
Connelly J.A., Basrur V., Elenitoba-Johnson K.S., Hess J.L.;
"The PAF complex synergizes with MLL fusion proteins at HOX loci to
promote leukemogenesis.";
Cancer Cell 17:609-621(2010).
[13]
IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX,
FUNCTION OF THE PAF1 COMPLEX, AND INTERACTION WITH TCEA1.
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).
[14]
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).
[15]
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).
[16]
FUNCTION, AND FUNCTION OF THE PAF1 COMPLEX.
PubMed=21329879; DOI=10.1016/j.molcel.2011.01.022;
Nagaike T., Logan C., Hotta I., Rozenblatt-Rosen O., Meyerson M.,
Manley J.L.;
"Transcriptional activators enhance polyadenylation of mRNA
precursors.";
Mol. Cell 41:409-418(2011).
[17]
FUNCTION OF THE PAF1 COMPLEX, AND INTERACTION WITH INFLUENZA A NS1
PROTEIN.
PubMed=22419161; DOI=10.1038/nature10892;
Marazzi I., Ho J.S., Kim J., Manicassamy B., Dewell S., Albrecht R.A.,
Seibert C.W., Schaefer U., Jeffrey K.L., Prinjha R.K., Lee K.,
Garcia-Sastre A., Roeder R.G., Tarakhovsky A.;
"Suppression of the antiviral response by an influenza histone
mimic.";
Nature 483:428-433(2012).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-133 AND LYS-154, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- 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. 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. {ECO:0000269|PubMed:16491129,
ECO:0000269|PubMed:19410543, ECO:0000269|PubMed:19952111,
ECO:0000269|PubMed:20178742, ECO:0000269|PubMed:20541477,
ECO:0000269|PubMed:21329879, ECO:0000269|PubMed:22419161}.
-!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73,
PAF1, LEO1, CTR9, RTF1 and WDR61 (PubMed:19952111,
PubMed:20178742). The PAF1 complex interacts with PHF5A (By
similarity). Interacts with POLR2A, TCEA1, TTC37, KMT2A/MLL1,
SUPT5H, RNF20 and RNF40 (PubMed:15923622, PubMed:16024656,
PubMed:19952111, PubMed:20178742, PubMed:20541477,
PubMed:16491129, PubMed:19410543). Interacts with UBE2E1
(PubMed:16307923). Interacts with influenza A strain H3N2 NS1
protein; the interaction interferes with host cell gene
transcription, specifically with that of antiviral genes
(PubMed:22419161). {ECO:0000250|UniProtKB:Q8K2T8,
ECO:0000269|PubMed:15923622, ECO:0000269|PubMed:16024656,
ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16491129,
ECO:0000269|PubMed:19410543, ECO:0000269|PubMed:19952111,
ECO:0000269|PubMed:20178742, ECO:0000269|PubMed:20541477,
ECO:0000269|PubMed:22419161}.
-!- INTERACTION:
Q6P1J9:CDC73; NbExp=27; IntAct=EBI-2607770, EBI-930143;
Q6PD62:CTR9; NbExp=23; IntAct=EBI-2607770, EBI-1019583;
P51116:FXR2; NbExp=4; IntAct=EBI-2607770, EBI-740459;
P04792:HSPB1; NbExp=2; IntAct=EBI-2607770, EBI-352682;
Q03164:KMT2A; NbExp=4; IntAct=EBI-2607770, EBI-591370;
Q8WVC0:LEO1; NbExp=23; IntAct=EBI-2607770, EBI-932432;
B2BUF1:NS1 (xeno); NbExp=6; IntAct=EBI-2607770, EBI-4291940;
P24928:POLR2A; NbExp=5; IntAct=EBI-2607770, EBI-295301;
Q92541:RTF1; NbExp=16; IntAct=EBI-2607770, EBI-1055239;
P23193:TCEA1; NbExp=4; IntAct=EBI-2607770, EBI-2608271;
Q6PGP7:TTC37; NbExp=2; IntAct=EBI-2607770, EBI-6083436;
P51965:UBE2E1; NbExp=2; IntAct=EBI-2607770, EBI-348546;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16491129}.
Note=Punctuate distribution throughout the nucleus except in
nucleoli and the perinuclear chromatin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8N7H5-1; Sequence=Displayed;
Name=2;
IsoId=Q8N7H5-2; Sequence=VSP_032650, VSP_032651, VSP_032652;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8N7H5-3; Sequence=VSP_032650, VSP_055740, VSP_055741;
-!- SIMILARITY: Belongs to the PAF1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC25503.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=EAW56880.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=EAW56881.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PAF1ID44202ch19q13.html";
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EMBL; AJ401156; CAC20564.1; -; mRNA.
EMBL; AK001985; BAA92020.1; -; mRNA.
EMBL; AK098423; BAC05305.1; -; mRNA.
EMBL; AC005239; AAC25503.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471126; EAW56880.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471126; EAW56881.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471126; EAW56883.1; -; Genomic_DNA.
EMBL; BC000017; AAH00017.1; -; mRNA.
EMBL; BC013402; AAH13402.1; -; mRNA.
CCDS; CCDS12533.1; -. [Q8N7H5-1]
CCDS; CCDS59387.1; -. [Q8N7H5-3]
RefSeq; NP_001243755.1; NM_001256826.1. [Q8N7H5-3]
RefSeq; NP_061961.2; NM_019088.3. [Q8N7H5-1]
UniGene; Hs.466714; -.
PDB; 4M6T; X-ray; 2.50 A; A=170-250.
PDBsum; 4M6T; -.
ProteinModelPortal; Q8N7H5; -.
SMR; Q8N7H5; -.
BioGrid; 120081; 67.
