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Ankyrin repeat and SAM domain-containing protein 6 (Ankyrin repeat domain-containing protein 14) (SamCystin) (Sterile alpha motif domain-containing protein 6) (SAM domain-containing protein 6)

 ANKS6_HUMAN             Reviewed;         871 AA.
Q68DC2; A0SE62; Q5VSL0; Q5VSL2; Q5VSL3; Q5VSL4; Q68DB8; Q6P2R2;
Q8N9L6; Q96D62;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 2.
23-MAY-2018, entry version 136.
RecName: Full=Ankyrin repeat and SAM domain-containing protein 6;
AltName: Full=Ankyrin repeat domain-containing protein 14;
AltName: Full=SamCystin;
AltName: Full=Sterile alpha motif domain-containing protein 6;
Short=SAM domain-containing protein 6;
Name=ANKS6; Synonyms=ANKRD14, PKDR1, SAMD6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=16207829; DOI=10.1681/ASN.2005060601;
Brown J.H., Bihoreau M.-T., Hoffmann S., Kranzlin B., Tychinskaya I.,
Obermuller N., Podlich D., Boehn S.N., Kaisaki P.J., Megel N.,
Danoy P., Copley R.R., Broxholme J., Witzgall R., Lathrop M.,
Gretz N., Gauguier D.;
"Missense mutation in sterile alpha motif of novel protein SamCystin
is associated with polycystic kidney disease in (cy/+) rat.";
J. Am. Soc. Nephrol. 16:3517-3526(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 94-871 (ISOFORM 1), AND
VARIANT ILE-644.
TISSUE=Fetal kidney, and Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 322-871 (ISOFORM 1), AND
VARIANT ILE-644.
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 533-871 (ISOFORM 3), AND
VARIANT ILE-644.
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657; SER-734 AND
SER-742, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 771-840 IN COMPLEX WITH
ANKS3, INTERACTION WITH ANKS3, DOMAIN, AND MUTAGENESIS OF GLU-798;
ASP-811 AND ARG-823.
PubMed=24998259; DOI=10.1186/1472-6807-14-17;
Leettola C.N., Knight M.J., Cascio D., Hoffman S., Bowie J.U.;
"Characterization of the SAM domain of the PKD-related protein ANKS6
and its interaction with ANKS3.";
BMC Struct. Biol. 14:17-17(2014).
[11]
VARIANTS TRP-222; GLN-440; SER-640; ILE-644 AND ALA-735.
PubMed=18434273; DOI=10.1016/j.ejmg.2008.02.007;
Kaisaki P.J., Bergmann C., Brown J.H., Outeda P., Lens X.M.,
Peters D.J., Gretz N., Gauguier D., Bihoreau M.T.;
"Genomic organization and mutation screening of the human ortholog of
Pkdr1 associated with polycystic kidney disease in the rat.";
Eur. J. Med. Genet. 51:325-331(2008).
[12]
VARIANTS NPHP16 PRO-312 AND GLN441ARG, FUNCTION, INTERACTION WITH
INVS; NEK8 AND NPHP3, AND DOMAIN.
PubMed=23793029; DOI=10.1038/ng.2681;
Hoff S., Halbritter J., Epting D., Frank V., Nguyen T.M.,
van Reeuwijk J., Boehlke C., Schell C., Yasunaga T., Helmstadter M.,
Mergen M., Filhol E., Boldt K., Horn N., Ueffing M., Otto E.A.,
Eisenberger T., Elting M.W., van Wijk J.A., Bockenhauer D.,
Sebire N.J., Rittig S., Vyberg M., Ring T., Pohl M., Pape L.,
Neuhaus T.J., Elshakhs N.A., Koon S.J., Harris P.C., Grahammer F.,
Huber T.B., Kuehn E.W., Kramer-Zucker A., Bolz H.J., Roepman R.,
Saunier S., Walz G., Hildebrandt F., Bergmann C., Lienkamp S.S.;
"ANKS6 is a central component of a nephronophthisis module linking
NEK8 to INVS and NPHP3.";
Nat. Genet. 45:951-956(2013).
