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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.
13-FEB-2019, entry version 143.
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};
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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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL807776; -; NOT_ANNOTATED_CDS; 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; 15.
CORUM; Q68DC2; -.
IntAct; Q68DC2; 15.
MINT; Q68DC2; -.
STRING; 9606.ENSP00000297837; -.
iPTMnet; Q68DC2; -.
PhosphoSitePlus; Q68DC2; -.
BioMuta; ANKS6; -.
DMDM; 83305683; -.
EPD; Q68DC2; -.
jPOST; Q68DC2; -.
MaxQB; Q68DC2; -.
PaxDb; Q68DC2; -.
PeptideAtlas; Q68DC2; -.
PRIDE; Q68DC2; -.
ProteomicsDB; 66071; -.
ProteomicsDB; 66072; -. [Q68DC2-3]
ProteomicsDB; 66073; -. [Q68DC2-4]
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; -.
GeneReviews; 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; ENSGT00940000157664; -.
HOVERGEN; HBG059049; -.
InParanoid; Q68DC2; -.
KO; K21415; -.
OMA; LPFCDEP; -.
OrthoDB; 1137424at2759; -.
PhylomeDB; Q68DC2; -.
TreeFam; TF328552; -.
ChiTaRS; ANKS6; human.
GenomeRNAi; 203286; -.
PRO; PR:Q68DC2; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000165138; Expressed in 156 organ(s), highest expression level in right hemisphere of cerebellum.
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; 2.
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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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1689: Porphyrin and chlorophyll metabolism
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP210: Cytoplasmic Ribosomal Proteins
WP2199: Seed Development
WP2292: Chemokine signaling pathway
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair

Related Genes :
[Ankrd17 Foe Gtar Kiaa0697] Ankyrin repeat domain-containing protein 17 (Ankyrin repeat domain-containing protein FOE) (Gene trap ankyrin repeat protein)
[Ankrd27 Varp] Ankyrin repeat domain-containing protein 27 (VPS9 domain-containing protein) (VPS9-ankyrin-repeat protein)
[KANK1 ANKRD15 KANK KIAA0172] KN motif and ankyrin repeat domain-containing protein 1 (Ankyrin repeat domain-containing protein 15) (Kidney ankyrin repeat-containing protein)
[mask CG33106] Ankyrin repeat and KH domain-containing protein mask (Multiple ankyrin repeat single KH domain-containing protein)
[Hace1 Kiaa1320] E3 ubiquitin-protein ligase HACE1 (EC 2.3.2.26) (HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1) (HECT-type E3 ubiquitin transferase HACE1)
[Fbxw7 Fbw7 Fbwd6 Fbxw6] F-box/WD repeat-containing protein 7 (F-box and WD-40 domain-containing protein 7) (F-box protein FBW7) (F-box protein Fbxw6) (F-box-WD40 repeat protein 6) (SEL-10)
[ANKRD17 GTAR KIAA0697] Ankyrin repeat domain-containing protein 17 (Gene trap ankyrin repeat protein) (Serologically defined breast cancer antigen NY-BR-16)
[PIA2 ANK6 At5g61230 MAF19.22] Phytochrome-interacting ankyrin-repeat protein 2 [Cleaved into: Protein ANKYRIN REPEAT 6, mitochondrial]
[ANKRD1 C193 CARP HA1A2] Ankyrin repeat domain-containing protein 1 (Cardiac ankyrin repeat protein) (Cytokine-inducible gene C-193 protein) (Cytokine-inducible nuclear protein)
