ANKS6_HUMAN
ID ANKS6_HUMAN Reviewed; 871 AA.
AC Q68DC2; A0SE62; Q5VSL0; Q5VSL2; Q5VSL3; Q5VSL4; Q68DB8; Q6P2R2; Q8N9L6;
AC Q96D62;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ankyrin repeat and SAM domain-containing protein 6;
DE AltName: Full=Ankyrin repeat domain-containing protein 14;
DE AltName: Full=SamCystin;
DE AltName: Full=Sterile alpha motif domain-containing protein 6;
DE Short=SAM domain-containing protein 6;
GN Name=ANKS6; Synonyms=ANKRD14, PKDR1, SAMD6;
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 [GENOMIC DNA].
RX PubMed=16207829; DOI=10.1681/asn.2005060601;
RA Brown J.H., Bihoreau M.-T., Hoffmann S., Kranzlin B., Tychinskaya I.,
RA Obermuller N., Podlich D., Boehn S.N., Kaisaki P.J., Megel N., Danoy P.,
RA Copley R.R., Broxholme J., Witzgall R., Lathrop M., Gretz N., Gauguier D.;
RT "Missense mutation in sterile alpha motif of novel protein SamCystin is
RT associated with polycystic kidney disease in (cy/+) rat.";
RL J. Am. Soc. Nephrol. 16:3517-3526(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 94-871 (ISOFORM 1), AND VARIANT
RP ILE-644.
RC TISSUE=Fetal kidney, and Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 322-871 (ISOFORM 1), AND VARIANT
RP ILE-644.
RC TISSUE=Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 533-871 (ISOFORM 3), AND VARIANT
RP ILE-644.
RC TISSUE=Cerebellum;
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657; SER-734 AND SER-742, AND
RP 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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 771-840 IN COMPLEX WITH ANKS3,
RP INTERACTION WITH ANKS3, DOMAIN, AND MUTAGENESIS OF GLU-798; ASP-811 AND
RP ARG-823.
RX PubMed=24998259; DOI=10.1186/1472-6807-14-17;
RA Leettola C.N., Knight M.J., Cascio D., Hoffman S., Bowie J.U.;
RT "Characterization of the SAM domain of the PKD-related protein ANKS6 and
RT its interaction with ANKS3.";
RL BMC Struct. Biol. 14:17-17(2014).
RN [11]
RP VARIANTS TRP-222; GLN-440; SER-640; ILE-644 AND ALA-735.
RX PubMed=18434273; DOI=10.1016/j.ejmg.2008.02.007;
RA Kaisaki P.J., Bergmann C., Brown J.H., Outeda P., Lens X.M., Peters D.J.,
RA Gretz N., Gauguier D., Bihoreau M.T.;
RT "Genomic organization and mutation screening of the human ortholog of Pkdr1
RT associated with polycystic kidney disease in the rat.";
RL Eur. J. Med. Genet. 51:325-331(2008).
RN [12]
RP VARIANTS NPHP16 PRO-312 AND GLN441ARG, FUNCTION, INTERACTION WITH INVS;
RP NEK8 AND NPHP3, AND DOMAIN.
RX PubMed=23793029; DOI=10.1038/ng.2681;
RA Hoff S., Halbritter J., Epting D., Frank V., Nguyen T.M., van Reeuwijk J.,
RA Boehlke C., Schell C., Yasunaga T., Helmstadter M., Mergen M., Filhol E.,
RA Boldt K., Horn N., Ueffing M., Otto E.A., Eisenberger T., Elting M.W.,
RA van Wijk J.A., Bockenhauer D., Sebire N.J., Rittig S., Vyberg M., Ring T.,
RA Pohl M., Pape L., Neuhaus T.J., Elshakhs N.A., Koon S.J., Harris P.C.,
RA Grahammer F., Huber T.B., Kuehn E.W., Kramer-Zucker A., Bolz H.J.,
RA Roepman R., Saunier S., Walz G., Hildebrandt F., Bergmann C.,
RA Lienkamp S.S.;
RT "ANKS6 is a central component of a nephronophthisis module linking NEK8 to
RT INVS and NPHP3.";
RL Nat. Genet. 45:951-956(2013).
CC -!- FUNCTION: Required for renal function. {ECO:0000269|PubMed:23793029}.
CC -!- SUBUNIT: Homooligomer (By similarity). Central component of a complex
CC containing at least ANKS6, INVS, NEK8 and NPHP3 (PubMed:23793029).
CC ANKS6 may organize complex assembly by linking INVS and NPHP3 to NEK8
CC and INVS may target the complex to the proximal ciliary axoneme
CC (PubMed:23793029). Interacts (via SAM domain) with BICC1 (via KH
CC domains) in an RNA-dependent manner (By similarity). Interacts (via SAM
CC domain) with ANKS3 (via SAM domain) (PubMed:24998259).
CC {ECO:0000250|UniProtKB:P0C0T2, ECO:0000269|PubMed:23793029,
CC ECO:0000269|PubMed:24998259}.
CC -!- INTERACTION:
CC Q68DC2; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-7054139, EBI-11522760;
CC Q68DC2; Q92843: BCL2L2; NbExp=3; IntAct=EBI-7054139, EBI-707714;
CC Q68DC2; O15155: BET1; NbExp=3; IntAct=EBI-7054139, EBI-749204;
CC Q68DC2; P01031: C5; NbExp=3; IntAct=EBI-7054139, EBI-8558308;
CC Q68DC2; P50402: EMD; NbExp=3; IntAct=EBI-7054139, EBI-489887;
CC Q68DC2; P54849: EMP1; NbExp=3; IntAct=EBI-7054139, EBI-4319440;
CC Q68DC2; P24593: IGFBP5; NbExp=3; IntAct=EBI-7054139, EBI-720480;
CC Q68DC2; Q9NX47: MARCHF5; NbExp=3; IntAct=EBI-7054139, EBI-2341610;
CC Q68DC2; Q9UKF7-2: PITPNC1; NbExp=3; IntAct=EBI-7054139, EBI-14223623;
CC Q68DC2; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-7054139, EBI-10244780;
CC Q68DC2; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-7054139, EBI-12188413;
CC Q68DC2; P0DN84: STRIT1; NbExp=3; IntAct=EBI-7054139, EBI-12200293;
CC Q68DC2; O15400: STX7; NbExp=3; IntAct=EBI-7054139, EBI-3221827;
CC Q68DC2; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-7054139, EBI-10171534;
CC Q68DC2; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-7054139, EBI-2852148;
CC Q68DC2; O75379: VAMP4; NbExp=3; IntAct=EBI-7054139, EBI-744953;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q6GQX6}. Cytoplasm
CC {ECO:0000250|UniProtKB:P0C0T2}. Note=Localizes to the proximal region
CC of the primary cilium in the presence of INVS.
CC {ECO:0000250|UniProtKB:Q6GQX6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q68DC2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68DC2-3; Sequence=VSP_016496, VSP_016497;
CC Name=3;
CC IsoId=Q68DC2-4; Sequence=VSP_016498;
CC -!- DOMAIN: The ankyrin repeats are necessary and sufficient for NEK8-
CC binding. {ECO:0000269|PubMed:23793029}.
CC -!- DOMAIN: The SAM domain mediates interaction with the SAM domain of
CC ANKS3. {ECO:0000269|PubMed:24998259}.
CC -!- PTM: Hydroxylated at Asn-138, most probably by HIF1AN. This
CC hydroxylation results in decreased NEK8-binding.
CC {ECO:0000250|UniProtKB:P0C0T2}.
CC -!- DISEASE: Nephronophthisis 16 (NPHP16) [MIM:615382]: A form of
CC nephronophthisis, a chronic tubulo-interstitial nephritis that
CC progresses to end-stage renal failure. Some patients have cystic
CC kidneys of normal size and no extrarenal manifestations, whereas others
CC have enlarged renal size and severe extrarenal defects, including
CC hypertrophic obstructive cardiomyopathy, aortic stenosis, pulmonary
CC stenosis, patent ductus arteriosus, situs inversus, and periportal
CC liver fibrosis. {ECO:0000269|PubMed:23793029}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH64367.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04317.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH18298.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ309791; ABC48694.1; -; Genomic_DNA.
DR EMBL; DQ309777; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; DQ309778; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; DQ309779; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; DQ309780; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; DQ309781; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; DQ309782; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; DQ309783; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; DQ309784; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; DQ309785; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; DQ309786; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; DQ309787; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; DQ309788; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; DQ309789; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; DQ309790; ABC48694.1; JOINED; Genomic_DNA.
DR EMBL; AL353782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR749467; CAH18298.1; ALT_INIT; mRNA.
DR EMBL; CR749472; CAH18302.1; -; mRNA.
DR EMBL; BC064367; AAH64367.1; ALT_INIT; mRNA.
DR EMBL; AK094247; BAC04317.1; ALT_INIT; mRNA.
DR CCDS; CCDS43856.1; -. [Q68DC2-1]
DR RefSeq; NP_775822.3; NM_173551.4. [Q68DC2-1]
DR RefSeq; XP_006717061.1; XM_006716998.3. [Q68DC2-4]
DR RefSeq; XP_016869934.1; XM_017014445.1. [Q68DC2-1]
DR PDB; 4NL9; X-ray; 1.50 A; C/D=771-840.
DR PDBsum; 4NL9; -.
DR AlphaFoldDB; Q68DC2; -.
DR SMR; Q68DC2; -.
DR BioGRID; 128464; 42.
DR CORUM; Q68DC2; -.
DR IntAct; Q68DC2; 30.
DR MINT; Q68DC2; -.
DR STRING; 9606.ENSP00000297837; -.
DR GlyGen; Q68DC2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q68DC2; -.
DR PhosphoSitePlus; Q68DC2; -.
DR BioMuta; ANKS6; -.
DR DMDM; 83305683; -.
DR EPD; Q68DC2; -.
DR jPOST; Q68DC2; -.
DR MassIVE; Q68DC2; -.
DR MaxQB; Q68DC2; -.
DR PaxDb; Q68DC2; -.
DR PeptideAtlas; Q68DC2; -.
DR PRIDE; Q68DC2; -.
DR ProteomicsDB; 66071; -. [Q68DC2-1]
DR ProteomicsDB; 66072; -. [Q68DC2-3]
DR ProteomicsDB; 66073; -. [Q68DC2-4]
DR Antibodypedia; 1903; 121 antibodies from 17 providers.
DR DNASU; 203286; -.
DR Ensembl; ENST00000353234.5; ENSP00000297837.6; ENSG00000165138.18. [Q68DC2-1]
DR GeneID; 203286; -.
DR KEGG; hsa:203286; -.
DR MANE-Select; ENST00000353234.5; ENSP00000297837.6; NM_173551.5; NP_775822.3.
DR UCSC; uc004ayu.4; human. [Q68DC2-1]
DR CTD; 203286; -.
DR DisGeNET; 203286; -.
DR GeneCards; ANKS6; -.
DR GeneReviews; ANKS6; -.
DR HGNC; HGNC:26724; ANKS6.
DR HPA; ENSG00000165138; Low tissue specificity.
DR MalaCards; ANKS6; -.
DR MIM; 615370; gene.
DR MIM; 615382; phenotype.
DR neXtProt; NX_Q68DC2; -.
DR OpenTargets; ENSG00000165138; -.
DR Orphanet; 93591; Infantile nephronophthisis.
DR Orphanet; 93592; Juvenile nephronophthisis.
DR PharmGKB; PA134931829; -.
DR VEuPathDB; HostDB:ENSG00000165138; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4374; Eukaryota.
DR GeneTree; ENSGT00940000157664; -.
DR InParanoid; Q68DC2; -.
DR OMA; RSPTTWM; -.
DR OrthoDB; 1137424at2759; -.
DR PhylomeDB; Q68DC2; -.
DR TreeFam; TF328552; -.
DR PathwayCommons; Q68DC2; -.
DR SignaLink; Q68DC2; -.
DR BioGRID-ORCS; 203286; 97 hits in 1076 CRISPR screens.
DR ChiTaRS; ANKS6; human.
DR GenomeRNAi; 203286; -.
DR Pharos; Q68DC2; Tbio.
DR PRO; PR:Q68DC2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q68DC2; protein.
DR Bgee; ENSG00000165138; Expressed in cerebellar hemisphere and 136 other tissues.
DR ExpressionAtlas; Q68DC2; baseline and differential.
DR Genevisible; Q68DC2; HS.
DR GO; GO:0097543; C:ciliary inversin compartment; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 7.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Cell projection;
KW Ciliopathy; Cilium; Cytoplasm; Disease variant; Hydroxylation;
KW Joubert syndrome; Nephronophthisis; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..871
FT /note="Ankyrin repeat and SAM domain-containing protein 6"
FT /id="PRO_0000067065"
FT REPEAT 8..37
FT /note="ANK 1"
FT REPEAT 77..106
FT /note="ANK 2"
FT REPEAT 110..139
FT /note="ANK 3"
FT REPEAT 143..172
FT /note="ANK 4"
FT REPEAT 190..219
FT /note="ANK 5"
FT REPEAT 224..253
FT /note="ANK 6"
FT REPEAT 257..289
FT /note="ANK 7"
FT REPEAT 291..321
FT /note="ANK 8"
FT REPEAT 325..354
FT /note="ANK 9"
FT REPEAT 359..388
FT /note="ANK 10"
FT REPEAT 392..423
FT /note="ANK 11"
FT DOMAIN 773..836
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 28..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 823
FT /note="Essential for ANKS3 interaction"
FT /evidence="ECO:0000250|UniProtKB:P0C0T2"
FT MOD_RES 138
FT /note="3-hydroxyasparagine"
FT /evidence="ECO:0000250"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 288..335
FT /note="DEEKRRPDIFHALKMGNFQLVKEIADEDPSHVNLVNGDGATPLMLAAV ->
FT GQAACPPWLHRGPQIVFMWLKLRIALLEGHAELRVQPCRPLRLRKWCA (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_016496"
FT VAR_SEQ 336..871
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_016497"
FT VAR_SEQ 714
FT /note="K -> KQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016498"
FT VARIANT 222
FT /note="R -> W (in dbSNP:rs41283630)"
FT /evidence="ECO:0000269|PubMed:18434273"
FT /id="VAR_070105"
FT VARIANT 312
FT /note="A -> P (in NPHP16)"
FT /evidence="ECO:0000269|PubMed:23793029"
FT /id="VAR_070106"
FT VARIANT 440
FT /note="R -> Q (in dbSNP:rs763855876)"
FT /evidence="ECO:0000269|PubMed:18434273"
FT /id="VAR_070107"
FT VARIANT 441
FT /note="Q -> R (in NPHP16; dbSNP:rs377750405)"
FT /id="VAR_070108"
FT VARIANT 640
FT /note="G -> S (in dbSNP:rs749102463)"
FT /evidence="ECO:0000269|PubMed:18434273"
FT /id="VAR_070109"
FT VARIANT 644
FT /note="V -> I (in dbSNP:rs6415847)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:18434273"
FT /id="VAR_034794"
FT VARIANT 735
FT /note="P -> A (in dbSNP:rs79414550)"
FT /evidence="ECO:0000269|PubMed:18434273"
FT /id="VAR_070110"
FT MUTAGEN 798
FT /note="E->K: Loss of interaction with ANKS3."
FT /evidence="ECO:0000269|PubMed:24998259"
FT MUTAGEN 811
FT /note="D->K: Loss of interaction with ANKS3."
FT /evidence="ECO:0000269|PubMed:24998259"
FT MUTAGEN 823
FT /note="R->W: Loss of interaction with ANKS3."
FT /evidence="ECO:0000269|PubMed:24998259"
FT CONFLICT 244
FT /note="L -> P (in Ref. 3; CAH18298)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="L -> P (in Ref. 4; CAH18302)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="S -> G (in Ref. 5; BAC04317)"
FT /evidence="ECO:0000305"
FT CONFLICT 808
FT /note="T -> A (in Ref. 4; CAH18302)"
FT /evidence="ECO:0000305"
FT HELIX 778..784
FT /evidence="ECO:0007829|PDB:4NL9"
FT HELIX 788..790
FT /evidence="ECO:0007829|PDB:4NL9"
FT HELIX 791..796
FT /evidence="ECO:0007829|PDB:4NL9"
FT HELIX 801..804
FT /evidence="ECO:0007829|PDB:4NL9"
FT HELIX 809..815
FT /evidence="ECO:0007829|PDB:4NL9"
FT HELIX 820..834
FT /evidence="ECO:0007829|PDB:4NL9"
SQ SEQUENCE 871 AA; 92219 MW; C4E3AFFE9C9DD6C8 CRC64;
MGEGGLPPAF QLLLRACDQG DTETARRLLE PGAAEPAERG AEPEAGAEPA GAEVAGPGAA
AAGAVGAPVP VDCSDEAGNT ALQFAAAGGH EPLVRFLLRR GASVNSRNHY GWSALMQAAR
FGHVSVAHLL LDHGADVNAQ NRLGASVLTV ASRGGHLGVV KLLLEAGAFV DHHHPSGEQL
GLGGSRDEPL DITALMAAIQ HGHEAVVRLL MEWGADPNHA ARTVGWSPLM LAALTGRLGV
AQQLVEKGAN PDHLSVLEKT AFEVALDCKH RDLVDYLDPL TTVRPKTDEE KRRPDIFHAL
KMGNFQLVKE IADEDPSHVN LVNGDGATPL MLAAVTGQLA LVQLLVERHA DVDKQDSVHG
WTALMQATYH GNKEIVKYLL NQGADVTLRA KNGYTAFDLV MLLNDPDTEL VRLLASVCMQ
VNKDKGRPSH QPPLPHSKVR QPWSIPVLPD DKGGLKSWWN RMSNRFRKLK LMQTLPRGLS
SNQPLPFSDE PEPALDSTMR AAPQDKTSRS ALPDAAPVTK DNGPGSTRGE KEDTLLTTML
RNGAPLTRLP SDKLKAVIPP FLPPSSFELW SSDRSRTRHN GKADPMKTAL PQRASRGHPV
GGGGTDTTPV RPVKFPSLPR SPASSANSGN FNHSPHSSGG SSGVGVSRHG GELLNRSGGS
IDNVLSQIAA QRKKAAGLLE QKPSHRSSPV GPAPGSSPSE LPASPAGGSA PVGKKLETSK
RPPSGTSTTS KSTSPTLTPS PSPKGHTAES SVSSSSSHRQ SKSSGGSSSG TITDEDELTG
ILKKLSLEKY QPIFEEQEVD MEAFLTLTDG DLKELGIKTD GSRQQILAAI SELNAGKGRE
RQILQETIHN FHSSFESSAS NTRAPGNSPC A
