ID PAPOA_HUMAN Reviewed; 745 AA. AC P51003; Q86SX4; Q86TV0; Q8IYF5; Q9BVU2; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 04-NOV-2026, entry version 221. DE RecName: Full=Poly(A) polymerase alpha; DE Short=PAP-alpha; DE EC=2.7.7.19 {ECO:0000269|PubMed:19224921, ECO:0000269|PubMed:8302877}; DE AltName: Full=Polynucleotide adenylyltransferase alpha; GN Name=PAPOLA; Synonyms=PAP; 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] (ISOFORMS 1 AND 2). RC TISSUE=Placenta, and Testis; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-725 (ISOFORMS 1 AND 2). RC TISSUE=B-cell, and Fetal brain; RA Li W.B., Gruber C., Jessee J., Polayes D.; RT "Full-length cDNA libraries and normalization."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-660 (ISOFORM 1), SUBCELLULAR LOCATION, RP FUNCTION, CATALYTIC ACTIVITY, AND PHOSPHORYLATION. RX PubMed=8302877; DOI=10.1073/pnas.91.3.979; RA Thuresson A.-C., Aastroem J., Aastroem A., Groenvik K.-O., Virtanen A.; RT "Multiple forms of poly(A) polymerases in human cells."; RL Proc. Natl. Acad. Sci. U.S.A. 91:979-983(1994). RN [4] RP INTERACTION WITH NUDT21/CPSF5. RX PubMed=15169763; DOI=10.1074/jbc.m403927200; RA Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M.; RT "Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im RT mediate RNA binding, protein-protein interactions, and subcellular RT localization."; RL J. Biol. Chem. 279:35788-35797(2004). RN [5] RP IDENTIFICATION IN A COMPLEX WITH CPSF1 AND FIP1L1, AND INTERACTION WITH RP FIP1L1. RX PubMed=14749727; DOI=10.1038/sj.emboj.7600070; RA Kaufmann I., Martin G., Friedlein A., Langen H., Keller W.; RT "Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and RT stimulates poly(A) polymerase."; RL EMBO J. 23:616-626(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, 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 [7] RP INTERACTION WITH AHCYL1 AND FIP1L1, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19224921; DOI=10.1074/jbc.m807136200; RA Kiefer H., Mizutani A., Iemura S., Natsume T., Ando H., Kuroda Y., RA Mikoshiba K.; RT "Inositol 1,4,5-triphosphate receptor-binding protein released with RT inositol 1,4,5-triphosphate (IRBIT) associates with components of the mRNA RT 3' processing machinery in a phosphorylation-dependent manner and inhibits RT polyadenylation."; RL J. Biol. Chem. 284:10694-10705(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-24 AND SER-738, 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. Also CC required for the endoribonucleolytic cleavage reaction at some CC polyadenylation sites. May acquire specificity through interaction with CC a cleavage and polyadenylation specificity factor (CPSF) at its C- CC terminus. {ECO:0000269|PubMed:19224921, ECO:0000269|PubMed:8302877}. CC -!- CATALYTIC ACTIVITY: CC Reaction=RNA(n) + ATP = RNA(n)-3'-adenine ribonucleotide + diphosphate; CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, CC ChEBI:CHEBI:173115; EC=2.7.7.19; CC Evidence={ECO:0000269|PubMed:19224921, ECO:0000269|PubMed:8302877}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333; CC Evidence={ECO:0000305|PubMed:19224921}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P25500}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:P25500}; CC Note=Binds 2 magnesium ions. Also active with manganese. CC {ECO:0000250|UniProtKB:P25500}; CC -!- SUBUNIT: Monomer. Found in a complex with CPSF1, FIP1L1 and PAPOLA. CC Interacts with AHCYL1 and FIP1L1; the interaction with AHCYL1 seems to CC increase interaction with FIP1L1 (PubMed:19224921). Interacts with CC NUDT21; the interaction is diminished by acetylation. Interacts with CC KPNB1; the interaction promotes PAP nuclear import and is inhibited by CC acetylation of PAP (By similarity). {ECO:0000250|UniProtKB:P25500, CC ECO:0000250|UniProtKB:Q61183, ECO:0000269|PubMed:19224921}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8302877}. Nucleus CC {ECO:0000269|PubMed:8302877}. Note=The 90 kDa form is nuclear while the CC 100 kDa and the 106 kDa forms are both nuclear and cytoplasmic. CC {ECO:0000269|PubMed:8302877}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P51003-1; Sequence=Displayed; CC Name=2; CC IsoId=P51003-2; Sequence=VSP_012895, VSP_012896; CC -!