ID NHS_HUMAN Reviewed; 1651 AA. AC Q6T4R5; B7ZVX8; E2DH69; Q5J7Q0; Q5J7Q1; Q68DR5; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2013, sequence version 2. DT 24-JAN-2024, entry version 150. DE RecName: Full=Actin remodeling regulator NHS {ECO:0000305}; DE AltName: Full=Congenital cataracts and dental anomalies protein; DE AltName: Full=Nance-Horan syndrome protein; GN Name=NHS; 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 2), TISSUE SPECIFICITY, AND INVOLVEMENT RP IN NANCE-HORAN SYNDROME. RX PubMed=14564667; DOI=10.1086/379381; RA Burdon K.P., McKay J.D., Sale M.M., Russell-Eggit I.M., Mackey D.A., RA Wirth M.G., Elder J.E., Nicoll A., Clark M.P., FitzGerald L.M., RA Stankovich J.M., Shaw M.A., Sharma S., Gajovic S., Gruss P., Ross S., RA Thomas P., Voss A.K., Thomas T., Gecz J., Craig J.E.; RT "Mutations in a novel gene, NHS, cause the pleiotropic effects of Nance- RT Horan syndrome, including severe congenital cataract, dental anomalies, and RT mental retardation."; RL Am. J. Hum. Genet. 73:1120-1130(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4). RA Dessay B., Ronce N., Kaplan J., Hartsfield J.K., Wallgren-Pettersson C., RA Walpole I., Russo S., Chelly J., Moraine C., Toutain A.; RT "Identification of the gene involved in Nance-Horan syndrome."; RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND RP ALTERNATIVE SPLICING. RX PubMed=16675532; DOI=10.1093/hmg/ddl120; RA Sharma S., Ang S.L., Shaw M., Mackey D.A., Gecz J., McAvoy J.W., RA Craig J.E.; RT "Nance-Horan syndrome protein, NHS, associates with epithelial cell RT junctions."; RL Hum. Mol. Genet. 15:1972-1983(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 964-1651. RC TISSUE=Fetal kidney; 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 [7] RP TISSUE SPECIFICITY, AND INVOLVEMENT IN NANCE-HORAN SYNDROME. RX PubMed=15466011; DOI=10.1136/jmg.2004.022517; RA Brooks S.P., Ebenezer N.D., Poopalasundaram S., Lehmann O.J., Moore A.T., RA Hardcastle A.J.; RT "Identification of the gene for Nance-Horan syndrome (NHS)."; RL J. Med. Genet. 41:768-771(2004). 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-1176; THR-1262; RP SER-1329 AND SER-1499, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 SUBCELLULAR LOCATION, AND INTERACTION WITH TJP1/ZO-1. RX PubMed=19447104; DOI=10.1016/j.yexcr.2009.05.008; RA Sharma S., Koh K.S., Collin C., Dave A., McMellon A., Sugiyama Y., RA McAvoy J.W., Voss A.K., Gecz J., Craig J.E.; RT "NHS-A isoform of the NHS gene is a novel interactor of ZO-1."; RL Exp. Cell Res. 315:2358-2372(2009). RN [11] RP INVOLVEMENT IN CTRCT40. RX PubMed=19414485; DOI=10.1093/hmg/ddp206; RA Coccia M., Brooks S.P., Webb T.R., Christodoulou K., Wozniak I.O., RA Murday V., Balicki M., Yee H.A., Wangensteen T., Riise R., Saggar A.K., RA Park S.M., Kanuga N., Francis P.J., Maher E.R., Moore A.T., RA Russell-Eggitt I.M., Hardcastle A.J.; RT "X-linked cataract and Nance-Horan syndrome are allelic disorders."; RL Hum. Mol. Genet. 18:2643-2655(2009). RN [12] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=20332100; DOI=10.1093/hmg/ddq125; RA Brooks S.P., Coccia M., Tang H.R., Kanuga N., Machesky L.M., Bailly M., RA Cheetham M.E., Hardcastle A.J.; RT "The Nance-Horan syndrome protein encodes a functional WAVE homology domain RT (WHD) and is important for co-ordinating actin remodelling and maintaining RT cell morphology."; RL Hum. Mol. Genet. 