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Pseudokinase FAM20A

 FA20A_HUMAN             Reviewed;         541 AA.
Q96MK3; B2RN47; B2RN49; Q9UF95;
19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 4.
25-OCT-2017, entry version 122.
RecName: Full=Pseudokinase FAM20A {ECO:0000305};
Flags: Precursor;
Name=FAM20A {ECO:0000312|HGNC:HGNC:23015};
ORFNames=UNQ9388/PRO34279 {ECO:0000303|PubMed:12975309};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-332 AND
SER-530.
TISSUE=Placenta;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-332 AND
SER-530.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-332 AND
SER-530.
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-541, AND VARIANT
SER-530.
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).
[6]
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).
[7]
INVOLVEMENT IN AI1G.
PubMed=21549343; DOI=10.1016/j.ajhg.2011.04.005;
O'Sullivan J., Bitu C.C., Daly S.B., Urquhart J.E., Barron M.J.,
Bhaskar S.S., Martelli-Junior H., dos Santos Neto P.E., Mansilla M.A.,
Murray J.C., Coletta R.D., Black G.C., Dixon M.J.;
"Whole-exome sequencing identifies FAM20A mutations as a cause of
amelogenesis imperfecta and gingival hyperplasia syndrome.";
Am. J. Hum. Genet. 88:616-620(2011).
[8]
INVOLVEMENT IN AI1G.
PubMed=23697977; DOI=10.1038/jhg.2013.44;
Cabral R.M., Kurban M., Rothman L., Wajid M., Shimomura Y.,
Petukhova L., Christiano A.M.;
"Autosomal recessive gingival hyperplasia and dental anomalies caused
by a 29-base pair duplication in the FAM20A gene.";
J. Hum. Genet. 58:566-567(2013).
[9]
INVOLVEMENT IN AI1G.
PubMed=24259279; DOI=10.1002/ajmg.a.36187;
Kantaputra P.N., Kaewgahya M., Khemaleelakul U., Dejkhamron P.,
Sutthimethakorn S., Thongboonkerd V., Iamaroon A.;
"Enamel-renal-gingival syndrome and FAM20A mutations.";
Am. J. Med. Genet. A 164A:1-9(2014).
[10]
INVOLVEMENT IN AI1G.
PubMed=24756937; DOI=10.1002/ajmg.a.36579;
Kantaputra P.N., Bongkochwilawan C., Kaewgahya M., Ohazama A.,
Kayserili H., Erdem A.P., Aktoren O., Guven Y.;
"Enamel-Renal-Gingival syndrome, hypodontia, and a novel FAM20A
mutation.";
Am. J. Med. Genet. A 164A:2124-2128(2014).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
INVOLVEMENT IN AI1G.
PubMed=25827751; DOI=10.1016/j.archoralbio.2015.02.018;
Volodarsky M., Zilberman U., Birk O.S.;
"Novel FAM20A mutation causes autosomal recessive amelogenesis
imperfecta.";
Arch. Oral Biol. 60:919-922(2015).
[13]
INVOLVEMENT IN AI1G.
PubMed=25636655; DOI=10.1186/1472-6831-15-14;
Cherkaoui Jaouad I., El Alloussi M., Chafai El Alaoui S.,
Laarabi F.Z., Lyahyai J., Sefiani A.;
"Further evidence for causal FAM20A mutations and first case of
amelogenesis imperfecta and gingival hyperplasia syndrome in Morocco:
a case report.";
BMC Oral Health 15:14-14(2015).
[14]
FUNCTION, INTERACTION WITH FAM20C, MUTAGENESIS OF GLN-258, AND
CHARACTERIZATION OF VARIANTS AI1G ARG-173; ASP-331 AND ASN-403.
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).
[15]
VARIANT AI1G 197-ASP--ILE-214 DELINS VAL-197.
PubMed=21990045; DOI=10.1002/humu.21621;
Cho S.H., Seymen F., Lee K.E., Lee S.K., Kweon Y.S., Kim K.J.,
Jung S.E., Song S.J., Yildirim M., Bayram M., Tuna E.B., Gencay K.,
Kim J.W.;
"Novel FAM20A mutations in hypoplastic amelogenesis imperfecta.";
Hum. Mutat. 33:91-94(2012).
[16]
VARIANT AI1G ARG-173.
