DMXL2_HUMAN
ID DMXL2_HUMAN Reviewed; 3036 AA.
AC Q8TDJ6; B2RTR3; B7ZMH3; F5GWF1; O94938;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=DmX-like protein 2;
DE AltName: Full=Rabconnectin-3;
GN Name=DMXL2; Synonyms=KIAA0856;
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), PROTEIN SEQUENCE OF 526-540;
RP 789-800; 814-829; 924-938; 1790-1795; 2069-2079 AND 2449-2463, FUNCTION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MADD AND RAB3GAP.
RX PubMed=11809763; DOI=10.1074/jbc.c100730200;
RA Nagano F., Kawabe H., Nakanishi H., Shinohara M., Deguchi-Tawarada M.,
RA Takeuchi M., Sasaki T., Takai Y.;
RT "Rabconnectin-3, a novel protein that binds both GDP/GTP exchange protein
RT and GTPase-activating protein for Rab3 small G protein family.";
RL J. Biol. Chem. 277:9629-9632(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 801-3036 (ISOFORM 3), AND VARIANT
RP PRO-1288.
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS
RP PRO-1288 AND SER-1698.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-944; SER-945; SER-1400 AND
RP SER-1857, AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-944; SER-945; SER-1140;
RP SER-1143 AND SER-1984, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-1151; SER-1857 AND
RP SER-2399, 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 [12]
RP INVOLVEMENT IN PEPNS, AND VARIANT PEPNS 1942-SER--GLY-1946 DEL.
RX PubMed=25248098; DOI=10.1371/journal.pbio.1001952;
RA Tata B., Huijbregts L., Jacquier S., Csaba Z., Genin E., Meyer V., Leka S.,
RA Dupont J., Charles P., Chevenne D., Carel J.C., Leger J., de Roux N.;
RT "Haploinsufficiency of Dmxl2, encoding a synaptic protein, causes
RT infertility associated with a loss of GnRH neurons in mouse.";
RL PLoS Biol. 12:E1001952-E1001952(2014).
RN [13]
RP INVOLVEMENT IN DFNA71, AND VARIANT DFNA71 HIS-2417.
RX PubMed=27657680; DOI=10.1038/gim.2016.142;
RA Chen D.Y., Liu X.F., Lin X.J., Zhang D., Chai Y.C., Yu D.H., Sun C.L.,
RA Wang X.L., Zhu W.D., Chen Y., Sun L.H., Wang X.W., Shi F.X., Huang Z.W.,
RA Yang T., Wu H.;
RT "A dominant variant in DMXL2 is linked to nonsyndromic hearing loss.";
RL Genet. Med. 19:553-558(2017).
RN [14]
RP INVOLVEMENT IN DEE81, AND VARIANTS DEE81 1493-SER--LEU-3036 DEL AND
RP VAL-1712.
RX PubMed=31688942; DOI=10.1093/brain/awz326;
RA Esposito A., Falace A., Wagner M., Gal M., Mei D., Conti V., Pisano T.,
RA Aprile D., Cerullo M.S., De Fusco A., Giovedi S., Seibt A., Magen D.,
RA Polster T., Eran A., Stenton S.L., Fiorillo C., Ravid S., Mayatepek E.,
RA Hafner H., Wortmann S., Levanon E.Y., Marini C., Mandel H., Benfenati F.,
RA Distelmaier F., Fassio A., Guerrini R.;
RT "Biallelic DMXL2 mutations impair autophagy and cause Ohtahara syndrome
RT with progressive course.";
RL Brain 142:3876-3891(2019).
RN [15]
RP INVOLVEMENT IN DEE81.
