PAPOA_HUMAN
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 03-AUG-2022, entry version 202.
DE RecName: Full=Poly(A) polymerase alpha;
DE Short=PAP-alpha;
DE EC=2.7.7.19;
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).
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, AND FUNCTION.
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}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions. Also active with manganese. {ECO:0000250};
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. Nucleus. Note=The 90 kDa form is
CC nuclear while the 100 kDa and the 106 kDa forms are both nuclear and
CC cytoplasmic.
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 sumolyation 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}.
CC -!- PTM: Hyperphosphorylation on multiple CDK2 consensus and non-consensus
CC sites in the C-terminal Ser/Thr-rich region represses PAP activity in
CC late M-phase. Phosphorylation/dephosphorylation may regulate the
CC interaction between PAP and CPSF (By similarity). {ECO:0000250}.
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}.
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_001293628.1.
DR RefSeq; NP_001280561.1; NM_001293632.1.
DR RefSeq; NP_116021.2; NM_032632.4. [P51003-1]
DR AlphaFoldDB; P51003; -.
DR SMR; P51003; -.
DR BioGRID; 116119; 86.
DR CORUM; P51003; -.
DR DIP; DIP-27610N; -.
DR DIP; DIP-40865N; -.
DR IntAct; P51003; 17.
DR MINT; P51003; -.
DR STRING; 9606.ENSP00000216277; -.
DR DrugBank; DB02153; 3-sulfino-L-alanine.
DR DrugBank; DB01860; Cordycepin Triphosphate.
DR DrugBank; DB03896; Triphosphoric acid.
DR GlyGen; P51003; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P51003; -.
DR MetOSite; P51003; -.
DR PhosphoSitePlus; P51003; -.
DR BioMuta; PAPOLA; -.
DR DMDM; 59803092; -.
DR EPD; P51003; -.
DR jPOST; P51003; -.
DR MassIVE; P51003; -.
DR MaxQB; P51003; -.
DR PaxDb; P51003; -.
DR PeptideAtlas; P51003; -.
DR PRIDE; P51003; -.
DR ProteomicsDB; 56276; -. [P51003-1]
DR ProteomicsDB; 56277; -. [P51003-2]
DR Antibodypedia; 86; 148 antibodies from 22 providers.
DR DNASU; 10914; -.
DR Ensembl; ENST00000216277.13; ENSP00000216277.8; ENSG00000090060.19. [P51003-1]
DR Ensembl; ENST00000557320.5; ENSP00000450437.1; ENSG00000090060.19. [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 CTD; 10914; -.
DR DisGeNET; 10914; -.
DR GeneCards; PAPOLA; -.
DR HGNC; HGNC:14981; PAPOLA.
DR HPA; ENSG00000090060; Low tissue specificity.
DR MIM; 605553; gene.
DR neXtProt; NX_P51003; -.
DR OpenTargets; ENSG00000090060; -.
DR PharmGKB; PA32932; -.
DR VEuPathDB; HostDB:ENSG00000090060; -.
DR eggNOG; KOG2245; Eukaryota.
DR GeneTree; ENSGT00940000154598; -.
DR HOGENOM; CLU_011511_0_0_1; -.
DR InParanoid; P51003; -.
DR OMA; PAYPAMC; -.
DR PhylomeDB; P51003; -.
DR TreeFam; TF300842; -.
DR BRENDA; 2.7.7.19; 2681.
DR PathwayCommons; P51003; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
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 SABIO-RK; P51003; -.
DR SignaLink; P51003; -.
DR SIGNOR; P51003; -.
DR BioGRID-ORCS; 10914; 141 hits in 1083 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 210 other tissues.
DR ExpressionAtlas; P51003; baseline and differential.
DR Genevisible; P51003; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004652; F:polynucleotide adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:UniProtKB.
DR GO; GO:0031440; P:regulation of mRNA 3'-end processing; IDA:UniProtKB.
DR GO; GO:0043631; P:RNA polyadenylation; ISS:UniProtKB.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR011068; NuclTrfase_I-like_C.
DR InterPro; IPR007012; PolA_pol_cen_dom.
DR InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR InterPro; IPR014492; PolyA_polymerase.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF04928; PAP_central; 1.
DR Pfam; PF04926; PAP_RNA-bind; 1.
DR PIRSF; PIRSF018425; PolyA_polymerase; 1.
DR SUPFAM; SSF55003; SSF55003; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Isopeptide bond;
KW Magnesium; Manganese; Metal-binding; mRNA processing; Nucleotide-binding;
KW Nucleus; Phosphoprotein; 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 MOTIF 490..507
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 650..665
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 113..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
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"
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"
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"
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"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
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"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 246..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
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 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