-!- FUNCTION: Required for renal function.
{ECO:0000269|PubMed:23793029}.
-!- SUBUNIT: Homooligomer (By similarity). Central component of a
complex containing at least ANKS6, INVS, NEK8 and NPHP3. ANKS6 may
organize complex assembly by linking INVS and NPHP3 to NEK8 and
INVS may target the complex to the proximal ciliary axoneme
(PubMed:23793029). Interacts (via SAM domain) with BICC1 (via KH
domains) in an RNA-dependent manner (By similarity). Interacts
with ANKS3 (PubMed:24998259). {ECO:0000250|UniProtKB:P0C0T2,
ECO:0000269|PubMed:23793029, ECO:0000269|PubMed:24998259}.
-!- SUBCELLULAR LOCATION: Cell projection, cilium
{ECO:0000250|UniProtKB:Q6GQX6}. Cytoplasm
{ECO:0000250|UniProtKB:P0C0T2}. Note=Localizes to the proximal
region of the primary cilium in the presence of INVS.
{ECO:0000250|UniProtKB:Q6GQX6}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q68DC2-1; Sequence=Displayed;
Name=2;
IsoId=Q68DC2-3; Sequence=VSP_016496, VSP_016497;
Note=Gene prediction confirmed by EST data.;
Name=3;
IsoId=Q68DC2-4; Sequence=VSP_016498;
Note=No experimental confirmation available.;
-!- DOMAIN: The ankyrin repeats are necessary and sufficient for NEK8-
binding. {ECO:0000269|PubMed:23793029}.
-!- DOMAIN: The SAM domain mediates interaction with the SAM domain of
ANKS3. {ECO:0000269|PubMed:24998259}.
-!- PTM: Hydroxylated at Asn-138, most probably by HIF1AN. This
hydroxylation results in decreased NEK8-binding.
{ECO:0000250|UniProtKB:P0C0T2}.
-!- DISEASE: Nephronophthisis 16 (NPHP16) [MIM:615382]: A form of
nephronophthisis, a chronic tubulo-interstitial nephritis that
progresses to end-stage renal failure. Some patients have cystic
kidneys of normal size and no extrarenal manifestations, whereas
others have enlarged renal size and severe extrarenal defects,
including hypertrophic obstructive cardiomyopathy, aortic
stenosis, pulmonary stenosis, patent ductus arteriosus, situs
inversus, and periportal liver fibrosis.
{ECO:0000269|PubMed:23793029}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAH64367.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC04317.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAH18298.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAH69985.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH69986.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH71295.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH71296.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; DQ309791; ABC48694.1; -; Genomic_DNA.
EMBL; DQ309777; ABC48694.1; JOINED; Genomic_DNA.
EMBL; DQ309778; ABC48694.1; JOINED; Genomic_DNA.
EMBL; DQ309779; ABC48694.1; JOINED; Genomic_DNA.
EMBL; DQ309780; ABC48694.1; JOINED; Genomic_DNA.
EMBL; DQ309781; ABC48694.1; JOINED; Genomic_DNA.
EMBL; DQ309782; ABC48694.1; JOINED; Genomic_DNA.
EMBL; DQ309783; ABC48694.1; JOINED; Genomic_DNA.
EMBL; DQ309784; ABC48694.1; JOINED; Genomic_DNA.
EMBL; DQ309785; ABC48694.1; JOINED; Genomic_DNA.
EMBL; DQ309786; ABC48694.1; JOINED; Genomic_DNA.
EMBL; DQ309787; ABC48694.1; JOINED; Genomic_DNA.
EMBL; DQ309788; ABC48694.1; JOINED; Genomic_DNA.
EMBL; DQ309789; ABC48694.1; JOINED; Genomic_DNA.
EMBL; DQ309790; ABC48694.1; JOINED; Genomic_DNA.
EMBL; AL353782; CAH71295.2; ALT_SEQ; Genomic_DNA.
