FCHO1_HUMAN
ID FCHO1_HUMAN Reviewed; 889 AA.
AC O14526; A6NHE6; A8K5U5; B4E120; Q05C93; Q8IW22;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=F-BAR domain only protein 1 {ECO:0000305};
GN Name=FCHO1 {ECO:0000312|HGNC:HGNC:29002}; Synonyms=KIAA0290;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9179496; DOI=10.1093/dnares/4.1.53;
RA Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA Nomura N.;
RT "Construction and characterization of human brain cDNA libraries suitable
RT for analysis of cDNA clones encoding relatively large proteins.";
RL DNA Res. 4:53-59(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood;
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 SUBCELLULAR LOCATION.
RX PubMed=17617719; DOI=10.1271/bbb.60720;
RA Sakaushi S., Inoue K., Zushi H., Senda-Murata K., Fukada T., Oka S.,
RA Sugimoto K.;
RT "Dynamic behavior of FCHO1 revealed by live-cell imaging microscopy: its
RT possible involvement in clathrin-coated vesicle formation.";
RL Biosci. Biotechnol. Biochem. 71:1764-1768(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [8]
RP FUNCTION IN CLATHRIN-COATED PITS NUCLEATION, AND SUBCELLULAR LOCATION.
RX PubMed=20448150; DOI=10.1126/science.1188462;
RA Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R.,
RA McMahon H.T.;
RT "FCHo proteins are nucleators of clathrin-mediated endocytosis.";
RL Science 328:1281-1284(2010).
RN [9]
RP LIPID-BINDING, AND INTERACTION WITH ACVR1; AGFG1; AP2A2; AP2B1; CALM; DAB2;
RP EPS15; EPS15R; ITSN1 AND CLATHRIN.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-347 AND SER-372, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [11]
RP INVOLVEMENT IN IMD76, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=30822429; DOI=10.1016/j.jaci.2019.02.014;
RA Calzoni E., Platt C.D., Keles S., Kuehn H.S., Beaussant-Cohen S., Zhang Y.,
RA Pazmandi J., Lanzi G., Pala F., Tahiat A., Artac H., Heredia R.J.,
RA Dmytrus J., Reisli I., Uygun V., Uygun D., Bingol A., Basaran E.,
RA Djenouhat K., Benhalla N., Bendahmane C., Emiroglu M., Kirchhausen T.,
RA Pasham M., Jones J., Wallace J.G., Zheng L., Boisson B., Porta F.,
RA Rosenzweig S.D., Su H., Giliani S., Lenardo M., Geha R.S., Boztug K.,
RA Chou J., Notarangelo L.D.;
RT "F-BAR domain only protein 1 (FCHO1) deficiency is a novel cause of
RT combined immune deficiency in human subjects.";
RL J. Allergy Clin. Immunol. 143:2317-2321.e12(2019).
RN [12]
RP VARIANTS IMD76 PRO-34; 650-ARG--CYS-889 DEL AND PRO-679, CHARACTERIZATION
RP OF VARIANTS IMD76 PRO-34; 650-ARG--CYS-889 DEL AND PRO-679, AND SUBCELLULAR
RP LOCATION.
RX PubMed=32098969; DOI=10.1038/s41467-020-14809-9;
RA Lyszkiewicz M., Zietara N., Frey L., Pannicke U., Stern M., Liu Y., Fan Y.,
RA Puchalka J., Hollizeck S., Somekh I., Rohlfs M., Yilmaz T., Uenal E.,
RA Karakukcu M., Patiroglu T., Kellerer C., Karasu E., Sykora K.W., Lev A.,
RA Simon A., Somech R., Roesler J., Hoenig M., Keppler O.T., Schwarz K.,
RA Klein C.;
RT "Human FCHO1 deficiency reveals role for clathrin-mediated endocytosis in
RT development and function of T cells.";
RL Nat. Commun. 11:1031-1031(2020).
RN [13]
RP ERRATUM OF PUBMED:32098969.
RX PubMed=32312977; DOI=10.1038/s41467-020-15946-x;
RA Lyszkiewicz M., Zietara N., Frey L., Pannicke U., Stern M., Liu Y., Fan Y.,
RA Puchalka J., Hollizeck S., Somekh I., Rohlfs M., Yilmaz T., Uenal E.,
RA Karakukcu M., Patiroglu T., Kellerer C., Karasu E., Sykora K.W., Lev A.,
RA Simon A., Somech R., Roesler J., Hoenig M., Keppler O.T., Schwarz K.,
RA Klein C.;
RT "Author Correction: Human FCHO1 deficiency reveals role for clathrin-
RT mediated endocytosis in development and function of T cells.";
RL Nat. Commun. 11:1963-1963(2020).
