ID   DBR1_HUMAN              Reviewed;         544 AA.
AC   Q9UK59; Q96GH0; Q9NXQ6;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Lariat debranching enzyme;
DE            EC=3.1.4.- {ECO:0000269|PubMed:2435736};
GN   Name=DBR1;
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 [MRNA] (ISOFORM 1), AND FUNCTION.
RX   PubMed=10982890; DOI=10.1093/nar/28.18.3666;
RA   Kim J.-W., Kim H.-C., Kim G.-M., Yang J.-M., Boeke J.D., Nam K.;
RT   "Human RNA lariat debranching enzyme cDNA complements the phenotypes of
RT   Saccharomyces cerevisiae dbr1 and Schizosaccharomyces pombe dbr1 mutants.";
RL   Nucleic Acids Res. 28:3666-3673(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Colon;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=2435736; DOI=10.1016/s0021-9258(18)61343-2;
RA   Arenas J., Hurwitz J.;
RT   "Purification of a RNA debranching activity from HeLa cells.";
RL   J. Biol. Chem. 262:4274-4279(1987).
RN   [5]
RP   FUNCTION.
RX   PubMed=16232320; DOI=10.1186/1742-4690-2-63;
RA   Ye Y., De Leon J., Yokoyama N., Naidu Y., Camerini D.;
RT   "DBR1 siRNA inhibition of HIV-1 replication.";
RL   Retrovirology 2:63-63(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; SER-478 AND SER-479, AND
RP   IDENTIFICATION BY 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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, AND IDENTIFICATION BY
RP   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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-464, 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).
RN   [14]
RP   INVOLVEMENT IN IIAE11, VARIANTS IIAE11 GLY-13; HIS-17; THR-120 AND
RP   197-ARG--ALA-544 DEL, CHARACTERIZATION OF VARIANTS IIAE11 GLY-13; HIS-17;
RP   THR-120 AND 197-ARG--ALA-544 DEL, FUNCTION, TISSUE SPECIFICITY, AND
RP   MUTAGENESIS OF HIS-85.
RX   PubMed=29474921; DOI=10.1016/j.cell.2018.02.019;
RA   Zhang S.Y., Clark N.E., Freije C.A., Pauwels E., Taggart A.J., Okada S.,
RA   Mandel H., Garcia P., Ciancanelli M.J., Biran A., Lafaille F.G.,
RA   Tsumura M., Cobat A., Luo J., Volpi S., Zimmer B., Sakata S., Dinis A.,
RA   Ohara O., Garcia Reino E.J., Dobbs K., Hasek M., Holloway S.P.,
RA   McCammon K., Hussong S.A., DeRosa N., Van Skike C.E., Katolik A.,
RA   Lorenzo L., Hyodo M., Faria E., Halwani R., Fukuhara R., Smith G.A.,
RA   Galvan V., Damha M.J., Al-Muhsen S., Itan Y., Boeke J.D., Notarangelo L.D.,
RA   Studer L., Kobayashi M., Diogo L., Fairbrother W.G., Abel L.,
RA   Rosenberg B.R., Hart P.J., Etzioni A., Casanova J.L.;
RT   "Inborn Errors of RNA Lariat Metabolism in Humans with Brainstem Viral
RT   Infection.";
RL   Cell 172:952.e18-965.e18(2018).
CC   -!- FUNCTION: Cleaves the 2'-5' phosphodiester linkage at the branch point
CC       of excised lariat intron RNA and converts them into linear molecules
CC       that can be subsequently degraded, thereby facilitating ribonucleotide
CC       turnover (PubMed:10982890, PubMed:2435736, PubMed:16232320). Linked to
CC       its role in pre-mRNA processing mechanism, may also participate in
CC       retrovirus replication via an RNA lariat intermediate in cDNA synthesis
CC       and have an antiviral cell-intrinsic defense function in the brainstem
CC       (PubMed:16232320, PubMed:29474921). {ECO:0000269|PubMed:10982890,
CC       ECO:0000269|PubMed:16232320, ECO:0000269|PubMed:2435736,
CC       ECO:0000269|PubMed:29474921}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:P24309};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P24309};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:2435736};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0000250|UniProtKB:P24309};
CC   -!- ACTIVITY REGULATION: Active in presence of diverse metals including
CC       Fe(2+), Zn(2+), Mn(2+) (By similarity). Also activated by Ca(2+)
CC       (PubMed:2435736). Binds two metal cations in two adjacent alpha and
CC       beta metal-binding pockets (By similarity).
