HYCCI_HUMAN
ID HYCCI_HUMAN Reviewed; 521 AA.
AC Q9BYI3; A0A024RA06; A4D145; B8ZZJ1; Q6N010; Q75MR4; Q7LDZ4; Q96MX1; Q96NQ6;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Hyccin {ECO:0000303|PubMed:16951682};
DE AltName: Full=Down-regulated by CTNNB1 protein A {ECO:0000303|PubMed:10910037};
DE AltName: Full=Protein FAM126A {ECO:0000305};
GN Name=FAM126A; Synonyms=DRCTNNB1A {ECO:0000303|PubMed:10910037};
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] (ISOFORM 1), POSSIBLE FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Fetal brain;
RX PubMed=10910037;
RA Kawasoe T., Furukawa Y., Daigo Y., Nishiwaki T., Ishiguro H., Fujita M.,
RA Satoh S., Miwa N., Nagasawa Y., Miyoshi Y., Ogawa M., Nakamura Y.;
RT "Isolation and characterization of a novel human gene, DRCTNNB1A, the
RT expression of which is down-regulated by beta-catenin.";
RL Cancer Res. 60:3354-3358(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RA Yang X., Coulombe-Huntington J., Kang S., Sheynkman G.M., Hao T.,
RA Richardson A., Sun S., Yang F., Shen Y.A., Murray R., Spirohn K.,
RA Begg B.E., Duran-Frigola M., MacWilliams A., Pevzner S.J., Zhong Q.,
RA Trigg S.A., Tam S., Ghamsari L., Sahni N., Yi S., Rodriguez M.D.,
RA Balcha D., Tan G., Costanzo M., Andrews B., Boone C., Zhou X.J.,
RA Salehi-Ashtiani K., Charloteaux B., Chen A., Calderwood M.A., Aloy P.,
RA Roth F.P., Hill D.E., Iakoucheva L.M., Xia Y., Vidal M.;
RT "Widespread expansion of protein interaction capabilities by alternative
RT splicing.";
RL Cell 0:0-0(2016).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP INVOLVEMENT IN HLD5.
RX PubMed=21911699; DOI=10.1001/archneurol.2011.201;
RA Biancheri R., Zara F., Rossi A., Mathot M., Nassogne M.C., Yalcinkaya C.,
RA Erturk O., Tuysuz B., Di Rocco M., Gazzerro E., Bugiani M.,
RA van Spaendonk R., Sistermans E.A., Minetti C., van der Knaap M.S.,
RA Wolf N.I.;
RT "Hypomyelination and congenital cataract: broadening the clinical
RT phenotype.";
RL Arch. Neurol. 68:1191-1194(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-306; SER-415; SER-422;
RP SER-433 AND SER-453, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 12-271 IN COMPLEX WITH TTC7B,
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TTC7B, IDENTIFICATION IN
RP THE PI4K COMPLEX, AND CHARACTERIZATION OF VARIANTS HLD5 PRO-53 AND ARG-57.
RX PubMed=26571211; DOI=10.1038/ncb3271;
RA Baskin J.M., Wu X., Christiano R., Oh M.S., Schauder C.M., Gazzerro E.,
RA Messa M., Baldassari S., Assereto S., Biancheri R., Zara F., Minetti C.,
RA Raimondi A., Simons M., Walther T.C., Reinisch K.M., De Camilli P.;
RT "The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis
RT at the plasma membrane.";
RL Nat. Cell Biol. 18:132-138(2016).
RN [13]
RP VARIANT HLD5 PRO-53, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16951682; DOI=10.1038/ng1870;
RA Zara F., Biancheri R., Bruno C., Bordo L., Assereto S., Gazzerro E.,
RA Sotgia F., Wang X.B., Gianotti S., Stringara S., Pedemonte M., Uziel G.,
RA Rossi A., Schenone A., Tortori-Donati P., van der Knaap M.S., Lisanti M.P.,
RA Minetti C.;
RT "Deficiency of hyccin, a newly identified membrane protein, causes
RT hypomyelination and congenital cataract.";
RL Nat. Genet. 38:1111-1113(2006).