RX PubMed=30237576; DOI=10.1038/s41436-018-0138-x;
RA Maddirevula S., Alzahrani F., Al-Owain M., Al Muhaizea M.A., Kayyali H.R.,
RA AlHashem A., Rahbeeni Z., Al-Otaibi M., Alzaidan H.I., Balobaid A.,
RA El Khashab H.Y., Bubshait D.K., Faden M., Yamani S.A., Dabbagh O.,
RA Al-Mureikhi M., Jasser A.A., Alsaif H.S., Alluhaydan I., Seidahmed M.Z.,
RA Alabbasi B.H., Almogarri I., Kurdi W., Akleh H., Qari A., Al Tala S.M.,
RA Alhomaidi S., Kentab A.Y., Salih M.A., Chedrawi A., Alameer S., Tabarki B.,
RA Shamseldin H.E., Patel N., Ibrahim N., Abdulwahab F., Samira M., Goljan E.,
RA Abouelhoda M., Meyer B.F., Hashem M., Shaheen R., AlShahwan S.,
RA Alfadhel M., Ben-Omran T., Al-Qattan M.M., Monies D., Alkuraya F.S.;
RT "Autozygome and high throughput confirmation of disease genes candidacy.";
RL Genet. Med. 21:736-742(2019).
CC -!- FUNCTION: May serve as a scaffold protein for MADD and RAB3GA on
CC synaptic vesicles (PubMed:11809763). Plays a role in the brain as a key
CC controller of neuronal and endocrine homeostatic processes (By
CC similarity). {ECO:0000250|UniProtKB:Q8BPN8,
CC ECO:0000269|PubMed:11809763}.
CC -!- SUBUNIT: Interacts with MADD and RAB3GAP.
CC {ECO:0000269|PubMed:11809763}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:11809763}; Peripheral membrane
CC protein {ECO:0000269|PubMed:11809763}. Cytoplasmic vesicle, secretory
CC vesicle, neuronal dense core vesicle {ECO:0000250|UniProtKB:Q8BPN8}.
CC Note=The external layer of the inferior boundary for the hypothalamus
CC part of the human brain (the so called median eminence (ME)) displayed
CC a punctate pattern of expression; expression also observed in the cell
CC bodies lining the third ventricle, in the long processes extending from
CC these cell bodies toward the external layer of the ME, in small clear
CC vesicles, and in large dense core vesicles.
CC {ECO:0000250|UniProtKB:Q8BPN8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TDJ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TDJ6-2; Sequence=VSP_043015;
CC Name=3;
CC IsoId=Q8TDJ6-3; Sequence=VSP_044977;
CC -!- DISEASE: Polyendocrine-polyneuropathy syndrome (PEPNS) [MIM:616113]: A
CC progressive endocrine and neurodevelopmental disorder manifesting early
CC in childhood with growth retardation and recurrent episodes of profound
CC asymptomatic hypoglycemia. PEPNS is characterized by central
CC hypothyroidism, hypogonadotropic hypogonadism, incomplete puberty,
CC progressive non-autoimmune insulin-dependent diabetes mellitus,
CC peripheral demyelinating sensorimotor polyneuropathy, and cerebellar
CC and pyramidal signs. {ECO:0000269|PubMed:25248098}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Deafness, autosomal dominant, 71 (DFNA71) [MIM:617605]: A form
CC of non-syndromic sensorineural hearing loss. Sensorineural deafness
CC results from damage to the neural receptors of the inner ear, the nerve
CC pathways to the brain, or the area of the brain that receives sound
CC information. DFNA71 is characterized by bilateral mild to moderate
CC hearing loss before age 20 years, which gradually progresses to severe
CC to profound hearing loss. {ECO:0000269|PubMed:27657680}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Developmental and epileptic encephalopathy 81 (DEE81)
CC [MIM:618663]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE81 is an autosomal recessive form characterized by
CC onset soon after birth, little developmental progress with no eye
CC contact and no motor or cognitive development. Other features may
CC include facial dysmorphism, such as hypotonic facies and epicanthal
CC folds, as well as sensorineural hearing loss and peripheral neuropathy.
CC {ECO:0000269|PubMed:30237576, ECO:0000269|PubMed:31688942}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; AF389880; AAL93215.1; -; mRNA.
