INT1_HUMAN
ID INT1_HUMAN Reviewed; 2190 AA.
AC Q8N201; A6NJ44; Q6NT70; Q6UX74; Q8WV40; Q96D36; Q9NTD1; Q9P2A8; Q9Y3W8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Integrator complex subunit 1;
DE Short=Int1;
GN Name=INTS1; Synonyms=KIAA1440; ORFNames=UNQ1821/PRO3434;
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 GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 814-2190.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1147-2190.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1291-2190.
RC TISSUE=Brain, Lymph, and Skin;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1558-2190.
RC TISSUE=Testis, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE INTEGRATOR
RP COMPLEX, AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=16239144; DOI=10.1016/j.cell.2005.08.019;
RA Baillat D., Hakimi M.-A., Naeaer A.M., Shilatifard A., Cooch N.,
RA Shiekhattar R.;
RT "Integrator, a multiprotein mediator of small nuclear RNA processing,
RT associates with the C-terminal repeat of RNA polymerase II.";
RL Cell 123:265-276(2005).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP IDENTIFICATION BY 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1318, 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; THR-83; SER-307 AND
RP SER-1395, AND 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 [18]
RP FUNCTION.
RX PubMed=23904267; DOI=10.1091/mbc.e13-05-0254;
RA Jodoin J.N., Sitaram P., Albrecht T.R., May S.B., Shboul M., Lee E.,
RA Reversade B., Wagner E.J., Lee L.A.;
RT "Nuclear-localized Asunder regulates cytoplasmic dynein localization via
RT its role in the integrator complex.";
RL Mol. Biol. Cell 24:2954-2965(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-307 AND SER-924, AND
RP IDENTIFICATION BY 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 [20]
RP INVOLVEMENT IN NDCAGF, VARIANT NDCAGF 1784-SER--MET-2190 DEL, AND
RP CHARACTERIZATION OF VARIANT NEDBAF 1784-SER--MET-2190 DEL.
RX PubMed=28542170; DOI=10.1371/journal.pgen.1006809;
RA Oegema R., Baillat D., Schot R., van Unen L.M., Brooks A., Kia S.K.,
RA Hoogeboom A.J.M., Xia Z., Li W., Cesaroni M., Lequin M.H.,
RA van Slegtenhorst M., Dobyns W.B., de Coo I.F.M., Verheijen F.W., Kremer A.,
RA van der Spek P.J., Heijsman D., Wagner E.J., Fornerod M., Mancini G.M.S.;
RT "Human mutations in integrator complex subunits link transcriptome
RT integrity to brain development.";
RL PLoS Genet. 13:e1006809-e1006809(2017).
RN [21]
RP VARIANTS NDCAGF CYS-77; LEU-1874 AND PRO-2164.
RX PubMed=30622326; DOI=10.1038/s41431-018-0298-9;
RG Care 4 Rare Canada Consortium;
RA Krall M., Htun S., Schnur R.E., Brooks A.S., Baker L.,
RA de Alba Campomanes A., Lamont R.E., Gripp K.W., Schneidman-Duhovny D.,
RA Innes A.M., Mancini G.M.S., Slavotinek A.M.;
RT "Biallelic sequence variants in INTS1 in patients with developmental
RT delays, cataracts, and craniofacial anomalies.";
RL Eur. J. Hum. Genet. 27:582-593(2019).
RN [22]
RP VARIANTS NDCAGF VAL-549 AND 1961-GLN--MET-2190 DEL.
RX PubMed=31428919; DOI=10.1007/s12031-019-01393-x;
RA Zhang X., Wang Y., Yang F., Tang J., Xu X., Yang L., Yang X.A., Wu D.;
RT "Biallelic INTS1 mutations cause a rare neurodevelopmental disorder in two
RT Chinese siblings.";
RL J. Mol. Neurosci. 70:1-8(2020).
CC -!- FUNCTION: Component of the Integrator (INT) complex, a complex involved
CC in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their
CC 3'-box-dependent processing. The Integrator complex is associated with
CC the C-terminal domain (CTD) of RNA polymerase II largest subunit
CC (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable).
CC Mediates recruitment of cytoplasmic dynein to the nuclear envelope,
CC probably as component of the INT complex (PubMed:23904267).
CC {ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:16239144}.
CC -!- SUBUNIT: Belongs to the multiprotein complex Integrator, at least
CC composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8,
CC INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12 (PubMed:16239144).
CC Interacts with ESRRB, ESRRB is probably not a core component of the
CC multiprotein complex Integrator and this association is a bridge for
CC the interaction with the multiprotein complex Integrator; attracts the
CC transcriptional machinery (By similarity).