CC -!- FUNCTION: Functions in an early step of clathrin-mediated endocytosis
CC (PubMed:30822429). Has both a membrane binding/bending activity and the
CC ability to recruit proteins essential to the formation of functional
CC clathrin-coated pits. May regulate Bmp signaling by regulating
CC clathrin-mediated endocytosis of Bmp receptors. Involved in the
CC regulation of T-cell poliferation and activation (PubMed:30822429,
CC PubMed:32098969). Affects TCR clustering upon receptor triggering and
CC modulates its internalisation, playing a role in TCR-dependent T-cell
CC activation (PubMed:32098969). {ECO:0000269|PubMed:20448150,
CC ECO:0000269|PubMed:30822429, ECO:0000269|PubMed:32098969}.
CC -!- SUBUNIT: May oligomerize and form homotetramer (By similarity).
CC Interacts with AP2A2 and AP2B1; 2 subunits of the adaptor protein
CC complex AP-2 (By similarity). Interacts with DAB2. Interacts with
CC clathrin (CLTC or CLTCL1). Interacts with EPS15, EPS15R and ITSN1.
CC Interacts with AGFG1 and CALM. May interact with ACVR1; linking this
CC receptor to clathrin-mediated endocytosis (PubMed:22484487).
CC {ECO:0000250|UniProtKB:Q8K285, ECO:0000269|PubMed:22484487}.
CC -!- INTERACTION:
CC O14526; Q9NQT4: EXOSC5; NbExp=4; IntAct=EBI-719823, EBI-371876;
CC O14526; Q8TCE9: LGALS14; NbExp=4; IntAct=EBI-719823, EBI-10274069;
CC O14526; Q13882: PTK6; NbExp=4; IntAct=EBI-719823, EBI-1383632;
CC O14526; A7BFV9; Xeno; NbExp=2; IntAct=EBI-719823, EBI-6095043;
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000305|PubMed:17617719, ECO:0000305|PubMed:20448150,
CC ECO:0000305|PubMed:32098969}; Peripheral membrane protein
CC {ECO:0000305|PubMed:17617719, ECO:0000305|PubMed:20448150}; Cytoplasmic
CC side {ECO:0000305|PubMed:17617719, ECO:0000305|PubMed:20448150}.
CC Note=Associated with forming but not mature clathrin-coated vesicles.
CC The recruitment to coated-pits precede the one of clathrin and the
CC adaptor protein complex AP-2. According to PubMed:17617719 it may also
CC dynamically associate with Golgi/TGN membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O14526-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14526-2; Sequence=VSP_022338;
CC Name=3;
CC IsoId=O14526-3; Sequence=VSP_046906;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in lymphoid cells.
CC {ECO:0000269|PubMed:30822429}.
CC -!- DISEASE: Immunodeficiency 76 (IMD76) [MIM:619164]: An autosomal
CC recessive immunologic disorder characterized by onset of recurrent
CC bacterial, viral, and fungal infections in early childhood. Affected
CC individuals have T-cell lymphopenia and variable B-cell or
CC immunoglobulin abnormalities. Some patients develop B-cell lymphoma,
CC others manifest neurologic features. {ECO:0000269|PubMed:30822429,
CC ECO:0000269|PubMed:32098969}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the FCHO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA22959.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB006628; BAA22959.1; ALT_INIT; mRNA.
DR EMBL; AK291410; BAF84099.1; -; mRNA.
DR EMBL; AK303623; BAG64632.1; -; mRNA.
DR EMBL; AC008761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84629.1; -; Genomic_DNA.
DR EMBL; BC028021; AAH28021.1; -; mRNA.
DR EMBL; BC041130; AAH41130.1; -; mRNA.
DR CCDS; CCDS32955.1; -. [O14526-1]
DR CCDS; CCDS59366.1; -. [O14526-3]
DR PIR; T00039; T00039.
DR RefSeq; NP_001154829.1; NM_001161357.1.