PubMed=23434854; DOI=10.1159/000349989;
Jaureguiberry G., De la Dure-Molla M., Parry D., Quentric M.,
Himmerkus N., Koike T., Poulter J., Klootwijk E., Robinette S.L.,
Howie A.J., Patel V., Figueres M.L., Stanescu H.C., Issler N.,
Nicholson J.K., Bockenhauer D., Laing C., Walsh S.B., McCredie D.A.,
Povey S., Asselin A., Picard A., Coulomb A., Medlar A.J.,
Bailleul-Forestier I., Verloes A., Le Caignec C., Roussey G.,
Guiol J., Isidor B., Logan C., Shore R., Johnson C., Inglehearn C.,
Al-Bahlani S., Schmittbuhl M., Clauss F., Huckert M., Laugel V.,
Ginglinger E., Pajarola S., Sparta G., Bartholdi D., Rauch A.,
Addor M.C., Yamaguti P.M., Safatle H.P., Acevedo A.C.,
Martelli-Junior H., dos Santos Netos P.E., Coletta R.D., Gruessel S.,
Sandmann C., Ruehmann D., Langman C.B., Scheinman S.J.,
Ozdemir-Ozenen D., Hart T.C., Hart P.S., Neugebauer U., Schlatter E.,
Houillier P., Gahl W.A., Vikkula M., Bloch-Zupan A., Bleich M.,
Kitagawa H., Unwin R.J., Mighell A., Berdal A., Kleta R.;
"Nephrocalcinosis (enamel renal syndrome) caused by autosomal
recessive FAM20A mutations.";
Nephron Physiol. 122:1-6(2012).
[17]
VARIANT AI1G ASP-331, AND SUBCELLULAR LOCATION.
PubMed=23468644; DOI=10.1371/journal.pgen.1003302;
Wang S.K., Aref P., Hu Y., Milkovich R.N., Simmer J.P., El-Khateeb M.,
Daggag H., Baqain Z.H., Hu J.C.;
"FAM20A mutations can cause enamel-renal syndrome (ERS).";
PLoS Genet. 9:E1003302-E1003302(2013).
[18]
VARIANT AI1G ASN-403.
PubMed=24196488; DOI=10.1177/0022034513512653;
Wang S.K., Reid B.M., Dugan S.L., Roggenbuck J.A., Read L., Aref P.,
Taheri A.P., Yeganeh M.Z., Simmer J.P., Hu J.C.;
"FAM20A mutations associated with enamel renal syndrome.";
J. Dent. Res. 93:42-48(2014).
-!- FUNCTION: Pseudokinase that acts as an allosteric activator of the
Golgi serine/threonine protein kinase FAM20C and is involved in
biomineralization of teeth. Forms a complex with FAM20C and
increases the ability of FAM20C to phosphorylate the proteins that
form the 'matrix' that guides the deposition of the enamel
minerals. {ECO:0000269|PubMed:25789606}.
-!- SUBUNIT: Interacts with FAM20C; probably forming a heterotetramer
of 2 subunits of FAM20A and 2 subunits of FAM20C.
{ECO:0000269|PubMed:25789606}.
-!- INTERACTION:
Q8IXL6:FAM20C; NbExp=3; IntAct=EBI-11892970, EBI-7147442;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8CID3}.
Golgi apparatus {ECO:0000269|PubMed:23468644}. Endoplasmic
reticulum {ECO:0000250|UniProtKB:Q8CID3}.
-!- TISSUE SPECIFICITY: Highly expressed in lung and liver.
Intermediate levels in thymus and ovary.
{ECO:0000269|PubMed:15676076}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8CID3}.
-!- DISEASE: Amelogenesis imperfecta 1G (AI1G) [MIM:204690]: A
disorder characterized by dental anomalies, gingival overgrowth,
and nephrocalcinosis. Dental anomalies include hypoplastic
amelogenesis imperfecta, intrapulpal calcifications, delay of
tooth eruption, hypodontia/oligodontia, pericoronal radiolucencies
and unerupted teeth. {ECO:0000269|PubMed:21549343,
ECO:0000269|PubMed:21990045, ECO:0000269|PubMed:23434854,
ECO:0000269|PubMed:23468644, ECO:0000269|PubMed:23697977,
ECO:0000269|PubMed:24196488, ECO:0000269|PubMed:24259279,
ECO:0000269|PubMed:24756937, ECO:0000269|PubMed:25636655,
ECO:0000269|PubMed:25789606, ECO:0000269|PubMed:25827751}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the FAM20 family. {ECO:0000305}.