DR EMBL; AB020663; BAA74879.2; -; mRNA.
DR EMBL; AC020892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC066613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140781; AAI40782.1; -; mRNA.
DR EMBL; BC144539; AAI44540.1; -; mRNA.
DR CCDS; CCDS10141.1; -. [Q8TDJ6-1]
DR CCDS; CCDS53945.1; -. [Q8TDJ6-2]
DR CCDS; CCDS53946.1; -. [Q8TDJ6-3]
DR RefSeq; NP_001167587.1; NM_001174116.1. [Q8TDJ6-3]
DR RefSeq; NP_001167588.1; NM_001174117.1. [Q8TDJ6-2]
DR RefSeq; NP_056078.2; NM_015263.3. [Q8TDJ6-1]
DR BioGRID; 116903; 51.
DR IntAct; Q8TDJ6; 13.
DR STRING; 9606.ENSP00000441858; -.
DR TCDB; 8.A.92.1.13; the g-protein AlphaBetaGama complex (gpc) family.
DR GlyGen; Q8TDJ6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TDJ6; -.
DR PhosphoSitePlus; Q8TDJ6; -.
DR BioMuta; DMXL2; -.
DR DMDM; 296434481; -.
DR EPD; Q8TDJ6; -.
DR jPOST; Q8TDJ6; -.
DR MassIVE; Q8TDJ6; -.
DR MaxQB; Q8TDJ6; -.
DR PaxDb; Q8TDJ6; -.
DR PeptideAtlas; Q8TDJ6; -.
DR PRIDE; Q8TDJ6; -.
DR ProteomicsDB; 24097; -.
DR ProteomicsDB; 74294; -. [Q8TDJ6-1]
DR ProteomicsDB; 74295; -. [Q8TDJ6-2]
DR Antibodypedia; 51332; 60 antibodies from 16 providers.
DR DNASU; 23312; -.
DR Ensembl; ENST00000251076.9; ENSP00000251076.5; ENSG00000104093.14. [Q8TDJ6-1]
DR Ensembl; ENST00000449909.7; ENSP00000400855.3; ENSG00000104093.14. [Q8TDJ6-2]
DR Ensembl; ENST00000543779.6; ENSP00000441858.2; ENSG00000104093.14. [Q8TDJ6-3]
DR GeneID; 23312; -.
DR KEGG; hsa:23312; -.
DR UCSC; uc002abf.4; human. [Q8TDJ6-1]
DR CTD; 23312; -.
DR DisGeNET; 23312; -.
DR GeneCards; DMXL2; -.
DR HGNC; HGNC:2938; DMXL2.
DR HPA; ENSG00000104093; Low tissue specificity.
DR MalaCards; DMXL2; -.
DR MIM; 612186; gene.
DR MIM; 616113; phenotype.
DR MIM; 617605; phenotype.
DR MIM; 618663; phenotype.
DR neXtProt; NX_Q8TDJ6; -.
DR OpenTargets; ENSG00000104093; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR Orphanet; 1934; Early infantile epileptic encephalopathy.
DR Orphanet; 453533; Polyendocrine-polyneuropathy syndrome.
DR PharmGKB; PA27392; -.
DR VEuPathDB; HostDB:ENSG00000104093; -.
DR eggNOG; KOG1064; Eukaryota.
DR GeneTree; ENSGT00390000000096; -.
DR HOGENOM; CLU_000267_0_0_1; -.
DR InParanoid; Q8TDJ6; -.
DR OrthoDB; 127808at2759; -.
DR PhylomeDB; Q8TDJ6; -.
DR TreeFam; TF312896; -.
DR PathwayCommons; Q8TDJ6; -.
DR SignaLink; Q8TDJ6; -.
DR SIGNOR; Q8TDJ6; -.
DR BioGRID-ORCS; 23312; 17 hits in 1078 CRISPR screens.
DR ChiTaRS; DMXL2; human.
DR GenomeRNAi; 23312; -.