EMBL; AL807776; CAH71295.2; JOINED; Genomic_DNA.
EMBL; AL353782; CAH71296.2; ALT_SEQ; Genomic_DNA.
EMBL; AL807776; CAH71296.2; JOINED; Genomic_DNA.
EMBL; AL353782; CAM14169.1; -; Genomic_DNA.
EMBL; AL807776; CAM14169.1; JOINED; Genomic_DNA.
EMBL; AL807776; CAH69985.2; ALT_SEQ; Genomic_DNA.
EMBL; AL353782; CAH69985.2; JOINED; Genomic_DNA.
EMBL; AL807776; CAH69986.2; ALT_SEQ; Genomic_DNA.
EMBL; AL353782; CAH69986.2; JOINED; Genomic_DNA.
EMBL; AL807776; CAM13062.1; -; Genomic_DNA.
EMBL; AL353782; CAM13062.1; JOINED; Genomic_DNA.
EMBL; CR749467; CAH18298.1; ALT_INIT; mRNA.
EMBL; CR749472; CAH18302.1; -; mRNA.
EMBL; BC064367; AAH64367.1; ALT_INIT; mRNA.
EMBL; AK094247; BAC04317.1; ALT_INIT; mRNA.
CCDS; CCDS43856.1; -. [Q68DC2-1]
RefSeq; NP_775822.3; NM_173551.4. [Q68DC2-1]
RefSeq; XP_006717061.1; XM_006716998.3. [Q68DC2-4]
RefSeq; XP_016869934.1; XM_017014445.1. [Q68DC2-1]
UniGene; Hs.406890; -.
PDB; 4NL9; X-ray; 1.50 A; C/D=771-840.
PDBsum; 4NL9; -.
ProteinModelPortal; Q68DC2; -.
SMR; Q68DC2; -.
BioGrid; 128464; 14.
CORUM; Q68DC2; -.
IntAct; Q68DC2; 14.
MINT; Q68DC2; -.
STRING; 9606.ENSP00000297837; -.
iPTMnet; Q68DC2; -.
PhosphoSitePlus; Q68DC2; -.
BioMuta; ANKS6; -.
DMDM; 83305683; -.
EPD; Q68DC2; -.
MaxQB; Q68DC2; -.
PaxDb; Q68DC2; -.
PeptideAtlas; Q68DC2; -.
PRIDE; Q68DC2; -.
DNASU; 203286; -.
Ensembl; ENST00000353234; ENSP00000297837; ENSG00000165138. [Q68DC2-1]
GeneID; 203286; -.
KEGG; hsa:203286; -.
UCSC; uc004ayu.4; human. [Q68DC2-1]
CTD; 203286; -.
DisGeNET; 203286; -.
EuPathDB; HostDB:ENSG00000165138.17; -.
GeneCards; ANKS6; -.
H-InvDB; HIX0025696; -.
HGNC; HGNC:26724; ANKS6.
HPA; HPA008355; -.
MalaCards; ANKS6; -.
MIM; 615370; gene.
MIM; 615382; phenotype.
neXtProt; NX_Q68DC2; -.
OpenTargets; ENSG00000165138; -.
Orphanet; 93591; Infantile nephronophthisis.
Orphanet; 93592; Juvenile nephronophthisis.
PharmGKB; PA134931829; -.
eggNOG; KOG0504; Eukaryota.
eggNOG; KOG4374; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00900000140968; -.
HOVERGEN; HBG059049; -.
InParanoid; Q68DC2; -.
KO; K21415; -.
OMA; CMQVDKD; -.
OrthoDB; EOG091G029E; -.
PhylomeDB; Q68DC2; -.
TreeFam; TF328552; -.
ChiTaRS; ANKS6; human.
GenomeRNAi; 203286; -.
PRO; PR:Q68DC2; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000165138; -.
CleanEx; HS_ANKS6; -.
ExpressionAtlas; Q68DC2; baseline and differential.
Genevisible; Q68DC2; HS.
GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
Pfam; PF12796; Ank_2; 3.
Pfam; PF00536; SAM_1; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 9.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF48403; SSF48403; 3.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 7.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ANK repeat; Cell projection;
Ciliopathy; Cilium; Complete proteome; Cytoplasm; Disease mutation;
Hydroxylation; Joubert syndrome; Nephronophthisis; Phosphoprotein;
Polymorphism; Reference proteome; Repeat.
CHAIN 1 871 Ankyrin repeat and SAM domain-containing
protein 6.
/FTId=PRO_0000067065.
REPEAT 8 37 ANK 1.
REPEAT 77 106 ANK 2.
REPEAT 110 139 ANK 3.
REPEAT 143 172 ANK 4.
REPEAT 190 219 ANK 5.
REPEAT 224 253 ANK 6.
REPEAT 257 289 ANK 7.
REPEAT 291 321 ANK 8.
REPEAT 325 354 ANK 9.
REPEAT 359 388 ANK 10.
REPEAT 392 423 ANK 11.
DOMAIN 773 836 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
COMPBIAS 617 769 Ser-rich.
MOD_RES 138 138 3-hydroxyasparagine. {ECO:0000250}.
MOD_RES 657 657 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 734 734 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 742 742 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 288 335 DEEKRRPDIFHALKMGNFQLVKEIADEDPSHVNLVNGDGAT
PLMLAAV -> GQAACPPWLHRGPQIVFMWLKLRIALLEGH
AELRVQPCRPLRLRKWCA (in isoform 2).
{ECO:0000305}.
/FTId=VSP_016496.
VAR_SEQ 336 871 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_016497.
VAR_SEQ 714 714 K -> KQ (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_016498.
VARIANT 222 222 R -> W (in dbSNP:rs41283630).
{ECO:0000269|PubMed:18434273}.
/FTId=VAR_070105.
VARIANT 312 312 A -> P (in NPHP16).
{ECO:0000269|PubMed:23793029}.
/FTId=VAR_070106.
VARIANT 440 440 R -> Q (in dbSNP:rs763855876).
{ECO:0000269|PubMed:18434273}.
/FTId=VAR_070107.
VARIANT 441 441 Q -> R (in NPHP16; dbSNP:rs377750405).
/FTId=VAR_070108.
VARIANT 640 640 G -> S (in dbSNP:rs749102463).
{ECO:0000269|PubMed:18434273}.
/FTId=VAR_070109.
VARIANT 644 644 V -> I (in dbSNP:rs6415847).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:18434273}.
/FTId=VAR_034794.
VARIANT 735 735 P -> A (in dbSNP:rs79414550).
{ECO:0000269|PubMed:18434273}.
/FTId=VAR_070110.
MUTAGEN 798 798 E->K: Loss of interaction with ANKS3.
{ECO:0000269|PubMed:24998259}.
MUTAGEN 811 811 D->K: Loss of interaction with ANKS3.
{ECO:0000269|PubMed:24998259}.
MUTAGEN 823 823 R->W: Loss of interaction with ANKS3.
{ECO:0000269|PubMed:24998259}.
CONFLICT 244 244 L -> P (in Ref. 3; CAH18298).
{ECO:0000305}.
CONFLICT 402 402 L -> P (in Ref. 4; CAH18302).
{ECO:0000305}.
CONFLICT 647 647 S -> G (in Ref. 5; BAC04317).
{ECO:0000305}.
CONFLICT 808 808 T -> A (in Ref. 4; CAH18302).
{ECO:0000305}.
HELIX 778 784 {ECO:0000244|PDB:4NL9}.
HELIX 788 790 {ECO:0000244|PDB:4NL9}.
HELIX 791 796 {ECO:0000244|PDB:4NL9}.
HELIX 801 804 {ECO:0000244|PDB:4NL9}.
HELIX 809 815 {ECO:0000244|PDB:4NL9}.
HELIX 820 834 {ECO:0000244|PDB:4NL9}.
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


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