Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Guanidinoacetate N-methyltransferase (EC 2.1.1.2)

 GAMT_HUMAN              Reviewed;         236 AA.
Q14353; A8K0A0; Q53Y34; Q8WVJ1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
27-SEP-2017, entry version 167.
RecName: Full=Guanidinoacetate N-methyltransferase;
EC=2.1.1.2;
Name=GAMT;
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=Liver;
PubMed=8547310; DOI=10.1016/0167-4781(95)00184-0;
Isbrandt D., von Figura K.;
"Cloning and sequence analysis of human guanidinoacetate N-
methyltransferase cDNA.";
Biochim. Biophys. Acta 1264:265-267(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9325156; DOI=10.1006/bbrc.1997.9992;
Jenne D.E., Olsen A.S., Zimmer M.;
"The human guanidinoacetate methyltransferase (GAMT) gene maps to a
syntenic region on 19p13.3, homologous to band C of mouse chromosome
10, but GAMT is not mutated in jittery mice.";
Biochem. Biophys. Res. Commun. 238:723-727(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Isbrandt D., Schmidt A.;
"Gene structure of human guanidinoacetate N-methyltransferase.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cerebellum;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
MET-209.
TISSUE=Lymph, and Skeletal muscle;
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).
[9]
TISSUE SPECIFICITY, AND INVOLVEMENT IN CCDS2.
PubMed=8651275;
Stoeckler S., Isbrandt D., Hanefeld F., Schmidt B., von Figura K.;
"Guanidinoacetate methyltransferase deficiency: the first inborn error
of creatine metabolism in man.";
Am. J. Hum. Genet. 58:914-922(1996).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[12]
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE.
Structural genomics consortium (SGC);
"The crystal structure of human guanidinoacetate N-methyltransferase
with SAH.";
Submitted (MAR-2006) to the PDB data bank.
[13]
VARIANT CCDS2 PRO-197.
PubMed=12468279; DOI=10.1016/S1096-7192(02)00175-0;
Battini R., Leuzzi V., Carducci C., Tosetti M., Bianchi M.C.,
Item C.B., Stoeckler-Ipsiroglu S., Cioni G.;
"Creatine depletion in a new case with AGAT deficiency: clinical and
genetic study in a large pedigree.";
Mol. Genet. Metab. 77:326-331(2002).
[14]
VARIANTS CCDS2 SER-20; PRO-51 AND PRO-54.
PubMed=15108290; DOI=10.1002/humu.9238;
Item C.B., Mercimek-Mahmutoglu S., Battini R., Edlinger-Horvat C.,
Stromberger C., Bodamer O., Muehl A., Vilaseca M.A., Korall H.,
Stoeckler-Ipsiroglu S.;
"Characterization of seven novel mutations in seven patients with GAMT
deficiency.";
Hum. Mutat. 23:524-524(2004).
[15]
VARIANTS CCDS2 SER-20 AND TYR-169.
PubMed=15651030; DOI=10.1002/ajmg.a.30226;
Caldeira Araujo H., Smit W., Verhoeven N.M., Salomons G.S., Silva S.,
Vasconcelos R., Tomas H., Tavares de Almeida I., Jakobs C., Duran M.;
"Guanidinoacetate methyltransferase deficiency identified in adults
and a child with mental retardation.";
Am. J. Med. Genet. A 133:122-127(2005).
[16]
VARIANT CCDS2 PRO-197.
PubMed=16293431; DOI=10.1016/j.ymgme.2005.09.017;
Leuzzi V., Carducci C., Carducci C., Matricardi M., Bianchi M.C.,
Di Sabato M.L., Artiola C., Antonozzi I.;
"A mutation on exon 6 of guanidinoacetate methyltransferase (GAMT)
gene supports a different function for isoform a and b of GAMT
enzyme.";
Mol. Genet. Metab. 87:88-90(2006).
[17]
VARIANT CCDS2 PRO-51.
