AP4E1_HUMAN
ID AP4E1_HUMAN Reviewed; 1137 AA.
AC Q9UPM8; A0AVD6; A1L4A9; A6NNX7; H0YKX4; Q68D31; Q9Y588;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=AP-4 complex subunit epsilon-1 {ECO:0000305};
DE AltName: Full=AP-4 adaptor complex subunit epsilon;
DE AltName: Full=Adaptor-related protein complex 4 subunit epsilon-1;
DE AltName: Full=Epsilon subunit of AP-4;
DE AltName: Full=Epsilon-adaptin;
GN Name=AP4E1 {ECO:0000312|HGNC:HGNC:573};
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), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Heart, and Testis;
RX PubMed=10436028; DOI=10.1091/mbc.10.8.2787;
RA Hirst J., Bright N.A., Rous B., Robinson M.S.;
RT "Characterization of a fourth adaptor-related protein complex.";
RL Mol. Biol. Cell 10:2787-2802(1999).
RN [2]
RP SEQUENCE REVISION.
RA Hirst J., Robinson M.S.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-163.
RX PubMed=11409905; DOI=10.1006/bbrc.2001.5081;
RA Takatsu H., Futatsumori M., Yoshino K., Yoshida Y., Shin H.W., Nakayama K.;
RT "Similar subunit interactions contribute to assembly of clathrin adaptor
RT complexes and COPI complex: analysis using yeast three-hybrid system.";
RL Biochem. Biophys. Res. Commun. 284:1083-1089(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ARG-163.
RC TISSUE=Uterine endothelium;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-163.
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 [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10066790; DOI=10.1074/jbc.274.11.7278;
RA Dell'Angelica E.C., Mullins C., Bonifacino J.S.;
RT "AP-4, a novel protein complex related to clathrin adaptors.";
RL J. Biol. Chem. 274:7278-7285(1999).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857, 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 [10]
RP INVOLVEMENT IN SPG51.
RX PubMed=20972249; DOI=10.1136/jmg.2010.082263;
RA Moreno-De-Luca A., Helmers S.L., Mao H., Burns T.G., Melton A.M.,
RA Schmidt K.R., Fernhoff P.M., Ledbetter D.H., Martin C.L.;
RT "Adaptor protein complex-4 (AP-4) deficiency causes a novel autosomal
RT recessive cerebral palsy syndrome with microcephaly and intellectual
RT disability.";
RL J. Med. Genet. 48:141-144(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-700, 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 [12]
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 [13]
RP INTERACTION WITH TEPSIN, AND REGION.
RX PubMed=26542808; DOI=10.1074/jbc.m115.683409;
RA Mattera R., Guardia C.M., Sidhu S.S., Bonifacino J.S.;
RT "Bivalent motif-ear interactions mediate the association of the accessory
RT protein tepsin with the AP-4 adaptor complex.";
RL J. Biol. Chem. 290:30736-30749(2015).
RN [14]
RP INVOLVEMENT IN STUT1, VARIANTS STUT1 VAL-96; ASN-205; SER-311; PHE-326;
RP ARG-384; VAL-475; ILE-517; VAL-542; PRO-623; LYS-801; PRO-905; SER-978;
RP VAL-1080; ARG-1089 AND GLN-1105, VARIANTS THR-85; SER-145; GLN-211;
RP SER-264; LEU-426; ILE-618; PRO-623; LYS-706 AND VAL-813, AND
RP CHARACTERIZATION OF VARIANTS STUT1 ILE-517 AND LYS-801.
RX PubMed=26544806; DOI=10.1016/j.ajhg.2015.10.007;
RA Raza M.H., Mattera R., Morell R., Sainz E., Rahn R., Gutierrez J.,
RA Paris E., Root J., Solomon B., Brewer C., Basra M.A., Khan S.,
RA Riazuddin S., Braun A., Bonifacino J.S., Drayna D.;
RT "Association between rare variants in AP4E1, a component of intracellular
RT trafficking, and persistent stuttering.";
RL Am. J. Hum. Genet. 97:715-725(2015).
RN [15]
RP VARIANT GLU-719.
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).
CC -!- FUNCTION: Component of the adaptor protein complex 4 (AP-4). Adaptor
CC protein complexes are vesicle coat components involved both in vesicle
CC formation and cargo selection. They control the vesicular transport of
CC proteins in different trafficking pathways (PubMed:10066790,
CC PubMed:10436028). AP-4 forms a non clathrin-associated coat on vesicles
CC departing the trans-Golgi network (TGN) and may be involved in the
CC targeting of proteins from the trans-Golgi network (TGN) to the
CC endosomal-lysosomal system. It is also involved in protein sorting to
CC the basolateral membrane in epithelial cells and the proper asymmetric
CC localization of somatodendritic proteins in neurons. AP-4 is involved
CC in the recognition and binding of tyrosine-based sorting signals found
CC in the cytoplasmic part of cargos, but may also recognize other types
CC of sorting signal (Probable). {ECO:0000269|PubMed:10066790,
CC ECO:0000269|PubMed:10436028, ECO:0000305|PubMed:10066790,
CC ECO:0000305|PubMed:10436028}.
