FA20A_HUMAN
ID FA20A_HUMAN Reviewed; 541 AA.
AC Q96MK3; B2RN47; B2RN49; Q9UF95;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 4.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Pseudokinase FAM20A {ECO:0000305};
DE Flags: Precursor;
GN Name=FAM20A {ECO:0000312|HGNC:HGNC:23015};
GN ORFNames=UNQ9388/PRO34279 {ECO:0000303|PubMed:12975309};
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 VARIANTS LYS-332 AND SER-530.
RC TISSUE=Placenta;
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 MRNA], AND VARIANTS LYS-332 AND SER-530.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-332 AND SER-530.
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-541, AND VARIANT SER-530.
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=15676076; DOI=10.1186/1471-2164-6-11;
RA Nalbant D., Youn H., Nalbant S.I., Sharma S., Cobos E., Beale E.G., Du Y.,
RA Williams S.C.;
RT "FAM20: an evolutionarily conserved family of secreted proteins expressed
RT in hematopoietic cells.";
RL BMC Genomics 6:11-11(2005).
RN [7]
RP INVOLVEMENT IN AI1G.
RX PubMed=21549343; DOI=10.1016/j.ajhg.2011.04.005;
RA O'Sullivan J., Bitu C.C., Daly S.B., Urquhart J.E., Barron M.J.,
RA Bhaskar S.S., Martelli-Junior H., dos Santos Neto P.E., Mansilla M.A.,
RA Murray J.C., Coletta R.D., Black G.C., Dixon M.J.;
RT "Whole-exome sequencing identifies FAM20A mutations as a cause of
RT amelogenesis imperfecta and gingival hyperplasia syndrome.";
RL Am. J. Hum. Genet. 88:616-620(2011).
RN [8]
RP INVOLVEMENT IN AI1G.
RX PubMed=23697977; DOI=10.1038/jhg.2013.44;
RA Cabral R.M., Kurban M., Rothman L., Wajid M., Shimomura Y., Petukhova L.,
RA Christiano A.M.;
RT "Autosomal recessive gingival hyperplasia and dental anomalies caused by a
RT 29-base pair duplication in the FAM20A gene.";
RL J. Hum. Genet. 58:566-567(2013).
RN [9]
RP INVOLVEMENT IN AI1G.
RX PubMed=24259279; DOI=10.1002/ajmg.a.36187;
RA Kantaputra P.N., Kaewgahya M., Khemaleelakul U., Dejkhamron P.,
RA Sutthimethakorn S., Thongboonkerd V., Iamaroon A.;
RT "Enamel-renal-gingival syndrome and FAM20A mutations.";
RL Am. J. Med. Genet. A 164A:1-9(2014).
RN [10]
RP INVOLVEMENT IN AI1G.
RX PubMed=24756937; DOI=10.1002/ajmg.a.36579;
RA Kantaputra P.N., Bongkochwilawan C., Kaewgahya M., Ohazama A.,
RA Kayserili H., Erdem A.P., Aktoren O., Guven Y.;
RT "Enamel-Renal-Gingival syndrome, hypodontia, and a novel FAM20A mutation.";
RL Am. J. Med. Genet. A 164A:2124-2128(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP INVOLVEMENT IN AI1G.
RX PubMed=25827751; DOI=10.1016/j.archoralbio.2015.02.018;
RA Volodarsky M., Zilberman U., Birk O.S.;
RT "Novel FAM20A mutation causes autosomal recessive amelogenesis
RT imperfecta.";
RL Arch. Oral Biol. 60:919-922(2015).
RN [13]
RP INVOLVEMENT IN AI1G.
RX PubMed=25636655; DOI=10.1186/1472-6831-15-14;
RA Cherkaoui Jaouad I., El Alloussi M., Chafai El Alaoui S., Laarabi F.Z.,
RA Lyahyai J., Sefiani A.;
RT "Further evidence for causal FAM20A mutations and first case of
RT amelogenesis imperfecta and gingival hyperplasia syndrome in Morocco: a
RT case report.";
RL BMC Oral Health 15:14-14(2015).
RN [14]
RP FUNCTION, INTERACTION WITH FAM20C, MUTAGENESIS OF GLN-258, AND
RP CHARACTERIZATION OF VARIANTS AI1G ARG-173; ASP-331 AND ASN-403.
RX PubMed=25789606; DOI=10.7554/elife.06120;
RA Cui J., Xiao J., Tagliabracci V.S., Wen J., Rahdar M., Dixon J.E.;
RT "A secretory kinase complex regulates extracellular protein
RT phosphorylation.";
RL Elife 4:0-0(2015).
