RPAP2_HUMAN
ID RPAP2_HUMAN Reviewed; 612 AA.
AC Q8IXW5; C9JKB5; Q49AS7; Q9H8Y2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2;
DE EC=3.1.3.16;
DE AltName: Full=RNA polymerase II-associated protein 2;
GN Name=RPAP2; Synonyms=C1orf82;
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 [LARGE SCALE MRNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP RNA POLYMERASE II COMPLEX.
RX PubMed=17643375; DOI=10.1016/j.molcel.2007.06.027;
RA Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C.,
RA Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B.,
RA Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.;
RT "Systematic analysis of the protein interaction network for the human
RT transcription machinery reveals the identity of the 7SK capping enzyme.";
RL Mol. Cell 27:262-274(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX.
RX PubMed=22231121; DOI=10.4161/trns.2.5.17803;
RA Ni Z., Olsen J.B., Guo X., Zhong G., Ruan E.D., Marcon E., Young P.,
RA Guo H., Li J., Moffat J., Emili A., Greenblatt J.F.;
RT "Control of the RNA polymerase II phosphorylation state in promoter regions
RT by CTD interaction domain-containing proteins RPRD1A and RPRD1B.";
RL Transcription 2:237-242(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-100; CYS-105;
RP CYS-136 AND CYS-140.
RX PubMed=22137580; DOI=10.1016/j.molcel.2011.11.006;
RA Egloff S., Zaborowska J., Laitem C., Kiss T., Murphy S.;
RT "Ser7 phosphorylation of the CTD recruits the RPAP2 Ser5 phosphatase to
RT snRNA genes.";
RL Mol. Cell 45:111-122(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-433, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [11]
RP FUNCTION.
RX PubMed=24997600; DOI=10.1038/nsmb.2853;
RA Ni Z., Xu C., Guo X., Hunter G.O., Kuznetsova O.V., Tempel W., Marcon E.,
RA Zhong G., Guo H., Kuo W.H., Li J., Young P., Olsen J.B., Wan C.,
RA Loppnau P., El Bakkouri M., Senisterra G.A., He H., Huang H., Sidhu S.S.,
RA Emili A., Murphy S., Mosley A.L., Arrowsmith C.H., Min J., Greenblatt J.F.;
RT "RPRD1A and RPRD1B are human RNA polymerase II C-terminal domain scaffolds
RT for Ser5 dephosphorylation.";
RL Nat. Struct. Mol. Biol. 21:686-695(2014).
CC -!- FUNCTION: Protein phosphatase that displays CTD phosphatase activity
CC and regulates transcription of snRNA genes. Recognizes and binds
CC phosphorylated 'Ser-7' of the C-terminal heptapeptide repeat domain
CC (CTD) of the largest RNA polymerase II subunit POLR2A, and mediates
CC dephosphorylation of 'Ser-5' of the CTD, thereby promoting
CC transcription of snRNA genes. {ECO:0000269|PubMed:17643375,
CC ECO:0000269|PubMed:22137580, ECO:0000269|PubMed:24997600}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Associates with the RNA polymerase II complex. Interacts with
CC transcribing RNA polymerase II phosphorylated on 'Ser-7' on CTD.
CC {ECO:0000269|PubMed:17643375, ECO:0000269|PubMed:22231121}.
CC -!- INTERACTION:
CC Q8IXW5; Q9HCN4: GPN1; NbExp=6; IntAct=EBI-395878, EBI-745137;
CC Q8IXW5; Q9NWS0: PIH1D1; NbExp=5; IntAct=EBI-395878, EBI-357318;
CC Q8IXW5; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-395878, EBI-742388;
CC Q8IXW5; Q96P16-1: RPRD1A; NbExp=3; IntAct=EBI-395878, EBI-16112633;
CC Q8IXW5; Q9NQG5: RPRD1B; NbExp=4; IntAct=EBI-395878, EBI-747925;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22137580}. Nucleus
CC {ECO:0000269|PubMed:22137580}. Note=Shuttles between the cytoplasm and
CC the nucleus in a CRM1-dependent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IXW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IXW5-2; Sequence=VSP_020680, VSP_020681;
CC -!- DOMAIN: The RTR1-type zinc finger mediates interactions with RNA
CC polymerase II complex subunits. {ECO:0000269|PubMed:22137580}.