-!- CAUTION: Although strongly related to other members of the family,
lacks the kinase activity. A conserved Asp/Glu residue present in
other members of the family, which coordinates the Mn(2+) ion and
the ion-pair Lys and is indispensable for kinase activity, is
replaced by a Gln in position 258. {ECO:0000269|PubMed:25789606}.
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EMBL; AK056789; BAB71285.1; -; mRNA.
EMBL; AY358197; AAQ88564.1; -; mRNA.
EMBL; AC079210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC136686; AAI36687.1; -; mRNA.
EMBL; BC136689; AAI36690.1; -; mRNA.
EMBL; AL133105; CAB61412.1; -; mRNA.
CCDS; CCDS11679.1; -.
PIR; T42684; T42684.
RefSeq; NP_001230675.1; NM_001243746.1.
RefSeq; NP_060035.2; NM_017565.3.
UniGene; Hs.268874; -.
PDB; 5WRR; X-ray; 2.51 A; A/B=89-526.
PDB; 5WRS; X-ray; 2.75 A; A/B=89-526.
PDBsum; 5WRR; -.
PDBsum; 5WRS; -.
ProteinModelPortal; Q96MK3; -.
SMR; Q96MK3; -.
IntAct; Q96MK3; 5.
STRING; 9606.ENSP00000468308; -.
iPTMnet; Q96MK3; -.
PhosphoSitePlus; Q96MK3; -.
BioMuta; FAM20A; -.
DMDM; 269849750; -.
EPD; Q96MK3; -.
PaxDb; Q96MK3; -.
PeptideAtlas; Q96MK3; -.
PRIDE; Q96MK3; -.
Ensembl; ENST00000592554; ENSP00000468308; ENSG00000108950.
GeneID; 54757; -.
KEGG; hsa:54757; -.
UCSC; uc002jho.4; human.
CTD; 54757; -.
DisGeNET; 54757; -.
EuPathDB; HostDB:ENSG00000108950.11; -.
GeneCards; FAM20A; -.
H-InvDB; HIX0014117; -.
HGNC; HGNC:23015; FAM20A.
HPA; HPA048964; -.
MalaCards; FAM20A; -.
MIM; 204690; phenotype.
MIM; 611062; gene.
neXtProt; NX_Q96MK3; -.
OpenTargets; ENSG00000108950; -.
Orphanet; 1031; Amelogenesis imperfecta - nephrocalcinosis.
Orphanet; 171836; Amelogenesis imperfecta and gingival hyperplasia syndrome.
PharmGKB; PA134888583; -.
eggNOG; KOG3829; Eukaryota.
eggNOG; ENOG410XQEJ; LUCA.
GeneTree; ENSGT00390000007484; -.
HOGENOM; HOG000231437; -.
HOVERGEN; HBG051635; -.
InParanoid; Q96MK3; -.
KO; K21957; -.
OMA; EASWVQF; -.
OrthoDB; EOG091G1BEO; -.
PhylomeDB; Q96MK3; -.
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; FAM20A; human.
GeneWiki; FAM20A; -.
GenomeRNAi; 54757; -.
PRO; PR:Q96MK3; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108950; -.
CleanEx; HS_FAM20A; -.
ExpressionAtlas; Q96MK3; baseline and differential.
Genevisible; Q96MK3; HS.
GO; GO:0005623; C:cell; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
GO; GO:0031214; P:biomineral tissue development; IMP:UniProtKB.
GO; GO:0055074; P:calcium ion homeostasis; IMP:UniProtKB.
GO; GO:0070166; P:enamel mineralization; IMP:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0044691; P:tooth eruption; IMP:UniProtKB.
InterPro; IPR024869; FAM20.
InterPro; IPR009581; FAM20_C.
PANTHER; PTHR12450; PTHR12450; 1.
Pfam; PF06702; Fam20C; 1.
1: Evidence at protein level;
3D-structure; Amelogenesis imperfecta; Biomineralization;
Complete proteome; Disease mutation; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 33 {ECO:0000255}.
CHAIN 34 541 Pseudokinase FAM20A.
/FTId=PRO_0000008743.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 287 287 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 388 388 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 538 538 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 314 330 {ECO:0000250|UniProtKB:Q9XTW2}.
DISULFID 319 323 {ECO:0000250|UniProtKB:Q9XTW2}.
DISULFID 378 452 {ECO:0000250|UniProtKB:Q9XTW2}.
DISULFID 453 512 {ECO:0000250|UniProtKB:Q9XTW2}.