RN [15]
RP VARIANT AI1G 197-ASP--ILE-214 DELINS VAL-197.
RX PubMed=21990045; DOI=10.1002/humu.21621;
RA Cho S.H., Seymen F., Lee K.E., Lee S.K., Kweon Y.S., Kim K.J., Jung S.E.,
RA Song S.J., Yildirim M., Bayram M., Tuna E.B., Gencay K., Kim J.W.;
RT "Novel FAM20A mutations in hypoplastic amelogenesis imperfecta.";
RL Hum. Mutat. 33:91-94(2012).
RN [16]
RP VARIANT AI1G ARG-173.
RX PubMed=23434854; DOI=10.1159/000349989;
RA Jaureguiberry G., De la Dure-Molla M., Parry D., Quentric M., Himmerkus N.,
RA Koike T., Poulter J., Klootwijk E., Robinette S.L., Howie A.J., Patel V.,
RA Figueres M.L., Stanescu H.C., Issler N., Nicholson J.K., Bockenhauer D.,
RA Laing C., Walsh S.B., McCredie D.A., Povey S., Asselin A., Picard A.,
RA Coulomb A., Medlar A.J., Bailleul-Forestier I., Verloes A., Le Caignec C.,
RA Roussey G., Guiol J., Isidor B., Logan C., Shore R., Johnson C.,
RA Inglehearn C., Al-Bahlani S., Schmittbuhl M., Clauss F., Huckert M.,
RA Laugel V., Ginglinger E., Pajarola S., Sparta G., Bartholdi D., Rauch A.,
RA Addor M.C., Yamaguti P.M., Safatle H.P., Acevedo A.C., Martelli-Junior H.,
RA dos Santos Netos P.E., Coletta R.D., Gruessel S., Sandmann C., Ruehmann D.,
RA Langman C.B., Scheinman S.J., Ozdemir-Ozenen D., Hart T.C., Hart P.S.,
RA Neugebauer U., Schlatter E., Houillier P., Gahl W.A., Vikkula M.,
RA Bloch-Zupan A., Bleich M., Kitagawa H., Unwin R.J., Mighell A., Berdal A.,
RA Kleta R.;
RT "Nephrocalcinosis (enamel renal syndrome) caused by autosomal recessive
RT FAM20A mutations.";
RL Nephron Physiol. 122:1-6(2012).
RN [17]
RP VARIANT AI1G ASP-331, AND SUBCELLULAR LOCATION.
RX PubMed=23468644; DOI=10.1371/journal.pgen.1003302;
RA Wang S.K., Aref P., Hu Y., Milkovich R.N., Simmer J.P., El-Khateeb M.,
RA Daggag H., Baqain Z.H., Hu J.C.;
RT "FAM20A mutations can cause enamel-renal syndrome (ERS).";
RL PLoS Genet. 9:E1003302-E1003302(2013).
RN [18]
RP VARIANT AI1G ASN-403.
RX PubMed=24196488; DOI=10.1177/0022034513512653;
RA Wang S.K., Reid B.M., Dugan S.L., Roggenbuck J.A., Read L., Aref P.,
RA Taheri A.P., Yeganeh M.Z., Simmer J.P., Hu J.C.;
RT "FAM20A mutations associated with enamel renal syndrome.";
RL J. Dent. Res. 93:42-48(2014).
CC -!- FUNCTION: Pseudokinase that acts as an allosteric activator of the
CC Golgi serine/threonine protein kinase FAM20C and is involved in
CC biomineralization of teeth. Forms a complex with FAM20C and increases
CC the ability of FAM20C to phosphorylate the proteins that form the
CC 'matrix' that guides the deposition of the enamel minerals.
CC {ECO:0000269|PubMed:25789606}.
CC -!- SUBUNIT: Interacts with FAM20C; probably forming a heterotetramer of 2
CC subunits of FAM20A and 2 subunits of FAM20C.
CC {ECO:0000269|PubMed:25789606}.
CC -!- INTERACTION:
CC Q96MK3; Q8IXL6: FAM20C; NbExp=3; IntAct=EBI-11892970, EBI-7147442;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8CID3}. Golgi
CC apparatus {ECO:0000269|PubMed:23468644}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8CID3}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung and liver. Intermediate
CC levels in thymus and ovary. {ECO:0000269|PubMed:15676076}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8CID3}.
CC -!- DISEASE: Amelogenesis imperfecta 1G (AI1G) [MIM:204690]: A disorder
CC characterized by dental anomalies, gingival overgrowth, and
CC nephrocalcinosis. Dental anomalies include hypoplastic amelogenesis
CC imperfecta, intrapulpal calcifications, delay of tooth eruption,
CC hypodontia/oligodontia, pericoronal radiolucencies and unerupted teeth.