CC       {ECO:0000250|UniProtKB:P24309, ECO:0000269|PubMed:2435736}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:2435736};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UK59-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UK59-2; Sequence=VSP_020631, VSP_020632;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, strongest expression in the
CC       spinal cord and brainstem. {ECO:0000269|PubMed:29474921}.
CC   -!- DISEASE: Encephalitis, acute, infection (viral)-induced, 11 (IIAE11)
CC       [MIM:619441]: An autosomal recessive disorder characterized by
CC       increased susceptibility to viral encephalitis affecting the brainstem
CC       and induced by neurotropic viruses, such as herpes simplex virus-1,
CC       influenza B virus or norovirus. {ECO:0000269|PubMed:29474921}.
CC       Note=Disease susceptibility is associated with variants affecting the
CC       gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the lariat debranching enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD53327.2; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF180919; AAD53327.2; ALT_FRAME; mRNA.
DR   EMBL; AK000116; BAA90954.1; -; mRNA.
DR   EMBL; BC009472; AAH09472.1; -; mRNA.
DR   CCDS; CCDS33863.1; -. [Q9UK59-1]
DR   RefSeq; NP_057300.2; NM_016216.3. [Q9UK59-1]
DR   AlphaFoldDB; Q9UK59; -.
DR   SMR; Q9UK59; -.
DR   BioGRID; 119344; 33.
DR   IntAct; Q9UK59; 14.
DR   STRING; 9606.ENSP00000260803; -.
DR   GlyGen; Q9UK59; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UK59; -.
DR   PhosphoSitePlus; Q9UK59; -.
DR   BioMuta; DBR1; -.
DR   DMDM; 115311701; -.
DR   EPD; Q9UK59; -.
DR   jPOST; Q9UK59; -.
DR   MassIVE; Q9UK59; -.
DR   MaxQB; Q9UK59; -.
DR   PaxDb; 9606-ENSP00000260803; -.
DR   PeptideAtlas; Q9UK59; -.
DR   ProteomicsDB; 84727; -. [Q9UK59-1]
DR   ProteomicsDB; 84728; -. [Q9UK59-2]
DR   Pumba; Q9UK59; -.
DR   Antibodypedia; 33423; 179 antibodies from 20 providers.
DR   DNASU; 51163; -.
DR   Ensembl; ENST00000260803.9; ENSP00000260803.4; ENSG00000138231.14. [Q9UK59-1]
DR   GeneID; 51163; -.
DR   KEGG; hsa:51163; -.
DR   MANE-Select; ENST00000260803.9; ENSP00000260803.4; NM_016216.4; NP_057300.2.
DR   UCSC; uc003erv.4; human. [Q9UK59-1]
DR   AGR; HGNC:15594; -.
DR   CTD; 51163; -.
DR   DisGeNET; 51163; -.
DR   GeneCards; DBR1; -.
DR   HGNC; HGNC:15594; DBR1.
DR   HPA; ENSG00000138231; Low tissue specificity.
DR   MalaCards; DBR1; -.
DR   MIM; 607024; gene.
DR   MIM; 619441; phenotype.
DR   neXtProt; NX_Q9UK59; -.
DR   OpenTargets; ENSG00000138231; -.
DR   PharmGKB; PA27166; -.
DR   VEuPathDB; HostDB:ENSG00000138231; -.
DR   eggNOG; KOG2863; Eukaryota.
DR   GeneTree; ENSGT00510000047481; -.
DR   HOGENOM; CLU_005893_0_2_1; -.
DR   InParanoid; Q9UK59; -.
DR   OMA; GIDDPLC; -.
DR   OrthoDB; 1220605at2759; -.
DR   PhylomeDB; Q9UK59; -.
DR   TreeFam; TF313221; -.
DR   PathwayCommons; Q9UK59; -.
DR   SignaLink; Q9UK59; -.
DR   BioGRID-ORCS; 51163; 835 hits in 1154 CRISPR screens.
DR   GeneWiki; DBR1; -.
DR   GenomeRNAi; 51163; -.
DR   Pharos; Q9UK59; Tbio.
DR   PRO; PR:Q9UK59; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9UK59; Protein.
DR   Bgee; ENSG00000138231; Expressed in buccal mucosa cell and 174 other cell types or tissues.
DR   ExpressionAtlas; Q9UK59; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0008419; F:RNA lariat debranching enzyme activity; IMP:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0000375; P:RNA splicing, via transesterification reactions; IMP:UniProtKB.
