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Hyccin (Down-regulated by CTNNB1 protein A) (Protein FAM126A)

 HYCCI_HUMAN             Reviewed;         521 AA.
Q9BYI3; A0A024RA06; A4D145; B8ZZJ1; Q6N010; Q75MR4; Q7LDZ4; Q96MX1; Q96NQ6;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 2.
11-DEC-2019, entry version 130.
RecName: Full=Hyccin {ECO:0000303|PubMed:16951682};
AltName: Full=Down-regulated by CTNNB1 protein A {ECO:0000303|PubMed:10910037};
AltName: Full=Protein FAM126A {ECO:0000305};
Name=FAM126A; Synonyms=DRCTNNB1A {ECO:0000303|PubMed:10910037};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POSSIBLE FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
TISSUE=Fetal brain;
PubMed=10910037;
Kawasoe T., Furukawa Y., Daigo Y., Nishiwaki T., Ishiguro H., Fujita M.,
Satoh S., Miwa N., Nagasawa Y., Miyoshi Y., Ogawa M., Nakamura Y.;
"Isolation and characterization of a novel human gene, DRCTNNB1A, the
expression of which is down-regulated by beta-catenin.";
Cancer Res. 60:3354-3358(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
Yang X., Coulombe-Huntington J., Kang S., Sheynkman G.M., Hao T.,
Richardson A., Sun S., Yang F., Shen Y.A., Murray R., Spirohn K.,
Begg B.E., Duran-Frigola M., MacWilliams A., Pevzner S.J., Zhong Q.,
Trigg S.A., Tam S., Ghamsari L., Sahni N., Yi S., Rodriguez M.D.,
Balcha D., Tan G., Costanzo M., Andrews B., Boone C., Zhou X.J.,
Salehi-Ashtiani K., Charloteaux B., Chen A., Calderwood M.A., Aloy P.,
Roth F.P., Hill D.E., Iakoucheva L.M., Xia Y., Vidal M.;
"Widespread expansion of protein interaction capabilities by alternative
splicing.";
Cell 0:0-0(2016).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Teratocarcinoma;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[10]
INVOLVEMENT IN HLD5.
PubMed=21911699; DOI=10.1001/archneurol.2011.201;
Biancheri R., Zara F., Rossi A., Mathot M., Nassogne M.C., Yalcinkaya C.,
Erturk O., Tuysuz B., Di Rocco M., Gazzerro E., Bugiani M.,
van Spaendonk R., Sistermans E.A., Minetti C., van der Knaap M.S.,
Wolf N.I.;
"Hypomyelination and congenital cataract: broadening the clinical
phenotype.";
Arch. Neurol. 68:1191-1194(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-306; SER-415; SER-422;
SER-433 AND SER-453, 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).
[12]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 12-271 IN COMPLEX WITH TTC7B,
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TTC7B, IDENTIFICATION IN
THE PI4K COMPLEX, AND CHARACTERIZATION OF VARIANTS HLD5 PRO-53 AND ARG-57.
PubMed=26571211; DOI=10.1038/ncb3271;
Baskin J.M., Wu X., Christiano R., Oh M.S., Schauder C.M., Gazzerro E.,
Messa M., Baldassari S., Assereto S., Biancheri R., Zara F., Minetti C.,
Raimondi A., Simons M., Walther T.C., Reinisch K.M., De Camilli P.;
"The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis
at the plasma membrane.";
Nat. Cell Biol. 18:132-138(2016).
[13]
VARIANT HLD5 PRO-53, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16951682; DOI=10.1038/ng1870;
Zara F., Biancheri R., Bruno C., Bordo L., Assereto S., Gazzerro E.,
Sotgia F., Wang X.B., Gianotti S., Stringara S., Pedemonte M., Uziel G.,
Rossi A., Schenone A., Tortori-Donati P., van der Knaap M.S., Lisanti M.P.,
Minetti C.;
"Deficiency of hyccin, a newly identified membrane protein, causes
hypomyelination and congenital cataract.";
Nat. Genet. 38:1111-1113(2006).
[14]
VARIANT HLD5 ARG-57.
PubMed=23998934; DOI=10.1016/j.bbrc.2013.08.077;
Traverso M., Assereto S., Gazzerro E., Savasta S., Abdalla E.M., Rossi A.,
Baldassari S., Fruscione F., Ruffinazzi G., Fassad M.R., El Beheiry A.,
Minetti C., Zara F., Biancheri R.;
"Novel FAM126A mutations in hypomyelination and congenital cataract
disease.";
Biochem. Biophys. Res. Commun. 439:369-372(2013).