PubMed=16855203; DOI=10.1212/01.wnl.0000234852.43688.bf;
Mercimek-Mahmutoglu S., Stoeckler-Ipsiroglu S., Adami A., Appleton R.,
Araujo H.C., Duran M., Ensenauer R., Fernandez-Alvarez E., Garcia P.,
Grolik C., Item C.B., Leuzzi V., Marquardt I., Muehl A.,
Saelke-Kellermann R.A., Salomons G.S., Schulze A., Surtees R.,
van der Knaap M.S., Vasconcelos R., Verhoeven N.M., Vilarinho L.,
Wilichowski E., Jakobs C.;
"GAMT deficiency: features, treatment, and outcome in an inborn error
of creatine synthesis.";
Neurology 67:480-484(2006).
[18]
VARIANT CCDS2 LEU-50.
PubMed=17101918; DOI=10.1212/01.wnl.0000239153.39710.81;
Lion-Francois L., Cheillan D., Pitelet G., Acquaviva-Bourdain C.,
Bussy G., Cotton F., Guibaud L., Gerard D., Rivier C.,
Vianey-Saban C., Jakobs C., Salomons G.S., des Portes V.;
"High frequency of creatine deficiency syndromes in patients with
unexplained mental retardation.";
Neurology 67:1713-1714(2006).
[19]
VARIANT CCDS2 PRO-166.
PubMed=17466557; DOI=10.1016/j.ymgme.2007.03.006;
Verbruggen K.T., Sijens P.E., Schulze A., Lunsing R.J., Jakobs C.,
Salomons G.S., van Spronsen F.J.;
"Successful treatment of a guanidinoacetate methyltransferase
deficient patient: findings with relevance to treatment strategy and
pathophysiology.";
Mol. Genet. Metab. 91:294-296(2007).
[20]
VARIANT CCDS2 ASN-135.
PubMed=19388150; DOI=10.1111/j.1469-8749.2008.03227.x;
O'Rourke D.J., Ryan S., Salomons G., Jakobs C., Monavari A.,
King M.D.;
"Guanidinoacetate methyltransferase (GAMT) deficiency: late onset of
movement disorder and preserved expressive language.";
Dev. Med. Child. Neurol. 51:404-407(2009).
[21]
VARIANTS CCDS2 ARG-45; GLU-78; ASP-164 AND ARG-169.
PubMed=23660394; DOI=10.1016/j.ymgme.2013.04.006;
Comeaux M.S., Wang J., Wang G., Kleppe S., Zhang V.W., Schmitt E.S.,
Craigen W.J., Renaud D., Sun Q., Wong L.J.;
"Biochemical, molecular, and clinical diagnoses of patients with
cerebral creatine deficiency syndromes.";
Mol. Genet. Metab. 109:260-268(2013).
[22]
VARIANTS CCDS2 CYS-68; VAL-75; PHE-110; TYR-147; PRO-159 AND PRO-208,
VARIANTS THR-8 AND HIS-27, CHARACTERIZATION OF VARIANTS CCDS2 ARG-45;
LEU-50; PRO-51; PRO-54; CYS-68; VAL-75; PHE-110; TYR-147; PRO-159;
PRO-166; TYR-169; PRO-197 AND PRO-208, CHARACTERIZATION OF VARIANTS
THR-8 AND HIS-27, AND FUNCTION.
PubMed=24415674; DOI=10.1002/humu.22511;
Mercimek-Mahmutoglu S., Ndika J., Kanhai W., de Villemeur T.B.,
Cheillan D., Christensen E., Dorison N., Hannig V., Hendriks Y.,
Hofstede F.C., Lion-Francois L., Lund A.M., Mundy H., Pitelet G.,
Raspall-Chaure M., Scott-Schwoerer J.A., Szakszon K.,
Valayannopoulos V., Williams M., Salomons G.S.;
"Thirteen new patients with guanidinoacetate methyltransferase
deficiency and functional characterization of nineteen novel missense
variants in the GAMT gene.";
Hum. Mutat. 35:462-469(2014).
[23]
VARIANTS VAL-71; MET-78; ILE-95; GLN-105; PRO-106; ARG-146; ASP-156;
LEU-157 AND ILE-167, CHARACTERIZATION OF VARIANTS VAL-71; MET-78;
ILE-95; GLN-105; PRO-106; ARG-146; ASP-156; LEU-157 AND ILE-167, AND
FUNCTION.