CC {ECO:0000269|PubMed:21549343, ECO:0000269|PubMed:21990045,
CC ECO:0000269|PubMed:23434854, ECO:0000269|PubMed:23468644,
CC ECO:0000269|PubMed:23697977, ECO:0000269|PubMed:24196488,
CC ECO:0000269|PubMed:24259279, ECO:0000269|PubMed:24756937,
CC ECO:0000269|PubMed:25636655, ECO:0000269|PubMed:25789606,
CC ECO:0000269|PubMed:25827751}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the FAM20 family. {ECO:0000305}.
CC -!- CAUTION: Although strongly related to other members of the family,
CC lacks the kinase activity. A conserved Asp/Glu residue present in other
CC members of the family, which coordinates the Mn(2+) ion and the ion-
CC pair Lys and is indispensable for kinase activity, is replaced by a Gln
CC in position 258. {ECO:0000269|PubMed:25789606}.
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DR EMBL; AK056789; BAB71285.1; -; mRNA.
DR EMBL; AY358197; AAQ88564.1; -; mRNA.
DR EMBL; AC079210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136686; AAI36687.1; -; mRNA.
DR EMBL; BC136689; AAI36690.1; -; mRNA.
DR EMBL; AL133105; CAB61412.1; -; mRNA.
DR CCDS; CCDS11679.1; -.
DR PIR; T42684; T42684.
DR RefSeq; NP_001230675.1; NM_001243746.1.
DR RefSeq; NP_060035.2; NM_017565.3.
DR PDB; 5WRR; X-ray; 2.51 A; A/B=89-526.
DR PDB; 5WRS; X-ray; 2.75 A; A/B=89-526.
DR PDB; 5YH2; X-ray; 3.55 A; A/B=63-529.
DR PDB; 5YH3; X-ray; 3.30 A; A/B=63-529.
DR PDBsum; 5WRR; -.
DR PDBsum; 5WRS; -.
DR PDBsum; 5YH2; -.
DR PDBsum; 5YH3; -.
DR AlphaFoldDB; Q96MK3; -.
DR SMR; Q96MK3; -.
DR IntAct; Q96MK3; 5.
DR STRING; 9606.ENSP00000468308; -.
DR GlyGen; Q96MK3; 7 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q96MK3; -.
DR PhosphoSitePlus; Q96MK3; -.
DR BioMuta; FAM20A; -.
DR DMDM; 269849750; -.
DR jPOST; Q96MK3; -.
DR MassIVE; Q96MK3; -.
DR PaxDb; Q96MK3; -.
DR PeptideAtlas; Q96MK3; -.
DR PRIDE; Q96MK3; -.
DR ProteomicsDB; 77370; -.
DR Antibodypedia; 31793; 120 antibodies from 23 providers.
DR DNASU; 54757; -.
DR Ensembl; ENST00000592554.2; ENSP00000468308.1; ENSG00000108950.12.
DR GeneID; 54757; -.
DR KEGG; hsa:54757; -.
DR MANE-Select; ENST00000592554.2; ENSP00000468308.1; NM_017565.4; NP_060035.2.
DR UCSC; uc002jho.4; human.
DR CTD; 54757; -.
DR DisGeNET; 54757; -.
DR GeneCards; FAM20A; -.
DR HGNC; HGNC:23015; FAM20A.
DR HPA; ENSG00000108950; Tissue enhanced (liver).
DR MalaCards; FAM20A; -.
DR MIM; 204690; phenotype.
DR MIM; 611062; gene.
DR neXtProt; NX_Q96MK3; -.
DR OpenTargets; ENSG00000108950; -.
DR Orphanet; 1031; Enamel-renal syndrome.
DR PharmGKB; PA134888583; -.
DR VEuPathDB; HostDB:ENSG00000108950; -.
DR eggNOG; KOG3829; Eukaryota.
DR GeneTree; ENSGT00950000182951; -.
DR HOGENOM; CLU_028926_2_0_1; -.
DR InParanoid; Q96MK3; -.
DR OMA; HDMRHLP; -.
DR OrthoDB; 484324at2759; -.
DR PhylomeDB; Q96MK3; -.
DR PathwayCommons; Q96MK3; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q96MK3; -.
DR BioGRID-ORCS; 54757; 21 hits in 1068 CRISPR screens.
DR ChiTaRS; FAM20A; human.
DR GeneWiki; FAM20A; -.
