GENTAUR Molecular Products.

 FA20C_HUMAN             Reviewed;         584 AA.
 Q8IXL6; A4D2Q5; L8B5W8; Q5I0W9; Q7Z4I0; Q9NPT2;
 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
 05-APR-2011, sequence version 2.
 18-JUL-2018, entry version 128.
 RecName: Full=Extracellular serine/threonine protein kinase FAM20C {ECO:0000305};
          EC=2.7.11.1 {ECO:0000269|PubMed:22582013, ECO:0000269|PubMed:23754375, ECO:0000269|PubMed:25789606};
 AltName: Full=Dentin matrix protein 4 {ECO:0000250|UniProtKB:Q5MJS3};
          Short=DMP-4 {ECO:0000250|UniProtKB:Q5MJS3};
 AltName: Full=Golgi casein kinase {ECO:0000303|PubMed:22582013};
 AltName: Full=Golgi-enriched fraction casein kinase {ECO:0000303|PubMed:22582013};
          Short=GEF-CK {ECO:0000303|PubMed:22582013};
 Flags: Precursor;
 Name=FAM20C {ECO:0000312|HGNC:HGNC:22140};
 Synonyms=DMP4 {ECO:0000250|UniProtKB:Q5MJS3};
 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).
 TISSUE=Brain;
 Wu C., Ding P., Han W., Rui M., Wang Y., Song Q., Ma D.;
 Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
 [2]
 NUCLEOTIDE SEQUENCE [MRNA].
 Kitagawa H., Izumikawa T., Koike T.;
 "Molecular cloning and characterization of a novel xylosylkinase.";
 Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
 [3]
 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).
 [4]
 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).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
 TISSUE=Brain;
 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).
 [6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
 TISSUE=Brain;
 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).
 [7]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Mural R.J., Istrail S., Sutton 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.
 [8]
 PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBCELLULAR LOCATION,
 AUTOPHOSPHORYLATION, GLYCOSYLATION AT ASN-101; ASN-335 AND ASN-470,
 AND MUTAGENESIS OF 93-LEU--ASP-95; ASN-101; ASN-335; ASN-470 AND
 ASP-478.
 PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
 Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
 Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
 Pinna L.A., Pagliarini D.J., Dixon J.E.;
 "A single kinase generates the majority of the secreted
 phosphoproteome.";
 Cell 161:1619-1632(2015).
 [9]
 TISSUE SPECIFICITY.
 PubMed=15676076; DOI=10.1186/1471-2164-6-11;
 Nalbant D., Youn H., Nalbant S.I., Sharma S., Cobos E., Beale E.G.,
 Du Y., Williams S.C.;
 "FAM20: an evolutionarily conserved family of secreted proteins
 expressed in hematopoietic cells.";
 BMC Genomics 6:11-11(2005).
 [10]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-470.
 TISSUE=Liver;
 PubMed=19159218; DOI=10.1021/pr8008012;
 Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
 "Glycoproteomics analysis of human liver tissue by combination of
 multiple enzyme digestion and hydrazide chemistry.";
 J. Proteome Res. 8:651-661(2009).
 [11]
 FUNCTION, CATALYTIC ACTIVITY, MANGANESE-BINDING, MUTAGENESIS OF
 ASP-478, VARIANTS RNS ASN-258; ARG-280; SER-328; ARG-379; GLU-379;
 ARG-388; ASN-451 AND TRP-549, AND CHARACTERIZATION OF VARIANTS RNS
 SER-328 AND ASN-451.
 PubMed=22582013; DOI=10.1126/science.1217817;
 Tagliabracci V.S., Engel J.L., Wen J., Wiley S.E., Worby C.A.,
 Kinch L.N., Xiao J., Grishin N.V., Dixon J.E.;
 "Secreted kinase phosphorylates extracellular proteins that regulate
 biomineralization.";
 Science 336:1150-1153(2012).
 [12]
 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
 ACTIVE SITE, AND MUTAGENESIS OF LYS-271; LYS-285; GLU-306; GLU-311;
 ARG-408; ASP-458 AND ASP-458.