19:2421-2432(2010). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-332; THR-401; SER-415; RP SER-533 AND SER-739, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [14] RP VARIANT [LARGE SCALE ANALYSIS] THR-865. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [15] RP VARIANT PRO-1628. RX PubMed=23092983; DOI=10.1038/tp.2012.102; RA Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B., Cohen D., RA Faudet A., Bouteiller D., Gilleron M., Jacquette A., Whalen S., Afenjar A., RA Perisse D., Laurent C., Dupuits C., Gautier C., Gerard M., Huguet G., RA Caillet S., Leheup B., Leboyer M., Gillberg C., Delorme R., Bourgeron T., RA Brice A., Depienne C.; RT "Analysis of the chromosome X exome in patients with autism spectrum RT disorders identified novel candidate genes, including TMLHE."; RL Transl. Psychiatry 2:E179-E179(2012). RN [16] RP VARIANT CYS-583. RX PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179; RA Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G., RA Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.; RT "Homozygous missense mutation in the LMAN2L gene segregates with RT intellectual disability in a large consanguineous Pakistani family."; RL J. Med. Genet. 53:138-144(2016). CC -!- FUNCTION: May function in cell morphology by maintaining the integrity CC of the circumferential actin ring and controlling lamellipod formation. CC Involved in the regulation eye, tooth, brain and craniofacial CC development. {ECO:0000269|PubMed:20332100}. CC -!- SUBUNIT: Interacts with the tight junction protein TJP1/ZO-1. CC Associates with actin-rich structures. Interacts with BRK1 and with all CC three members of the WAVE protein family, WASF1, WASF2 and WASF3. CC {ECO:0000269|PubMed:19447104, ECO:0000269|PubMed:20332100}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Apical cell membrane; Peripheral CC membrane protein. Cell projection, lamellipodium. Cell junction, tight CC junction. Cell junction, focal adhesion. Note=Colocalizes with the CC tight junction protein TJP1 in epithelial cells. Localizes to the CC leading edge of lamellipodia in motile cells. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=NHS-A; CC IsoId=Q6T4R5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6T4R5-2; Sequence=VSP_046541; CC Name=3; Synonyms=NHS-1A; CC IsoId=Q6T4R5-3; Sequence=VSP_046537, VSP_046540; CC Name=4; CC IsoId=Q6T4R5-4; Sequence=VSP_046538, VSP_046539, VSP_046540; CC -!- TISSUE SPECIFICITY: Detected at low levels in all tissues analyzed. CC Detected in fetal and adult brain, lens, retina, retinal pigment CC epithelium, placenta, lymphocytes and fibroblasts. Levels in retinal CC pigment epithelium, placenta, lymphocytes, and fibroblasts are very CC low. Expressed also in kidney, lung and thymus. CC {ECO:0000269|PubMed:14564667, ECO:0000269|PubMed:15466011}. CC -!