PubMed=26003046; DOI=10.1007/s00438-015-1067-x;
Desroches C.L., Patel J., Wang P., Minassian B., Marshall C.R.,
Salomons G.S., Mercimek-Mahmutoglu S.;
"Carrier frequency of guanidinoacetate methyltransferase deficiency in
the general population by functional characterization of missense
variants in the GAMT gene.";
Mol. Genet. Genomics 290:2163-2171(2015).
[24]
VARIANTS LEU-44; LEU-76; THR-196; VAL-196 AND THR-224,
CHARACTERIZATION OF VARIANTS LEU-44; LEU-76; THR-196; VAL-196 AND
THR-224, AND FUNCTION.
PubMed=26319512; DOI=10.1016/j.gene.2015.08.045;
Mercimek-Mahmutoglu S., Pop A., Kanhai W., Fernandez Ojeda M.,
Holwerda U., Smith D., Loeber J.G., Schielen P.C., Salomons G.S.;
"A pilot study to estimate incidence of guanidinoacetate
methyltransferase deficiency in newborns by direct sequencing of the
GAMT gene.";
Gene 575:127-131(2016).
-!- FUNCTION: Converts guanidinoacetate to creatine, using S-
adenosylmethionine as the methyl donor (PubMed:26003046,
PubMed:24415674, PubMed:26319512). Important in nervous system
development (PubMed:24415674). {ECO:0000269|PubMed:24415674,
ECO:0000269|PubMed:26003046, ECO:0000269|PubMed:26319512}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanidinoacetate =
S-adenosyl-L-homocysteine + creatine. {ECO:0000255|PROSITE-
ProRule:PRU00892}.
-!- PATHWAY: Amine and polyamine biosynthesis; creatine biosynthesis;
creatine from L-arginine and glycine: step 2/2.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- INTERACTION:
Q9HCM9-2:TRIM39; NbExp=4; IntAct=EBI-3909086, EBI-11523450;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14353-1; Sequence=Displayed;
Name=2;
IsoId=Q14353-2; Sequence=VSP_042722;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in liver.
{ECO:0000269|PubMed:8651275}.
-!- DISEASE: Cerebral creatine deficiency syndrome 2 (CCDS2)
[MIM:612736]: An autosomal recessive disorder characterized by
developmental delay and regression, mental retardation, severe
disturbance of expressive and cognitive speech, intractable
seizures, movement disturbances, severe depletion of creatine and
phosphocreatine in the brain, and accumulation of guanidinoacetic
acid in brain and body fluids. {ECO:0000269|PubMed:12468279,
ECO:0000269|PubMed:15108290, ECO:0000269|PubMed:15651030,
ECO:0000269|PubMed:16293431, ECO:0000269|PubMed:16855203,
ECO:0000269|PubMed:17101918, ECO:0000269|PubMed:17466557,
ECO:0000269|PubMed:19388150, ECO:0000269|PubMed:23660394,
ECO:0000269|PubMed:24415674, ECO:0000269|PubMed:8651275}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. RMT2 methyltransferase family.
{ECO:0000255|PROSITE-ProRule:PRU00892}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z49878; CAA90035.1; -; mRNA.
EMBL; AF010248; AAD04781.1; -; Genomic_DNA.
EMBL; AF010246; AAD04781.1; JOINED; Genomic_DNA.
EMBL; AF010247; AAD04781.1; JOINED; Genomic_DNA.
EMBL; AF188893; AAF01461.1; -; Genomic_DNA.
EMBL; BT007034; AAP35682.1; -; mRNA.
EMBL; AK289465; BAF82154.1; -; mRNA.
EMBL; AC005329; AAC27668.1; -; Genomic_DNA.
EMBL; CH471139; EAW69505.1; -; Genomic_DNA.
EMBL; BC016760; AAH16760.1; -; mRNA.
EMBL; BC017936; AAH17936.1; -; mRNA.
CCDS; CCDS12064.1; -. [Q14353-1]
CCDS; CCDS45897.1; -. [Q14353-2]
PIR; S62732; S62732.
RefSeq; NP_000147.1; NM_000156.5. [Q14353-1]
RefSeq; NP_620279.1; NM_138924.2. [Q14353-2]
UniGene; Hs.81131; -.