- PTM: Polysumoylated. Varying sumoylation depending on tissue- and cell- CC type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is CC required for nuclear localization and enhances PAP stability. CC Desumoylated by SENP1. Inhibits polymerase activity (By similarity). CC {ECO:0000250|UniProtKB:Q61183}. CC -!- PTM: Phosphorylated (PubMed:8302877). Hyperphosphorylation on multiple CC CDK2 consensus and non-consensus sites in the C-terminal Ser/Thr-rich CC region represses PAP activity in late M-phase (By similarity). CC Phosphorylation/dephosphorylation may regulate the interaction between CC PAP and CPSF (PubMed:8302877). {ECO:0000250|UniProtKB:P25500, CC ECO:0000269|PubMed:8302877}. CC -!- PTM: Acetylated in the C-terminus. Acetylation decreases interaction CC with NUDT21 and KPNB1, and inhibits nuclear localization through CC inhibiting binding to the importin alpha/beta complex (By similarity). CC {ECO:0000250|UniProtKB:P25500}. CC -!- SIMILARITY: Belongs to the poly(A) polymerase family. {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; BC000927; AAH00927.1; -; mRNA. DR EMBL; BC036014; AAH36014.1; -; mRNA. DR EMBL; BX248301; CAD62628.1; -; mRNA. DR EMBL; BX248753; CAD66560.1; -; mRNA. DR EMBL; BX161482; CAD61935.1; -; mRNA. DR EMBL; X76770; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS58334.1; -. [P51003-2] DR CCDS; CCDS9946.1; -. [P51003-1] DR RefSeq; NP_001238935.1; NM_001252006.1. [P51003-2] DR RefSeq; NP_001238936.1; NM_001252007.1. DR RefSeq; NP_001280556.1; NM_001293627.1. DR RefSeq; NP_001280557.1; NM_001293628.2. DR RefSeq; NP_001280561.1; NM_001293632.3. DR RefSeq; NP_116021.2; NM_032632.5. [P51003-1] DR PDB; 8R8R; EM; 2.79 A; D=720-745. DR AlphaFoldDB; P51003; -. DR SMR; P51003; -. DR BioGRID; 116119; 108. DR CORUM; P51003; -. DR DIP; DIP-27610N; -. DR DIP; DIP-40865N; -. DR FunCoup; P51003; 5346. DR IntAct; P51003; 31. DR NDEx; IQUERY-CP-PAPOLA; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000216277; -. DR DrugBank; DB02153; 3-sulfino-L-alanine. DR DrugBank; DB01860; Cordycepin Triphosphate. DR DrugBank; DB03896; Triphosphoric acid. DR GlyCosmos; P51003; 11 sites, 2 glycans. DR GlyGen; P51003; 12 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (8 sites). DR iPTMnet; P51003; -. DR MetOSite; P51003; -. DR PhosphoSitePlus; P51003; -. DR BioMuta; PAPOLA; -. DR DMDM; 59803092; -. DR jPOST; P51003; -. DR MassIVE; P51003; -. DR PaxDb; 9606-ENSP00000216277; -. DR PeptideAtlas; P51003; -. DR ProteomicsDB; 56276; -. [P51003-1] DR ProteomicsDB; 56277; -. [P51003-2] DR Pumba; P51003; -. DR Antibodypedia; 86; 153 antibodies from 24 providers. DR DNASU; 10914; -. DR Ensembl; ENST00000216277.13; ENSP00000216277.8; ENSG00000090060.20. [P51003-1] DR Ensembl; ENST00000557320.5; ENSP00000450437.1; ENSG00000090060.20. [P51003-2] DR GeneID; 10914; -. DR KEGG; hsa:10914; -. DR MANE-Select; ENST00000216277.13; ENSP00000216277.8; NM_032632.5; NP_116021.2. DR UCSC; uc001yfo.5; human. [P51003-1] DR AGR; HGNC:14981; -. DR ClinPGx; PA32932; -. DR CTD; 10914; -. DR DisGeNET; 10914; -. DR GeneCards; PAPOLA; -. DR HGNC; HGNC:14981; PAPOLA. DR HPA; ENSG00000090060; Low tissue specificity. DR MIM; 605553; gene. DR OpenTargets; ENSG00000090060; -. DR VEuPathDB; HostDB:ENSG00000090060; -. DR eggNOG; KOG2245; Eukaryota. DR GeneTree; ENSGT00940000154598; -. DR HOGENOM; CLU_011511_0_0_1; -. DR