- DISEASE: Nance-Horan syndrome (NHS) [MIM:302350]: Rare X-linked CC disorder characterized by congenital cataracts, dental anomalies, CC dysmorphic features, and, in some cases, intellectual disability. CC Distinctive dental anomalies are seen in affected males, including CC supernumerary incisors and crown shaped permanent teeth. Characteristic CC facial features are anteverted pinnae, long face, and prominent nasal CC bridge and nose. Carrier females display milder variable symptoms of CC disease with lens opacities often involving the posterior Y sutures, CC and on occasion dental anomalies and the characteristic facial features CC described. {ECO:0000269|PubMed:14564667, ECO:0000269|PubMed:15466011}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Cataract 40 (CTRCT40) [MIM:302200]: An opacification of the CC crystalline lens of the eye that frequently results in visual CC impairment or blindness. Opacities vary in morphology, are often CC confined to a portion of the lens, and may be static or progressive. CC CTRCT40 manifests as a congenital nuclear opacity with severe visual CC impairment in affected males. Heterozygous females have suture CC cataracts and only slight reduction in vision. In some cases, cataract CC is associated with microcornea without any other systemic anomaly or CC dysmorphism. Microcornea is defined by a corneal diameter inferior to CC 10 mm in both meridians in an otherwise normal eye. CC {ECO:0000269|PubMed:19414485}. Note=The disease is caused by variants CC affecting the gene represented in this entry. Caused by copy number CC variations predicted to result in altered transcriptional regulation of CC the NHS gene: a 0.8 Mb segmental duplication-triplication encompassing CC the NHS, SCML1 and RAI2 genes, and an 4.8 kb intragenic deletion in NHS CC intron 1. CC -!- SIMILARITY: Belongs to the NHS family. {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; AY436752; AAR03104.1; -; mRNA. DR EMBL; AY456993; AAS13456.1; -; mRNA. DR EMBL; AY456992; AAS13455.1; -; mRNA. DR EMBL; GQ988776; ADN85614.1; -; mRNA. DR EMBL; AL845433; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z93242; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC136415; AAI36416.1; -; mRNA. DR EMBL; BC171763; AAI71763.1; -; mRNA. DR EMBL; CR749300; CAH18155.1; -; mRNA. DR CCDS; CCDS14181.1; -. [Q6T4R5-2] DR CCDS; CCDS48087.1; -. [Q6T4R5-3] DR CCDS; CCDS94562.1; -. [Q6T4R5-1] DR RefSeq; NP_001129496.1; NM_001136024.3. [Q6T4R5-3] DR RefSeq; NP_001278796.1; NM_001291867.1. [Q6T4R5-1] DR RefSeq; NP_001278797.1; NM_001291868.1. DR RefSeq; NP_938011.1; NM_198270.3. [Q6T4R5-2] DR AlphaFoldDB; Q6T4R5; -. DR BioGRID; 110875; 56. DR ELM; Q6T4R5; -. DR IntAct; Q6T4R5; 25. DR MINT; Q6T4R5; -. DR STRING; 9606.ENSP00000369400; -. DR GlyGen; Q6T4R5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6T4R5; -. DR PhosphoSitePlus; Q6T4R5; -. DR BioMuta; NHS; -. DR DMDM; 510120778; -. DR EPD; Q6T4R5; -. DR jPOST; Q6T4R5; -. DR MassIVE; Q6T4R5; -. DR MaxQB; Q6T4R5; -. DR PaxDb; 9606-ENSP00000369400; -. DR PeptideAtlas; Q6T4R5; -. DR ProteomicsDB; 67371; -. [Q6T4R5-1] DR ProteomicsDB; 67372; -. [Q6T4R5-2] DR ProteomicsDB; 67373; -. [Q6T4R5-3] DR Pumba; Q6T4R5; -. DR Antibodypedia; 24084; 41 antibodies from 13 providers. DR DNASU; 4810; -. DR Ensembl; ENST00000380060.7; ENSP00000369400.3; ENSG00000188158.17. [Q6T4R5-2] DR Ensembl; ENST00000398097.7; ENSP00000381170.3; ENSG00000188158.17. [Q6T4R5-3] DR Ensembl; ENST00000676302.1; ENSP00000502262.1; ENSG00000188158.17. [Q6T4R5-1] DR GeneID; 4810; -. DR KEGG; hsa:4810; -. DR MANE-Select; ENST00000676302.1; ENSP00000502262.1; NM_001291867.2; NP_001278796.1. DR UCSC; uc004cxx.4; human. [Q6T4R5-1] DR AGR; HGNC:7820; -. DR CTD; 4810; -. DR DisGeNET; 4810; -. DR GeneCards; NHS; -. DR HGNC; HGNC:7820; NHS. DR