CC -!- SUBUNIT: Adaptor protein complex 4 (AP-4) is a heterotetramer composed
CC of two large adaptins (epsilon-type subunit AP4E1 and beta-type subunit
CC AP4B1), a medium adaptin (mu-type subunit AP4M1) and a small adaptin
CC (sigma-type AP4S1) (PubMed:10436028, PubMed:10066790). Interacts with
CC TEPSIN (PubMed:26542808). Interacts with GRIA2; probably indirect it
CC mediates the somatodendritic localization of GRIA2 in neurons (By
CC similarity). {ECO:0000250|UniProtKB:Q80V94,
CC ECO:0000269|PubMed:10066790, ECO:0000269|PubMed:10436028,
CC ECO:0000269|PubMed:26542808}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000305|PubMed:10436028}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UPM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPM8-2; Sequence=VSP_046009;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10436028}.
CC -!- DISEASE: Spastic paraplegia 51, autosomal recessive (SPG51)
CC [MIM:613744]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. SPG51 is a non-progressive disorder of
CC movement and/or posture resulting from defects in the developing
CC central nervous system. Affected individuals manifest motor and posture
CC impairments often associated with epilepsy and disturbances of
CC cognition, behavior, sensation, and communication.
CC {ECO:0000269|PubMed:20972249}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Stuttering, familial persistent 1 (STUT1) [MIM:184450]: A
CC familial form of stuttering, a disturbance in the normal fluency and
CC time patterning of speech, characterized by frequent repetitions or
CC prolongations of sounds or syllables, and by interruptions of speech
CC known as blocks. STUT1 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:26544806}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; AF155156; AAD43326.2; -; mRNA.
DR EMBL; AB030653; BAA82969.1; -; mRNA.
DR EMBL; CR749604; CAH18399.1; -; mRNA.
DR EMBL; AC021752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77411.1; -; Genomic_DNA.
DR EMBL; BC126308; AAI26309.1; -; mRNA.
DR EMBL; BC130466; AAI30467.1; -; mRNA.
DR CCDS; CCDS32240.1; -. [Q9UPM8-1]
DR CCDS; CCDS58362.1; -. [Q9UPM8-2]
DR RefSeq; NP_001239056.1; NM_001252127.1. [Q9UPM8-2]
DR RefSeq; NP_031373.2; NM_007347.4. [Q9UPM8-1]
DR RefSeq; XP_005254321.1; XM_005254264.3. [Q9UPM8-2]
DR RefSeq; XP_006720510.1; XM_006720447.3. [Q9UPM8-2]
DR AlphaFoldDB; Q9UPM8; -.
DR SMR; Q9UPM8; -.
DR BioGRID; 116999; 46.
DR ComplexPortal; CPX-5151; AP-4 Adaptor complex.
DR CORUM; Q9UPM8; -.
DR IntAct; Q9UPM8; 18.
DR STRING; 9606.ENSP00000261842; -.
DR TCDB; 9.B.278.1.5; the organellar-targeting adaptor protein complex (o-apc) family.
DR iPTMnet; Q9UPM8; -.
DR PhosphoSitePlus; Q9UPM8; -.
DR BioMuta; AP4E1; -.
DR DMDM; 145559441; -.
DR EPD; Q9UPM8; -.
DR jPOST; Q9UPM8; -.
DR MassIVE; Q9UPM8; -.
DR MaxQB; Q9UPM8; -.
DR PaxDb; Q9UPM8; -.
DR PeptideAtlas; Q9UPM8; -.
DR PRIDE; Q9UPM8; -.
DR ProteomicsDB; 39780; -.
DR ProteomicsDB; 85379; -. [Q9UPM8-1]
DR Antibodypedia; 24780; 29 antibodies from 11 providers.
DR DNASU; 23431; -.
DR Ensembl; ENST00000261842.10; ENSP00000261842.5; ENSG00000081014.11. [Q9UPM8-1]
DR Ensembl; ENST00000560508.1; ENSP00000452976.1; ENSG00000081014.11. [Q9UPM8-2]
DR GeneID; 23431; -.
DR KEGG; hsa:23431; -.
DR MANE-Select; ENST00000261842.10; ENSP00000261842.5; NM_007347.5; NP_031373.2.