DR Pharos; Q8TDJ6; Tbio.
DR PRO; PR:Q8TDJ6; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8TDJ6; protein.
DR Bgee; ENSG00000104093; Expressed in monocyte and 183 other tissues.
DR ExpressionAtlas; Q8TDJ6; baseline and differential.
DR Genevisible; Q8TDJ6; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0098992; C:neuronal dense core vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0043291; C:RAVE complex; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; IDA:MGI.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR022033; Rav1p_C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12234; Rav1p_C; 2.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 13.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasmic vesicle; Deafness;
KW Diabetes mellitus; Direct protein sequencing; Disease variant; Epilepsy;
KW Hypogonadotropic hypogonadism; Membrane; Neuropathy;
KW Non-syndromic deafness; Phosphoprotein; Reference proteome; Repeat;
KW Synapse; WD repeat.
FT CHAIN 1..3036
FT /note="DmX-like protein 2"
FT /id="PRO_0000223324"
FT REPEAT 108..145
FT /note="WD 1"
FT REPEAT 167..207
FT /note="WD 2"
FT REPEAT 230..278
FT /note="WD 3"
FT REPEAT 492..532
FT /note="WD 4"
FT REPEAT 595..634
FT /note="WD 5"
FT REPEAT 751..803
FT /note="WD 6"
FT REPEAT 878..920
FT /note="WD 7"
FT REPEAT 1000..1037
FT /note="WD 8"
FT REPEAT 1163..1204
FT /note="WD 9"
FT REPEAT 1244..1281
FT /note="WD 10"
FT REPEAT 2761..2800
FT /note="WD 11"
FT REPEAT 2804..2843
FT /note="WD 12"
FT REPEAT 2850..2892
FT /note="WD 13"
FT REPEAT 2898..2937
FT /note="WD 14"
FT REPEAT 2940..2979
FT /note="WD 15"
FT REPEAT 2992..3030
FT /note="WD 16"
FT REGION 417..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1927..1952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1999..2033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2122..2153
FT /evidence="ECO:0000255"
FT COMPBIAS 433..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1999..2013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BPN8"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BPN8"
FT MOD_RES 944
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 945
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BPN8"
FT MOD_RES 1400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1417
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BPN8"
FT MOD_RES 1857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1984
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 2022
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BPN8"