CC -!- SIMILARITY: Belongs to the RPAP2 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00812, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK023212; BAB14465.1; -; mRNA.
DR EMBL; AL451010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031070; AAH31070.1; -; mRNA.
DR EMBL; BC039014; AAH39014.1; -; mRNA.
DR CCDS; CCDS740.1; -. [Q8IXW5-1]
DR RefSeq; NP_079089.2; NM_024813.2. [Q8IXW5-1]
DR PDB; 7B7U; EM; 2.80 A; M=1-612.
DR PDB; 7F4G; EM; 2.78 A; R=1-612.
DR PDBsum; 7B7U; -.
DR PDBsum; 7F4G; -.
DR AlphaFoldDB; Q8IXW5; -.
DR SMR; Q8IXW5; -.
DR BioGRID; 122959; 145.
DR DIP; DIP-32939N; -.
DR IntAct; Q8IXW5; 50.
DR MINT; Q8IXW5; -.
DR STRING; 9606.ENSP00000476948; -.
DR DEPOD; SGPP2; -.
DR iPTMnet; Q8IXW5; -.
DR PhosphoSitePlus; Q8IXW5; -.
DR BioMuta; RPAP2; -.
DR DMDM; 74750745; -.
DR EPD; Q8IXW5; -.
DR jPOST; Q8IXW5; -.
DR MassIVE; Q8IXW5; -.
DR MaxQB; Q8IXW5; -.
DR PaxDb; Q8IXW5; -.
DR PeptideAtlas; Q8IXW5; -.
DR PRIDE; Q8IXW5; -.
DR ProteomicsDB; 71070; -. [Q8IXW5-1]
DR ProteomicsDB; 71071; -. [Q8IXW5-2]
DR Antibodypedia; 46923; 64 antibodies from 20 providers.
DR DNASU; 79871; -.
DR Ensembl; ENST00000610020.2; ENSP00000476948.1; ENSG00000122484.9. [Q8IXW5-1]
DR GeneID; 79871; -.
DR KEGG; hsa:79871; -.
DR MANE-Select; ENST00000610020.2; ENSP00000476948.1; NM_024813.3; NP_079089.2.
DR UCSC; uc001dot.3; human. [Q8IXW5-1]
DR CTD; 79871; -.
DR DisGeNET; 79871; -.
DR GeneCards; RPAP2; -.
DR HGNC; HGNC:25791; RPAP2.
DR HPA; ENSG00000122484; Tissue enhanced (brain).
DR MIM; 611476; gene.
DR neXtProt; NX_Q8IXW5; -.
DR OpenTargets; ENSG00000122484; -.
DR PharmGKB; PA162401981; -.
DR VEuPathDB; HostDB:ENSG00000122484; -.
DR eggNOG; KOG4780; Eukaryota.
DR GeneTree; ENSGT00390000017965; -.
DR HOGENOM; CLU_019258_1_0_1; -.
DR InParanoid; Q8IXW5; -.
DR OMA; DFLIDCA; -.
DR OrthoDB; 1506260at2759; -.
DR PhylomeDB; Q8IXW5; -.
DR TreeFam; TF331431; -.
DR PathwayCommons; Q8IXW5; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q8IXW5; -.
DR SIGNOR; Q8IXW5; -.
DR BioGRID-ORCS; 79871; 678 hits in 1090 CRISPR screens.
DR ChiTaRS; RPAP2; human.
DR GeneWiki; RPAP2; -.
DR GenomeRNAi; 79871; -.
DR Pharos; Q8IXW5; Tbio.
DR PRO; PR:Q8IXW5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8IXW5; protein.
DR Bgee; ENSG00000122484; Expressed in calcaneal tendon and 177 other tissues.
DR Genevisible; Q8IXW5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0043175; F:RNA polymerase core enzyme binding; IEA:InterPro.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IMP:UniProtKB.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IMP:UniProtKB.
DR GO; GO:0009301; P:snRNA transcription; IMP:UniProtKB.