[15]
VARIANT GLN-217.
PubMed=28887846; DOI=10.1002/humu.23335;
Zhou X.L., He L.X., Yu L.J., Wang Y., Wang X.J., Wang E.D., Yang T.;
"Mutations in KARS cause early-onset hearing loss and leukoencephalopathy:
Potential pathogenic mechanism.";
Hum. Mutat. 38:1740-1750(2017).
-!- FUNCTION: Component of a complex required to localize
phosphatidylinositol 4-kinase (PI4K) to the plasma membrane
(PubMed:26571211). The complex acts as a regulator of
phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis
(PubMed:26571211). FAM126A plays a key role in oligodendrocytes
formation, a cell type with expanded plasma membrane that requires
generation of PtdIns(4)P (PubMed:26571211). Its role in
oligodendrocytes formation probably explains its importance in
myelination of the central and peripheral nervous system
(PubMed:26571211, PubMed:16951682). May also have a role in the beta-
catenin/Lef signaling pathway (Probable). {ECO:0000269|PubMed:16951682,
ECO:0000269|PubMed:26571211, ECO:0000305|PubMed:10910037}.
-!- SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex,
composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and
FAM126 (FAM126A or FAM126B) (PubMed:26571211). Interacts with TTC7
(TTC7A or TTC7B), interaction is direct (PubMed:26571211).
{ECO:0000269|PubMed:26571211}.
-!- INTERACTION:
O95273:CCNDBP1; NbExp=3; IntAct=EBI-11065686, EBI-748961;
Q13643:FHL3; NbExp=3; IntAct=EBI-11065686, EBI-741101;
Q6FHY5:MEOX2; NbExp=3; IntAct=EBI-11065686, EBI-16439278;
P14373:TRIM27; NbExp=6; IntAct=EBI-11065686, EBI-719493;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10910037,
ECO:0000269|PubMed:26571211}. Cell membrane
{ECO:0000269|PubMed:16951682, ECO:0000269|PubMed:26571211}.
Note=Localizes to the cytosol and is recruited to the plasma membrane
following interaction with other components of the phosphatidylinositol
4-kinase (PI4K) complex. {ECO:0000269|PubMed:26571211}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9BYI3-1; Sequence=Displayed;
Name=2;
IsoId=Q9BYI3-2; Sequence=VSP_023126;
Name=3;
IsoId=Q9BYI3-3; Sequence=VSP_058128, VSP_058129;
-!- TISSUE SPECIFICITY: Widely expressed. Highest levels in heart, brain,
placenta, spleen and testis. {ECO:0000269|PubMed:10910037}.
-!- INDUCTION: Down-regulated by beta-catenin.
{ECO:0000269|PubMed:10910037}.
-!- DISEASE: Leukodystrophy, hypomyelinating, 5 (HLD5) [MIM:610532]: A
hypomyelinating leukodystrophy associated with congenital cataract. It
is clinically characterized by congenital cataract, progressive
neurologic impairment, and diffuse myelin deficiency. Affected
individuals experience progressive pyramidal and cerebellar
dysfunction, muscle weakness and wasting prevailingly in the lower
limbs. Mental deficiency ranges from mild to moderate. HLD5 shows
clinical variability, but features of hypomyelination combined with
increased periventricular white matter water content are consistently
observed. {ECO:0000269|PubMed:16951682, ECO:0000269|PubMed:21911699,
ECO:0000269|PubMed:23998934, ECO:0000269|PubMed:26571211}. Note=The
disease is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the FAM126 family. {ECO:0000305}.
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EMBL; AB030241; BAB39849.1; -; mRNA.
EMBL; KU178808; ALQ34266.1; -; mRNA.
EMBL; KU178809; ALQ34267.1; -; mRNA.
EMBL; AK056319; BAB71148.1; -; mRNA.
EMBL; AK054887; BAB70823.1; -; mRNA.
EMBL; AC005682; AAS01991.1; -; Genomic_DNA.
EMBL; AC006039; AAS07519.1; -; Genomic_DNA.
EMBL; CH236948; EAL24262.1; -; Genomic_DNA.
EMBL; CH471073; EAW93767.1; -; Genomic_DNA.
EMBL; CH471073; EAW93768.1; -; Genomic_DNA.
EMBL; BC018710; AAH18710.1; -; mRNA.
EMBL; BX640757; CAE45864.1; -; mRNA.