FT MOD_RES 2399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BPN8"
FT VAR_SEQ 922..1557
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043015"
FT VAR_SEQ 2278
FT /note="S -> SS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10048485,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_044977"
FT VARIANT 144
FT /note="E -> Q (in dbSNP:rs35097381)"
FT /id="VAR_062094"
FT VARIANT 497
FT /note="T -> M (in dbSNP:rs17524906)"
FT /id="VAR_057593"
FT VARIANT 903
FT /note="N -> D (in dbSNP:rs16953073)"
FT /id="VAR_057594"
FT VARIANT 1288
FT /note="S -> P (in dbSNP:rs12102203)"
FT /evidence="ECO:0000269|PubMed:10048485,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_057595"
FT VARIANT 1481
FT /note="D -> G (in dbSNP:rs35349640)"
FT /id="VAR_057596"
FT VARIANT 1493..3036
FT /note="Missing (in DEE81)"
FT /evidence="ECO:0000269|PubMed:31688942"
FT /id="VAR_083446"
FT VARIANT 1698
FT /note="N -> S (in dbSNP:rs149028181)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_069028"
FT VARIANT 1712
FT /note="A -> V (in DEE81; dbSNP:rs372749193)"
FT /evidence="ECO:0000269|PubMed:31688942"
FT /id="VAR_083447"
FT VARIANT 1942..1946
FT /note="Missing (in PEPNS)"
FT /evidence="ECO:0000269|PubMed:25248098"
FT /id="VAR_072642"
FT VARIANT 2417
FT /note="R -> H (in DFNA71)"
FT /evidence="ECO:0000269|PubMed:27657680"
FT /id="VAR_079484"
FT CONFLICT 128
FT /note="A -> T (in Ref. 1; AAL93215)"
FT /evidence="ECO:0000305"
FT CONFLICT 974
FT /note="S -> F (in Ref. 1; AAL93215)"
FT /evidence="ECO:0000305"
FT CONFLICT 2984
FT /note="H -> Y (in Ref. 1; AAL93215)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3036 AA; 339641 MW; 25E9B1D05C69882C CRC64;
MHLHQVLTGA VNPGDNCYSV GSVGDVPFTA YGSGCDIVIL ANDFECVQII PGAKHGNIQV
SCVECSNQQG RIAASYGNAV CIFEPLGINS HKRNCQLKCQ WLKTGQFFLS SVTYNLAWDP
QDNRLLTATD SIQLWAPPGD DILEEEEEID NTVPPVLNDW KCVWQCKTSV SVHLMEWSPD
GEYFATAGKD DCLLKVWYPM TGWKSSIIPQ DHHEVKRRQS STQFSFVYLA HPRAVTGFSW
RKTSKYMPRG SVCNVLLTSC HDGVCRLWAE TLLPEDCLLG EQICETTTSS IASSLSHAGR
HKDRIQHALE TIHHLKNLRK GQRRSSVLVT HAELMPDQTA MHEVQRHISH HANALCHFHI
AASINPATDI PNVLVGTAFN VDDGNGGFVV HWLNNKEFHF TSSTEVFMHQ LRKLSDKQVD
HENDDADRED EEHSQEDRER GLHMKLDHDL SLDRESEAGT GSSEHEDGER EGSPRTYSRL
SVPMPLPTVL LDRKIETLLT EWNKNPDMLF TIHPVDGTFL VWHVKYLDEY NPGIFRQVQV
SFSSRIPVAF PSGDASSLSK NIMMYACINA TKDSHHTLLH QEGMSVGSPH GSQPHSRSHS
THMNILAPTV MMISKHIDGS LNQWAVTFAD KSAFTTVLTV SHKFRYCGHR FHLNDLACHS
VLPLLLTSSH HNALLTPELD CQWDSDNKLS RLMDPVKHIK GSSKQPLRNA ATRTFHDPNA
IYSELILWRV DPIGPLSYTG GVSELARINS LHTSAFSNVA WLPTLIPSYC LGTYCNSASA