 PubMed=23754375; DOI=10.1073/pnas.1309211110;
 Xiao J., Tagliabracci V.S., Wen J., Kim S.A., Dixon J.E.;
 "Crystal structure of the Golgi casein kinase.";
 Proc. Natl. Acad. Sci. U.S.A. 110:10574-10579(2013).
 [13]
 FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH
 FAM20A, MUTAGENESIS OF GLU-306 AND ASP-478, VARIANTS RNS MET-268 AND
 SER-328, AND CHARACTERIZATION OF VARIANTS RNS MET-268 AND SER-328.
 PubMed=25789606; DOI=10.7554/eLife.06120;
 Cui J., Xiao J., Tagliabracci V.S., Wen J., Rahdar M., Dixon J.E.;
 "A secretory kinase complex regulates extracellular protein
 phosphorylation.";
 Elife 4:0-0(2015).
 [14]
 VARIANTS RNS ARG-379; GLU-379; ARG-388 AND TRP-549.
 PubMed=17924334; DOI=10.1086/522240;
 Simpson M.A., Hsu R., Keir L.S., Hao J., Sivapalan G., Ernst L.M.,
 Zackai E.H., Al-Gazali L.I., Hulskamp G., Kingston H.M.,
 Prescott T.E., Ion A., Patton M.A., Murday V., George A., Crosby A.H.;
 "Mutations in FAM20C are associated with lethal osteosclerotic bone
 dysplasia (Raine syndrome), highlighting a crucial molecule in bone
 development.";
 Am. J. Hum. Genet. 81:906-912(2007).
 -!- FUNCTION: Golgi serine/threonine protein kinase that
     phosphorylates secretory pathway proteins within Ser-x-Glu/pSer
     motifs and plays a key role in biomineralization of bones and
     teeth (PubMed:22582013, PubMed:23754375, PubMed:25789606).
     Constitutes the main protein kinase for extracellular proteins,
     generating the majority of the extracellular phosphoproteome
     (PubMed:26091039). Mainly phosphorylates proteins within the Ser-
     x-Glu/pSer motif, but also displays a broader substrate
     specificity (PubMed:26091039). Phosphorylates casein as well as a
     number of proteins involved in biomineralization such as AMELX,
     AMTN, ENAM and SPP1 (PubMed:22582013, PubMed:25789606). In
     addition to its role in biomineralization, also plays a role in
     lipid homeostasis, wound healing and cell migration and adhesion
     (PubMed:26091039). {ECO:0000269|PubMed:22582013,
     ECO:0000269|PubMed:23754375, ECO:0000269|PubMed:25789606,
     ECO:0000269|PubMed:26091039}.
 -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
     {ECO:0000269|PubMed:22582013, ECO:0000269|PubMed:23754375,
     ECO:0000269|PubMed:25789606}.
 -!- COFACTOR:
     Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
       Evidence={ECO:0000269|PubMed:23754375,
       ECO:0000305|PubMed:22582013};
 -!- ENZYME REGULATION: Serine/threonine protein kinase activity is
     increased upon interaction with FAM20A.
     {ECO:0000269|PubMed:25789606}.
 -!- BIOPHYSICOCHEMICAL PROPERTIES:
     Kinetic parameters:
       KM=0.8 uM for manganese/ATP {ECO:0000269|PubMed:23754375};
 -!- SUBUNIT: Interacts with FAM20A; probably forming a heterotetramer
     of 2 subunits of FAM20A and 2 subunits of FAM20C.
     {ECO:0000269|PubMed:25789606}.
 -!- INTERACTION:
     Q9NP70:AMBN; NbExp=2; IntAct=EBI-7147442, EBI-11893530;
     Q6UX39:AMTN; NbExp=2; IntAct=EBI-7147442, EBI-11892684;
     O14791:APOL1; NbExp=2; IntAct=EBI-7147442, EBI-1221934;
     P05060:CHGB; NbExp=2; IntAct=EBI-7147442, EBI-712619;
     P02666:CSN2 (xeno); NbExp=3; IntAct=EBI-7147442, EBI-5260183;
     Q9NRM1:ENAM; NbExp=2; IntAct=EBI-7147442, EBI-11892601;
     Q96MK3:FAM20A; NbExp=3; IntAct=EBI-7147442, EBI-11892970;
     P02671:FGA; NbExp=2; IntAct=EBI-7147442, EBI-348571;
     P08833:IGFBP1; NbExp=2; IntAct=EBI-7147442, EBI-13646303;
     P02810:PRH2; NbExp=2; IntAct=EBI-7147442, EBI-738601;
     P01008:SERPINC1; NbExp=2; IntAct=EBI-7147442, EBI-1039832;
     P10451:SPP1; NbExp=3; IntAct=EBI-7147442, EBI-723648;
 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26091039}.