CORUM; Q8N7H5; -.
DIP; DIP-48673N; -.
IntAct; Q8N7H5; 32.
MINT; Q8N7H5; -.
STRING; 9606.ENSP00000221265; -.
iPTMnet; Q8N7H5; -.
PhosphoSitePlus; Q8N7H5; -.
BioMuta; PAF1; -.
DMDM; 182670295; -.
EPD; Q8N7H5; -.
MaxQB; Q8N7H5; -.
PaxDb; Q8N7H5; -.
PeptideAtlas; Q8N7H5; -.
PRIDE; Q8N7H5; -.
ProteomicsDB; 72295; -.
ProteomicsDB; 72296; -. [Q8N7H5-2]
Ensembl; ENST00000221265; ENSP00000221265; ENSG00000006712. [Q8N7H5-1]
Ensembl; ENST00000595564; ENSP00000468874; ENSG00000006712. [Q8N7H5-3]
GeneID; 54623; -.
KEGG; hsa:54623; -.
UCSC; uc002old.5; human. [Q8N7H5-1]
CTD; 54623; -.
DisGeNET; 54623; -.
EuPathDB; HostDB:ENSG00000006712.14; -.
GeneCards; PAF1; -.
HGNC; HGNC:25459; PAF1.
HPA; HPA041875; -.
HPA; HPA043637; -.
MIM; 610506; gene.
neXtProt; NX_Q8N7H5; -.
OpenTargets; ENSG00000006712; -.
PharmGKB; PA142671206; -.
eggNOG; KOG2478; Eukaryota.
eggNOG; ENOG410YZXE; LUCA.
GeneTree; ENSGT00390000001474; -.
HOGENOM; HOG000115425; -.
HOVERGEN; HBG053131; -.
InParanoid; Q8N7H5; -.
KO; K15174; -.
OMA; DPRLDCA; -.
OrthoDB; EOG091G0C3Y; -.
PhylomeDB; Q8N7H5; -.
TreeFam; TF313642; -.
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; PAF1; human.
GenomeRNAi; 54623; -.
PRO; PR:Q8N7H5; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000006712; -.
CleanEx; HS_PAF1; -.
ExpressionAtlas; Q8N7H5; baseline and differential.
Genevisible; Q8N7H5; HS.
GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005737; C:cytoplasm; IDA:CACAO.
GO; GO:0016020; C:membrane; IDA:CACAO.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0000993; F:RNA polymerase II core binding; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
GO; GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
GO; GO:0006378; P:mRNA polyadenylation; IMP:UniProtKB.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0016584; P:nucleosome positioning; IMP:CACAO.
GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
GO; GO:0031062; P:positive regulation of histone methylation; IMP:CACAO.
GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; IMP:UniProtKB.
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:0034504; P:protein localization to nucleus; IMP:CACAO.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
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.
InterPro; IPR007133; RNA_pol_II-assoc_Paf1.
PANTHER; PTHR23188; PTHR23188; 2.
Pfam; PF03985; Paf1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Tumor suppressor;
Ubl conjugation; Wnt signaling pathway.
CHAIN 1 531 RNA polymerase II-associated factor 1
homolog.
/FTId=PRO_0000326400.
COILED 352 400 {ECO:0000255}.
COMPBIAS 358 452 Glu-rich.
MOD_RES 117 117 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 456 456 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K2T8}.
CROSSLNK 133 133 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 154 154 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 17 26 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032650.
VAR_SEQ 190 212 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_032651.
VAR_SEQ 395 508 DEEQEKGSSSEKEGSEDEHSGSESEREEGDRDEASDKSGSG
EDESSEDEARAARDKEEIFGSDADSEDDADSDDEDRGQAQG
GSDNDSDSGSNGGGQRSRSHSRSASPFPSGSE -> VMLIL
RTMPTLMMRTEDRPKVAVTMIQTAAAMGVASGAGATAAAPV
PSPVAASTRPRRMAVKLQLLIPVKLIVTVTESQGIQGWFRH
HYCEQQSTFLVVCL (in isoform 2).
{ECO:0000305}.
/FTId=VSP_032652.
VAR_SEQ 395 495 DEEQEKGSSSEKEGSEDEHSGSESEREEGDRDEASDKSGSG
EDESSEDEARAARDKEEIFGSDADSEDDADSDDEDRGQAQG
GSDNDSDSGSNGGGQRSRS -> VMLILRTMPTLMMRTEDR
PKVAVTMIQTAAAMGVASGAGATAAAPVPSPVAASTRPRRM
AVKLQLLIPVKLIVTVTESQGIQGWFRHHYCEQQSTFLVVC
L (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055740.
VAR_SEQ 496 531 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055741.
CONFLICT 58 58 F -> I (in Ref. 3; BAA92020).
{ECO:0000305}.
CONFLICT 68 68 K -> R (in Ref. 3; BAC05305).
{ECO:0000305}.
CONFLICT 152 152 E -> G (in Ref. 3; BAA92020).
{ECO:0000305}.
CONFLICT 378 378 E -> G (in Ref. 3; BAA92020).
{ECO:0000305}.
HELIX 172 187 {ECO:0000244|PDB:4M6T}.
STRAND 201 206 {ECO:0000244|PDB:4M6T}.
STRAND 211 215 {ECO:0000244|PDB:4M6T}.
STRAND 231 234 {ECO:0000244|PDB:4M6T}.
STRAND 238 241 {ECO:0000244|PDB:4M6T}.
HELIX 246 249 {ECO:0000244|PDB:4M6T}.
TURN 250 252 {ECO:0000244|PDB:4M6T}.
STRAND 253 259 {ECO:0000244|PDB:4M6T}.
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


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