DR GenomeRNAi; 54757; -.
DR Pharos; Q96MK3; Tbio.
DR PRO; PR:Q96MK3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96MK3; protein.
DR Bgee; ENSG00000108950; Expressed in right lobe of liver and 126 other tissues.
DR ExpressionAtlas; Q96MK3; baseline and differential.
DR Genevisible; Q96MK3; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
DR GO; GO:0031214; P:biomineral tissue development; IMP:UniProtKB.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0070166; P:enamel mineralization; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0044691; P:tooth eruption; IMP:UniProtKB.
DR InterPro; IPR024869; FAM20.
DR InterPro; IPR009581; FAM20_C.
DR PANTHER; PTHR12450; PTHR12450; 1.
DR Pfam; PF06702; Fam20C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amelogenesis imperfecta; Biomineralization; Disease variant;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..541
FT /note="Pseudokinase FAM20A"
FT /id="PRO_0000008743"
FT REGION 38..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 314..330
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 319..323
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 378..452
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 453..512
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT VARIANT 173
FT /note="L -> R (in AI1G; impaired folding of the protein;
FT abolishes ability to activate FAM20C protein kinase
FT activity)"
FT /evidence="ECO:0000269|PubMed:23434854,
FT ECO:0000269|PubMed:25789606"
FT /id="VAR_072170"
FT VARIANT 197..214
FT /note="DYSQDEKALLGACDCTQI -> V (in AI1G)"
FT /evidence="ECO:0000269|PubMed:21990045"
FT /id="VAR_066859"
FT VARIANT 331
FT /note="G -> D (in AI1G; impaired folding of the protein;
FT abolishes ability to activate FAM20C protein kinase
FT activity; dbSNP:rs981673034)"
FT /evidence="ECO:0000269|PubMed:23468644,
FT ECO:0000269|PubMed:25789606"
FT /id="VAR_072171"
FT VARIANT 332
FT /note="N -> K (in dbSNP:rs2302234)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_059282"
FT VARIANT 403
FT /note="D -> N (in AI1G; impaired folding of the protein;
FT abolishes ability to activate FAM20C protein kinase
FT activity; dbSNP:rs377432171)"
FT /evidence="ECO:0000269|PubMed:24196488,
FT ECO:0000269|PubMed:25789606"
FT /id="VAR_072172"
FT VARIANT 530
FT /note="L -> S (in dbSNP:rs2907373)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_059283"
FT MUTAGEN 258
FT /note="Q->E: Able to hydrolyze ATP and display some protein
FT kinase activity."
FT /evidence="ECO:0000269|PubMed:25789606"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:5WRR"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 119..143
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:5WRR"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5YH3"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 259..272
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:5WRR"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 299..303
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 332..342
FT /evidence="ECO:0007829|PDB:5WRR"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:5YH3"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:5WRR"
FT TURN 385..388
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 390..406
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:5WRR"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 447..452
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 457..466
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 473..481
FT /evidence="ECO:0007829|PDB:5WRR"
FT TURN 485..488
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 492..516
FT /evidence="ECO:0007829|PDB:5WRR"
FT HELIX 518..521
FT /evidence="ECO:0007829|PDB:5WRR"
SQ SEQUENCE 541 AA; 61417 MW; B44A4655996279A1 CRC64;
MPGLRRDRLL TLLLLGALLS ADLYFHLWPQ VQRQLRPRER PRGCPCTGRA SSLARDSAAA
ASDPGTIVHN FSRTEPRTEP AGGSHSGSSS KLQALFAHPL YNVPEEPPLL GAEDSLLASQ
EALRYYRRKV ARWNRRHKMY REQMNLTSLD PPLQLRLEAS WVQFHLGINR HGLYSRSSPV
VSKLLQDMRH FPTISADYSQ DEKALLGACD CTQIVKPSGV HLKLVLRFSD FGKAMFKPMR
QQRDEETPVD FFYFIDFQRH NAEIAAFHLD RILDFRRVPP TVGRIVNVTK EILEVTKNEI
LQSVFFVSPA SNVCFFAKCP YMCKTEYAVC GNPHLLEGSL SAFLPSLNLA PRLSVPNPWI
RSYTLAGKEE WEVNPLYCDT VKQIYPYNNS QRLLNVIDMA IFDFLIGNMD RHHYEMFTKF
GDDGFLIHLD NARGFGRHSH DEISILSPLS QCCMIKKKTL LHLQLLAQAD YRLSDVMRES
LLEDQLSPVL TEPHLLALDR RLQTILRTVE GCIVAHGQQS VIVDGPVEQL APDSGQANLT
S
