HYLS1_HUMAN
ID HYLS1_HUMAN Reviewed; 299 AA.
AC Q96M11; B3KXI8; Q96BX9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Centriolar and ciliogenesis-associated protein HYLS1 {ECO:0000305};
DE AltName: Full=Hydrolethalus syndrome protein 1;
GN Name=HYLS1 {ECO:0000312|HGNC:HGNC:26558}; Synonyms=HLS;
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 [LARGE SCALE MRNA], AND VARIANT ARG-31.
RC TISSUE=Testis, and Thalamus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-31.
RC TISSUE=Uterus;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [6]
RP VARIANT HLS1 GLY-211, CHARACTERIZATION OF VARIANT HLS1 GLY-211, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15843405; DOI=10.1093/hmg/ddi157;
RA Mee L., Honkala H., Kopra O., Vesa J., Finnilae S., Visapaeae I.,
RA Sang T.-K., Jackson G.R., Salonen R., Kestilae M., Peltonen L.;
RT "Hydrolethalus syndrome is caused by a missense mutation in a novel gene
RT HYLS1.";
RL Hum. Mol. Genet. 14:1475-1488(2005).
RN [7]
RP POSSIBLE INVOLVEMENT IN JOUBERT SYNDROME.
RX PubMed=26830932; DOI=10.1111/cge.12752;
RA Oka M., Shimojima K., Yamamoto T., Hanaoka Y., Sato S., Yasuhara T.,
RA Yoshinaga H., Kobayashi K.;
RT "A novel HYLS1 homozygous mutation in living siblings with Joubert
RT syndrome.";
RL Clin. Genet. 89:739-743(2016).
CC -!- FUNCTION: Plays a role in ciliogenesis.
CC {ECO:0000250|UniProtKB:A0A1L8ER70, ECO:0000250|UniProtKB:Q95X94}.
CC -!- INTERACTION:
CC Q96M11; Q08379: GOLGA2; NbExp=3; IntAct=EBI-720016, EBI-618309;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15843405}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:A0A1L8ER70,
CC ECO:0000250|UniProtKB:Q95X94}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:A0A1L8ER70, ECO:0000250|UniProtKB:Q95X94}.
CC -!- DISEASE: Hydrolethalus syndrome 1 (HLS1) [MIM:236680]: A lethal
CC syndrome characterized by polydactyly, central nervous system
CC malformation, and hydrocephalus. The polydactyly is postaxial in the
CC hands and preaxial in the feet. A highly characteristic hallux duplex
CC is seen in almost no other situation. In half of the cases, a large
CC atrioventricular communis defect of the heart is found. The pregnancy
CC is characterized by hydramnios, which is often massive, and by preterm
CC delivery. {ECO:0000269|PubMed:15843405}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Note=Defects in HYLS1 may be involved in ciliopathies other
CC than hydrolethalus syndrome 1. A homozygous mutation resulting in a C-
CC terminal extension of 11 residues has been found in patients diagnosed
CC as Joubert syndrome, a ciliopathy presenting with cerebellar ataxia,
CC oculomotor apraxia, hypotonia, neonatal breathing abnormalities and
CC psychomotor delay. Neuroradiologically, it is characterized by
CC cerebellar vermian hypoplasia/aplasia, thickened and reoriented
CC superior cerebellar peduncles, and an abnormally large interpeduncular
CC fossa, giving the appearance of a molar tooth on transaxial slices
CC (molar tooth sign). Additional variable features include retinal
CC dystrophy and renal disease. {ECO:0000269|PubMed:26830932}.
CC -!- SIMILARITY: Belongs to the HYLS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15047.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK057477; BAB71503.1; -; mRNA.
DR EMBL; AK127394; BAG54500.1; -; mRNA.
DR EMBL; AP000842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015047; AAH15047.1; ALT_INIT; mRNA.
DR CCDS; CCDS8467.1; -.
DR RefSeq; NP_001128265.1; NM_001134793.1.
DR RefSeq; NP_659451.1; NM_145014.2.
DR RefSeq; XP_005271487.1; XM_005271430.2.
DR RefSeq; XP_006718840.1; XM_006718777.3.
DR RefSeq; XP_011540961.1; XM_011542659.2.
DR RefSeq; XP_016872809.1; XM_017017320.1.
DR RefSeq; XP_016872810.1; XM_017017321.1.
DR AlphaFoldDB; Q96M11; -.
DR BioGRID; 128581; 7.
DR IntAct; Q96M11; 6.
DR MINT; Q96M11; -.
DR STRING; 9606.ENSP00000414884; -.
