NHS_HUMAN
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 03-AUG-2022, entry version 142.
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 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; 47.
DR ELM; Q6T4R5; -.
DR IntAct; Q6T4R5; 19.
DR MINT; Q6T4R5; -.
DR STRING; 9606.ENSP00000369400; -.
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; Q6T4R5; -.
DR PeptideAtlas; Q6T4R5; -.
DR PRIDE; Q6T4R5; -.
DR ProteomicsDB; 67371; -. [Q6T4R5-1]
DR ProteomicsDB; 67372; -. [Q6T4R5-2]
DR ProteomicsDB; 67373; -. [Q6T4R5-3]
DR Antibodypedia; 24084; 27 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 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; VMSHHHD; -.
DR OrthoDB; 60972at2759; -.
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; 13 hits in 695 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 151 other tissues.
DR ExpressionAtlas; Q6T4R5; baseline and differential.
DR Genevisible; Q6T4R5; HS.
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 InterPro; IPR024845; NHS_fam.
DR Pfam; PF15273; NHS; 1.
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