CCDS; CCDS5377.1; -. [Q9BYI3-1]
CCDS; CCDS87486.1; -. [Q9BYI3-3]
RefSeq; NP_115970.2; NM_032581.3. [Q9BYI3-1]
RefSeq; XP_005249951.1; XM_005249894.3.
RefSeq; XP_011513891.1; XM_011515589.2. [Q9BYI3-1]
PDB; 5DSE; X-ray; 2.90 A; B/D=2-308.
PDB; 6BQ1; EM; 3.60 A; C/G=2-289.
PDBsum; 5DSE; -.
PDBsum; 6BQ1; -.
SMR; Q9BYI3; -.
BioGrid; 124188; 18.
CORUM; Q9BYI3; -.
IntAct; Q9BYI3; 14.
STRING; 9606.ENSP00000403396; -.
iPTMnet; Q9BYI3; -.
PhosphoSitePlus; Q9BYI3; -.
BioMuta; FAM126A; -.
DMDM; 77416421; -.
EPD; Q9BYI3; -.
jPOST; Q9BYI3; -.
MassIVE; Q9BYI3; -.
MaxQB; Q9BYI3; -.
PaxDb; Q9BYI3; -.
PeptideAtlas; Q9BYI3; -.
PRIDE; Q9BYI3; -.
ProteomicsDB; 7387; -.
ProteomicsDB; 79652; -. [Q9BYI3-1]
ProteomicsDB; 79653; -. [Q9BYI3-2]
DNASU; 84668; -.
Ensembl; ENST00000409923; ENSP00000386246; ENSG00000122591. [Q9BYI3-3]
Ensembl; ENST00000432176; ENSP00000403396; ENSG00000122591. [Q9BYI3-1]
GeneID; 84668; -.
KEGG; hsa:84668; -.
UCSC; uc003svm.5; human. [Q9BYI3-1]
UCSC; uc064byk.1; human.
CTD; 84668; -.
DisGeNET; 84668; -.
EuPathDB; HostDB:ENSG00000122591.11; -.
GeneCards; FAM126A; -.
GeneReviews; FAM126A; -.
HGNC; HGNC:24587; FAM126A.
HPA; HPA042873; -.
MalaCards; FAM126A; -.
MIM; 610531; gene.
MIM; 610532; phenotype.
neXtProt; NX_Q9BYI3; -.
OpenTargets; ENSG00000122591; -.
Orphanet; 85163; Hypomyelination-congenital cataract syndrome.
PharmGKB; PA162385852; -.
eggNOG; KOG4688; Eukaryota.
eggNOG; ENOG410ZXRB; LUCA.
GeneTree; ENSGT00390000011295; -.
HOGENOM; HOG000252938; -.
InParanoid; Q9BYI3; -.
KO; K21844; -.
OMA; NRATYEM; -.
OrthoDB; 673408at2759; -.
PhylomeDB; Q9BYI3; -.
TreeFam; TF317153; -.
ChiTaRS; FAM126A; human.
GenomeRNAi; 84668; -.
Pharos; Q9BYI3; Tbio.
PRO; PR:Q9BYI3; -.
Proteomes; UP000005640; Chromosome 7.
RNAct; Q9BYI3; protein.
Bgee; ENSG00000122591; Expressed in 198 organ(s), highest expression level in gastrocnemius.
ExpressionAtlas; Q9BYI3; baseline and differential.
Genevisible; Q9BYI3; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042552; P:myelination; ISS:UniProtKB.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; IDA:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
InterPro; IPR018619; Hyccin.
PANTHER; PTHR31220; PTHR31220; 1.
Pfam; PF09790; Hyccin; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cataract; Cell membrane; Cytoplasm;
Disease mutation; Leukodystrophy; Membrane; Phosphoprotein;
Reference proteome.