DR UCSC; uc001zyx.3; human. [Q9UPM8-1]
DR CTD; 23431; -.
DR DisGeNET; 23431; -.
DR GeneCards; AP4E1; -.
DR GeneReviews; AP4E1; -.
DR HGNC; HGNC:573; AP4E1.
DR HPA; ENSG00000081014; Low tissue specificity.
DR MalaCards; AP4E1; -.
DR MIM; 184450; phenotype.
DR MIM; 607244; gene.
DR MIM; 613744; phenotype.
DR neXtProt; NX_Q9UPM8; -.
DR OpenTargets; ENSG00000081014; -.
DR Orphanet; 280763; Severe intellectual disability and progressive spastic paraplegia.
DR PharmGKB; PA24865; -.
DR VEuPathDB; HostDB:ENSG00000081014; -.
DR eggNOG; KOG1062; Eukaryota.
DR GeneTree; ENSGT00950000182838; -.
DR HOGENOM; CLU_003824_3_1_1; -.
DR InParanoid; Q9UPM8; -.
DR OMA; VLMAMTK; -.
DR PhylomeDB; Q9UPM8; -.
DR TreeFam; TF332488; -.
DR PathwayCommons; Q9UPM8; -.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; Q9UPM8; -.
DR BioGRID-ORCS; 23431; 14 hits in 1087 CRISPR screens.
DR ChiTaRS; AP4E1; human.
DR GeneWiki; AP4E1; -.
DR GenomeRNAi; 23431; -.
DR Pharos; Q9UPM8; Tdark.
DR PRO; PR:Q9UPM8; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9UPM8; protein.
DR Bgee; ENSG00000081014; Expressed in gingival epithelium and 181 other tissues.
DR ExpressionAtlas; Q9UPM8; baseline and differential.
DR Genevisible; Q9UPM8; HS.
DR GO; GO:0030124; C:AP-4 adaptor complex; IDA:UniProtKB.
DR GO; GO:0031904; C:endosome lumen; TAS:Reactome.
DR GO; GO:0005802; C:trans-Golgi network; IC:ComplexPortal.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0140312; F:cargo adaptor activity; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IC:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IC:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IC:ComplexPortal.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR017109; AP4_complex_esu.
DR InterPro; IPR028269; AP4E1_C.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF14807; AP4E_app_platf; 1.
DR PIRSF; PIRSF037097; AP4_complex_epsilon; 1.
DR SMART; SM01356; AP4E_app_platf; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Golgi apparatus; Hereditary spastic paraplegia;
KW Membrane; Neurodegeneration; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1137
FT /note="AP-4 complex subunit epsilon-1"
FT /id="PRO_0000193769"
FT REGION 727..1137
FT /note="Interaction with TEPSIN"
FT /evidence="ECO:0000269|PubMed:26542808"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_046009"
FT VARIANT 85
FT /note="I -> T (in dbSNP:rs147005786)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076619"
FT VARIANT 96
FT /note="F -> V (in STUT1; unknown pathological significance;
FT dbSNP:rs566579877)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076620"
FT VARIANT 145
FT /note="T -> S (in dbSNP:rs200034177)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076621"
FT VARIANT 163
FT /note="C -> R (in dbSNP:rs2306331)"
FT /evidence="ECO:0000269|PubMed:11409905,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_031621"
FT VARIANT 205
FT /note="H -> N (in STUT1; unknown pathological significance;
FT dbSNP:rs148499164)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076622"
FT VARIANT 211
FT /note="R -> Q (in dbSNP:rs750328226)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076623"
FT VARIANT 264
FT /note="N -> S (in dbSNP:rs145541719)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076624"
FT VARIANT 311
FT /note="N -> S (in STUT1; unknown pathological significance;
FT dbSNP:rs536656846)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076625"
FT VARIANT 326
FT /note="S -> F (in STUT1; unknown pathological significance;
FT dbSNP:rs372479885)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076626"
FT VARIANT 384
FT /note="H -> R (in STUT1; unknown pathological significance;
FT dbSNP:rs866266998)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076627"
FT VARIANT 426
FT /note="I -> L (in dbSNP:rs148817957)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076628"
FT VARIANT 475
FT /note="A -> V (in STUT1; unknown pathological significance;