DR RefSeq; NP_001154830.1; NM_001161358.1. [O14526-1]
DR RefSeq; NP_001154831.1; NM_001161359.1. [O14526-3]
DR RefSeq; NP_055937.1; NM_015122.2. [O14526-1]
DR RefSeq; XP_006722764.1; XM_006722701.3.
DR RefSeq; XP_006722765.1; XM_006722702.3.
DR RefSeq; XP_011526126.1; XM_011527824.2.
DR RefSeq; XP_011526127.1; XM_011527825.2. [O14526-1]
DR RefSeq; XP_011526128.1; XM_011527826.2.
DR RefSeq; XP_011526130.1; XM_011527828.2.
DR RefSeq; XP_016882008.1; XM_017026519.1.
DR RefSeq; XP_016882009.1; XM_017026520.1.
DR RefSeq; XP_016882010.1; XM_017026521.1.
DR AlphaFoldDB; O14526; -.
DR SMR; O14526; -.
DR BioGRID; 116764; 72.
DR IntAct; O14526; 17.
DR MINT; O14526; -.
DR STRING; 9606.ENSP00000473001; -.
DR iPTMnet; O14526; -.
DR MetOSite; O14526; -.
DR PhosphoSitePlus; O14526; -.
DR BioMuta; FCHO1; -.
DR EPD; O14526; -.
DR jPOST; O14526; -.
DR MassIVE; O14526; -.
DR MaxQB; O14526; -.
DR PaxDb; O14526; -.
DR PeptideAtlas; O14526; -.
DR PRIDE; O14526; -.
DR ProteomicsDB; 48073; -. [O14526-1]
DR ProteomicsDB; 48074; -. [O14526-2]
DR Antibodypedia; 27790; 116 antibodies from 21 providers.
DR DNASU; 23149; -.
DR Ensembl; ENST00000252771.11; ENSP00000252771.7; ENSG00000130475.15. [O14526-1]
DR Ensembl; ENST00000595033.5; ENSP00000472668.1; ENSG00000130475.15. [O14526-3]
DR Ensembl; ENST00000596536.6; ENSP00000470731.1; ENSG00000130475.15. [O14526-1]
DR Ensembl; ENST00000596951.5; ENSP00000472417.1; ENSG00000130475.15. [O14526-1]
DR Ensembl; ENST00000600676.5; ENSP00000470493.1; ENSG00000130475.15. [O14526-1]
DR GeneID; 23149; -.
DR KEGG; hsa:23149; -.
DR MANE-Select; ENST00000596536.6; ENSP00000470731.1; NM_015122.3; NP_055937.1.
DR UCSC; uc010ebb.3; human. [O14526-1]
DR CTD; 23149; -.
DR DisGeNET; 23149; -.
DR GeneCards; FCHO1; -.
DR HGNC; HGNC:29002; FCHO1.
DR HPA; ENSG00000130475; Tissue enhanced (brain, lymphoid tissue).
DR MalaCards; FCHO1; -.
DR MIM; 613437; gene.
DR MIM; 619164; phenotype.
DR neXtProt; NX_O14526; -.
DR OpenTargets; ENSG00000130475; -.
DR PharmGKB; PA134870625; -.
DR VEuPathDB; HostDB:ENSG00000130475; -.
DR eggNOG; KOG2398; Eukaryota.
DR GeneTree; ENSGT00940000160489; -.
DR HOGENOM; CLU_007107_0_0_1; -.
DR InParanoid; O14526; -.
DR OMA; YCPSAMA; -.
DR OrthoDB; 638761at2759; -.
DR PhylomeDB; O14526; -.
DR TreeFam; TF328986; -.
DR PathwayCommons; O14526; -.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; O14526; -.
DR SIGNOR; O14526; -.
DR BioGRID-ORCS; 23149; 18 hits in 1074 CRISPR screens.
DR ChiTaRS; FCHO1; human.
DR GenomeRNAi; 23149; -.
DR Pharos; O14526; Tbio.
DR PRO; PR:O14526; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O14526; protein.
DR Bgee; ENSG00000130475; Expressed in granulocyte and 134 other tissues.
DR ExpressionAtlas; O14526; baseline and differential.
DR Genevisible; O14526; HS.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; IDA:MGI.
DR GO; GO:0048268; P:clathrin coat assembly; IMP:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:UniProtKB.