PDB; 3ORH; X-ray; 1.86 A; A/B/C/D=1-236.
PDBsum; 3ORH; -.
ProteinModelPortal; Q14353; -.
SMR; Q14353; -.
BioGrid; 108865; 8.
IntAct; Q14353; 6.
STRING; 9606.ENSP00000403536; -.
DrugBank; DB00148; Creatine.
DrugBank; DB00536; Guanidine.
DrugBank; DB02751; N-[Amino(Imino)Methyl]Glycine.
DrugBank; DB01752; S-Adenosyl-L-Homocysteine.
iPTMnet; Q14353; -.
PhosphoSitePlus; Q14353; -.
BioMuta; GAMT; -.
DMDM; 2498404; -.
OGP; Q14353; -.
EPD; Q14353; -.
PaxDb; Q14353; -.
PeptideAtlas; Q14353; -.
PRIDE; Q14353; -.
DNASU; 2593; -.
Ensembl; ENST00000252288; ENSP00000252288; ENSG00000130005. [Q14353-1]
Ensembl; ENST00000447102; ENSP00000403536; ENSG00000130005. [Q14353-2]
GeneID; 2593; -.
KEGG; hsa:2593; -.
UCSC; uc002lsk.5; human. [Q14353-1]
CTD; 2593; -.
DisGeNET; 2593; -.
EuPathDB; HostDB:ENSG00000130005.11; -.
GeneCards; GAMT; -.
GeneReviews; GAMT; -.
H-InvDB; HIX0030201; -.
HGNC; HGNC:4136; GAMT.
HPA; HPA051806; -.
MalaCards; GAMT; -.
MIM; 601240; gene.
MIM; 612736; phenotype.
neXtProt; NX_Q14353; -.
OpenTargets; ENSG00000130005; -.
Orphanet; 382; Guanidinoacetate methyltransferase deficiency.
PharmGKB; PA28549; -.
eggNOG; KOG1709; Eukaryota.
eggNOG; ENOG4110T2S; LUCA.
GeneTree; ENSGT00390000018061; -.
HOGENOM; HOG000010290; -.
HOVERGEN; HBG005801; -.
InParanoid; Q14353; -.
KO; K00542; -.
OMA; RYYAFPQ; -.
OrthoDB; EOG091G0EPW; -.
PhylomeDB; Q14353; -.
TreeFam; TF328555; -.
BioCyc; MetaCyc:HS05327-MONOMER; -.
BRENDA; 2.1.1.2; 2681.
Reactome; R-HSA-71288; Creatine metabolism.
UniPathway; UPA00104; UER00580.
EvolutionaryTrace; Q14353; -.
GeneWiki; Guanidinoacetate_N-methyltransferase; -.
GenomeRNAi; 2593; -.
PRO; PR:Q14353; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000130005; -.
CleanEx; HS_GAMT; -.
ExpressionAtlas; Q14353; baseline and differential.
Genevisible; Q14353; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0030731; F:guanidinoacetate N-methyltransferase activity; IMP:UniProtKB.
GO; GO:0008168; F:methyltransferase activity; TAS:Reactome.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0006601; P:creatine biosynthetic process; IDA:UniProtKB.
GO; GO:0006600; P:creatine metabolic process; TAS:Reactome.
GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0046498; P:S-adenosylhomocysteine metabolic process; IBA:GO_Central.
GO; GO:0046500; P:S-adenosylmethionine metabolic process; IBA:GO_Central.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
InterPro; IPR016550; GuanidinoAc_N-MeTrfase.
InterPro; IPR026480; RMT2_dom.
InterPro; IPR029063; SAM-dependent_MTases.
PIRSF; PIRSF009285; GAMT; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51559; SAM_RMT2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Disease mutation; Methyltransferase; Polymorphism; Reference proteome;
S-adenosyl-L-methionine; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 236 Guanidinoacetate N-methyltransferase.
/FTId=PRO_0000087430.
DOMAIN 13 236 RMT2. {ECO:0000255|PROSITE-
ProRule:PRU00892}.
REGION 69 74 S-adenosyl-L-methionine binding.
REGION 90 92 S-adenosyl-L-methionine.
REGION 117 118 S-adenosyl-L-methionine binding.