     Golgi apparatus {ECO:0000250|UniProtKB:Q5MJS3}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=2;
     Name=1;
       IsoId=Q8IXL6-1; Sequence=Displayed;
     Name=2;
       IsoId=Q8IXL6-2; Sequence=VSP_040834;
       Note=No experimental confirmation available.;
 -!- TISSUE SPECIFICITY: Widely expressed.
     {ECO:0000269|PubMed:15676076}.
 -!- PTM: N-glycosylation is required for folding.
     {ECO:0000305|PubMed:26091039}.
 -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:26091039}.
 -!- DISEASE: Raine syndrome (RNS) [MIM:259775]: Autosomal recessive
     osteosclerotic bone dysplasia with neonatal lethal outcome.
     Clinical features include generalized osteosclerosis, craniofacial
     dysplasia and microcephaly. {ECO:0000269|PubMed:17924334,
     ECO:0000269|PubMed:22582013, ECO:0000269|PubMed:25789606}.
     Note=The disease is caused by mutations affecting the gene
     represented in this entry.
 -!- SIMILARITY: Belongs to the FAM20 family. {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=AAH40074.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
     Sequence=EAL23705.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
 -----------------------------------------------------------------------
 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
 Distributed under the Creative Commons Attribution (CC BY 4.0) License
 -----------------------------------------------------------------------
 EMBL; AF533706; AAQ09019.1; -; mRNA.
 EMBL; AB545605; BAM78534.1; -; mRNA.
 EMBL; AC093627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AC145676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AC187652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; CH236966; EAL23705.1; ALT_INIT; Genomic_DNA.
 EMBL; CH471144; EAW87149.1; -; Genomic_DNA.
 EMBL; BC040074; AAH40074.1; ALT_INIT; mRNA.
 EMBL; BC087853; AAH87853.1; -; mRNA.
 EMBL; AL390147; CAB99089.2; -; mRNA.
 CCDS; CCDS47522.1; -. [Q8IXL6-1]
 PIR; T51872; T51872.
 RefSeq; NP_064608.2; NM_020223.3. [Q8IXL6-1]
 UniGene; Hs.134742; -.
 UniGene; Hs.733582; -.
 PDB; 5YH3; X-ray; 3.30 A; C/D=141-578.
 PDBsum; 5YH3; -.
 ProteinModelPortal; Q8IXL6; -.
 SMR; Q8IXL6; -.
 BioGrid; 121294; 8.
 IntAct; Q8IXL6; 71.
 MINT; Q8IXL6; -.
 STRING; 9606.ENSP00000322323; -.
 iPTMnet; Q8IXL6; -.
 PhosphoSitePlus; Q8IXL6; -.
 BioMuta; FAM20C; -.
 DMDM; 327478506; -.
 EPD; Q8IXL6; -.
 MaxQB; Q8IXL6; -.
 PaxDb; Q8IXL6; -.
 PeptideAtlas; Q8IXL6; -.
 PRIDE; Q8IXL6; -.
 ProteomicsDB; 71022; -.
 ProteomicsDB; 71023; -. [Q8IXL6-2]
 Ensembl; ENST00000313766; ENSP00000322323; ENSG00000177706. [Q8IXL6-1]
 GeneID; 56975; -.
 KEGG; hsa:56975; -.
 UCSC; uc003sip.4; human. [Q8IXL6-1]
 CTD; 56975; -.
 DisGeNET; 56975; -.
 EuPathDB; HostDB:ENSG00000177706.8; -.
 GeneCards; FAM20C; -.
 H-InvDB; HIX0019573; -.
 HGNC; HGNC:22140; FAM20C.
 HPA; HPA019823; -.
 MalaCards; FAM20C; -.
 MIM; 259775; phenotype.