InParanoid; P51003; -. DR OMA; AACQSWD; -. DR OrthoDB; 412748at2759; -. DR PAN-GO; P51003; 2 GO annotations based on evolutionary models. DR PhylomeDB; P51003; -. DR BRENDA; 2.7.7.19; 2681. DR PathwayCommons; P51003; -. DR Reactome; R-HSA-72187; mRNA 3'-end processing. DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination. DR Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs. DR Reactome; R-HSA-9770562; mRNA Polyadenylation. DR Reactome; R-HSA-9918481; Dengue Virus-Host Interactions. DR SABIO-RK; P51003; -. DR SignaLink; P51003; -. DR SIGNOR; P51003; -. DR Agora; ENSG00000090060; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 10914; 149 hits in 1161 CRISPR screens. DR ChiTaRS; PAPOLA; human. DR GeneWiki; PAPOLA; -. DR GenomeRNAi; 10914; -. DR Pharos; P51003; Tbio. DR PRO; PR:P51003; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; P51003; protein. DR Bgee; ENSG00000090060; Expressed in colonic epithelium and 212 other cell types or tissues. DR ExpressionAtlas; P51003; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB. DR GO; GO:1990817; F:poly(A) RNA polymerase activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0180010; P:co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway; IDA:UniProtKB. DR GO; GO:0031124; P:mRNA 3'-end processing; IDA:UniProtKB. DR CDD; cd05402; NT_PAP_TUTase; 1. DR FunFam; 1.10.1410.10:FF:000021; poly(A) polymerase alpha isoform X7; 1. DR FunFam; 3.30.460.10:FF:000002; Poly(A) polymerase alpha, putative; 1. DR FunFam; 3.30.70.590:FF:000001; Putative poly(A) polymerase gamma; 1. DR Gene3D; 1.10.1410.10; -; 1. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1. DR Gene3D; 3.30.70.590; Poly(A) polymerase predicted RNA binding domain; 1. DR InterPro; IPR043519; NT_sf. DR InterPro; IPR011068; NuclTrfase_I-like_C. DR InterPro; IPR007012; PolA_pol_cen_dom. DR InterPro; IPR048840; PolA_pol_NTPase. DR InterPro; IPR007010; PolA_pol_RNA-bd_dom. DR InterPro; IPR014492; PolyA_polymerase. DR PANTHER; PTHR10682; POLY A POLYMERASE; 1. DR PANTHER; PTHR10682:SF9; POLY(A) POLYMERASE ALPHA; 1. DR Pfam; PF04928; PAP_central; 1. DR Pfam; PF20750; PAP_NTPase; 1. DR Pfam; PF04926; PAP_RNA-bind; 1. DR PIRSF; PIRSF018425; PolyA_polymerase; 1. DR SUPFAM; SSF81301; Nucleotidyltransferase; 1. DR SUPFAM; SSF55003; PAP/Archaeal CCA-adding enzyme, C-terminal domain; 1. DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm; KW Isopeptide bond; Magnesium; Manganese; Metal-binding; mRNA processing; KW Nucleotide-binding; Nucleus; Oxidation; Phosphoprotein; KW Proteomics identification; Reference proteome; RNA-binding; Transferase; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..745 FT /note="Poly(A) polymerase alpha" FT /id="PRO_0000051612" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 508..643 FT /note="Ser/Thr-rich" FT REGION 523..565 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 577..704 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 677..745 FT /note="Required for interaction with NUDT21" FT /evidence="ECO:0000250|UniProtKB:P25500" FT MOTIF 490..507 FT /note="Nuclear localization signal 1" FT /evidence="ECO:0000250|UniProtKB:P25500" FT MOTIF 650..665 FT /note="Nuclear localization signal 2" FT /evidence="ECO:0000250|UniProtKB:P25500" FT COMPBIAS 1..17 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 523..534 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 535..557 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 583..594 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 611..640 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 655..666 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 682..692 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 694..704 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 102 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P25500" FT