CHAIN 1..521
/note="Hyccin"
/id="PRO_0000080005"
MOD_RES 306
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 321
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q6P9N1"
MOD_RES 415
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 422
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 433
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 453
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:23186163"
VAR_SEQ 1..341
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:17974005"
/id="VSP_023126"
VAR_SEQ 331..419
/note="GNTELTGQEELMEISEVDEGFYSRAASSTSQSGLSNSSHNCSNKPSIGKNHR
RSGGSKTGGKEKETTGESCKDHFARKQTQRAQSENLE -> EQPDNNNDATELGILVIP
EISVTNVAGERTGNGEKGRTLGEIDAQHIQGVQETATDPRTESKGLPEIRRQKSVRKMM
EDGINSPGRVQF (in isoform 3)"
/id="VSP_058128"
VAR_SEQ 420..521
/note="Missing (in isoform 3)"
/id="VSP_058129"
VARIANT 53
/note="L -> P (in HLD5; induces misfolding and degradation,
leading to destabilization of the PI4K complex;
dbSNP:rs72549407)"
/evidence="ECO:0000269|PubMed:16951682,
ECO:0000269|PubMed:26571211"
/id="VAR_030647"
VARIANT 57
/note="C -> R (in HLD5; induces misfolding and degradation,
leading to destabilization of the PI4K complex)"
/evidence="ECO:0000269|PubMed:23998934,
ECO:0000269|PubMed:26571211"
/id="VAR_075100"
VARIANT 217
/note="R -> Q (in dbSNP:rs192409840)"
/evidence="ECO:0000269|PubMed:28887846"
/id="VAR_079751"
CONFLICT 160
/note="V -> A (in Ref. 1; BAB39849)"
/evidence="ECO:0000305"
CONFLICT 194
/note="Y -> C (in Ref. 1; BAB39849)"
/evidence="ECO:0000305"
CONFLICT 474
/note="A -> V (in Ref. 4; CAE45864)"
/evidence="ECO:0000305"
HELIX 8..14
/evidence="ECO:0000244|PDB:5DSE"
TURN 26..28
/evidence="ECO:0000244|PDB:5DSE"
HELIX 37..46
/evidence="ECO:0000244|PDB:5DSE"
HELIX 54..65
/evidence="ECO:0000244|PDB:5DSE"
HELIX 69..76
/evidence="ECO:0000244|PDB:5DSE"
HELIX 79..91
/evidence="ECO:0000244|PDB:5DSE"
HELIX 100..112
/evidence="ECO:0000244|PDB:5DSE"
STRAND 116..119
/evidence="ECO:0000244|PDB:5DSE"
STRAND 123..126
/evidence="ECO:0000244|PDB:5DSE"
HELIX 144..147
/evidence="ECO:0000244|PDB:5DSE"
STRAND 159..163
/evidence="ECO:0000244|PDB:5DSE"
HELIX 176..190
/evidence="ECO:0000244|PDB:5DSE"
HELIX 197..212
/evidence="ECO:0000244|PDB:5DSE"
HELIX 217..221
/evidence="ECO:0000244|PDB:5DSE"
HELIX 234..248
/evidence="ECO:0000244|PDB:5DSE"
TURN 249..251
/evidence="ECO:0000244|PDB:5DSE"
HELIX 253..269
/evidence="ECO:0000244|PDB:5DSE"
HELIX 273..285
/evidence="ECO:0000244|PDB:5DSE"
SEQUENCE 521 AA; 57625 MW; 722D7A9CFD5EC060 CRC64;
MFTSEKGVVE EWLSEFKTLP ETSLPNYATN LKDKSSLVSS LYKVIQEPQS ELLEPVCHQL
FEFYRSGEEQ LLQFTLQFLP ELIWCYLAVS ASRNVHSSGC IEALLLGVYN LEIVDKQGHT
KVLSFTIPSL SKPSVYHEPS SIGSMALTES ALSQHGLSKV VYSGPHPQRE MLTAQNRFEV
LTFLLLCYNA ALTYMPSVSL QSLCQICSRI CVCGYPRQHV RKYKGISSRI PVSSGFMVQM
LTGIYFAFYN GEWDLAQKAL DDIIYRAQLE LYPEPLLVAN AIKASLPHGP MKSNKEGTRC
IQVEITPTSS RISRNAVTSM SIRGHRWKRH GNTELTGQEE LMEISEVDEG FYSRAASSTS
QSGLSNSSHN CSNKPSIGKN HRRSGGSKTG GKEKETTGES CKDHFARKQT QRAQSENLEL
LSLKRLTLTT SQSLPKPSSH GLAKTAATVF SKSFEQVSGV TVPHNPSSAV GCGAGTDANR
FSACSLQEEK LIYVSERTEL PMKHQSGQQR PPSISITLST D


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WP35: G Protein Signaling Pathways
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WP1438: Influenza A virus infection
WP1694: Pyrimidine metabolism
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Related Genes :
[FAM126A DRCTNNB1A] Hyccin (Down-regulated by CTNNB1 protein A) (Protein FAM126A)