REGION 171 172 Substrate binding.
BINDING 20 20 S-adenosyl-L-methionine.
BINDING 42 42 Substrate. {ECO:0000255|PROSITE-
ProRule:PRU00892}.
BINDING 46 46 Substrate. {ECO:0000255|PROSITE-
ProRule:PRU00892}.
BINDING 50 50 S-adenosyl-L-methionine.
BINDING 135 135 S-adenosyl-L-methionine and substrate.
{ECO:0000255|PROSITE-ProRule:PRU00892}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
VAR_SEQ 191 236 ETQVPALLEAGFRRENIRTEVMALVPPADCRYYAFPQMITP
LVTKG -> VRPPEVPHGSPGSDLGWGWEGAAGATLLPGEG
PFLTPWVGWTVLVHLEIKVLCLAQWLPGAVAQVYNPSTVEG
RGGQIA (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042722.
VARIANT 8 8 P -> T (rare polymorphism; no effect on
activity; dbSNP:rs776498025).
{ECO:0000269|PubMed:24415674}.
/FTId=VAR_071775.
VARIANT 20 20 W -> S (in CCDS2; dbSNP:rs80338734).
{ECO:0000269|PubMed:15108290,
ECO:0000269|PubMed:15651030}.
/FTId=VAR_058102.
VARIANT 27 27 Y -> H (polymorphism; no effect on
activity; dbSNP:rs200833152).
{ECO:0000269|PubMed:24415674}.
/FTId=VAR_071776.
VARIANT 44 44 R -> L (polymorphism; no effect on
enzymatic activity; dbSNP:rs200339910).
{ECO:0000269|PubMed:26319512}.
/FTId=VAR_075290.
VARIANT 45 45 W -> R (in CCDS2; loss of activity).
{ECO:0000269|PubMed:23660394,
ECO:0000269|PubMed:24415674}.
/FTId=VAR_071777.
VARIANT 50 50 M -> L (in CCDS2; retains no significant
activity; dbSNP:rs104894694).
{ECO:0000269|PubMed:17101918,
ECO:0000269|PubMed:24415674}.
/FTId=VAR_058103.
VARIANT 51 51 H -> P (in CCDS2; retains no significant
activity). {ECO:0000269|PubMed:15108290,
ECO:0000269|PubMed:16855203,
ECO:0000269|PubMed:24415674}.
/FTId=VAR_058104.
VARIANT 54 54 A -> P (in CCDS2; loss of activity).
{ECO:0000269|PubMed:15108290,
ECO:0000269|PubMed:24415674}.
/FTId=VAR_058105.
VARIANT 68 68 G -> C (in CCDS2; retains no significant
activity). {ECO:0000269|PubMed:24415674}.
/FTId=VAR_071778.
VARIANT 71 71 M -> V (polymorphism; no effect on
enzymatic activity; dbSNP:rs372027428).
{ECO:0000269|PubMed:26003046}.
/FTId=VAR_075291.
VARIANT 75 75 A -> V (in CCDS2; retains no significant
activity). {ECO:0000269|PubMed:24415674}.
/FTId=VAR_071779.
VARIANT 76 76 S -> L (polymorphism; no effect on
enzymatic activity; dbSNP:rs150338273).
{ECO:0000269|PubMed:26319512}.
/FTId=VAR_075292.
VARIANT 78 78 V -> E (in CCDS2).
{ECO:0000269|PubMed:23660394}.
/FTId=VAR_071780.
VARIANT 78 78 V -> M (polymorphism; no effect on
enzymatic activity; dbSNP:rs141358977).
{ECO:0000269|PubMed:26003046}.
/FTId=VAR_075293.
VARIANT 95 95 V -> I (polymorphism; no effect on
enzymatic activity; dbSNP:rs140778208).
{ECO:0000269|PubMed:26003046}.
/FTId=VAR_075294.
VARIANT 105 105 R -> Q (polymorphism; no effect on
enzymatic activity; dbSNP:rs148838075).
{ECO:0000269|PubMed:26003046}.
/FTId=VAR_075295.
VARIANT 106 106 Q -> P (disrupts enzymatic activity;
dbSNP:rs145817990).