CC {ECO:0000250|UniProtKB:Q6P4S8, ECO:0000269|PubMed:16239144}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- DISEASE: Neurodevelopmental disorder with cataracts, poor growth, and
CC dysmorphic facies (NDCAGF) [MIM:618571]: An autosomal recessive
CC neurodevelopmental disorder characterized by severe global
CC developmental delay with motor impairment, cognitive delays, absent or
CC severely limited speech, dysmorphic features, hypotonia and cataracts.
CC {ECO:0000269|PubMed:28542170, ECO:0000269|PubMed:30622326,
CC ECO:0000269|PubMed:31428919}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the Integrator subunit 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ88846.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC102953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB037861; BAA92678.1; -; mRNA.
DR EMBL; AY358482; AAQ88846.1; ALT_INIT; mRNA.
DR EMBL; BC013367; AAH13367.2; -; mRNA.
DR EMBL; BC018777; AAH18777.1; -; mRNA.
DR EMBL; BC069262; AAH69262.1; -; mRNA.
DR EMBL; AL050110; CAB43278.2; -; mRNA.
DR EMBL; AL137358; CAB70710.3; -; mRNA.
DR EMBL; BK005720; DAA05720.1; -; mRNA.
DR CCDS; CCDS47526.1; -.
DR PIR; T08758; T08758.
DR PIR; T46429; T46429.
DR RefSeq; NP_001073922.2; NM_001080453.2.
DR PDB; 7CUN; EM; 3.50 A; A=1-2190.
DR PDB; 7PKS; EM; 3.60 A; a=1-2190.
DR PDBsum; 7CUN; -.
DR PDBsum; 7PKS; -.
DR AlphaFoldDB; Q8N201; -.
DR SMR; Q8N201; -.
DR BioGRID; 117596; 166.
DR ComplexPortal; CPX-6441; Integrator complex.
DR CORUM; Q8N201; -.
DR DIP; DIP-48476N; -.
DR IntAct; Q8N201; 29.
DR MINT; Q8N201; -.
DR STRING; 9606.ENSP00000385722; -.
DR iPTMnet; Q8N201; -.
DR PhosphoSitePlus; Q8N201; -.
DR BioMuta; INTS1; -.
DR DMDM; 97052424; -.
DR EPD; Q8N201; -.
DR jPOST; Q8N201; -.
DR MassIVE; Q8N201; -.
DR MaxQB; Q8N201; -.
DR PaxDb; Q8N201; -.
DR PeptideAtlas; Q8N201; -.
DR PRIDE; Q8N201; -.
DR ProteomicsDB; 71646; -.
DR Antibodypedia; 5500; 105 antibodies from 18 providers.
DR DNASU; 26173; -.
DR Ensembl; ENST00000404767.8; ENSP00000385722.3; ENSG00000164880.16.
DR GeneID; 26173; -.
DR KEGG; hsa:26173; -.
DR MANE-Select; ENST00000404767.8; ENSP00000385722.3; NM_001080453.3; NP_001073922.2.
DR UCSC; uc003skn.3; human.
DR CTD; 26173; -.
DR DisGeNET; 26173; -.
DR GeneCards; INTS1; -.
DR HGNC; HGNC:24555; INTS1.
DR HPA; ENSG00000164880; Low tissue specificity.
DR MalaCards; INTS1; -.
DR MIM; 611345; gene.
DR MIM; 618571; phenotype.
DR neXtProt; NX_Q8N201; -.
DR OpenTargets; ENSG00000164880; -.
DR PharmGKB; PA144596420; -.
DR VEuPathDB; HostDB:ENSG00000164880; -.
DR eggNOG; KOG4596; Eukaryota.
DR GeneTree; ENSGT00390000015743; -.
DR HOGENOM; CLU_001690_0_0_1; -.
DR InParanoid; Q8N201; -.
DR OMA; NWDTIER; -.
DR OrthoDB; 357673at2759; -.
DR PhylomeDB; Q8N201; -.
DR TreeFam; TF313809; -.
DR PathwayCommons; Q8N201; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q8N201; -.
DR SIGNOR; Q8N201; -.
DR BioGRID-ORCS; 26173; 632 hits in 1071 CRISPR screens.
DR ChiTaRS; INTS1; human.
DR GenomeRNAi; 26173; -.
DR Pharos; Q8N201; Tbio.
DR PRO; PR:Q8N201; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8N201; protein.
DR Bgee; ENSG00000164880; Expressed in left testis and 185 other tissues.
DR ExpressionAtlas; Q8N201; baseline and differential.