HPA; ENSG00000188158; Low tissue specificity. DR MalaCards; NHS; -. DR MIM; 300457; gene. DR MIM; 302200; phenotype. DR MIM; 302350; phenotype. DR neXtProt; NX_Q6T4R5; -. DR OpenTargets; ENSG00000188158; -. DR Orphanet; 98991; Early-onset nuclear cataract. DR Orphanet; 627; Nance-Horan syndrome. DR Orphanet; 98994; Total early-onset cataract. DR PharmGKB; PA31622; -. DR VEuPathDB; HostDB:ENSG00000188158; -. DR eggNOG; ENOG502QSCT; Eukaryota. DR GeneTree; ENSGT00950000182963; -. DR InParanoid; Q6T4R5; -. DR OMA; CAWPDYL; -. DR OrthoDB; 5355272at2759; -. DR TreeFam; TF333323; -. DR PathwayCommons; Q6T4R5; -. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013404; RAC2 GTPase cycle. DR Reactome; R-HSA-9013423; RAC3 GTPase cycle. DR SignaLink; Q6T4R5; -. DR SIGNOR; Q6T4R5; -. DR BioGRID-ORCS; 4810; 15 hits in 769 CRISPR screens. DR ChiTaRS; NHS; human. DR GeneWiki; NHS_(gene); -. DR GenomeRNAi; 4810; -. DR Pharos; Q6T4R5; Tbio. DR PRO; PR:Q6T4R5; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q6T4R5; Protein. DR Bgee; ENSG00000188158; Expressed in oviduct epithelium and 152 other cell types or tissues. DR ExpressionAtlas; Q6T4R5; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central. DR Gene3D; 1.20.5.340; -; 1. DR InterPro; IPR024845; NHS-like. DR PANTHER; PTHR23039; NANCE-HORAN SYNDROME PROTEIN; 1. DR PANTHER; PTHR23039:SF5; NANCE-HORAN SYNDROME PROTEIN; 1. DR Pfam; PF15273; NHS; 1. DR Genevisible; Q6T4R5; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cataract; Cell junction; Cell membrane; KW Cell projection; Cytoplasm; Membrane; Phosphoprotein; Reference proteome; KW Tight junction. FT CHAIN 1..1651 FT /note="Actin remodeling regulator NHS" FT /id="PRO_0000096810" FT REGION 1..262 FT /note="WAVE homology domain (WHD)" FT REGION 1..104 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 235..274 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 288..314 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 494..598 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 620..669 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 835..888 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 980..1004 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1017..1071 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1383..1436 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1454..1509 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1526..1651 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 57..80 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 235..251 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 545..571 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 628..669 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 859..877 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1020..1041 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1403..1422 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1468..1509 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1553..1574 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1583..1599 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 332 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 401 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 415 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 533 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 739 