FT dbSNP:rs200678853)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076629"
FT VARIANT 517
FT /note="V -> I (in STUT1; slightly decreased assembly of the
FT AP-4 complex; dbSNP:rs760021635)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076630"
FT VARIANT 542
FT /note="M -> V (in STUT1; unknown pathological significance;
FT dbSNP:rs542940704)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076631"
FT VARIANT 618
FT /note="V -> I (in dbSNP:rs142215198)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076632"
FT VARIANT 623
FT /note="S -> P (in STUT1; unknown pathological significance;
FT dbSNP:rs766696884)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076633"
FT VARIANT 706
FT /note="I -> K (in dbSNP:rs865868636)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076634"
FT VARIANT 719
FT /note="K -> E (found in deaf patients; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27657680"
FT /id="VAR_079485"
FT VARIANT 801
FT /note="E -> K (in STUT1; slightly decreased assembly of the
FT AP-4 complex; dbSNP:rs556450190)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076635"
FT VARIANT 813
FT /note="M -> V (in dbSNP:rs779094838)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076636"
FT VARIANT 905
FT /note="S -> P (in STUT1; unknown pathological significance;
FT dbSNP:rs780520338)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076637"
FT VARIANT 978
FT /note="P -> S (in STUT1; unknown pathological significance;
FT dbSNP:rs141278078)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076638"
FT VARIANT 1080
FT /note="I -> V (in STUT1; unknown pathological significance;
FT dbSNP:rs767423538)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076639"
FT VARIANT 1089
FT /note="L -> R (in STUT1; unknown pathological significance;
FT dbSNP:rs550237440)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076640"
FT VARIANT 1105
FT /note="R -> Q (in STUT1; unknown pathological significance;
FT dbSNP:rs139640763)"
FT /evidence="ECO:0000269|PubMed:26544806"
FT /id="VAR_076641"
FT CONFLICT 30
FT /note="A -> G (in Ref. 1; AAD43326)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="L -> F (in Ref. 1; AAD43326)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="L -> P (in Ref. 1; AAD43326)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..265
FT /note="EFNY -> NF (in Ref. 1; AAD43326)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="A -> V (in Ref. 4; CAH18399)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="R -> G (in Ref. 4; CAH18399)"
FT /evidence="ECO:0000305"
FT CONFLICT 991
FT /note="S -> G (in Ref. 4; CAH18399)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1137 AA; 127287 MW; 1784E886EC922875 CRC64;
MSDIVEKTLT ALPGLFLQNQ PGGGPAAAKA SFSSRLGSLV RGITALTSKH EEEKLIQQEL
SSLKATVSAP TTTLKMMKEC MVRLIYCEML GYDASFGYIH AIKLAQQGNL LEKRVGYLAV
SLFLHESHEL LLLLVNTVVK DLQSTNLVEV CMALTVVSQI FPCEMIPAVL PLIEDKLQHS
KEIVRRKAVL ALYKFHLIAP NQVQHIHIKF RKALCDRDVG VMAASLHIYL RMIKENSSGY
KDLTGSFVTI LKQVVGGKLP VEFNYHSVPA PWLQIQLLRI LGLLGKDDQR TSELMYDVLD
ESLRRAELNH NVTYAILFEC VHTVYSIYPK SELLEKAAKC IGKFVLSPKI NLKYLGLKAL
TYVIQQDPTL ALQHQMTIIE CLDHPDPIIK RETLELLYRI TNAQNITVIV QKMLEYLHQS
KEEYVIVNLV GKIAELAEKY APDNAWFIQT MNAVFSVGGD VMHPDIPNNF LRLLAEGFDD
ETEDQQLRLY AVQSYLTLLD MENVFYPQRF LQVMSWVLGE YSYLLDKETP EEVIAKLYKL
LMNDSVSSET KAWLIAAVTK LTSQAHSSNT VERLIHEFTI SLDTCMRQHA FELKHLHENV
ELMKSLLPVD RSCEDLVVDA SLSFLDGFVA EGLSQGAAPY KPPHQRQEEK LSQEKVLNFE
PYGLSFSSSG FTGRQSPAGI SLGSDVSGNS AETGLKETNS LKLEGIKKLW GKEGYLPKKE
SKTGDESGAL PVPQESIMEN VDQAITKKDQ SQVLTQSKEE KEKQLLASSL FVGLGSESTI
NLLGKADTVS HKFRRKSKVK EAKSGETTST HNMTCSSFSS LSNVAYEDDY YSNTLHDTGD
KELKKFSLTS ELLDSESLTE LPLVEKFSYC SLSTPSLFAN NNMEIFHPPQ STAASVAKES
SLASSFLEET TEYIHSNAME VCNNETISVS SYKIWKDDCL LMVWSVTNKS GLELKSADLE
IFPAENFKVT EQPGCCLPVM EAESTKSFQY SVQIEKPFTE GNLTGFISYH MMDTHSAQLE
FSVNLSLLDF IRPLKISSDD FGKLWLSFAN DVKQNVKMSE SQAALPSALK TLQQKLRLHI
IEIIGNEGLL ACQLLPSIPC LLHCRVHADV LALWFRSSCS TLPDYLLYQC QKVMEGS