DR GO; GO:0050870; P:positive regulation of T cell activation; IMP:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
DR CDD; cd07674; F-BAR_FCHO1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR030121; FCHo1.
DR InterPro; IPR042735; FCHo1_F-BAR.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR PANTHER; PTHR23065:SF6; PTHR23065:SF6; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF10291; muHD; 1.
DR SMART; SM00055; FCH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coated pit; Coiled coil; Disease variant;
KW Endocytosis; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..889
FT /note="F-BAR domain only protein 1"
FT /id="PRO_0000271759"
FT DOMAIN 1..248
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 625..888
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 1..275
FT /note="Mediates membrane-binding"
FT REGION 267..442
FT /note="Mediates interaction with the adaptor protein
FT complex AP-2"
FT REGION 294..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..889
FT /note="Mediates interaction with AGFG1, CALM, DAB2, EPS15,
FT EPS15R, ITSN1 and clathrin"
FT /evidence="ECO:0000269|PubMed:22484487"
FT REGION 826..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 156..195
FT /evidence="ECO:0000255"
FT COMPBIAS 328..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..528
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K285"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046906"
FT VAR_SEQ 883..889
FT /note="GMYLVSC -> AAPPQG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022338"
FT VARIANT 34
FT /note="A -> P (in IMD76; no effect on protein levels;
FT formation of large cell membrane-dissociated
FT agglomerations; failed to facilitate the formation of
FT clathrin-coated vesicles; impaired TCR internalization)"
FT /evidence="ECO:0000269|PubMed:32098969"
FT /id="VAR_085363"
FT VARIANT 650..889
FT /note="Missing (in IMD76)"
FT /evidence="ECO:0000269|PubMed:32098969"
FT /id="VAR_085364"
FT VARIANT 679
FT /note="R -> P (in IMD76; no effect on protein levels; loss
FT of clathrin-coated vesicles location and association with
FT cell membrane; failed to facilitate the formation of
FT clathrin-coated vesicles; impaired TCR internalization)"
FT /evidence="ECO:0000269|PubMed:32098969"
FT /id="VAR_085365"
SQ SEQUENCE 889 AA; 96861 MW; 8CDA1F24F42256D2 CRC64;
MSYFGEHFWG EKNHGFEVLY HSVKQGPIST KELADFIRER ATIEETYSKA MAKLSKLASN
GTPMGTFAPL WEVFRVSSDK LALCHLELTR KLQDLIKDVL RYGEEQLKTH KKCKEEVVST
LDAVQVLSGV SQLLPKSREN YLNRCMDQER LRRESTSQKE MDKAETKTKK AAESLRRSVE
KYNSARADFE QKMLDSALRF QAMEETHLRH MKALLGSYAH SVEDTHVQIG QVHEEFKQNI
ENVSVEMLLR KFAESKGTGR EKPGPLDFEA YSAAALQEAM KRLRGAKAFR LPGLSRRERE
PEPPAAVDFL EPDSGTCPEV DEEGFTVRPD VTQNSTAEPS RFSSSDSDFD DEEPRKFYVH
IKPAPARAPA CSPEAAAAQL RATAGSLILP PGPGGTMKRH SSRDAAGKPQ RPRSAPRTSS
CAERLQSEEQ VSKNLFGPPL ESAFDHEDFT GSSSLGFTSS PSPFSSSSPE NVEDSGLDSP
SHAAPGPSPD SWVPRPGTPQ SPPSCRAPPP EARGIRAPPL PDSPQPLASS PGPWGLEALA
GGDLMPAPAD PTAREGLAAP PRRLRSRKVS CPLTRSNGDL SRSLSPSPLG SSAASTALER
PSFLSQTGHG VSRGPSPVVL GSQDALPIAT AFTEYVHAYF RGHSPSCLAR VTGELTMTFP
AGIVRVFSGT PPPPVLSFRL VHTTAIEHFQ PNADLLFSDP SQSDPETKDF WLNMAALTEA
LQRQAEQNPT ASYYNVVLLR YQFSRPGPQS VPLQLSAHWQ CGATLTQVSV EYGYRPGATA
VPTPLTNVQI LLPVGEPVTN VRLQPAATWN LEEKRLTWRL PDVSEAGGSG RLSASWEPLS
GPSTPSPVAA QFTSEGTTLS GVDLELVGSG YRMSLVKRRF ATGMYLVSC