CFVASDGKNL RLYQAVVDAR KLLDELSDPE SSKLIGEVFN IVSQQSTARP GCIIELDAIT
NQCGSNTQLL HVFQEDFIIG YKPHKEDMEK KETEIFFQPS QGYRPPPFSE KFFLVVIEKD
SNNNSILHMW HLHLKSVQAC LAKASEGASS ESLLSVPGQK NVDSSPETSP SVSPMPHSSS
IANLQTASKL ILSSRLVYSQ PLDLPESVEV IRATPSAGHL SSSSIYPVCL APYLVVTTCS
DNKVRFWKCC MEANPECNKS DEKEIYHWKR WPLMNDEGED NSSTVSIVGR PVAVSCSYTG
RLAVAYKQPI HHNGFVSKEF SMHVCIFECE STGGSEWVLE QTIHLDDLVK VGSVLDSRVS
VDSNLFVYSK SDALLSKDRY LIPNIKHLVH LDWVSKEDGS HILTVGVGAN IFMYGRLSGI
VTEQTNSKDG VAVITLPLGG SIKQGVKSRW VLLRSIDLVS SVDGTPSLPV SLSWVRDGIL
VVGMDCEMHV YAQWKHAVKF GDTEADSSNA EEAAMQDHST FKSNMLARKS VVEGTAISDD
VFCSPTVIQD GGLFEAAHVL SPTLPQYHPT QLLELMDLGK VRRAKAILSH LVKCIAGEVA
IVRDPDAGEG TKRHLSRTIS VSGSTAKETV TVGKDGTRDY TEIDSIPPLP LYALLAADQD
TSYRISEEST KIPQSYEDQT VSQPEDQYSE LFQIQDIPTD DIDLEPEKRE NKSKVINLSQ
YGPAYFGQEH ARVLSSHLMH SSLPGLTRLE QMFLVALADT VATTSTELDE SRDKSCSGRD
TLDECGLRYL LAMRLHTCLL TSLPPLYRVQ LLHQGVSTCH FAWAFHSEAE EELINMIPAI
QRGDPQWSEL RAMGIGWWVR NINTLRRCIE KVAKASFQRN NDALDAALFY LSMKKKAVVW
GLFRSQHDEK MTTFFSHNFN EDRWRKAALK NAFSLLGKQR FEQSAAFFLL AGSLKDAIEV
CLEKMEDIQL AMVIARLYES EFETSSTYIS ILNQKILGCQ KDGSGFSCKR LHPDPFLRSL
AYWVMKDYTR ALDTLLEQTP KEDDEHQVII KSCNPVAFSF YNYLRTHPLL IRRNLASPEG
TLATLGLKTE KNFVDKINLI ERKLFFTTAN AHFKVGCPVL ALEVLSKIPK VTKTSALSAK
KDQPDFISHR MDDVPSHSKA LSDGNGSSGI EWSNVTSSQY DWSQPIVKVD EEPLNLDWGE
DHDSALDEEE DDAVGLVMKS TDAREKDKQS DQKASDPNML LTPQEEDDPE GDTEVDVIAE
QLKFRACLKI LMTELRTLAT GYEVDGGKLR FQLYNWLEKE IAALHEICNH ESVIKEYSSK
TYSKVESDLL DQEEMVDKPD IGSYERHQIE RRRLQAKREH AERRKSWLQK NQDLLRVFLS
YCSLHGAQGG GLASVRMELK FLLQESQQET TVKQLQSPLP LPTTLPLLSA SIASTKTVIA
NPVLYLNNHI HDILYTIVQM KTPPHPSIED VKVHTLHSLA ASLSASIYQA LCDSHSYSQT
EGNQFTGMAY QGLLLSDRRR LRTESIEEHA TPNSSPAQWP GVSSLINLLS SAQDEDQPKL
NILLCEAVVA VYLSLLIHAL ATNSSSELFR LAAHPLNNRM WAAVFGGGVK LVVKPRRQSE
NISAPPVLSE DIDKHRRRFN MRMLVPGRPV KDATPPPVPA ERPSYKEKFI PPELSMWDYF
VAKPFLPLSD SGVIYDSDES IHSDEEDDAF FSDTQIQEHQ DPNSYSWALL HLTMVKLALH
NVKNFFPIAG LEFSELPVTS PLGIAVIKNL ENWEQILQEK MDQFEGPPPN YINTYPTDLS
VGAGPAILRN KAMLEPENTP FKSRDSSAFP VKRLWHFLVK QEVLQETFIR YIFTKKRKQS
EVEADLGYPG GKAKVIHKES DMIMAFSVNK ANCNEIVLAS THDVQELDVT SLLACQSYIW
IGEEYDRESK SSDDVDYRGS TTTLYQPSAT SYSASQVHPP SSLPWLGTGQ TSTGASVLMK
RNLHNVKRMT SHPVHQYYLT GAQDGSVRMF EWTRPQQLVC FRQAGNARVT RLYFNSQGNK
CGVADGEGFL SIWQVNQTAS NPKPYMSWQC HSKATSDFAF ITSSSLVATS GHSNDNRNVC
LWDTLISPGN SLIHGFTCHD HGATVLQYAP KQQLLISGGR KGHVCIFDIR QRQLIHTFQA
HDSAIKALAL DPYEEYFTTG SAEGNIKVWR LTGHGLIHSF KSEHAKQSIF RNIGAGVMQI
DIIQGNRLFS CGADGTLKTR VLPNAFNIPN RILDIL