 MIM; 611061; gene.
 neXtProt; NX_Q8IXL6; -.
 OpenTargets; ENSG00000177706; -.
 Orphanet; 1832; Lethal osteosclerotic bone dysplasia.
 PharmGKB; PA134898453; -.
 eggNOG; KOG3829; Eukaryota.
 eggNOG; ENOG410XQEJ; LUCA.
 GeneTree; ENSGT00390000007484; -.
 HOGENOM; HOG000231437; -.
 HOVERGEN; HBG051635; -.
 InParanoid; Q8IXL6; -.
 KO; K21958; -.
 OMA; LPLRQCC; -.
 OrthoDB; EOG091G1BEO; -.
 PhylomeDB; Q8IXL6; -.
 TreeFam; TF313276; -.
 Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
 Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
 ChiTaRS; FAM20C; human.
 GeneWiki; FAM20C; -.
 GenomeRNAi; 56975; -.
 PRO; PR:Q8IXL6; -.
 Proteomes; UP000005640; Chromosome 7.
 Bgee; ENSG00000177706; -.
 CleanEx; HS_FAM20C; -.
 Genevisible; Q8IXL6; HS.
 GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
 GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
 GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
 GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
 GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
 GO; GO:0031214; P:biomineral tissue development; IMP:UniProtKB.
 GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
 GO; GO:0097187; P:dentinogenesis; IEA:Ensembl.
 GO; GO:0070166; P:enamel mineralization; IEA:Ensembl.
 GO; GO:0071895; P:odontoblast differentiation; IEA:Ensembl.
 GO; GO:0036179; P:osteoclast maturation; IEA:Ensembl.
 GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
 GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
 GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
 GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
 GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
 GO; GO:0051174; P:regulation of phosphorus metabolic process; IEA:Ensembl.
 InterPro; IPR024869; FAM20.
 InterPro; IPR009581; FAM20_C.
 PANTHER; PTHR12450; PTHR12450; 1.
 Pfam; PF06702; Fam20C; 1.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; ATP-binding; Biomineralization;
 Calcium; Complete proteome; Direct protein sequencing;
 Disease mutation; Disulfide bond; Glycoprotein; Golgi apparatus;
 Kinase; Manganese; Metal-binding; Nucleotide-binding; Phosphoprotein;
 Reference proteome; Secreted; Serine/threonine-protein kinase; Signal;
 Transferase.
 SIGNAL        1     22       {ECO:0000255}.
 PROPEP       23     92       {ECO:0000269|PubMed:26091039}.
                              /FTId=PRO_0000433883.
 CHAIN        93    584       Extracellular serine/threonine protein
                              kinase FAM20C.
                              /FTId=PRO_0000008747.
 NP_BIND     389    392       ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
 REGION      354    565       Kinase domain.
                              {ECO:0000305|PubMed:22582013}.
 ACT_SITE    458    458       {ECO:0000269|PubMed:23754375}.
 METAL       306    306       Manganese.
                              {ECO:0000250|UniProtKB:Q9XTW2}.
 METAL       478    478       Manganese. {ECO:0000305|PubMed:22582013}.
 BINDING     269    269       ATP; via amide nitrogen.
                              {ECO:0000250|UniProtKB:Q9XTW2}.
 BINDING     285    285       ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
 BINDING     306    306       ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
 BINDING     463    463       ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
 BINDING     478    478       ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
 CARBOHYD    101    101       N-linked (GlcNAc...) asparagine.
                              {ECO:0000269|PubMed:26091039}.
 CARBOHYD    335    335       N-linked (GlcNAc...) asparagine.
                              {ECO:0000269|PubMed:26091039}.
 CARBOHYD    470    470       N-linked (GlcNAc...) asparagine.
                              {ECO:0000269|PubMed:19159218,
                              ECO:0000269|PubMed:26091039}.
 DISULFID    362    378       {ECO:0000250|UniProtKB:Q9XTW2}.
 DISULFID    367    371       {ECO:0000250|UniProtKB:Q9XTW2}.
 DISULFID    426    500       {ECO:0000250|UniProtKB:Q9XTW2}.
 DISULFID    501    560       {ECO:0000250|UniProtKB:Q9XTW2}.
 VAR_SEQ       1    332       Missing (in isoform 2).