DR iPTMnet; Q96M11; -.
DR PhosphoSitePlus; Q96M11; -.
DR BioMuta; HYLS1; -.
DR DMDM; 74732277; -.
DR EPD; Q96M11; -.
DR jPOST; Q96M11; -.
DR MassIVE; Q96M11; -.
DR MaxQB; Q96M11; -.
DR PaxDb; Q96M11; -.
DR PeptideAtlas; Q96M11; -.
DR PRIDE; Q96M11; -.
DR ProteomicsDB; 77278; -.
DR Antibodypedia; 32968; 73 antibodies from 19 providers.
DR DNASU; 219844; -.
DR Ensembl; ENST00000356438.7; ENSP00000348815.3; ENSG00000198331.11.
DR Ensembl; ENST00000425380.7; ENSP00000414884.2; ENSG00000198331.11.
DR Ensembl; ENST00000526028.1; ENSP00000436833.1; ENSG00000198331.11.
DR GeneID; 219844; -.
DR KEGG; hsa:219844; -.
DR MANE-Select; ENST00000425380.7; ENSP00000414884.2; NM_001134793.2; NP_001128265.1.
DR UCSC; uc001qcx.5; human.
DR CTD; 219844; -.
DR DisGeNET; 219844; -.
DR GeneCards; HYLS1; -.
DR HGNC; HGNC:26558; HYLS1.
DR HPA; ENSG00000198331; Tissue enhanced (testis).
DR MalaCards; HYLS1; -.
DR MIM; 236680; phenotype.
DR MIM; 610693; gene.
DR neXtProt; NX_Q96M11; -.
DR OpenTargets; ENSG00000198331; -.
DR Orphanet; 2189; Hydrolethalus.
DR Orphanet; 475; Joubert syndrome.
DR PharmGKB; PA142671669; -.
DR VEuPathDB; HostDB:ENSG00000198331; -.
DR eggNOG; ENOG502QVD7; Eukaryota.
DR GeneTree; ENSGT00390000008848; -.
DR HOGENOM; CLU_079788_0_0_1; -.
DR InParanoid; Q96M11; -.
DR OMA; QKWANMD; -.
DR PhylomeDB; Q96M11; -.
DR TreeFam; TF336132; -.
DR PathwayCommons; Q96M11; -.
DR SignaLink; Q96M11; -.
DR BioGRID-ORCS; 219844; 28 hits in 1082 CRISPR screens.
DR ChiTaRS; HYLS1; human.
DR GeneWiki; HYLS1; -.
DR GenomeRNAi; 219844; -.
DR Pharos; Q96M11; Tbio.
DR PRO; PR:Q96M11; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96M11; protein.
DR Bgee; ENSG00000198331; Expressed in oocyte and 137 other tissues.
DR ExpressionAtlas; Q96M11; baseline and differential.
DR Genevisible; Q96M11; HS.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0097730; C:non-motile cilium; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR InterPro; IPR026227; HYLS1.
DR InterPro; IPR027918; HYLS1_C_dom.
DR Pfam; PF15311; HYLS1_C; 1.
DR PRINTS; PR02098; HYLETHALUSS1.
PE 1: Evidence at protein level;
KW Cell projection; Ciliopathy; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Disease variant; Phosphoprotein; Reference proteome.
FT CHAIN 1..299
FT /note="Centriolar and ciliogenesis-associated protein
FT HYLS1"
FT /id="PRO_0000284925"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 31
FT /note="C -> R (in dbSNP:rs667782)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_031866"
FT VARIANT 211
FT /note="D -> G (in HLS1; altered subcellular localization,
FT becomes localized to nuclear structures;
FT dbSNP:rs104894232)"
FT /evidence="ECO:0000269|PubMed:15843405"
FT /id="VAR_031867"
SQ SEQUENCE 299 AA; 34359 MW; D1EAF5F7D638802D CRC64;
MEELLPDGQI WANMDPEERM LAAATAFTHI CAGQGEGDVR REAQSIQYDP YSKASVAPGK
RPALPVQLQY PHVESNVPSE TVSEASQRLR KPVMKRKVLR RKPDGEVLVT DESIISESES
GTENDQDLWD LRQRLMNVQF QEDKESSFDV SQKFNLPHEY QGISQDQLIC SLQREGMGSP
AYEQDLIVAS RPKSFILPKL DQLSRNRGKT DRVARYFEYK RDWDSIRLPG EDHRKELRWG
VREQMLCRAE PQSKPQHIYV PNNYLVPTEK KRSALRWGVR CDLANGVIPR KLPFPLSPS