DR Gene3D; 1.25.40.820; -; 1.
DR InterPro; IPR039693; Rtr1/RPAP2.
DR InterPro; IPR007308; Rtr1/RPAP2_dom.
DR InterPro; IPR038534; Rtr1/RPAP2_sf.
DR PANTHER; PTHR14732; PTHR14732; 1.
DR Pfam; PF04181; RPAP2_Rtr1; 1.
DR PROSITE; PS51479; ZF_RTR1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Hydrolase; Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..612
FT /note="Putative RNA polymerase II subunit B1 CTD
FT phosphatase RPAP2"
FT /id="PRO_0000250648"
FT ZN_FING 77..160
FT /note="RTR1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 33..68
FT /evidence="ECO:0000255"
FT COMPBIAS 201..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5I0E6"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 563..596
FT /note="LLTPILGIQKHSQEGMVFTRFLDTLLEELHLKNE -> FLLNVKTRIKTFMM
FT IYFHLMNS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020680"
FT VAR_SEQ 597..612
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020681"
FT MUTAGEN 100
FT /note="C->A: Abolishes interaction with RNA polymerase II
FT complex subunits; when associated with A-105."
FT /evidence="ECO:0000269|PubMed:22137580"
FT MUTAGEN 105
FT /note="C->A: Abolishes interaction with RNA polymerase II
FT complex subunits; when associated with A-100."
FT /evidence="ECO:0000269|PubMed:22137580"
FT MUTAGEN 136
FT /note="C->A: Abolishes interaction with RNA polymerase II
FT complex subunits; when associated with A-140."
FT /evidence="ECO:0000269|PubMed:22137580"
FT MUTAGEN 140
FT /note="C->A: Abolishes interaction with RNA polymerase II
FT complex subunits; when associated with A-136."
FT /evidence="ECO:0000269|PubMed:22137580"
FT CONFLICT 421
FT /note="P -> R (in Ref. 3; AAH31070)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="Y -> C (in Ref. 1; BAB14465)"
FT /evidence="ECO:0000305"
FT HELIX 44..65
FT /evidence="ECO:0007829|PDB:7F4G"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:7F4G"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:7F4G"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:7F4G"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:7F4G"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:7F4G"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:7F4G"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:7F4G"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:7F4G"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:7F4G"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:7F4G"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:7F4G"
FT HELIX 163..182
FT /evidence="ECO:0007829|PDB:7F4G"
FT CONFLICT Q8IXW5-2:584
FT /note="S -> N (in Ref. 3; AAH31070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 612 AA; 69509 MW; 43D6DE7C30BB5C96 CRC64;
MADFAGPSSA GRKAGAPRCS RKAAGTKQTS TLKQEDASKR KAELEAAVRK KIEFERKALH
IVEQLLEENI TEEFLMECGR FITPAHYSDV VDERSIVKLC GYPLCQKKLG IVPKQKYKIS
TKTNKVYDIT ERKSFCSNFC YQASKFFEAQ IPKTPVWVRE EERHPDFQLL KEEQSGHSGE
EVQLCSKAIK TSDIDNPSHF EKQYESSSSS THSDSSSDNE QDFVSSILPG NRPNSTNIRP
QLHQKSIMKK KAGHKANSKH KDKEQTVVDV TEQLGDCKLD SQEKDATCEL PLQKVNTQSS
SNSTLPERLK ASENSESEYS RSEITLVGIS KKSAEHFKRK FAKSNQVSRS VSSSVQVCPE
VGKRNLLKVL KETLIEWKTE ETLRFLYGQN YASVCLKPEA SLVKEELDED DIISDPDSHF
PAWRESQNSL DESLPFRGSG TAIKPLPSYE NLKKETEKLN LRIREFYRGR YVLGEETTKS
QDSEEHDSTF PLIDSSSQNQ IRKRIVLEKL SKVLPGLLVP LQITLGDIYT QLKNLVRTFR
LTNRNIIHKP AEWTLIAMVL LSLLTPILGI QKHSQEGMVF TRFLDTLLEE LHLKNEDLES
LTIIFRTSCL PE
