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 27-MAR-2024, entry version 163. DE RecName: Full=Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2; DE EC=3.1.3.16 {ECO:0000269|PubMed:30118681}; 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). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 2-ALA--LEU-32 AND RP 275-GLY--GLU-612. RX PubMed=30118681; DOI=10.1016/j.molcel.2018.06.038; RA Chang T.K., Lawrence D.A., Lu M., Tan J., Harnoss J.M., Marsters S.A., RA Liu P., Sandoval W., Martin S.E., Ashkenazi A.; RT "Coordination between Two Branches of the Unfolded Protein Response RT Determines Apoptotic Cell Fate."; RL Mol. Cell 71:629-636.e5(2018). 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 (PubMed:17643375, PubMed:22137580, CC PubMed:24997600). Downstream of EIF2AK3/PERK, dephosphorylates ERN1, a CC sensor for the endoplasmic reticulum unfolded protein response (UPR), CC to abort failed ER-stress adaptation and trigger apoptosis CC (PubMed:30118681). {ECO:0000269|PubMed:17643375, CC ECO:0000269|PubMed:22137580, ECO:0000269|PubMed:24997600, CC ECO:0000269|PubMed:30118681}. 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 Evidence={ECO:0000269|PubMed:30118681}; 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 EMDB; EMD-12087; -. DR EMDB; EMD-31450; -. DR SMR; Q8IXW5; -. DR BioGRID; 122959; 167. DR DIP; DIP-32939N; -. DR IntAct; Q8IXW5; 50. DR MINT; Q8IXW5; -. DR STRING; 9606.ENSP00000476948; -. DR DEPOD; SGPP2; -. DR GlyGen; Q8IXW5; 3 sites, 1 O-linked glycan (3 sites). 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; 9606-ENSP00000476948; -. DR PeptideAtlas; Q8IXW5; -. DR ProteomicsDB; 71070; -. [Q8IXW5-1] DR ProteomicsDB; 71071; -. [Q8IXW5-2] DR Pumba; Q8IXW5; -. DR Antibodypedia; 46923; 77 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 AGR; HGNC:25791; -. DR CTD; 79871; -. DR DisGeNET; 79871; -. DR GeneCards; RPAP2; -. DR HGNC; HGNC:25791; RPAP2. DR HPA; ENSG00000122484; Low tissue specificity. 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; WCTDETL; -. DR OrthoDB; 1410801at2759; -. 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; 709 hits in 1173 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 178 other cell types or tissues. 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:0097550; C:transcription preinitiation complex; 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:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB. 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:0036499; P:PERK-mediated unfolded protein response; IDA: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:SF0; RNA POLYMERASE II SUBUNIT B1 CTD PHOSPHATASE RPAP2-RELATED; 1. DR PANTHER; PTHR14732; UNCHARACTERIZED; 1. DR Pfam; PF04181; RPAP2_Rtr1; 1. DR PROSITE; PS51479; ZF_RTR1; 1. DR Genevisible; Q8IXW5; HS. 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 2..32 FT /note="Missing: Abolishes dephosphorylation of ERN1; when FT associated with 275-G--E-612 DEL." FT /evidence="ECO:0000269|PubMed:30118681" 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 MUTAGEN 275..612 FT /note="Missing: Abolishes dephosphorylation of ERN1; when FT associated with 2-A--L-32 DEL." FT /evidence="ECO:0000269|PubMed:30118681" 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 //