{ECO:0000269|PubMed:26003046}.
/FTId=VAR_075296.
VARIANT 110 110 V -> F (in CCDS2; retains no significant
activity; dbSNP:rs753198836).
{ECO:0000269|PubMed:24415674}.
/FTId=VAR_071781.
VARIANT 135 135 D -> N (in CCDS2; dbSNP:rs774144200).
{ECO:0000269|PubMed:19388150}.
/FTId=VAR_071782.
VARIANT 146 146 T -> R (polymorphism; no effect on
enzymatic activity; dbSNP:rs149821870).
{ECO:0000269|PubMed:26003046}.
/FTId=VAR_075297.
VARIANT 147 147 H -> Y (in CCDS2; retains no significant
activity). {ECO:0000269|PubMed:24415674}.
/FTId=VAR_071783.
VARIANT 156 156 A -> D (disrupts enzymatic activity;
dbSNP:rs368221789).
{ECO:0000269|PubMed:26003046}.
/FTId=VAR_075298.
VARIANT 157 157 F -> L (polymorphism; no effect on
enzymatic activity; dbSNP:rs372260609).
{ECO:0000269|PubMed:26003046}.
/FTId=VAR_075299.
VARIANT 159 159 L -> P (in CCDS2; loss of activity).
{ECO:0000269|PubMed:24415674}.
/FTId=VAR_071784.
VARIANT 164 164 G -> D (in CCDS2; dbSNP:rs760101382).
{ECO:0000269|PubMed:23660394}.
/FTId=VAR_071785.
VARIANT 166 166 L -> P (in CCDS2; loss of activity).
{ECO:0000269|PubMed:17466557,
ECO:0000269|PubMed:24415674}.
/FTId=VAR_071786.
VARIANT 167 167 T -> I (disrupts enzymatic activity;
dbSNP:rs374762419).
{ECO:0000269|PubMed:26003046}.
/FTId=VAR_075300.
VARIANT 169 169 C -> R (in CCDS2).
{ECO:0000269|PubMed:23660394}.
/FTId=VAR_071787.
VARIANT 169 169 C -> Y (in CCDS2; retains no significant
activity; dbSNP:rs121909272).
{ECO:0000269|PubMed:15651030,
ECO:0000269|PubMed:24415674}.
/FTId=VAR_058106.
VARIANT 196 196 A -> T (polymorphism; no effect on
enzymatic activity).
{ECO:0000269|PubMed:26319512}.
/FTId=VAR_075301.
VARIANT 196 196 A -> V (polymorphism; no effect on
enzymatic activity; dbSNP:rs565109128).
{ECO:0000269|PubMed:26319512}.
/FTId=VAR_075302.
VARIANT 197 197 L -> P (in CCDS2; loss of activity).
{ECO:0000269|PubMed:12468279,
ECO:0000269|PubMed:16293431,
ECO:0000269|PubMed:24415674}.
/FTId=VAR_058107.
VARIANT 208 208 R -> P (in CCDS2; retains no significant
activity; dbSNP:rs767887772).
{ECO:0000269|PubMed:24415674}.
/FTId=VAR_071788.
VARIANT 209 209 T -> M (in dbSNP:rs17851582).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_025723.
VARIANT 224 224 A -> T (polymorphism; no effect on
enzymatic activity; dbSNP:rs141471799).
{ECO:0000269|PubMed:26319512}.
/FTId=VAR_075303.
HELIX 17 20 {ECO:0000244|PDB:3ORH}.
STRAND 25 27 {ECO:0000244|PDB:3ORH}.
STRAND 31 36 {ECO:0000244|PDB:3ORH}.
STRAND 39 43 {ECO:0000244|PDB:3ORH}.
HELIX 44 46 {ECO:0000244|PDB:3ORH}.
HELIX 47 57 {ECO:0000244|PDB:3ORH}.
TURN 58 60 {ECO:0000244|PDB:3ORH}.
STRAND 62 67 {ECO:0000244|PDB:3ORH}.
HELIX 73 78 {ECO:0000244|PDB:3ORH}.
STRAND 83 90 {ECO:0000244|PDB:3ORH}.
HELIX 93 102 {ECO:0000244|PDB:3ORH}.