                              {ECO:0000303|PubMed:17974005}.
                              /FTId=VSP_040834.
 VARIANT     258    258       I -> N (in RNS).
                              {ECO:0000269|PubMed:22582013}.
                              /FTId=VAR_073660.
 VARIANT     268    268       T -> M (in RNS; mild non-lethal form;
                              decreased protein kinase activity;
                              dbSNP:rs778899041).
                              {ECO:0000269|PubMed:25789606}.
                              /FTId=VAR_073661.
 VARIANT     280    280       G -> R (in RNS; dbSNP:rs779708323).
                              {ECO:0000269|PubMed:22582013}.
                              /FTId=VAR_073662.
 VARIANT     328    328       P -> S (in RNS; mild non-lethal form;
                              decreased protein kinase activity; FAM20A
                              is still able to increase remaining
                              protein kinase activity;
                              dbSNP:rs797044462).
                              {ECO:0000269|PubMed:22582013,
                              ECO:0000269|PubMed:25789606}.
                              /FTId=VAR_073663.
 VARIANT     379    379       G -> E (in RNS; dbSNP:rs796051852).
                              {ECO:0000269|PubMed:17924334,
                              ECO:0000269|PubMed:22582013}.
                              /FTId=VAR_037530.
 VARIANT     379    379       G -> R (in RNS).
                              {ECO:0000269|PubMed:17924334,
                              ECO:0000269|PubMed:22582013}.
                              /FTId=VAR_037531.
 VARIANT     388    388       L -> R (in RNS; dbSNP:rs796051849).
                              {ECO:0000269|PubMed:17924334,
                              ECO:0000269|PubMed:22582013}.
                              /FTId=VAR_037532.
 VARIANT     451    451       D -> N (in RNS; mild non-lethal form;
                              decreased protein kinase activity).
                              {ECO:0000269|PubMed:22582013}.
                              /FTId=VAR_073664.
 VARIANT     549    549       R -> W (in RNS; dbSNP:rs796051850).
                              {ECO:0000269|PubMed:17924334,
                              ECO:0000269|PubMed:22582013}.
                              /FTId=VAR_037533.
 MUTAGEN      91     93       LQD->AAA: Does not affect secretion or
                              activity. {ECO:0000269|PubMed:26091039}.
 MUTAGEN     101    101       N->A: Impaired secretion; when associated
                              with A-335 and A-470.
                              {ECO:0000269|PubMed:26091039}.
 MUTAGEN     271    271       K->A: Reduced kinase activity.
                              {ECO:0000269|PubMed:23754375}.
 MUTAGEN     285    285       K->A: Reduced kinase activity.
                              {ECO:0000269|PubMed:23754375}.
 MUTAGEN     306    306       E->A,Q: Strongly reduced kinase activity.
                              {ECO:0000269|PubMed:23754375,
                              ECO:0000269|PubMed:25789606}.
 MUTAGEN     311    311       E->A: Reduced kinase activity.
                              {ECO:0000269|PubMed:23754375}.
 MUTAGEN     335    335       N->A: Impaired secretion; when associated
                              with A-101 and A-470.
                              {ECO:0000269|PubMed:26091039}.
 MUTAGEN     408    408       R->A: Reduced kinase activity.
                              {ECO:0000269|PubMed:23754375}.
 MUTAGEN     458    458       D->A: Abrogates kinase activity.
                              {ECO:0000269|PubMed:23754375}.
 MUTAGEN     470    470       N->A: Impaired secretion; when associated
                              with A-101 and A-335.
                              {ECO:0000269|PubMed:26091039}.
 MUTAGEN     478    478       D->A: Unable to bind manganese; abrogates
                              kinase activity.
                              {ECO:0000269|PubMed:22582013,
                              ECO:0000269|PubMed:23754375,
                              ECO:0000269|PubMed:25789606,
                              ECO:0000269|PubMed:26091039}.
 CONFLICT    274    288       MTFQNYGQALFKPMK -> FLSDKPFLFLSCFLR (in
                              Ref. 6; CAB99089). {ECO:0000305}.
 CONFLICT    564    564       N -> D (in Ref. 5; AAH87853 and 6;
                              CAB99089). {ECO:0000305}.