[Fam126a Drctnnb1a] Hyccin (Down-regulated by CTNNB1 protein A) (Protein FAM126A)
[CTNNB1 CTNNB OK/SW-cl.35 PRO2286] Catenin beta-1 (Beta-catenin)
[Ctnnb1 Catnb] Catenin beta-1 (Beta-catenin)
[Ctnnb1 Catnb] Catenin beta-1 (Beta-catenin)
[CTNNB1] Catenin beta-1 (Beta-catenin)
[CTNNB1] Catenin beta-1 (Beta-catenin)
[LEO1 RDL] RNA polymerase-associated protein LEO1 (Replicative senescence down-regulated leo1-like protein)
[Cdon Cdo] Cell adhesion molecule-related/down-regulated by oncogenes
[HEXIM1 CLP1 EDG1 HIS1 MAQ1] Protein HEXIM1 (Cardiac lineage protein 1) (Estrogen down-regulated gene 1 protein) (Hexamethylene bis-acetamide-inducible protein 1) (Menage a quatre protein 1)
[FAM107A DRR1 TU3A] Actin-associated protein FAM107A (Down-regulated in renal cell carcinoma 1) (Protein TU3A)
[NAV2 HELAD1 KIAA1419 POMFIL2 RAINB1 STEERIN2] Neuron navigator 2 (EC 3.6.4.12) (Helicase APC down-regulated 1) (Pore membrane and/or filament-interacting-like protein 2) (Retinoic acid inducible in neuroblastoma 1) (Steerin-2) (Unc-53 homolog 2) (unc53H2)
[Ndrg2 Kiaa1248 Ndr2] Protein NDRG2 (N-myc downstream-regulated gene 2 protein) (Protein Ndr2)
[WDR26 CDW2 MIP2 PRO0852] WD repeat-containing protein 26 (CUL4- and DDB1-associated WDR protein 2) (Myocardial ischemic preconditioning up-regulated protein 2)
[Sgk1 Sgk] Serine/threonine-protein kinase Sgk1 (EC 2.7.11.1) (Serum/glucocorticoid-regulated kinase 1)
[Nedd8 Nedd-8] NEDD8 (Neddylin) (Neural precursor cell expressed developmentally down-regulated protein 8) (NEDD-8) (Ubiquitin-like protein Nedd8)
[Nedd1 Nedd-1] Protein NEDD1 (Neural precursor cell expressed developmentally down-regulated protein 1) (NEDD-1)
[LDOC1 BCUR1] Protein LDOC1 (Leucine zipper protein down-regulated in cancer cells)
[GREM1 CKTSF1B1 DAND2 DRM PIG2] Gremlin-1 (Cell proliferation-inducing gene 2 protein) (Cysteine knot superfamily 1, BMP antagonist 1) (DAN domain family member 2) (Down-regulated in Mos-transformed cells protein) (Increased in high glucose protein 2) (IHG-2)
[NEDD8] NEDD8 (Neddylin) (Neural precursor cell expressed developmentally down-regulated protein 8) (NEDD-8) (Ubiquitin-like protein Nedd8)
[Grem1 Cktsf1b1 Drm] Gremlin-1 (Cysteine knot superfamily 1, BMP antagonist 1) (Down-regulated in Mos-transformed cells protein)
[Casp2 Ich1 Nedd-2 Nedd2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[Grem1 Cktsf1b1 Drm] Gremlin-1 (Cysteine knot superfamily 1, BMP antagonist 1) (Down-regulated in Mos-transformed cells protein)
[BTRC BTRCP FBW1A FBXW1A] F-box/WD repeat-containing protein 1A (E3RSIkappaB) (Epididymis tissue protein Li 2a) (F-box and WD repeats protein beta-TrCP) (pIkappaBalpha-E3 receptor subunit)
[EFR3A KIAA0143] Protein EFR3 homolog A (Protein EFR3-like)
[SGK1 SGK] Serine/threonine-protein kinase Sgk1 (EC 2.7.11.1) (Serum/glucocorticoid-regulated kinase 1)
[PI4KA PIK4 PIK4CA] Phosphatidylinositol 4-kinase alpha (PI4-kinase alpha) (PI4K-alpha) (PtdIns-4-kinase alpha) (EC 2.7.1.67)
[Sgk1 Sgk] Serine/threonine-protein kinase Sgk1 (EC 2.7.11.1) (Serum/glucocorticoid-regulated kinase 1)
[SIAH1 HUMSIAH] E3 ubiquitin-protein ligase SIAH1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH1) (Seven in absentia homolog 1) (Siah-1) (Siah-1a)
[] Testis cDNA clone: QtsA-17763, similar to human catenin (cadherin-associated protein), beta 1, 88kDa(CTNNB1)

Bibliography :