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1176 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1262 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1329 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1499 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 1..12 FT /note="MPFAKRIVEPQW -> MALACCMPKNAA (in isoform 3)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_046537" FT VAR_SEQ 1..11 FT /note="MPFAKRIVEPQ -> MDNALFLCLAA (in isoform 4)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_046538" FT VAR_SEQ 12 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_046539" FT VAR_SEQ 13..189 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_046540" FT VAR_SEQ 285..305 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14564667" FT /id="VSP_046541" FT VARIANT 583 FT /note="R -> C (in dbSNP:rs753449273)" FT /evidence="ECO:0000269|PubMed:26566883" FT /id="VAR_076438" FT VARIANT 865 FT /note="A -> T (in a breast cancer sample; somatic mutation; FT dbSNP:rs149609550)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036225" FT VARIANT 1340 FT /note="F -> L (in dbSNP:rs3747295)" FT /id="VAR_021527" FT VARIANT 1531 FT /note="S -> T (in dbSNP:rs2071848)" FT /id="VAR_051234" FT VARIANT 1556 FT /note="S -> T (in dbSNP:rs2071848)" FT /id="VAR_021528" FT VARIANT 1628 FT /note="A -> P" FT /evidence="ECO:0000269|PubMed:23092983" FT /id="VAR_076261" FT CONFLICT 305 FT /note="K -> KQ (in Ref. 1; ADN85614)" FT /evidence="ECO:0000305" SQ SEQUENCE 1651 AA; 179135 MW; 9B98C97BA0109F82 CRC64; MPFAKRIVEP QWLCRQRRPA PGPAVDASGG SAEPPPPLQP PGRRDLDEVE APGPEEPARA VPAPSGLPPP PPPLPAPADQ TQPPHGEASV AGEESTAGIP EAAPAAGEAS SAAAAAAVLL MLDLCAVSNA ALARVLRQLS DVARHACSLF QELESDIQLT HRRVWALQGK LGGVQRVLST LDPKQEAVPV SNLDIESKLS VYYRAPWHQQ RNIFLPATRP PCVEELHRHA RQSLQALRRE HRSRSDRREQ RAAAPLSIAA PPLPAYPPAH SQRRREFKDR HFLTFNSTRS PSPTECCHMT PWSRKSHPPE DEDTDVMLGQ RPKNPIHNIP STLDKQTNWS KALPLPTPEE KMKQDAQVIS SCIIPINVTG VGFDREASIR CSLVHSQSVL QRRRKLRRRK TISGIPRRVQ QEIDSDESPV ARERNVIVHT NPDPSNTVNR ISGTRDSECQ TEDILIAAPS RRRIRAQRGQ SIAASLSHSA GNISALADKG DTMFTPAVSS RTRSRSLPRE GNRGGDAEPK VGAKPSAYEE GESFVGDHER TPNDFSEAPS SPSAQDHQPT LGLACSQHLH SPQHKLSERG RSRLSRMAAD SGSCDISSNS DTFGSPIHCI STAGVLLSSH MDQKDDHQSS SGNWSGSSST CPSQTSETIP PAASPPLTGS SHCDSELSLN TAPHANEDAS VFVTEQYNDH LDKVRGHRAN SFTSTVADLL DDPNNSNTSD SEWNYLHHHH DASCRQDFSP ERPKADSLGC PSFTSMATYD SFLEKSPSDK ADTSSHFSVD TEGYYTSMHF DCGLKGNKSY VCHYAALGPE NGQGVGASPG LPDCAWQDYL DHKRQGRPSI SFRKPKAKPT PPKRSSSLRK SDGNADISEK KEPKISSGQH LPHSSREMKL PLDFANTPSR MENANLPTKQ EPSWINQSEQ GIKEPQLDAS DIPPFKDEVA ESTHYADLWL LNDLKTNDPY RSLSNSSTAT GTTVIECIKS PESSESQTSQ SESRATTPSL PSVDNEFKLA SPEKLAGLAS PSSGYSSQSE TPTSSFPTAF FSGPLSPGGS KRKPKVPERK SSLQQPSLKD GTISLSKDLE LPIIPPTHLD LSALHNVLNK PFHHRHPLHV FTHNKQNTVG ETLRSNPPPS LAITPTILKS VNLRSINKSE EVKQKEENNT DLPYLEESTL TTAALSPSKI RPHTANKSVS RQYSTEDTIL SFLDSSAVEM GPDKLHLEKN STFDVKNRCD PETITSAGSS LLDSNVTKDQ VRTETEPIPE NTPTKNCAFP TEGFQRVSAA RPNDLDGKII QYGPGPDETL EQVQKAPSAG LEEVAQPESV DVITSQSDSP TRATDVSNQF KHQFVMSRHH DKVPGTISYE SEITSVNSFP EKCSKQENIA SGISAKSASD NSKAEETQGN VDEASLKESS PSDDSIISPL SEDSQAEAEG VFVSPNKPRT TEDLFAVIHR SKRKVLGRKD SGDMSVRSKS RAPLSSSSSS ASSITSPSSN VTTPNSQRSP GLIYRNAKKS NTSNEEFKLL LLKKGSRSDS SYRMSATEIL KSPILPKPPG ELTAESPQST DDAHQGSQGA EALSPLSPCS PRVNAEGFSS KSFATSASAR VGRSRAPPAA SSSRYSVRCR LYNTPMQAIS EGETENSDGS PHDDRSSQSS T //