DR   CDD; cd00844; MPP_Dbr1_N; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR007708; DBR1_C.
DR   InterPro; IPR041816; Dbr1_N.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR12849:SF0; LARIAT DEBRANCHING ENZYME; 1.
DR   PANTHER; PTHR12849; RNA LARIAT DEBRANCHING ENZYME; 1.
DR   Pfam; PF05011; DBR1; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SMART; SM01124; DBR1; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   Genevisible; Q9UK59; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Disease variant; Hydrolase; Iron;
KW   Manganese; Metal-binding; mRNA processing; Nucleus; Phosphoprotein;
KW   Reference proteome; Zinc.
FT   CHAIN           1..544
FT                   /note="Lariat debranching enzyme"
FT                   /id="PRO_0000250358"
FT   REGION          124..154
FT                   /note="Lariat recognition loop"
FT                   /evidence="ECO:0000250|UniProtKB:C4M1P9"
FT   REGION          395..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..535
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         8
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:C4M1P9"
FT   BINDING         10
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:C4M1P9"
FT   BINDING         39
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:C4M1P9"
FT   BINDING         84
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:C4M1P9"
FT   BINDING         174
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:C4M1P9"
FT   BINDING         226
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:C4M1P9"
FT   BINDING         228
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:C4M1P9"
FT   MOD_RES         128
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         464
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         474
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         479
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         485
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q923B1"
FT   MOD_RES         499
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q923B1"
FT   MOD_RES         514
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..232
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_020631"
FT   VAR_SEQ         233..237
FT                   /note="ALMQH -> MIHIV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_020632"
FT   VARIANT         13
FT                   /note="L -> G (in IIAE11; decreased protein abundance;
FT                   decreased RNA lariat debranching enzyme activity; requires
FT                   2 nucleotide substitutions)"
FT                   /evidence="ECO:0000269|PubMed:29474921"
FT                   /id="VAR_086073"
FT   VARIANT         17
FT                   /note="Y -> H (in IIAE11; decreased protein abundance;
FT                   decreased RNA lariat debranching enzyme activity)"
FT                   /evidence="ECO:0000269|PubMed:29474921"
FT                   /id="VAR_086074"
FT   VARIANT         120
FT                   /note="I -> T (in IIAE11; decreased protein abundance;
FT                   decreased RNA lariat debranching enzyme activity)"
FT                   /evidence="ECO:0000269|PubMed:29474921"
FT                   /id="VAR_086075"
FT   VARIANT         197..544
FT                   /note="Missing (in IIAE11; loss of protein expression)"
FT                   /evidence="ECO:0000269|PubMed:29474921"
FT                   /id="VAR_086076"
FT   MUTAGEN         85
FT                   /note="H->N: No effect on protein abundance. Loss of RNA
FT                   lariat debranching enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:29474921"
FT   CONFLICT        308
FT                   /note="N -> S (in Ref. 2; BAA90954)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        496
FT                   /note="T -> L (in Ref. 1; AAD53327)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   544 AA;  61555 MW;  DDA5F4FADA194BAA CRC64;
     MRVAVAGCCH GELDKIYETL ALAERRGPGP VDLLLCCGDF QAVRNEADLR CMAVPPKYRH
     MQTFYRYYSG EKKAPVLTLF IGGNHEASNH LQELPYGGWV APNIYYLGLA GVVKYRGVRI
     GGISGIFKSH DYRKGHFECP PYNSSTIRSI YHVRNIEVYK LKQLKQPIDI FLSHDWPRSI
     YHYGNKKQLL KTKSFFRQEV ENNTLGSPAA SELLEHLKPT YWFSAHLHVK FAALMQHQAK
     DKGQTARATK FLALDKCLPH RDFLQILEIE HDPSAPDYLE YDIEWLTILR ATDDLINVTG
     RLWNMPENNG LHARWDYSAT EEGMKEVLEK LNHDLKVPCN FSVTAACYDP SKPQTQMQLI
     HRINPQTTEF CAQLGIIDIN VRLQKSKEEH HVCGEYEEQD DVESNDSGED QSEYNTDTSA
     LSSINPDEIM LDEEEDEDSI VSAHSGMNTP SVEPSDQASE FSASFSDVRI LPGSMIVSSD
     DTVDSTIDRE GKPGGTVESG NGEDLTKVPL KRLSDEHEPE QRKKIKRRNQ AIYAAVDDDD
     DDAA
//