RN [14]
RP VARIANT HLD5 ARG-57.
RX PubMed=23998934; DOI=10.1016/j.bbrc.2013.08.077;
RA Traverso M., Assereto S., Gazzerro E., Savasta S., Abdalla E.M., Rossi A.,
RA Baldassari S., Fruscione F., Ruffinazzi G., Fassad M.R., El Beheiry A.,
RA Minetti C., Zara F., Biancheri R.;
RT "Novel FAM126A mutations in hypomyelination and congenital cataract
RT disease.";
RL Biochem. Biophys. Res. Commun. 439:369-372(2013).
RN [15]
RP VARIANT GLN-217.
RX PubMed=28887846; DOI=10.1002/humu.23335;
RA Zhou X.L., He L.X., Yu L.J., Wang Y., Wang X.J., Wang E.D., Yang T.;
RT "Mutations in KARS cause early-onset hearing loss and leukoencephalopathy:
RT Potential pathogenic mechanism.";
RL Hum. Mutat. 38:1740-1750(2017).
CC -!- FUNCTION: Component of a complex required to localize
CC phosphatidylinositol 4-kinase (PI4K) to the plasma membrane
CC (PubMed:26571211). The complex acts as a regulator of
CC phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis
CC (PubMed:26571211). FAM126A plays a key role in oligodendrocytes
CC formation, a cell type with expanded plasma membrane that requires
CC generation of PtdIns(4)P (PubMed:26571211). Its role in
CC oligodendrocytes formation probably explains its importance in
CC myelination of the central and peripheral nervous system
CC (PubMed:26571211, PubMed:16951682). May also have a role in the beta-
CC catenin/Lef signaling pathway (Probable). {ECO:0000269|PubMed:16951682,
CC ECO:0000269|PubMed:26571211, ECO:0000305|PubMed:10910037}.
CC -!- SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex,
CC composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and
CC FAM126 (FAM126A or FAM126B) (PubMed:26571211). Interacts with TTC7
CC (TTC7A or TTC7B), interaction is direct (PubMed:26571211).
CC {ECO:0000269|PubMed:26571211}.
CC -!- INTERACTION:
CC Q9BYI3; O95273: CCNDBP1; NbExp=3; IntAct=EBI-11065686, EBI-748961;
CC Q9BYI3; Q13643: FHL3; NbExp=3; IntAct=EBI-11065686, EBI-741101;
CC Q9BYI3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11065686, EBI-16439278;
CC Q9BYI3; P14373: TRIM27; NbExp=6; IntAct=EBI-11065686, EBI-719493;
CC Q9BYI3; Q86TV6: TTC7B; NbExp=5; IntAct=EBI-11065686, EBI-12006098;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10910037,
CC ECO:0000269|PubMed:26571211}. Cell membrane
CC {ECO:0000269|PubMed:16951682, ECO:0000269|PubMed:26571211}.
CC Note=Localizes to the cytosol and is recruited to the plasma membrane
CC following interaction with other components of the phosphatidylinositol
CC 4-kinase (PI4K) complex. {ECO:0000269|PubMed:26571211}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BYI3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BYI3-2; Sequence=VSP_023126;
CC Name=3;
CC IsoId=Q9BYI3-3; Sequence=VSP_058128, VSP_058129;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels in heart, brain,
CC placenta, spleen and testis. {ECO:0000269|PubMed:10910037}.
CC -!- INDUCTION: Down-regulated by beta-catenin.
CC {ECO:0000269|PubMed:10910037}.