DR Genevisible; Q8N201; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032039; C:integrator complex; IDA:HGNC-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IEA:Ensembl.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0016180; P:snRNA processing; IDA:HGNC-UCL.
DR GO; GO:0034474; P:U2 snRNA 3'-end processing; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR022145; DUF3677.
DR InterPro; IPR038902; INTS1.
DR PANTHER; PTHR21224; PTHR21224; 1.
DR Pfam; PF12432; DUF3677; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; Intellectual disability;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..2190
FT /note="Integrator complex subunit 1"
FT /id="PRO_0000236044"
FT TRANSMEM 1159..1179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 47
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4S8"
FT MOD_RES 1327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4S8"
FT MOD_RES 1395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 77
FT /note="R -> C (in NDCAGF; unknown pathological
FT significance; dbSNP:rs200649090)"
FT /evidence="ECO:0000269|PubMed:30622326"
FT /id="VAR_083352"
FT VARIANT 172
FT /note="P -> L (in dbSNP:rs3752714)"
FT /id="VAR_049627"
FT VARIANT 549
FT /note="M -> V (in NDCAGF; dbSNP:rs1030646527)"
FT /evidence="ECO:0000269|PubMed:31428919"
FT /id="VAR_083353"
FT VARIANT 1784..2190
FT /note="Missing (in NDCAGF; decreased protein abundance)"
FT /evidence="ECO:0000269|PubMed:28542170"
FT /id="VAR_083354"
FT VARIANT 1874
FT /note="P -> L (in NDCAGF; unknown pathological
FT significance; dbSNP:rs1162809128)"
FT /evidence="ECO:0000269|PubMed:30622326"
FT /id="VAR_083355"
FT VARIANT 1961..2190
FT /note="Missing (in NDCAGF)"
FT /evidence="ECO:0000269|PubMed:31428919"
FT /id="VAR_083356"
FT VARIANT 2164
FT /note="L -> P (in NDCAGF; unknown pathological
FT significance; dbSNP:rs1302980015)"
FT /evidence="ECO:0000269|PubMed:30622326"
FT /id="VAR_083357"
FT CONFLICT 636
FT /note="R -> Y (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1862
FT /note="A -> G (in Ref. 2; BAA92678)"
FT /evidence="ECO:0000305"
FT CONFLICT 2004
FT /note="G -> V (in Ref. 5; CAB70710)"
FT /evidence="ECO:0000305"
FT CONFLICT 2105
FT /note="S -> C (in Ref. 5; CAB70710)"
FT /evidence="ECO:0000305"
FT CONFLICT 2162
FT /note="A -> AF (in Ref. 5; CAB70710)"
FT /evidence="ECO:0000305"
FT HELIX 1394..1402
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1407..1424
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1432..1444
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1448..1455
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1458..1474
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 1478..1481
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1482..1499
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 1501..1503
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1508..1518
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 1526..1528
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1529..1536
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 1537..1540
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1543..1557
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 1565..1567
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1568..1571
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1573..1577
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1583..1591
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1598..1608
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1615..1624
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 1627..1632
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1634..1641
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1657..1667
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1670..1680
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 1681..1683
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1691..1702
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 1705..1707
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 1708..1711
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1729..1742
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1752..1769
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1772..1779
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 1786..1788
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1792..1796
