IFT20_HUMAN
ID IFT20_HUMAN Reviewed; 132 AA.
AC Q8IY31; J3QL09; Q5GLZ2; Q9BUG5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Intraflagellar transport protein 20 homolog;
DE Short=hIFT20;
GN Name=IFT20;
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), AND TISSUE SPECIFICITY.
RX PubMed=14672413; DOI=10.1023/a:1026365124176;
RA Yin G., Dai J., Ji C., Ni X., Shu G., Ye X., Dai J., Wu Q., Gu S., Xie Y.,
RA Zhao R.C., Mao Y.;
RT "Cloning and characterization of the human IFT20 gene.";
RL Mol. Biol. Rep. 30:255-260(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=12107411;
RA Wistow G., Berstein S.L., Wyatt M.K., Ray S., Behal A., Touchman J.W.,
RA Bouffard G., Smith D., Peterson K.;
RT "Expressed sequence tag analysis of human retina for the NEIBank project:
RT retbindin, an abundant, novel retinal cDNA and alternative splicing of
RT other retina-preferred gene transcripts.";
RL Mol. Vis. 8:196-204(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Uterus;
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 [5]
RP FUNCTION.
RX PubMed=16775004; DOI=10.1091/mbc.e06-02-0133;
RA Follit J.A., Tuft R.A., Fogarty K.E., Pazour G.J.;
RT "The intraflagellar transport protein IFT20 is associated with the Golgi
RT complex and is required for cilia assembly.";
RL Mol. Biol. Cell 17:3781-3792(2006).
RN [6]
RP FUNCTION.
RX PubMed=17604723; DOI=10.1016/j.cell.2007.04.035;
RA Pugacheva E.N., Jablonski S.A., Hartman T.R., Henske E.P., Golemis E.A.;
RT "HEF1-dependent Aurora A activation induces disassembly of the primary
RT cilium.";
RL Cell 129:1351-1363(2007).
RN [7]
RP INTERACTION WITH TRIP11.
RX PubMed=19112494; DOI=10.1371/journal.pgen.1000315;
RA Follit J.A., San Agustin J.T., Xu F., Jonassen J.A., Samtani R., Lo C.W.,
RA Pazour G.J.;
RT "The Golgin GMAP210/TRIP11 anchors IFT20 to the Golgi complex.";
RL PLoS Genet. 4:E1000315-E1000315(2008).
RN [8]
RP INTERACTION WITH SPEF2.
RX PubMed=19889948; DOI=10.1095/biolreprod.108.074971;
RA Sironen A., Hansen J., Thomsen B., Andersson M., Vilkki J., Toppari J.,
RA Kotaja N.;
RT "Expression of SPEF2 during mouse spermatogenesis and identification of
RT IFT20 as an interacting protein.";
RL Biol. Reprod. 82:580-590(2010).
RN [9]
RP INTERACTION WITH CEP83.
RX PubMed=23530209; DOI=10.1073/pnas.1220927110;
RA Joo K., Kim C.G., Lee M.S., Moon H.Y., Lee S.H., Kim M.J., Kweon H.S.,
RA Park W.Y., Kim C.H., Gleeson J.G., Kim J.;
RT "CCDC41 is required for ciliary vesicle docking to the mother centriole.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5987-5992(2013).
RN [10]
RP FUNCTION, AND INTERACTION WITH CBL AND CBLB.
RX PubMed=29237719; DOI=10.1083/jcb.201611050;
RA Schmid F.M., Schou K.B., Vilhelm M.J., Holm M.S., Breslin L., Farinelli P.,
RA Larsen L.A., Andersen J.S., Pedersen L.B., Christensen S.T.;
RT "IFT20 modulates ciliary PDGFRalpha signaling by regulating the stability
RT of Cbl E3 ubiquitin ligases.";
RL J. Cell Biol. 217:151-161(2018).
RN [11]
RP INTERACTION WITH TTC21A.
RX PubMed=30929735; DOI=10.1016/j.ajhg.2019.02.020;
RA Liu W., He X., Yang S., Zouari R., Wang J., Wu H., Kherraf Z.E., Liu C.,
RA Coutton C., Zhao R., Tang D., Tang S., Lv M., Fang Y., Li W., Li H.,
RA Zhao J., Wang X., Zhao S., Zhang J., Arnoult C., Jin L., Zhang Z.,
RA Ray P.F., Cao Y., Zhang F.;
RT "Bi-allelic mutations in TTC21A induce asthenoteratospermia in humans and
RT mice.";
RL Am. J. Hum. Genet. 104:738-748(2019).
RN [12]
RP INTERACTION WITH USH1G.
RX PubMed=31637240; DOI=10.3389/fcell.2019.00216;
RA Sorusch N., Yildirim A., Knapp B., Janson J., Fleck W., Scharf C.,
RA Wolfrum U.;
RT "SANS (USH1G) Molecularly Links the Human Usher Syndrome Protein Network to
RT the Intraflagellar Transport Module by Direct Binding to IFT-B Proteins.";
RL Front. Cell Dev. Biol. 7:216-216(2019).
CC -!- FUNCTION: Part of intraflagellar transport (IFT) particles involved in
CC ciliary process assembly (PubMed:17604723). May play a role in the
CC trafficking of ciliary membrane proteins from the Golgi complex to the
CC cilium (PubMed:16775004). Regulates the platelet-derived growth factor
CC receptor-alpha (PDGFRA) signaling pathway. Required for protein
CC stability of E3 ubiquitin ligases CBL and CBLB that mediate
CC ubiquitination and internalization of PDGFRA for proper feedback
CC inhibition of PDGFRA signaling (PubMed:29237719). Essential for male
CC fertility. Plays an important role in spermatogenesis, particularly
CC spermiogenesis, when germ cells form flagella. May play a role in the
CC transport of flagellar proteins ODF2 and SPAG16 to build sperm flagella
CC and in the removal of redundant sperm cytoplasm (By similarity). Also
CC involved in autophagy since it is required for trafficking of ATG16L
CC and the expansion of the autophagic compartment (By similarity).
CC {ECO:0000250|UniProtKB:Q61025, ECO:0000269|PubMed:16775004,
CC ECO:0000269|PubMed:17604723, ECO:0000269|PubMed:29237719}.
CC -!- SUBUNIT: Component of the IFT complex B, at least composed of IFT20,
CC IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74,
CC IFT80, IFT81, and IFT88. Interacts directly with IFT57 and
CC KIF3B/Kinesin II subunit (By similarity). Interacts with IFT88 (By
CC similarity). Interacts with CEP83 (PubMed:23530209). Interacts with
CC SPEF2 (via C-terminus) (PubMed:19889948). Interacts with CBL and CBLB
CC (PubMed:29237719). Interacts with TRIP11 (PubMed:19112494). Interacts
CC with TTC21A (PubMed:30929735). Interacts with SPATA1 (By similarity).
CC Interacts with USH1G (PubMed:31637240). {ECO:0000250|UniProtKB:Q61025,
CC ECO:0000269|PubMed:19112494, ECO:0000269|PubMed:19889948,
CC ECO:0000269|PubMed:23530209, ECO:0000269|PubMed:29237719,
CC ECO:0000269|PubMed:31637240}.
CC -!- INTERACTION:
CC Q8IY31; Q9NYB9: ABI2; NbExp=6; IntAct=EBI-744203, EBI-743598;
CC Q8IY31; Q86T23: CROCCP2; NbExp=3; IntAct=EBI-744203, EBI-2872397;
CC Q8IY31; Q05D60: DEUP1; NbExp=3; IntAct=EBI-744203, EBI-748597;
CC Q8IY31; Q96EV8: DTNBP1; NbExp=3; IntAct=EBI-744203, EBI-465804;
CC Q8IY31; Q9Y6C2: EMILIN1; NbExp=6; IntAct=EBI-744203, EBI-744586;
CC Q8IY31; Q9UPT5: EXOC7; NbExp=4; IntAct=EBI-744203, EBI-720048;
CC Q8IY31; A1L4K1: FSD2; NbExp=3; IntAct=EBI-744203, EBI-5661036;
CC Q8IY31; Q08379: GOLGA2; NbExp=3; IntAct=EBI-744203, EBI-618309;
CC Q8IY31; Q96CS2: HAUS1; NbExp=5; IntAct=EBI-744203, EBI-2514791;
CC Q8IY31; A1A4E9: KRT13; NbExp=3; IntAct=EBI-744203, EBI-10171552;
CC Q8IY31; Q9BQD3: KXD1; NbExp=5; IntAct=EBI-744203, EBI-739657;
CC Q8IY31; Q9NPJ6: MED4; NbExp=4; IntAct=EBI-744203, EBI-394607;
CC Q8IY31; O14777: NDC80; NbExp=5; IntAct=EBI-744203, EBI-715849;
CC Q8IY31; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-744203, EBI-741048;
CC Q8IY31; P37198: NUP62; NbExp=3; IntAct=EBI-744203, EBI-347978;
CC Q8IY31; P25786: PSMA1; NbExp=3; IntAct=EBI-744203, EBI-359352;
CC Q8IY31; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-744203, EBI-739895;
CC Q8IY31; Q9Y3C0: WASHC3; NbExp=4; IntAct=EBI-744203, EBI-712969;
CC Q8IY31-2; P22607: FGFR3; NbExp=3; IntAct=EBI-11742277, EBI-348399;
CC Q8IY31-2; P14136: GFAP; NbExp=3; IntAct=EBI-11742277, EBI-744302;
CC Q8IY31-2; P06396: GSN; NbExp=3; IntAct=EBI-11742277, EBI-351506;
CC Q8IY31-2; P01112: HRAS; NbExp=3; IntAct=EBI-11742277, EBI-350145;
CC Q8IY31-2; O43464: HTRA2; NbExp=3; IntAct=EBI-11742277, EBI-517086;
CC Q8IY31-2; P42858: HTT; NbExp=6; IntAct=EBI-11742277, EBI-466029;
CC Q8IY31-2; O14901: KLF11; NbExp=3; IntAct=EBI-11742277, EBI-948266;
CC Q8IY31-2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-11742277, EBI-2811583;
CC Q8IY31-2; P41219: PRPH; NbExp=3; IntAct=EBI-11742277, EBI-752074;
CC Q8IY31-2; Q9Y649; NbExp=3; IntAct=EBI-11742277, EBI-25900580;
CC Q8IY31-3; Q9NYB9-2: ABI2; NbExp=7; IntAct=EBI-9091197, EBI-11096309;
CC Q8IY31-3; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-9091197, EBI-742038;
CC Q8IY31-3; P29972: AQP1; NbExp=3; IntAct=EBI-9091197, EBI-745213;
CC Q8IY31-3; P54253: ATXN1; NbExp=3; IntAct=EBI-9091197, EBI-930964;
CC Q8IY31-3; Q9UL45: BLOC1S6; NbExp=3; IntAct=EBI-9091197, EBI-465781;
CC Q8IY31-3; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-9091197, EBI-2837444;
CC Q8IY31-3; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-9091197, EBI-747505;
CC Q8IY31-3; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-9091197, EBI-10175300;
CC Q8IY31-3; Q9NNX6-10: CD209; NbExp=3; IntAct=EBI-9091197, EBI-12300031;
CC Q8IY31-3; Q9H2X3: CLEC4M; NbExp=3; IntAct=EBI-9091197, EBI-1391211;
CC Q8IY31-3; Q13286: CLN3; NbExp=3; IntAct=EBI-9091197, EBI-3248760;
CC Q8IY31-3; P31146: CORO1A; NbExp=3; IntAct=EBI-9091197, EBI-1046676;
CC Q8IY31-3; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-9091197, EBI-25840379;
CC Q8IY31-3; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-9091197, EBI-11988027;
CC Q8IY31-3; Q9Y6C2-2: EMILIN1; NbExp=5; IntAct=EBI-9091197, EBI-11748557;
CC Q8IY31-3; Q96LP2: FAM81B; NbExp=3; IntAct=EBI-9091197, EBI-10290827;
CC Q8IY31-3; Q53GS7: GLE1; NbExp=3; IntAct=EBI-9091197, EBI-1955541;
CC Q8IY31-3; P42858: HTT; NbExp=18; IntAct=EBI-9091197, EBI-466029;
CC Q8IY31-3; Q9NWB7: IFT57; NbExp=3; IntAct=EBI-9091197, EBI-725672;
CC Q8IY31-3; Q92993: KAT5; NbExp=3; IntAct=EBI-9091197, EBI-399080;
CC Q8IY31-3; Q8N371-3: KDM8; NbExp=3; IntAct=EBI-9091197, EBI-12161375;
CC Q8IY31-3; O60333-2: KIF1B; NbExp=3; IntAct=EBI-9091197, EBI-10975473;
CC Q8IY31-3; O14901: KLF11; NbExp=3; IntAct=EBI-9091197, EBI-948266;
CC Q8IY31-3; Q9Y448: KNSTRN; NbExp=3; IntAct=EBI-9091197, EBI-373334;
CC Q8IY31-3; Q96HR3: MED30; NbExp=3; IntAct=EBI-9091197, EBI-394659;
CC Q8IY31-3; Q9NYP9: MIS18A; NbExp=3; IntAct=EBI-9091197, EBI-1104552;
CC Q8IY31-3; Q7Z3B4: NUP54; NbExp=5; IntAct=EBI-9091197, EBI-741048;
CC Q8IY31-3; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-9091197, EBI-2811583;
CC Q8IY31-3; Q96HP4: OXNAD1; NbExp=3; IntAct=EBI-9091197, EBI-2862111;
CC Q8IY31-3; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-9091197, EBI-10302990;
CC Q8IY31-3; O43933: PEX1; NbExp=3; IntAct=EBI-9091197, EBI-988601;
CC Q8IY31-3; O60927: PPP1R11; NbExp=3; IntAct=EBI-9091197, EBI-1048104;
CC Q8IY31-3; Q9H2L5: RASSF4; NbExp=3; IntAct=EBI-9091197, EBI-2933362;
CC Q8IY31-3; O60239: SH3BP5; NbExp=3; IntAct=EBI-9091197, EBI-624860;
CC Q8IY31-3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-9091197, EBI-5235340;
CC Q8IY31-3; Q6PIF2: SYCE2; NbExp=3; IntAct=EBI-9091197, EBI-11958386;
CC Q8IY31-3; O76024: WFS1; NbExp=3; IntAct=EBI-9091197, EBI-720609;
CC Q8IY31-3; Q8IUH5: ZDHHC17; NbExp=3; IntAct=EBI-9091197, EBI-524753;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network
CC {ECO:0000250|UniProtKB:Q61025}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q61025}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q61025}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q61025}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q61025}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q61025}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:Q61025}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q61025}. Note=Present at the centrosomes during
CC the cell cycle and associated with the proximal portion of the mother
CC centriole and the lateral aspect of the daughter centriole. Associated
CC with basal body at the base of primary cilia. Detected in the Golgi
CC apparatus of round spermatids and late spermatocytes. Also detected in
CC the manchette of step 10-12 spermatids. In step 14 spermatids, found in
CC the basal body of the sperm tail. Localization in the manchette of
CC elongating spermatids is dependent on SPAG17.
CC {ECO:0000250|UniProtKB:Q61025}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8IY31-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IY31-2; Sequence=VSP_020390;
CC Name=3;
CC IsoId=Q8IY31-3; Sequence=VSP_020391;
CC Name=4;
CC IsoId=Q8IY31-4; Sequence=VSP_046026;
CC -!- TISSUE SPECIFICITY: Expressed in almost all tissues.
CC {ECO:0000269|PubMed:14672413}.
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; AY224601; AAP50265.1; -; mRNA.
DR EMBL; BQ639919; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC002094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002640; AAH02640.1; -; mRNA.
DR EMBL; BC038094; AAH38094.1; -; mRNA.
DR CCDS; CCDS32593.1; -. [Q8IY31-3]
DR CCDS; CCDS58533.1; -. [Q8IY31-4]
DR CCDS; CCDS58534.1; -. [Q8IY31-1]
DR CCDS; CCDS58535.1; -. [Q8IY31-2]
DR RefSeq; NP_001254703.1; NM_001267774.1. [Q8IY31-2]
DR RefSeq; NP_001254704.1; NM_001267775.1. [Q8IY31-1]
DR RefSeq; NP_001254705.1; NM_001267776.1. [Q8IY31-1]
DR RefSeq; NP_001254706.1; NM_001267777.1. [Q8IY31-4]
DR RefSeq; NP_001254707.1; NM_001267778.1.
DR RefSeq; NP_777547.1; NM_174887.3. [Q8IY31-3]
DR AlphaFoldDB; Q8IY31; -.
DR SMR; Q8IY31; -.
DR BioGRID; 124711; 138.
DR ComplexPortal; CPX-5022; IFT-B complex.
DR CORUM; Q8IY31; -.
DR IntAct; Q8IY31; 93.
DR MINT; Q8IY31; -.
DR STRING; 9606.ENSP00000464443; -.
DR iPTMnet; Q8IY31; -.
DR PhosphoSitePlus; Q8IY31; -.
DR BioMuta; IFT20; -.
DR DMDM; 74728279; -.
DR EPD; Q8IY31; -.
DR jPOST; Q8IY31; -.
DR MassIVE; Q8IY31; -.
DR MaxQB; Q8IY31; -.
DR PaxDb; Q8IY31; -.
DR PeptideAtlas; Q8IY31; -.
DR PRIDE; Q8IY31; -.
DR ProteomicsDB; 71093; -. [Q8IY31-1]
DR ProteomicsDB; 71094; -. [Q8IY31-2]
DR ProteomicsDB; 71095; -. [Q8IY31-3]
DR TopDownProteomics; Q8IY31-3; -. [Q8IY31-3]
DR Antibodypedia; 13983; 127 antibodies from 22 providers.
DR DNASU; 90410; -.
DR Ensembl; ENST00000357896.7; ENSP00000350570.3; ENSG00000109083.14. [Q8IY31-3]
DR Ensembl; ENST00000395418.8; ENSP00000378809.3; ENSG00000109083.14. [Q8IY31-1]
DR Ensembl; ENST00000579419.5; ENSP00000463322.1; ENSG00000109083.14. [Q8IY31-4]
DR Ensembl; ENST00000585089.5; ENSP00000464443.1; ENSG00000109083.14. [Q8IY31-2]
DR Ensembl; ENST00000585313.5; ENSP00000463138.1; ENSG00000109083.14. [Q8IY31-1]
DR GeneID; 90410; -.
DR KEGG; hsa:90410; -.
DR MANE-Select; ENST00000395418.8; ENSP00000378809.3; NM_001267776.2; NP_001254705.1.
DR UCSC; uc002hau.3; human. [Q8IY31-1]
DR CTD; 90410; -.
DR DisGeNET; 90410; -.
DR GeneCards; IFT20; -.