VARIANT 173 173 L -> R (in AI1G; impaired folding of the
protein; abolishes ability to activate
FAM20C protein kinase activity).
{ECO:0000269|PubMed:23434854,
ECO:0000269|PubMed:25789606}.
/FTId=VAR_072170.
VARIANT 197 214 DYSQDEKALLGACDCTQI -> V (in AI1G).
{ECO:0000269|PubMed:21990045}.
/FTId=VAR_066859.
VARIANT 331 331 G -> D (in AI1G; impaired folding of the
protein; abolishes ability to activate
FAM20C protein kinase activity).
{ECO:0000269|PubMed:23468644,
ECO:0000269|PubMed:25789606}.
/FTId=VAR_072171.
VARIANT 332 332 N -> K (in dbSNP:rs2302234).
{ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_059282.
VARIANT 403 403 D -> N (in AI1G; impaired folding of the
protein; abolishes ability to activate
FAM20C protein kinase activity;
dbSNP:rs377432171).
{ECO:0000269|PubMed:24196488,
ECO:0000269|PubMed:25789606}.
/FTId=VAR_072172.
VARIANT 530 530 L -> S (in dbSNP:rs2907373).
{ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_059283.
MUTAGEN 258 258 Q->E: Able to hydrolyze ATP and display
some protein kinase activity.
{ECO:0000269|PubMed:25789606}.
HELIX 91 97 {ECO:0000244|PDB:5WRR}.
HELIX 99 102 {ECO:0000244|PDB:5WRR}.
TURN 112 114 {ECO:0000244|PDB:5WRR}.
STRAND 115 117 {ECO:0000244|PDB:5WRR}.
HELIX 119 143 {ECO:0000244|PDB:5WRR}.
HELIX 160 167 {ECO:0000244|PDB:5WRR}.
STRAND 172 174 {ECO:0000244|PDB:5WRR}.
HELIX 179 190 {ECO:0000244|PDB:5WRR}.
STRAND 193 198 {ECO:0000244|PDB:5WRR}.
HELIX 200 203 {ECO:0000244|PDB:5WRR}.
STRAND 206 208 {ECO:0000244|PDB:5WRR}.
TURN 212 214 {ECO:0000244|PDB:5WRR}.
STRAND 224 228 {ECO:0000244|PDB:5WRR}.
STRAND 233 238 {ECO:0000244|PDB:5WRR}.
HELIX 244 246 {ECO:0000244|PDB:5WRR}.
HELIX 252 254 {ECO:0000244|PDB:5WRR}.
HELIX 259 272 {ECO:0000244|PDB:5WRR}.
STRAND 281 287 {ECO:0000244|PDB:5WRR}.
HELIX 288 291 {ECO:0000244|PDB:5WRR}.
TURN 292 295 {ECO:0000244|PDB:5WRR}.
HELIX 299 303 {ECO:0000244|PDB:5WRR}.
STRAND 305 307 {ECO:0000244|PDB:5WRR}.
STRAND 313 316 {ECO:0000244|PDB:5WRR}.
HELIX 318 322 {ECO:0000244|PDB:5WRR}.
STRAND 328 330 {ECO:0000244|PDB:5WRR}.
STRAND 332 342 {ECO:0000244|PDB:5WRR}.
TURN 347 349 {ECO:0000244|PDB:5WRR}.
STRAND 352 356 {ECO:0000244|PDB:5WRR}.
TURN 371 373 {ECO:0000244|PDB:5WRR}.
HELIX 376 381 {ECO:0000244|PDB:5WRR}.
TURN 385 388 {ECO:0000244|PDB:5WRR}.
HELIX 390 406 {ECO:0000244|PDB:5WRR}.
STRAND 413 417 {ECO:0000244|PDB:5WRR}.
HELIX 418 420 {ECO:0000244|PDB:5WRR}.
STRAND 434 436 {ECO:0000244|PDB:5WRR}.
HELIX 443 446 {ECO:0000244|PDB:5WRR}.
HELIX 447 452 {ECO:0000244|PDB:5WRR}.
HELIX 457 466 {ECO:0000244|PDB:5WRR}.
HELIX 469 471 {ECO:0000244|PDB:5WRR}.
HELIX 473 481 {ECO:0000244|PDB:5WRR}.
TURN 485 488 {ECO:0000244|PDB:5WRR}.
HELIX 492 516 {ECO:0000244|PDB:5WRR}.
HELIX 518 521 {ECO:0000244|PDB:5WRR}.
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


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