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1797..1800
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1806..1814
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1826..1842
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1860..1863
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1865..1872
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1874..1885
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 1891..1893
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 1903..1905
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1906..1916
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1919..1922
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1929..1944
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 1946..1949
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1953..1968
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1971..1980
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1983..1985
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 1990..1995
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 2045..2047
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 2048..2056
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 2060..2073
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 2078..2083
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 2085..2092
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 2098..2113
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 2115..2121
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 2122..2129
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 2136..2151
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 2152..2154
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 2155..2168
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 2174..2184
FT /evidence="ECO:0007829|PDB:7CUN"
SQ SEQUENCE 2190 AA; 244297 MW; 342FF560BF3F61F6 CRC64;
MNRAKPTTVR RPSAAAKPSG HPPPGDFIAL GSKGQANESK TASTLLKPAP SGLPSERKRD
AAAALSSASA LTGLTKRPKL SSTPPLSALG RLAEAAVAEK RAISPSIKEP SVVPIEVLPT
VLLDEIEAAE LEGNDDRIEG VLCGAVKQLK VTRAKPDSTL YLSLMYLAKI KPNIFATEGV
IEALCSLLRR DASINFKAKG NSLVSVLACN LLMAAYEEDE NWPEIFVKVY IEDSLGERIW
VDSPHCKTFV DNIQTAFNTR MPPRSVLLQG EAGRVAGDLG AGSSPHPSLT EEEDSQTELL
IAEEKLSPEQ EGQLMPRYEE LAESVEEYVL DMLRDQLNRR QPIDNVSRNL LRLLTSTCGY
KEVRLLAVQK LEMWLQNPKL TRPAQDLLMS VCMNCNTHGS EDMDVISHLI KIRLKPKVLL
NHFMLCIREL LSAHKDNLGT TIKLVIFNEL SSARNPNNMQ VLYTALQHSS ELAPKFLAMV
FQDLLTNKDD YLRASRALLR EIIKQTKHEI NFQAFCLGLM QERKEPQYLE MEFKERFVVH
ITDVLAVSMM LGITAQVKEA GIAWDKGEKR NLEVLRSFQN QIAAIQRDAV WWLHTVVPSI
SKLAPKDYVH CLHKVLFTEQ PETYYKWDNW PPESDRNFFL RLCSEVPILE DTLMRILVIG
LSRELPLGPA DAMELADHLV KRAAAVQADD VEVLKVGRTQ LIDAVLNLCT YHHPENIQLP
PGYQPPNLAI STLYWKAWPL LLVVAAFNPE NIGLAAWEEY PTLKMLMEMV MTNNYSYPPC
TLTDEETRTE MLNRELQTAQ REKQEILAFE GHLAAASTKQ TITESSSLLL SQLTSLDPQG
PPRRPPPHIL DQVKSLNQSL RLGHLLCRSR NPDFLLHIIQ RQASSQSMPW LADLVQSSEG
SLDVLPVQCL CEFLLHDAVD DAASGEEDDE GESKEQKAKK RQRQQKQRQL LGRLQDLLLG
PKADEQTTCE VLDYFLRRLG SSQVASRVLA MKGLSLVLSE GSLRDGEEKE PPMEEDVGDT
DVLQGYQWLL RDLPRLPLFD SVRSTTALAL QQAIHMETDP QTISAYLIYL SQHTPVEEQA
QHSDLALDVA RLVVERSTIM SHLFSKLSPS AASDAVLSAL LSIFSRYVRR MRQSKEGEEV
YSWSESQDQV FLRWSSGETA TMHILVVHAM VILLTLGPPR ADDSEFQALL DIWFPEEKPL
PTAFLVDTSE EALLLPDWLK LRMIRSEVLR LVDAALQDLE PQQLLLFVQS FGIPVSSMSK
LLQFLDQAVA HDPQTLEQNI MDKNYMAHLV EVQHERGASG GQTFHSLLTA SLPPRRDSTE
APKPKSSPEQ PIGQGRIRVG TQLRVLGPED DLAGMFLQIF PLSPDPRWQS SSPRPVALAL
QQALGQELAR VVQGSPEVPG ITVRVLQALA TLLSSPHGGA LVMSMHRSHF LACPLLRQLC
QYQRCVPQDT GFSSLFLKVL LQMLQWLDSP GVEGGPLRAQ LRMLASQASA GRRLSDVRGG
LLRLAEALAF RQDLEVVSST VRAVIATLRS GEQCSVEPDL ISKVLQGLIE VRSPHLEELL
TAFFSATADA ASPFPACKPV VVVSSLLLQE EEPLAGGKPG ADGGSLEAVR LGPSSGLLVD
WLEMLDPEVV SSCPDLQLRL LFSRRKGKGQ AQVPSFRPYL LTLFTHQSSW PTLHQCIRVL
LGKSREQRFD PSASLDFLWA CIHVPRIWQG RDQRTPQKRR EELVLRVQGP ELISLVELIL
AEAETRSQDG DTAACSLIQA RLPLLLSCCC GDDESVRKVT EHLSGCIQQW GDSVLGRRCR
DLLLQLYLQR PELRVPVPEV LLHSEGAASS SVCKLDGLIH RFITLLADTS DSRALENRGA
DASMACRKLA VAHPLLLLRH LPMIAALLHG RTHLNFQEFR QQNHLSCFLH VLGLLELLQP
HVFRSEHQGA LWDCLLSFIR LLLNYRKSSR HLAAFINKFV QFIHKYITYN APAAISFLQK
HADPLHDLSF DNSDLVMLKS LLAGLSLPSR DDRTDRGLDE EGEEESSAGS LPLVSVSLFT
PLTAAEMAPY MKRLSRGQTV EDLLEVLSDI DEMSRRRPEI LSFFSTNLQR LMSSAEECCR
NLAFSLALRS MQNSPSIAAA FLPTFMYCLG SQDFEVVQTA LRNLPEYALL CQEHAAVLLH
RAFLVGMYGQ MDPSAQISEA LRILHMEAVM