BINDING 109 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P25500" FT BINDING 113 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P25500" FT BINDING 113 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P25500" FT BINDING 115 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P25500" FT BINDING 115 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P25500" FT BINDING 167 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P25500" FT BINDING 167 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P25500" FT BINDING 228 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P25500" FT BINDING 237 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P25500" FT BINDING 247 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P25500" FT SITE 153 FT /note="Interaction with RNA" FT /evidence="ECO:0000250" FT SITE 158 FT /note="Interaction with RNA" FT /evidence="ECO:0000250" FT SITE 328 FT /note="Interaction with RNA" FT /evidence="ECO:0000250" FT SITE 399 FT /note="Interaction with RNA" FT /evidence="ECO:0000250" FT SITE 524 FT /note="Interaction with RNA" FT /evidence="ECO:0000250" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 36 FT /note="Cysteine sulfinic acid (-SO2H)" FT /evidence="ECO:0000250|UniProtKB:P25500" FT MOD_RES 160 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000250|UniProtKB:P25500" FT MOD_RES 197 FT /note="Cysteine sulfinic acid (-SO2H)" FT /evidence="ECO:0000250|UniProtKB:P25500" FT MOD_RES 537 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61183" FT MOD_RES 558 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 641 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P25500" FT MOD_RES 650 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P25500" FT MOD_RES 736 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P25500" FT MOD_RES 738 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 740 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P25500" FT CROSSLNK 444 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000305" FT CROSSLNK 445 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000305" FT CROSSLNK 506 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000305" FT CROSSLNK 507 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000305" FT CROSSLNK 736 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250" FT CROSSLNK 740 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250" FT VAR_SEQ 280..285 FT /note="EWPNPV -> YVFRLY (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2" FT /id="VSP_012895" FT VAR_SEQ 286..745 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2" FT /id="VSP_012896" FT CONFLICT 2..3 FT /note="PF -> GTSNSPGHSSFSAPSTKKIKTTRKQNIAWC (in Ref. 2; FT CAD62628)" FT /evidence="ECO:0000305" FT CONFLICT 204..238 FT /note="CRVTDEILHLVPNIDNFRLTLRAIKLWAKRHNIYS -> MRKPTSFCVLQFL FT SDISCFYTSFVLKLFIAILLTQ (in Ref. 2; CAD61935)" FT /evidence="ECO:0000305" SQ SEQUENCE 745 AA; 82843 MW; 14A00CCCDAD9B374 CRC64; MPFPVTTQGS QQTQPPQKHY GITSPISLAA PKETDCVLTQ KLIETLKPFG VFEEEEELQR RILILGKLNN LVKEWIREIS ESKNLPQSVI ENVGGKIFTF GSYRLGVHTK GADIDALCVA PRHVDRSDFF TSFYDKLKLQ EEVKDLRAVE EAFVPVIKLC FDGIEIDILF ARLALQTIPE DLDLRDDSLL KNLDIRCIRS LNGCRVTDEI LHLVPNIDNF RLTLRAIKLW AKRHNIYSNI LGFLGGVSWA MLVARTCQLY PNAIASTLVH KFFLVFSKWE WPNPVLLKQP EECNLNLPVW DPRVNPSDRY HLMPIITPAY PQQNSTYNVS VSTRMVMVEE FKQGLAITDE ILLSKAEWSK LFEAPNFFQK YKHYIVLLAS APTEKQRLEW VGLVESKIRI LVGSLEKNEF ITLAHVNPQS FPAPKENPDK EEFRTMWVIG LVFKKTENSE NLSVDLTYDI QSFTDTVYRQ AINSKMFEVD MKIAAMHVKR KQLHQLLPNH VLQKKKKHST EGVKLTALND SSLDLSMDSD NSMSVPSPTS ATKTSPLNSS GSSQGRNSPA PAVTAASVTN IQATEVSVPQ VNSSESSGGT SSESIPQTAT QPAISPPPKP TVSRVVSSTR LVNPPPRSSG NAATSGNAAT KIPTPIVGVK RTSSPHKEES PKKTKTEEDE TSEDANCLAL SGHDKTEAKE QLDTETSTTQ SETIQTAASL LASQKTSSTD LSDIPALPAN PIPVIKNSIK LRLNR //