HELIX 103 105 {ECO:0000244|PDB:3ORH}.
STRAND 107 115 {ECO:0000244|PDB:3ORH}.
HELIX 117 120 {ECO:0000244|PDB:3ORH}.
HELIX 121 123 {ECO:0000244|PDB:3ORH}.
STRAND 129 134 {ECO:0000244|PDB:3ORH}.
HELIX 141 143 {ECO:0000244|PDB:3ORH}.
TURN 144 146 {ECO:0000244|PDB:3ORH}.
HELIX 147 154 {ECO:0000244|PDB:3ORH}.
HELIX 156 159 {ECO:0000244|PDB:3ORH}.
STRAND 160 168 {ECO:0000244|PDB:3ORH}.
HELIX 171 177 {ECO:0000244|PDB:3ORH}.
TURN 178 181 {ECO:0000244|PDB:3ORH}.
HELIX 185 192 {ECO:0000244|PDB:3ORH}.
HELIX 194 200 {ECO:0000244|PDB:3ORH}.
HELIX 204 206 {ECO:0000244|PDB:3ORH}.
STRAND 207 213 {ECO:0000244|PDB:3ORH}.
STRAND 226 234 {ECO:0000244|PDB:3ORH}.
SEQUENCE 236 AA; 26318 MW; 6B8E845CE56189F5 CRC64;
MSAPSATPIF APGENCSPAW GAAPAAYDAA DTHLRILGKP VMERWETPYM HALAAAASSK
GGRVLEVGFG MAIAASKVQE APIDEHWIIE CNDGVFQRLR DWAPRQTHKV IPLKGLWEDV
APTLPDGHFD GILYDTYPLS EETWHTHQFN FIKNHAFRLL KPGGVLTYCN LTSWGELMKS
KYSDITIMFE ETQVPALLEA GFRRENIRTE VMALVPPADC RYYAFPQMIT PLVTKG


Related products :

Catalog number Product name Quantity
enz-460 Recombinant Human Guanidinoacetate N-Methyltransferase 1mg
REN-60 Recombinant Human Guanidinoacetate N-Methyltransferase 5
enz-460 Recombinant Human Guanidinoacetate N-Methyltransferase 25
CG67 Guanidinoacetate N-methyltransferase GAMT 500
enz-460 Recombinant Human Guanidinoacetate N-Methyltransferase 5
CG67 Guanidinoacetate N-methyltransferase GAMT lmg
7-02799 Recombinant Human Guanidinoacetate N-Methyltransferase 1mg
enz-460 Recombinant Human Guanidinoacetate N-Methyltransferase ENZYMES 5
enz-460 Recombinant Human Guanidinoacetate N-Methyltransferase ENZYMES 25
enz-460 Recombinant Human Guanidinoacetate N-Methyltransferase GAMT 25
GANAB GAMT Gene guanidinoacetate N-methyltransferase
OETENZ-460 Guanidinoacetate N-Methyltransferase Human Recombinant 25
E9701h Human Guanidinoacetate N Methyltransferase ELISA K 96T
201-20-2182 GAMT{guanidinoacetate N-methyltransferase}rabbit.pAb 0.2ml
OETENZ-460 Guanidinoacetate N-Methyltransferase Human Recombinant 5
enz-460 Recombinant Human Guanidinoacetate N-Methyltransferase ENZYMES 1mg
enz-460 Recombinant Human Guanidinoacetate N-Methyltransferase GAMT 5
CSB-EL009227RA Rat Guanidinoacetate N-methyltransferase(GAMT) ELISA kit 96T
enz-460 Recombinant Human Guanidinoacetate N-Methyltransferase GAMT 1mg
7-02798 Recombinant Human Guanidinoacetate N-Methyltransferase 25
7-02797 Recombinant Human Guanidinoacetate N-Methyltransferase 5
C284 Human Guanidinoacetate N-methyltransferase GAMT 50
C274 Human Guanidinoacetate N-methyltransferase GAMT l0
CSB-EL009227BO Bovine Guanidinoacetate N-methyltransferase(GAMT) ELISA kit 96T
GWB-59A362 Anti- GAMT (guanidinoacetate N-methyltransferase) Antibody


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur