AHI1_HUMAN
ID AHI1_HUMAN Reviewed; 1196 AA.
AC Q8N157; E1P584; Q4FD35; Q504T3; Q5TCP9; Q6P098; Q6PIT6; Q8NDX0; Q9H0H2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Jouberin;
DE AltName: Full=Abelson helper integration site 1 protein homolog;
DE Short=AHI-1;
GN Name=AHI1;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Small intestine;
RX PubMed=15169551; DOI=10.1186/1471-2164-5-33;
RA Close J.P., Game L., Clark B., Bergounioux J., Gerovassili A., Thein S.L.;
RT "Genome annotation of a 1.5 Mb region of human chromosome 6q23 encompassing
RT a quantitative trait locus for fetal hemoglobin expression in adults.";
RL BMC Genomics 5:33-33(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Westin E.H., Zhang Y.;
RT "Full sequence of DKFZp686J1653.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-301.
RC TISSUE=Bone marrow, and 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 [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14751929; DOI=10.1182/blood-2003-11-4026;
RA Jiang X., Zhao Y., Chan W.-Y., Vercauteren S., Pang E., Kennedy S.,
RA Nicolini F., Eaves A., Eaves C.;
RT "Deregulated expression in Ph+ human leukemias of AHI-1, a gene activated
RT by insertional mutagenesis in mouse models of leukemia.";
RL Blood 103:3897-3904(2004).
RN [9]
RP TISSUE SPECIFICITY, AND VARIANT JBTS3 ASP-443.
RX PubMed=15322546; DOI=10.1038/ng1419;
RA Ferland R.J., Eyaid W., Collura R.V., Tully L.D., Hill R.S., Al-Nouri D.,
RA Al-Rumayyan A., Topcu M., Gascon G., Bodell A., Shugart Y.Y., Ruvolo M.,
RA Walsh C.A.;
RT "Abnormal cerebellar development and axonal decussation due to mutations in
RT AHI1 in Joubert syndrome.";
RL Nat. Genet. 36:1008-1013(2004).
RN [10]
RP ERRATUM OF PUBMED:15322546.
RA Ferland R.J., Eyaid W., Collura R.V., Tully L.D., Hill R.S., Al-Nouri D.,
RA Al-Rumayyan A., Topcu M., Gascon G., Bodell A., Shugart Y.Y., Ruvolo M.,
RA Walsh C.A.;
RL Nat. Genet. 36:1126-1126(2004).
RN [11]
RP INTERACTION WITH NPHP1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18633336; DOI=10.1038/ki.2008.377;
RA Eley L., Gabrielides C., Adams M., Johnson C.A., Hildebrandt F.,
RA Sayer J.A.;
RT "Jouberin localizes to collecting ducts and interacts with nephrocystin-
RT 1.";
RL Kidney Int. 74:1139-1149(2008).
RN [12]
RP IDENTIFICATION BY 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 [13]
RP FUNCTION, INTERACTION WITH CTNNB1, SUBCELLULAR LOCATION, AND
RP CHARACTERIZATION OF VARIANTS JBTS3 ASP-443; GLN-723 AND ARG-896.
RX PubMed=21623382; DOI=10.1038/nm.2380;
RA Lancaster M.A., Gopal D.J., Kim J., Saleem S.N., Silhavy J.L., Louie C.M.,
RA Thacker B.E., Williams Y., Zaki M.S., Gleeson J.G.;
RT "Defective Wnt-dependent cerebellar midline fusion in a mouse model of
RT Joubert syndrome.";
RL Nat. Med. 17:726-731(2011).
RN [14]
RP SELF-ASSOCIATION, INTERACTION WITH NPHP1 AND HAP1, SUBCELLULAR LOCATION,
RP VARIANT JBTS3 LEU-351, AND CHARACTERIZATION OF VARIANTS JBTS3 LEU-351 AND
RP ASP-443.
RX PubMed=23532844; DOI=10.1074/jbc.m112.420786;
RA Tuz K., Hsiao Y.C., Juarez O., Shi B., Harmon E.Y., Phelps I.G.,
RA Lennartz M.R., Glass I.A., Doherty D., Ferland R.J.;
RT "The Joubert syndrome-associated missense mutation (V443D) in the Abelson-
RT helper integration site 1 (AHI1) protein alters its localization and
RT protein-protein interactions.";
RL J. Biol. Chem. 288:13676-13694(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-1002 AND SER-1123,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [16]
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 1048-1116, AND INTERACTION WITH
RP DNM2.
RX PubMed=22623184; DOI=10.1002/pmic.201100553;
RA Liu X., Chen M., Lobo P., An J., Grace Cheng S.W., Moradian A., Morin G.B.,
RA Van Petegem F., Jiang X.;
RT "Molecular and structural characterization of the SH3 domain of AHI-1 in
RT regulation of cellular resistance of BCR-ABL(+) chronic myeloid leukemia
RT cells to tyrosine kinase inhibitors.";
RL Proteomics 12:2094-2106(2012).
RN [17]
RP VARIANT JBTS3 ASP-443.
RX PubMed=15467982; DOI=10.1086/425985;
RA Dixon-Salazar T., Silhavy J.L., Marsh S.E., Louie C.M., Scott L.C.,
RA Gururaj A., Al-Gazali L., Al-Tawari A.A., Kayserili H., Sztriha L.,
RA Gleeson J.G.;
RT "Mutations in the AHI1 gene, encoding jouberin, cause Joubert syndrome with
RT cortical polymicrogyria.";
RL Am. J. Hum. Genet. 75:979-987(2004).
RN [18]
RP VARIANTS JBTS3 589-ARG--GLU-1196 DEL AND GLN-723, AND VARIANTS ASN-49;
RP HIS-548; LEU-761; TRP-830; SER-856; CYS-933; PHE-1123 AND SER-1140.
RX PubMed=16453322; DOI=10.1002/ana.20749;
RG International JSRD study group;
RA Valente E.M., Brancati F., Silhavy J.L., Castori M., Marsh S.E.,
RA Barrano G., Bertini E., Boltshauser E., Zaki M.S., Abdel-Aleem A.,
RA Abdel-Salam G.M.H., Bellacchio E., Battini R., Cruse R.P., Dobyns W.B.,
RA Krishnamoorthy K.S., Lagier-Tourenne C., Magee A., Pascual-Castroviejo I.,
RA Salpietro C.D., Sarco D., Dallapiccola B., Gleeson J.G.;
RT "AHI1 gene mutations cause specific forms of Joubert syndrome-related
RT disorders.";
RL Ann. Neurol. 59:527-534(2006).
RN [19]
RP VARIANTS HIS-548 AND TRP-830, AND VARIANTS JBTS3 ILE-671; GLY-719 AND
RP ARG-896.
RX PubMed=16155189; DOI=10.1136/jmg.2005.036608;
RA Parisi M.A., Doherty D., Eckert M.L., Shaw D.W., Ozyurek H., Aysun S.,
RA Giray O., Al Swaid A., Al Shahwan S., Dohayan N., Bakhsh E.,
RA Indridason O.S., Dobyns W.B., Bennett C.L., Chance P.F., Glass I.A.;
RT "AHI1 mutations cause both retinal dystrophy and renal cystic disease in
RT Joubert syndrome.";
RL J. Med. Genet. 43:334-339(2006).
RN [20]
RP VARIANT GLY-1086.
RX PubMed=22425360; DOI=10.1016/j.ajhg.2012.02.011;
RA Srour M., Schwartzentruber J., Hamdan F.F., Ospina L.H., Patry L.,
RA Labuda D., Massicotte C., Dobrzeniecka S., Capo-Chichi J.M.,
RA Papillon-Cavanagh S., Samuels M.E., Boycott K.M., Shevell M.I.,
RA Laframboise R., Desilets V., Maranda B., Rouleau G.A., Majewski J.,
RA Michaud J.L.;
RT "Mutations in C5ORF42 cause Joubert syndrome in the French Canadian
RT population.";
RL Am. J. Hum. Genet. 90:693-700(2012).
CC -!- FUNCTION: Involved in vesicle trafficking and required for
CC ciliogenesis, formation of primary non-motile cilium, and recruitment
CC of RAB8A to the basal body of primary cilium. Component of the
CC tectonic-like complex, a complex localized at the transition zone of
CC primary cilia and acting as a barrier that prevents diffusion of
CC transmembrane proteins between the cilia and plasma membranes. Involved
CC in neuronal differentiation. As a positive modulator of classical Wnt
CC signaling, may play a crucial role in ciliary signaling during
CC cerebellum embryonic development (PubMed:21623382).
CC {ECO:0000250|UniProtKB:Q8K3E5, ECO:0000269|PubMed:21623382}.
CC -!- SUBUNIT: Self-associates (PubMed:23532844). Part of the tectonic-like
CC complex (also named B9 complex). Interacts with MKS1. Interacts with
CC NPHP1; probably as heterodimers and/or AHI1(2):NPHP1(2)
CC heterotetramers. Interacts (via SH3 domain) with the dynamin GTPase
CC DNM2. Interacts with HAP1; probably as AHI1(2):HAP1(2) heterotetramers.
CC Interacts with RAB8A (By similarity). Interacts with CEND1 (By
CC similarity). Interacts with CTNNB1/beta-catenin (PubMed:21623382).
CC Interacts with SPATA7 (By similarity). {ECO:0000250|UniProtKB:Q8K3E5,
CC ECO:0000269|PubMed:18633336, ECO:0000269|PubMed:21623382,
CC ECO:0000269|PubMed:22623184, ECO:0000269|PubMed:23532844}.
CC -!- INTERACTION:
CC Q8N157; O43184: ADAM12; NbExp=2; IntAct=EBI-1049056, EBI-2625825;
CC Q8N157; Q8N157: AHI1; NbExp=2; IntAct=EBI-1049056, EBI-1049056;
CC Q8N157; P50570: DNM2; NbExp=2; IntAct=EBI-1049056, EBI-346547;
CC Q8N157; P54257: HAP1; NbExp=3; IntAct=EBI-1049056, EBI-712814;
CC Q8N157; O15259: NPHP1; NbExp=4; IntAct=EBI-1049056, EBI-953828;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:21623382, ECO:0000269|PubMed:23532844}. Cell
CC junction, adherens junction {ECO:0000269|PubMed:18633336,
CC ECO:0000269|PubMed:23532844}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q8K3E5}. Note=In the retinal photoreceptor cell
CC layer, localizes at the connecting cilium.
CC {ECO:0000250|UniProtKB:Q8K3E5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N157-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N157-2; Sequence=VSP_015355, VSP_015356;
CC Name=3;
CC IsoId=Q8N157-3; Sequence=VSP_015353, VSP_015354;
CC -!- TISSUE SPECIFICITY: Highly expressed in the most primitive normal
CC hematopoietic cells. Expressed in brain, particularly in neurons that
CC give rise to the crossing axons of the corticospinal tract and superior
CC cerebellar peduncles. Expressed in kidney (renal collecting duct cells)
CC (at protein level). {ECO:0000269|PubMed:14751929,
CC ECO:0000269|PubMed:15322546, ECO:0000269|PubMed:18633336}.
CC -!- INDUCTION: Down-regulated during early differentiation of normal
CC hematopoietic cells. Up-regulated in leukemic cells at all stages of
CC differentiation from patients with chronic myeloid leukemia.
CC {ECO:0000269|PubMed:14751929}.
CC -!- DISEASE: Joubert syndrome 3 (JBTS3) [MIM:608629]: A disorder presenting
CC with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal
CC breathing abnormalities and psychomotor delay. Neuroradiologically, it
CC is characterized by cerebellar vermian hypoplasia/aplasia, thickened
CC and reoriented superior cerebellar peduncles, and an abnormally large
CC interpeduncular fossa, giving the appearance of a molar tooth on
CC transaxial slices (molar tooth sign). Additional variable features
CC include retinal dystrophy and renal disease. Joubert syndrome type 3
CC shows minimal extra central nervous system involvement and appears not
CC to be associated with renal dysfunction. {ECO:0000269|PubMed:15322546,
CC ECO:0000269|PubMed:15467982, ECO:0000269|PubMed:16155189,
CC ECO:0000269|PubMed:16453322, ECO:0000269|PubMed:21623382,
CC ECO:0000269|PubMed:23532844}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29417.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH65712.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AJ459824; CAD30871.1; -; mRNA.
DR EMBL; AJ459825; CAD30872.1; -; mRNA.
DR EMBL; AJ606362; CAE54481.1; -; mRNA.
DR EMBL; DQ090887; AAY99645.1; -; mRNA.
DR EMBL; AL136797; CAB66731.1; -; mRNA.
DR EMBL; AK092262; BAC03840.1; -; mRNA.
DR EMBL; AL023693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47962.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47963.1; -; Genomic_DNA.
DR EMBL; BC029417; AAH29417.1; ALT_SEQ; mRNA.
DR EMBL; BC065712; AAH65712.1; ALT_SEQ; mRNA.
DR EMBL; BC094800; AAH94800.1; -; mRNA.
DR CCDS; CCDS47483.1; -. [Q8N157-1]
DR CCDS; CCDS47484.1; -. [Q8N157-2]
DR RefSeq; NP_001128302.1; NM_001134830.1. [Q8N157-1]
DR RefSeq; NP_001128303.1; NM_001134831.1. [Q8N157-1]
DR RefSeq; NP_001128304.1; NM_001134832.1. [Q8N157-2]
DR RefSeq; NP_060121.3; NM_017651.4. [Q8N157-1]
DR RefSeq; XP_011534212.1; XM_011535910.2. [Q8N157-1]
DR RefSeq; XP_011534213.1; XM_011535911.2. [Q8N157-1]
DR RefSeq; XP_016866466.1; XM_017010977.1.
DR RefSeq; XP_016866473.1; XM_017010984.1. [Q8N157-2]
DR PDB; 4ESR; X-ray; 1.53 A; A/B=1048-1116.
DR PDBsum; 4ESR; -.
DR AlphaFoldDB; Q8N157; -.
DR SMR; Q8N157; -.
DR BioGRID; 120163; 43.
DR CORUM; Q8N157; -.
DR IntAct; Q8N157; 35.
DR STRING; 9606.ENSP00000356774; -.
DR iPTMnet; Q8N157; -.
DR PhosphoSitePlus; Q8N157; -.
DR BioMuta; AHI1; -.
DR DMDM; 73921659; -.
DR EPD; Q8N157; -.
DR jPOST; Q8N157; -.
DR MassIVE; Q8N157; -.
DR MaxQB; Q8N157; -.
DR PaxDb; Q8N157; -.
DR PeptideAtlas; Q8N157; -.
DR PRIDE; Q8N157; -.
DR ProteomicsDB; 71560; -. [Q8N157-1]
DR ProteomicsDB; 71561; -. [Q8N157-2]
DR ProteomicsDB; 71562; -. [Q8N157-3]
DR Antibodypedia; 32983; 204 antibodies from 30 providers.
DR DNASU; 54806; -.
DR Ensembl; ENST00000265602.11; ENSP00000265602.6; ENSG00000135541.22. [Q8N157-1]
DR Ensembl; ENST00000327035.10; ENSP00000322478.6; ENSG00000135541.22. [Q8N157-2]
DR Ensembl; ENST00000367800.8; ENSP00000356774.4; ENSG00000135541.22. [Q8N157-1]
DR Ensembl; ENST00000457866.6; ENSP00000388650.2; ENSG00000135541.22. [Q8N157-1]
DR Ensembl; ENST00000531788.5; ENSP00000432167.1; ENSG00000135541.22. [Q8N157-3]
DR Ensembl; ENST00000681022.1; ENSP00000505121.1; ENSG00000135541.22. [Q8N157-1]
DR Ensembl; ENST00000681340.1; ENSP00000505666.1; ENSG00000135541.22. [Q8N157-1]
DR Ensembl; ENST00000681365.1; ENSP00000506604.1; ENSG00000135541.22. [Q8N157-1]
DR Ensembl; ENST00000681522.1; ENSP00000506005.1; ENSG00000135541.22. [Q8N157-1]
DR Ensembl; ENST00000681841.1; ENSP00000504965.1; ENSG00000135541.22. [Q8N157-1]
DR GeneID; 54806; -.
DR KEGG; hsa:54806; -.
DR MANE-Select; ENST00000265602.11; ENSP00000265602.6; NM_001134831.2; NP_001128303.1.
DR UCSC; uc003qgh.4; human. [Q8N157-1]
DR CTD; 54806; -.
DR DisGeNET; 54806; -.
DR GeneCards; AHI1; -.
DR GeneReviews; AHI1; -.
DR HGNC; HGNC:21575; AHI1.
DR HPA; ENSG00000135541; Low tissue specificity.
DR MalaCards; AHI1; -.
DR MIM; 608629; phenotype.
DR MIM; 608894; gene.
DR neXtProt; NX_Q8N157; -.
DR OpenTargets; ENSG00000135541; -.
DR Orphanet; 475; Joubert syndrome.
DR Orphanet; 220493; Joubert syndrome with ocular defect.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA134874587; -.
DR VEuPathDB; HostDB:ENSG00000135541; -.
DR eggNOG; KOG0266; Eukaryota.
DR GeneTree; ENSGT00940000156509; -.
DR HOGENOM; CLU_007778_0_0_1; -.
DR InParanoid; Q8N157; -.
DR OMA; ELQREGC; -.
DR OrthoDB; 1176970at2759; -.
DR PhylomeDB; Q8N157; -.
DR TreeFam; TF329226; -.
DR PathwayCommons; Q8N157; -.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR SignaLink; Q8N157; -.
DR BioGRID-ORCS; 54806; 6 hits in 1080 CRISPR screens.
DR ChiTaRS; AHI1; human.
DR GeneWiki; AHI1; -.
DR GenomeRNAi; 54806; -.
DR Pharos; Q8N157; Tbio.
DR PRO; PR:Q8N157; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8N157; protein.
DR Bgee; ENSG00000135541; Expressed in pituitary gland and 188 other tissues.
DR ExpressionAtlas; Q8N157; baseline and differential.
DR Genevisible; Q8N157; HS.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0036038; C:MKS complex; ISS:UniProtKB.
DR GO; GO:0097730; C:non-motile cilium; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0035844; P:cloaca development; ISS:UniProtKB.
DR GO; GO:0001947; P:heart looping; ISS:UniProtKB.
DR GO; GO:0030902; P:hindbrain development; ISS:UniProtKB.
DR GO; GO:0070121; P:Kupffer's vesicle development; ISS:UniProtKB.
DR GO; GO:0070986; P:left/right axis specification; ISS:UniProtKB.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; ISS:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0071599; P:otic vesicle development; ISS:UniProtKB.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; ISS:UniProtKB.
DR GO; GO:0030862; P:positive regulation of polarized epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0039023; P:pronephric duct morphogenesis; ISS:UniProtKB.
DR GO; GO:0039008; P:pronephric nephron tubule morphogenesis; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0050795; P:regulation of behavior; ISS:UniProtKB.
DR GO; GO:0010842; P:retina layer formation; ISS:UniProtKB.
DR GO; GO:0065001; P:specification of axis polarity; ISS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR CDD; cd11812; SH3_AHI-1; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR035832; AHI1_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell projection;
KW Ciliopathy; Cilium; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Disease variant;
KW Joubert syndrome; Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW WD repeat.
FT CHAIN 1..1196
FT /note="Jouberin"
FT /id="PRO_0000050838"
FT REPEAT 607..649
FT /note="WD 1"
FT REPEAT 652..691
FT /note="WD 2"
FT REPEAT 695..735
FT /note="WD 3"
FT REPEAT 742..781
FT /note="WD 4"
FT REPEAT 797..837
FT /note="WD 5"
FT REPEAT 841..880
FT /note="WD 6"
FT REPEAT 885..926
FT /note="WD 7"
FT DOMAIN 1051..1111
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 56..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..434
FT /note="Interaction with HAP1"
FT /evidence="ECO:0000269|PubMed:23532844"
FT REGION 215..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..45
FT /evidence="ECO:0000255"
FT COMPBIAS 56..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1002
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 594..609
FT /note="ACRIPNKHLFSLNAGE -> ENEDVFVLISPTMEEY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015353"
FT VAR_SEQ 610..1196
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015354"
FT VAR_SEQ 1037..1053
FT /note="GIISIERKPCNHQVDTA -> DSHFAEFNTCILWWKKH (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15169551"
FT /id="VSP_015355"
FT VAR_SEQ 1054..1196
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15169551"
FT /id="VSP_015356"
FT VARIANT 49
FT /note="I -> N"
FT /evidence="ECO:0000269|PubMed:16453322"
FT /id="VAR_037892"
FT VARIANT 351
FT /note="R -> L (in JBTS3; loss of localization at cilium
FT basal body and cell-cell junctions; dbSNP:rs397514726)"
FT /evidence="ECO:0000269|PubMed:23532844"
FT /id="VAR_071194"
FT VARIANT 443
FT /note="V -> D (in JBTS3; alters interaction with HAP1 and
FT NPHP1; loss of NPHP1AHI1(2):NPHP1(2) tetramers; loss of
FT localization at cilium basal body and cell-cell junctions;
FT loss of positive modulation of classical Wnt signaling;
FT decreased interaction with CTNNB1; dbSNP:rs121434350)"
FT /evidence="ECO:0000269|PubMed:15322546,
FT ECO:0000269|PubMed:15467982, ECO:0000269|PubMed:21623382,
FT ECO:0000269|PubMed:23532844"
FT /id="VAR_023391"
FT VARIANT 548
FT /note="R -> H (in dbSNP:rs35433555)"
FT /evidence="ECO:0000269|PubMed:16155189,
FT ECO:0000269|PubMed:16453322"
FT /id="VAR_037893"
FT VARIANT 589..1196
FT /note="Missing (in JBTS3; dbSNP:rs267606641)"
FT /evidence="ECO:0000269|PubMed:16453322"
FT /id="VAR_080417"
FT VARIANT 671
FT /note="T -> I (in JBTS3; dbSNP:rs772989270)"
FT /evidence="ECO:0000269|PubMed:16155189"
FT /id="VAR_076820"
FT VARIANT 719
FT /note="D -> G (in JBTS3; dbSNP:rs863225134)"
FT /evidence="ECO:0000269|PubMed:16155189"
FT /id="VAR_076821"
FT VARIANT 723
FT /note="R -> Q (in JBTS3; loss of localization at the
FT primary cilium; loss of positive modulation of classical
FT Wnt signaling; no effect on interaction with CTNNB1;
FT dbSNP:rs121434351)"
FT /evidence="ECO:0000269|PubMed:16453322,
FT ECO:0000269|PubMed:21623382"
FT /id="VAR_037894"
FT VARIANT 761
FT /note="S -> L (in dbSNP:rs794727174)"
FT /evidence="ECO:0000269|PubMed:16453322"
FT /id="VAR_037895"
FT VARIANT 830
FT /note="R -> W (in dbSNP:rs13312995)"
FT /evidence="ECO:0000269|PubMed:16155189,
FT ECO:0000269|PubMed:16453322"
FT /id="VAR_037896"
FT VARIANT 856
FT /note="T -> S (in dbSNP:rs199736888)"
FT /evidence="ECO:0000269|PubMed:16453322"
FT /id="VAR_037897"
FT VARIANT 896
FT /note="H -> R (in JBTS3; loss of localization at the
FT primary cilium; loss of positive modulation of classical
FT Wnt signaling; no effect on interaction with CTNNB1;
FT dbSNP:rs863225135)"
FT /evidence="ECO:0000269|PubMed:16155189,
FT ECO:0000269|PubMed:21623382"
FT /id="VAR_076822"
FT VARIANT 933
FT /note="Y -> C (in dbSNP:rs41288013)"
FT /evidence="ECO:0000269|PubMed:16453322"
FT /id="VAR_037898"
FT VARIANT 1018
FT /note="Q -> P (in dbSNP:rs6940875)"
FT /id="VAR_037899"
FT VARIANT 1086
FT /note="E -> G (in dbSNP:rs148000791)"
FT /evidence="ECO:0000269|PubMed:22425360"
FT /id="VAR_068171"
FT VARIANT 1123
FT /note="S -> F (in dbSNP:rs117447608)"
FT /evidence="ECO:0000269|PubMed:16453322"
FT /id="VAR_037900"
FT VARIANT 1140
FT /note="P -> S (in dbSNP:rs201148693)"
FT /evidence="ECO:0000269|PubMed:16453322"
FT /id="VAR_037901"
FT CONFLICT 18
FT /note="E -> K (in Ref. 3; CAB66731)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="L -> P (in Ref. 2; AAY99645)"
FT /evidence="ECO:0000305"
FT STRAND 1055..1060
FT /evidence="ECO:0007829|PDB:4ESR"
FT STRAND 1077..1083
FT /evidence="ECO:0007829|PDB:4ESR"
FT STRAND 1085..1094
FT /evidence="ECO:0007829|PDB:4ESR"
FT STRAND 1097..1102
FT /evidence="ECO:0007829|PDB:4ESR"
FT HELIX 1103..1105
FT /evidence="ECO:0007829|PDB:4ESR"
FT STRAND 1106..1108
FT /evidence="ECO:0007829|PDB:4ESR"
FT HELIX 1109..1114
FT /evidence="ECO:0007829|PDB:4ESR"
SQ SEQUENCE 1196 AA; 137115 MW; 16A237C915DABF0F CRC64;
MPTAESEAKV KTKVRFEELL KTHSDLMREK KKLKKKLVRS EENISPDTIR SNLHYMKETT
SDDPDTIRSN LPHIKETTSD DVSAANTNNL KKSTRVTKNK LRNTQLATEN PNGDASVEED
KQGKPNKKVI KTVPQLTTQD LKPETPENKV DSTHQKTHTK PQPGVDHQKS EKANEGREET
DLEEDEELMQ AYQCHVTEEM AKEIKRKIRK KLKEQLTYFP SDTLFHDDKL SSEKRKKKKE
VPVFSKAETS TLTISGDTVE GEQKKESSVR SVSSDSHQDD EISSMEQSTE DSMQDDTKPK
PKKTKKKTKA VADNNEDVDG DGVHEITSRD SPVYPKCLLD DDLVLGVYIH RTDRLKSDFM
ISHPMVKIHV VDEHTGQYVK KDDSGRPVSS YYEKENVDYI LPIMTQPYDF KQLKSRLPEW
EEQIVFNENF PYLLRGSDES PKVILFFEIL DFLSVDEIKN NSEVQNQECG FRKIAWAFLK
LLGANGNANI NSKLRLQLYY PPTKPRSPLS VVEAFEWWSK CPRNHYPSTL YVTVRGLKVP
DCIKPSYRSM MALQEEKGKP VHCERHHESS SVDTEPGLEE SKEVIKWKRL PGQACRIPNK
HLFSLNAGER GCFCLDFSHN GRILAAACAS RDGYPIILYE IPSGRFMREL CGHLNIIYDL
SWSKDDHYIL TSSSDGTARI WKNEINNTNT FRVLPHPSFV YTAKFHPAVR ELVVTGCYDS
MIRIWKVEMR EDSAILVRQF DVHKSFINSL CFDTEGHHMY SGDCTGVIVV WNTYVKINDL
EHSVHHWTIN KEIKETEFKG IPISYLEIHP NGKRLLIHTK DSTLRIMDLR ILVARKFVGA
ANYREKIHST LTPCGTFLFA GSEDGIVYVW NPETGEQVAM YSDLPFKSPI RDISYHPFEN
MVAFCAFGQN EPILLYIYDF HVAQQEAEMF KRYNGTFPLP GIHQSQDALC TCPKLPHQGS
FQIDEFVHTE SSSTKMQLVK QRLETVTEVI RSCAAKVNKN LSFTSPPAVS SQQSKLKQSN
MLTAQEILHQ FGFTQTGIIS IERKPCNHQV DTAPTVVALY DYTANRSDEL TIHRGDIIRV
FFKDNEDWWY GSIGKGQEGY FPANHVASET LYQELPPEIK ERSPPLSPEE KTKIEKSPAP
QKQSINKNKS QDFRLGSESM THSEMRKEQS HEDQGHIMDT RMRKNKQAGR KVTLIE