CC -!- DISEASE: Leukodystrophy, hypomyelinating, 5 (HLD5) [MIM:610532]: A
CC hypomyelinating leukodystrophy associated with congenital cataract. It
CC is clinically characterized by congenital cataract, progressive
CC neurologic impairment, and diffuse myelin deficiency. Affected
CC individuals experience progressive pyramidal and cerebellar
CC dysfunction, muscle weakness and wasting prevailingly in the lower
CC limbs. Mental deficiency ranges from mild to moderate. HLD5 shows
CC clinical variability, but features of hypomyelination combined with
CC increased periventricular white matter water content are consistently
CC observed. {ECO:0000269|PubMed:16951682, ECO:0000269|PubMed:21911699,
CC ECO:0000269|PubMed:23998934, ECO:0000269|PubMed:26571211}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the FAM126 family. {ECO:0000305}.
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DR EMBL; AB030241; BAB39849.1; -; mRNA.
DR EMBL; KU178808; ALQ34266.1; -; mRNA.
DR EMBL; KU178809; ALQ34267.1; -; mRNA.
DR EMBL; AK056319; BAB71148.1; -; mRNA.
DR EMBL; AK054887; BAB70823.1; -; mRNA.
DR EMBL; AC005682; AAS01991.1; -; Genomic_DNA.
DR EMBL; AC006039; AAS07519.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24262.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93767.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93768.1; -; Genomic_DNA.
DR EMBL; BC018710; AAH18710.1; -; mRNA.
DR EMBL; BX640757; CAE45864.1; -; mRNA.
DR CCDS; CCDS5377.1; -. [Q9BYI3-1]
DR CCDS; CCDS87486.1; -. [Q9BYI3-3]
DR RefSeq; NP_115970.2; NM_032581.3. [Q9BYI3-1]
DR RefSeq; XP_005249951.1; XM_005249894.3.
DR RefSeq; XP_011513891.1; XM_011515589.2. [Q9BYI3-1]
DR PDB; 5DSE; X-ray; 2.90 A; B/D=2-308.
DR PDB; 6BQ1; EM; 3.60 A; C/G=2-289.
DR PDBsum; 5DSE; -.
DR PDBsum; 6BQ1; -.
DR AlphaFoldDB; Q9BYI3; -.
DR SMR; Q9BYI3; -.
DR BioGRID; 124188; 38.
DR CORUM; Q9BYI3; -.
DR IntAct; Q9BYI3; 18.
DR MINT; Q9BYI3; -.
DR STRING; 9606.ENSP00000403396; -.
DR iPTMnet; Q9BYI3; -.
DR PhosphoSitePlus; Q9BYI3; -.
DR BioMuta; FAM126A; -.
DR DMDM; 77416421; -.
DR EPD; Q9BYI3; -.
DR jPOST; Q9BYI3; -.
DR MassIVE; Q9BYI3; -.
DR MaxQB; Q9BYI3; -.
DR PaxDb; Q9BYI3; -.
DR PeptideAtlas; Q9BYI3; -.
DR PRIDE; Q9BYI3; -.
DR ProteomicsDB; 7387; -.
DR ProteomicsDB; 79652; -. [Q9BYI3-1]
DR ProteomicsDB; 79653; -. [Q9BYI3-2]
DR Antibodypedia; 53361; 65 antibodies from 19 providers.
DR DNASU; 84668; -.
DR Ensembl; ENST00000409923.5; ENSP00000386246.1; ENSG00000122591.13. [Q9BYI3-3]
DR Ensembl; ENST00000432176.7; ENSP00000403396.2; ENSG00000122591.13. [Q9BYI3-1]
DR GeneID; 84668; -.
DR KEGG; hsa:84668; -.
DR MANE-Select; ENST00000432176.7; ENSP00000403396.2; NM_032581.4; NP_115970.2.
DR UCSC; uc003svm.5; human. [Q9BYI3-1]
DR UCSC; uc064byk.1; human.
DR CTD; 84668; -.
DR DisGeNET; 84668; -.
DR GeneCards; FAM126A; -.
DR GeneReviews; FAM126A; -.
DR HGNC; HGNC:24587; FAM126A.
