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 27-MAR-2024, entry version 185. 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 -!- INTERACTION: CC Q9UPM8; Q96N21: TEPSIN; NbExp=4; IntAct=EBI-1222435, EBI-11139477; 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}. 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; 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; 54. DR ComplexPortal; CPX-5151; AP-4 Adaptor complex. DR CORUM; Q9UPM8; -. DR IntAct; Q9UPM8; 23. 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; 9606-ENSP00000261842; -. DR PeptideAtlas; Q9UPM8; -. DR ProteomicsDB; 39780; -. DR ProteomicsDB; 85379; -. [Q9UPM8-1] DR Pumba; Q9UPM8; -. DR Antibodypedia; 24780; 31 antibodies from 12 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 AGR; HGNC:573; -. 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; ADNNMEI; -. DR OrthoDB; 25313at2759; -. 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; 16 hits in 1165 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 183 other cell types or tissues. DR ExpressionAtlas; Q9UPM8; baseline and differential. 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; NAS: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:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0008104; P:protein localization; IC:UniProtKB. DR GO; GO:0006605; P:protein targeting; IC:UniProtKB. DR GO; GO:0016192; P:vesicle-mediated transport; NAS:ComplexPortal. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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 PANTHER; PTHR22780; ADAPTIN, ALPHA/GAMMA/EPSILON; 1. DR PANTHER; PTHR22780:SF13; AP-4 COMPLEX SUBUNIT EPSILON-1; 1. 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; ARM repeat; 1. DR Genevisible; Q9UPM8; HS. 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; uncertain 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; uncertain 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; uncertain significance; FT dbSNP:rs536656846)" FT /evidence="ECO:0000269|PubMed:26544806" FT /id="VAR_076625" FT VARIANT 326 FT /note="S -> F (in STUT1; uncertain significance; FT dbSNP:rs372479885)" FT /evidence="ECO:0000269|PubMed:26544806" FT /id="VAR_076626" FT VARIANT 384 FT /note="H -> R (in STUT1; uncertain 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; uncertain 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; uncertain 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; uncertain 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; uncertain 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; uncertain significance; FT dbSNP:rs780520338)" FT /evidence="ECO:0000269|PubMed:26544806" FT /id="VAR_076637" FT VARIANT 978 FT /note="P -> S (in STUT1; uncertain significance; FT dbSNP:rs141278078)" FT /evidence="ECO:0000269|PubMed:26544806" FT /id="VAR_076638" FT VARIANT 1080 FT /note="I -> V (in STUT1; uncertain significance; FT dbSNP:rs767423538)" FT /evidence="ECO:0000269|PubMed:26544806" FT /id="VAR_076639" FT VARIANT 1089 FT /note="L -> R (in STUT1; uncertain significance; FT dbSNP:rs550237440)" FT /evidence="ECO:0000269|PubMed:26544806" FT /id="VAR_076640" FT VARIANT 1105 FT /note="R -> Q (in STUT1; uncertain 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 //