 HELIX       160    164       {ECO:0000244|PDB:5YH3}.
 HELIX       168    170       {ECO:0000244|PDB:5YH3}.
 TURN        179    181       {ECO:0000244|PDB:5YH3}.
 STRAND      182    184       {ECO:0000244|PDB:5YH3}.
 HELIX       225    231       {ECO:0000244|PDB:5YH3}.
 STRAND      237    239       {ECO:0000244|PDB:5YH3}.
 HELIX       244    255       {ECO:0000244|PDB:5YH3}.
 STRAND      258    263       {ECO:0000244|PDB:5YH3}.
 STRAND      272    276       {ECO:0000244|PDB:5YH3}.
 STRAND      281    286       {ECO:0000244|PDB:5YH3}.
 HELIX       301    303       {ECO:0000244|PDB:5YH3}.
 HELIX       308    320       {ECO:0000244|PDB:5YH3}.
 STRAND      329    335       {ECO:0000244|PDB:5YH3}.
 TURN        336    340       {ECO:0000244|PDB:5YH3}.
 HELIX       341    343       {ECO:0000244|PDB:5YH3}.
 HELIX       347    350       {ECO:0000244|PDB:5YH3}.
 STRAND      361    363       {ECO:0000244|PDB:5YH3}.
 STRAND      368    370       {ECO:0000244|PDB:5YH3}.
 HELIX       373    375       {ECO:0000244|PDB:5YH3}.
 STRAND      380    390       {ECO:0000244|PDB:5YH3}.
 TURN        419    421       {ECO:0000244|PDB:5YH3}.
 TURN        423    425       {ECO:0000244|PDB:5YH3}.
 HELIX       426    429       {ECO:0000244|PDB:5YH3}.
 TURN        433    436       {ECO:0000244|PDB:5YH3}.
 HELIX       438    454       {ECO:0000244|PDB:5YH3}.
 STRAND      461    463       {ECO:0000244|PDB:5YH3}.
 TURN        467    470       {ECO:0000244|PDB:5YH3}.
 HELIX       491    494       {ECO:0000244|PDB:5YH3}.
 HELIX       495    500       {ECO:0000244|PDB:5YH3}.
 HELIX       505    513       {ECO:0000244|PDB:5YH3}.
 HELIX       517    519       {ECO:0000244|PDB:5YH3}.
 HELIX       521    528       {ECO:0000244|PDB:5YH3}.
 STRAND      530    534       {ECO:0000244|PDB:5YH3}.
 HELIX       540    564       {ECO:0000244|PDB:5YH3}.
 TURN        567    569       {ECO:0000244|PDB:5YH3}.
 SEQUENCE   584 AA;  66234 MW;  ECD278B5EA681FEF CRC64;
 MKMMLVRRFR VLILMVFLVA CALHIALDLL PRLERRGARP SGEPGCSCAQ PAAEVAAPGW
 AQVRGRPGEP PAASSAAGDA GWPNKHTLRI LQDFSSDPSS NLSSHSLEKL PPAAEPAERA
 LRGRDPGALR PHDPAHRPLL RDPGPRRSES PPGPGGDASL LARLFEHPLY RVAVPPLTEE
 DVLFNVNSDT RLSPKAAENP DWPHAGAEGA EFLSPGEAAV DSYPNWLKFH IGINRYELYS
 RHNPAIEALL HDLSSQRITS VAMKSGGTQL KLIMTFQNYG QALFKPMKQT REQETPPDFF
 YFSDYERHNA EIAAFHLDRI LDFRRVPPVA GRMVNMTKEI RDVTRDKKLW RTFFISPANN
 ICFYGECSYY CSTEHALCGK PDQIEGSLAA FLPDLSLAKR KTWRNPWRRS YHKRKKAEWE
 VDPDYCEEVK QTPPYDSSHR ILDVMDMTIF DFLMGNMDRH HYETFEKFGN ETFIIHLDNG
 RGFGKYSHDE LSILVPLQQC CRIRKSTYLR LQLLAKEEYK LSLLMAESLR GDQVAPVLYQ
 PHLEALDRRL RVVLKAVRDC VERNGLHSVV DDDLDTEHRA ASAR

Related products :