[Shank3 Kiaa1650 Prosap2] SH3 and multiple ankyrin repeat domains protein 3 (Shank3) (Proline-rich synapse-associated protein 2) (ProSAP2) (SPANK-2)
[Asap1 Ddef1 Kiaa1249 Shag1] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[Asb4] Ankyrin repeat and SOCS box protein 4 (ASB-4)
[KDM2B CXXC2 FBL10 FBXL10 JHDM1B PCCX2] Lysine-specific demethylase 2B (EC 1.14.11.27) (CXXC-type zinc finger protein 2) (F-box and leucine-rich repeat protein 10) (F-box protein FBL10) (F-box/LRR-repeat protein 10) (JmjC domain-containing histone demethylation protein 1B) (Jumonji domain-containing EMSY-interactor methyltransferase motif protein) (Protein JEMMA) (Protein-containing CXXC domain 2) ([Histone-H3]-lysine-36 demethylase 1B)
[ANKLE2 KIAA0692 LEM4] Ankyrin repeat and LEM domain-containing protein 2 (LEM domain-containing protein 4)
[ANKRD27 PP12899] Ankyrin repeat domain-containing protein 27 (VPS9 domain-containing protein)
[ANKRD1 CARP] Ankyrin repeat domain-containing protein 1 (Cardiac ankyrin repeat protein)
[Ank2 AnkB] Ankyrin-2 (ANK-2) (Ankyrin-B) (Brain ankyrin)
[Kdm2b Fbl10 Fbxl10 Jhdm1b Kiaa3014] Lysine-specific demethylase 2B (EC 1.14.11.27) (F-box and leucine-rich repeat protein 10) (F-box protein FBL10) (F-box/LRR-repeat protein 10) (JmjC domain-containing histone demethylation protein 1B) ([Histone-H3]-lysine-36 demethylase 1B)
[Samhd1 Mg11] Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Interferon-gamma-inducible protein Mg11) (SAM domain and HD domain-containing protein 1) (mSAMHD1)
[USH1G SANS] Usher syndrome type-1G protein (Scaffold protein containing ankyrin repeats and SAM domain)
[Ankrd6 Kiaa0957] Ankyrin repeat domain-containing protein 6 (Diversin)
[Jmjd6 Kiaa0585 Ptdsr] Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-) (Histone arginine demethylase JMJD6) (JmjC domain-containing protein 6) (Jumonji domain-containing protein 6) (Lysyl-hydroxylase JMJD6) (Peptide-lysine 5-dioxygenase JMJD6) (Phosphatidylserine receptor) (Protein PTDSR)
[Kdm2a Fbxl11 Jhdm1a Kiaa1004] Lysine-specific demethylase 2A (EC 1.14.11.27) (F-box and leucine-rich repeat protein 11) (F-box/LRR-repeat protein 11) (JmjC domain-containing histone demethylation protein 1A) ([Histone-H3]-lysine-36 demethylase 1A)
[HACE1 KIAA1320] E3 ubiquitin-protein ligase HACE1 (EC 2.3.2.26) (HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1) (HECT-type E3 ubiquitin transferase HACE1)
[Ush1g Sans] Usher syndrome type-1G protein homolog (Jackson shaker protein) (Scaffold protein containing ankyrin repeats and SAM domain)
[Ank1 Ank-1] Ankyrin-1 (ANK-1) (Erythrocyte ankyrin)
[MIB1 DIP1 KIAA1323 ZZANK2] E3 ubiquitin-protein ligase MIB1 (EC 2.3.2.27) (DAPK-interacting protein 1) (DIP-1) (Mind bomb homolog 1) (RING-type E3 ubiquitin transferase MIB1) (Zinc finger ZZ type with ankyrin repeat domain protein 2)
[Wdfy3] WD repeat and FYVE domain-containing protein 3 (Beach domain, WD repeat and FYVE domain-containing protein 1) (BWF1)
[Ank3] Ankyrin-3 (ANK-3) (Ankyrin-G)
[Mettl16 Mett10d] RNA N6-adenosine-methyltransferase METTL16 (Methyltransferase 10 domain-containing protein) (Methyltransferase-like protein 16) (N6-adenosine-methyltransferase METTL16) (EC 2.1.1.348) (U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase) (EC 2.1.1.346)

Bibliography :
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