DR HPA; ENSG00000122591; Low tissue specificity.
DR MalaCards; FAM126A; -.
DR MIM; 610531; gene.
DR MIM; 610532; phenotype.
DR neXtProt; NX_Q9BYI3; -.
DR OpenTargets; ENSG00000122591; -.
DR Orphanet; 85163; Hypomyelination-congenital cataract syndrome.
DR PharmGKB; PA162385852; -.
DR VEuPathDB; HostDB:ENSG00000122591; -.
DR eggNOG; KOG4688; Eukaryota.
DR GeneTree; ENSGT00390000011295; -.
DR HOGENOM; CLU_027457_3_0_1; -.
DR InParanoid; Q9BYI3; -.
DR OMA; TAGESCK; -.
DR OrthoDB; 673408at2759; -.
DR PhylomeDB; Q9BYI3; -.
DR TreeFam; TF317153; -.
DR PathwayCommons; Q9BYI3; -.
DR SignaLink; Q9BYI3; -.
DR BioGRID-ORCS; 84668; 11 hits in 1083 CRISPR screens.
DR ChiTaRS; FAM126A; human.
DR GenomeRNAi; 84668; -.
DR Pharos; Q9BYI3; Tbio.
DR PRO; PR:Q9BYI3; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9BYI3; protein.
DR Bgee; ENSG00000122591; Expressed in calcaneal tendon and 187 other tissues.
DR ExpressionAtlas; Q9BYI3; baseline and differential.
DR Genevisible; Q9BYI3; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR InterPro; IPR018619; Hyccin.
DR PANTHER; PTHR31220; PTHR31220; 1.
DR Pfam; PF09790; Hyccin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cataract; Cell membrane; Cytoplasm;
KW Disease variant; Leukodystrophy; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..521
FT /note="Hyccin"
FT /id="PRO_0000080005"
FT REGION 355..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 306
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9N1"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..341
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_023126"
FT VAR_SEQ 331..419
FT /note="GNTELTGQEELMEISEVDEGFYSRAASSTSQSGLSNSSHNCSNKPSIGKNHR
FT RSGGSKTGGKEKETTGESCKDHFARKQTQRAQSENLE -> EQPDNNNDATELGILVIP
FT EISVTNVAGERTGNGEKGRTLGEIDAQHIQGVQETATDPRTESKGLPEIRRQKSVRKMM
FT EDGINSPGRVQF (in isoform 3)"
FT /id="VSP_058128"
FT VAR_SEQ 420..521
FT /note="Missing (in isoform 3)"
FT /id="VSP_058129"
FT VARIANT 53
FT /note="L -> P (in HLD5; induces misfolding and degradation,
FT leading to destabilization of the PI4K complex;
FT dbSNP:rs72549407)"
FT /evidence="ECO:0000269|PubMed:16951682,
FT ECO:0000269|PubMed:26571211"
FT /id="VAR_030647"
FT VARIANT 57
FT /note="C -> R (in HLD5; induces misfolding and degradation,
FT leading to destabilization of the PI4K complex)"
FT /evidence="ECO:0000269|PubMed:23998934,
FT ECO:0000269|PubMed:26571211"
FT /id="VAR_075100"
FT VARIANT 217
FT /note="R -> Q (in dbSNP:rs192409840)"
FT /evidence="ECO:0000269|PubMed:28887846"
FT /id="VAR_079751"
FT CONFLICT 160
FT /note="V -> A (in Ref. 1; BAB39849)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="Y -> C (in Ref. 1; BAB39849)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="A -> V (in Ref. 4; CAE45864)"
FT /evidence="ECO:0000305"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:5DSE"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:5DSE"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:5DSE"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:5DSE"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 176..190
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 197..212
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 234..248
FT /evidence="ECO:0007829|PDB:5DSE"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 253..269
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 273..285
FT /evidence="ECO:0007829|PDB:5DSE"
SQ 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