DR HGNC; HGNC:30989; IFT20.
DR HPA; ENSG00000109083; Low tissue specificity.
DR MIM; 614394; gene.
DR neXtProt; NX_Q8IY31; -.
DR OpenTargets; ENSG00000109083; -.
DR PharmGKB; PA142671663; -.
DR VEuPathDB; HostDB:ENSG00000109083; -.
DR eggNOG; ENOG502RYYR; Eukaryota.
DR GeneTree; ENSGT00390000003413; -.
DR HOGENOM; CLU_1758238_0_0_1; -.
DR InParanoid; Q8IY31; -.
DR OMA; TMAKQRQ; -.
DR OrthoDB; 1589590at2759; -.
DR PhylomeDB; Q8IY31; -.
DR TreeFam; TF319434; -.
DR PathwayCommons; Q8IY31; -.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR SignaLink; Q8IY31; -.
DR BioGRID-ORCS; 90410; 11 hits in 1074 CRISPR screens.
DR ChiTaRS; IFT20; human.
DR GeneWiki; IFT20; -.
DR GenomeRNAi; 90410; -.
DR Pharos; Q8IY31; Tbio.
DR PRO; PR:Q8IY31; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8IY31; protein.
DR Bgee; ENSG00000109083; Expressed in body of pancreas and 212 other tissues.
DR ExpressionAtlas; Q8IY31; baseline and differential.
DR Genevisible; Q8IY31; HS.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IDA:UniProtKB.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005801; C:cis-Golgi network; IDA:SYSCILIA_CCNET.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0044292; C:dendrite terminus; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030992; C:intraciliary transport particle B; IPI:ComplexPortal.
DR GO; GO:1902636; C:kinociliary basal body; IEA:Ensembl.
DR GO; GO:0002177; C:manchette; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0031514; C:motile cilium; IEA:Ensembl.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0032420; C:stereocilium; IEA:Ensembl.
DR GO; GO:0002046; F:opsin binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0051642; P:centrosome localization; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
DR GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IEA:Ensembl.
DR GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0061351; P:neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0036372; P:opsin transport; IEA:Ensembl.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; IBA:GO_Central.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:2000785; P:regulation of autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:2000583; P:regulation of platelet-derived growth factor receptor-alpha signaling pathway; ISS:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR InterPro; IPR028172; FT20.
DR PANTHER; PTHR31978; PTHR31978; 1.
DR Pfam; PF14931; IFT20; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Differentiation; Golgi apparatus; Reference proteome;
KW Spermatogenesis.
FT CHAIN 1..132
FT /note="Intraflagellar transport protein 20 homolog"
FT /id="PRO_0000249303"
FT REGION 70..132
FT /note="IFT57-binding"
FT /evidence="ECO:0000250"
FT COILED 74..114
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MTHLLLTATVTPSEQNSSREPGWETAM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14672413"
FT /id="VSP_020390"
FT VAR_SEQ 72..132
FT /note="AIGARNLLKSIAKQREAQQQQLQALIAEKKMQLERYRVEYEALCKVEAEQNE
FT FIDQFIFQK -> SLAVSPRLECTGAISAHCKLCLSDSSDSPTSPSRVGGTTGHRCSEL
FT AQIYSKAERSSTAATSSPNSRKENAARKVSG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020391"
FT VAR_SEQ 107..132
FT /note="YRVEYEALCKVEAEQNEFIDQFIFQK -> NELKISLL (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:12107411"
FT /id="VSP_046026"
SQ SEQUENCE 132 AA; 15281 MW; 8C751DE18FEEB30F CRC64;
MAKDILGEAG LHFDELNKLR VLDPEVTQQT IELKEECKDF VDKIGQFQKI VGGLIELVDQ
LAKEAENEKM KAIGARNLLK SIAKQREAQQ QQLQALIAEK KMQLERYRVE YEALCKVEAE
QNEFIDQFIF QK
