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Q14353

- GAMT_HUMAN

UniProt

Q14353 - GAMT_HUMAN

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Protein

Guanidinoacetate N-methyltransferase

Gene

GAMT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201S-adenosyl-L-methionine
Binding sitei42 – 421SubstratePROSITE-ProRule annotation
Binding sitei46 – 461SubstratePROSITE-ProRule annotation
Binding sitei50 – 501S-adenosyl-L-methionine
Binding sitei135 – 1351S-adenosyl-L-methionine and substratePROSITE-ProRule annotation

GO - Molecular functioni

  1. guanidinoacetate N-methyltransferase activity Source: UniProtKB
  2. methyltransferase activity Source: ProtInc

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. creatine biosynthetic process Source: UniProtKB
  3. creatine metabolic process Source: Reactome
  4. muscle contraction Source: ProtInc
  5. organ morphogenesis Source: Ensembl
  6. regulation of multicellular organism growth Source: Ensembl
  7. small molecule metabolic process Source: Reactome
  8. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:HS05327-MONOMER.
BRENDAi2.1.1.2. 2681.
ReactomeiREACT_813. Creatine metabolism.
UniPathwayiUPA00104; UER00580.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanidinoacetate N-methyltransferase (EC:2.1.1.2)
Gene namesi
Name:GAMT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:4136. GAMT.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.11 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201W → S in CCDS2. 2 Publications
VAR_058102
Natural varianti45 – 451W → R in CCDS2; loss of activity. 2 Publications
VAR_071777
Natural varianti50 – 501M → L in CCDS2; retains no significant activity. 2 Publications
VAR_058103
Natural varianti51 – 511H → P in CCDS2; retains no significant activity. 3 Publications
VAR_058104
Natural varianti54 – 541A → P in CCDS2; loss of activity. 2 Publications
VAR_058105
Natural varianti68 – 681G → C in CCDS2; retains no significant activity. 1 Publication
VAR_071778
Natural varianti75 – 751A → V in CCDS2; retains no significant activity. 1 Publication
VAR_071779
Natural varianti78 – 781V → E in CCDS2. 1 Publication
VAR_071780
Natural varianti110 – 1101V → F in CCDS2; retains no significant activity. 1 Publication
VAR_071781
Natural varianti135 – 1351D → N in CCDS2. 1 Publication
VAR_071782
Natural varianti147 – 1471H → Y in CCDS2; retains no significant activity. 1 Publication
VAR_071783
Natural varianti159 – 1591L → P in CCDS2; loss of activity. 1 Publication
VAR_071784
Natural varianti164 – 1641G → D in CCDS2. 1 Publication
VAR_071785
Natural varianti166 – 1661L → P in CCDS2; loss of activity. 2 Publications
VAR_071786
Natural varianti169 – 1691C → R in CCDS2. 1 Publication
VAR_071787
Natural varianti169 – 1691C → Y in CCDS2; retains no significant activity. 2 Publications
VAR_058106
Natural varianti197 – 1971L → P in CCDS2; loss of activity. 3 Publications
VAR_058107
Natural varianti208 – 2081R → P in CCDS2; retains no significant activity. 1 Publication
VAR_071788

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi612736. phenotype.
Orphaneti382. Guanidinoacetate methyltransferase deficiency.
PharmGKBiPA28549.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 236235Guanidinoacetate N-methyltransferasePRO_0000087430Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ14353.
PaxDbiQ14353.
PeptideAtlasiQ14353.
PRIDEiQ14353.

2D gel databases

OGPiQ14353.

PTM databases

PhosphoSiteiQ14353.

Expressioni

Tissue specificityi

Expressed in liver.1 Publication

Gene expression databases

BgeeiQ14353.
CleanExiHS_GAMT.
ExpressionAtlasiQ14353. baseline and differential.
GenevestigatoriQ14353.

Organism-specific databases

HPAiHPA051806.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi108865. 7 interactions.
IntActiQ14353. 2 interactions.
STRINGi9606.ENSP00000403536.

Structurei

Secondary structure

1
236
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 204Combined sources
Beta strandi25 – 273Combined sources
Beta strandi31 – 366Combined sources
Beta strandi39 – 435Combined sources
Helixi44 – 463Combined sources
Helixi47 – 5711Combined sources
Turni58 – 603Combined sources
Beta strandi62 – 676Combined sources
Helixi73 – 786Combined sources
Beta strandi83 – 908Combined sources
Helixi93 – 10210Combined sources
Helixi103 – 1053Combined sources
Beta strandi107 – 1159Combined sources
Helixi117 – 1204Combined sources
Helixi121 – 1233Combined sources
Beta strandi129 – 1346Combined sources
Helixi141 – 1433Combined sources
Turni144 – 1463Combined sources
Helixi147 – 1548Combined sources
Helixi156 – 1594Combined sources
Beta strandi160 – 1689Combined sources
Helixi171 – 1777Combined sources
Turni178 – 1814Combined sources
Helixi185 – 1928Combined sources
Helixi194 – 2007Combined sources
Helixi204 – 2063Combined sources
Beta strandi207 – 2137Combined sources
Beta strandi226 – 2349Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ORHX-ray1.86A/B/C/D1-236[»]
ProteinModelPortaliQ14353.
SMRiQ14353. Positions 7-236.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14353.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 236224RMT2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni69 – 746S-adenosyl-L-methionine binding
Regioni90 – 923S-adenosyl-L-methionine
Regioni117 – 1182S-adenosyl-L-methionine binding
Regioni171 – 1722Substrate binding

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family.PROSITE-ProRule annotation
Contains 1 RMT2 (arginine N-methyltransferase 2-like) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG235457.
GeneTreeiENSGT00390000018061.
HOGENOMiHOG000010290.
HOVERGENiHBG005801.
InParanoidiQ14353.
KOiK00542.
OMAiRYYAFPQ.
OrthoDBiEOG75QR4S.
PhylomeDBiQ14353.
TreeFamiTF328555.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR016550. GuanidinoAc_N-MeTrfase.
IPR026480. RMT2_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PIRSFiPIRSF009285. GAMT. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51559. SAM_RMT2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14353-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSAPSATPIF APGENCSPAW GAAPAAYDAA DTHLRILGKP VMERWETPYM
60 70 80 90 100
HALAAAASSK GGRVLEVGFG MAIAASKVQE APIDEHWIIE CNDGVFQRLR
110 120 130 140 150
DWAPRQTHKV IPLKGLWEDV APTLPDGHFD GILYDTYPLS EETWHTHQFN
160 170 180 190 200
FIKNHAFRLL KPGGVLTYCN LTSWGELMKS KYSDITIMFE ETQVPALLEA
210 220 230
GFRRENIRTE VMALVPPADC RYYAFPQMIT PLVTKG
Length:236
Mass (Da):26,318
Last modified:November 1, 1996 - v1
Checksum:i6B8E845CE56189F5
GO
Isoform 2 (identifier: Q14353-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     191-236: ETQVPALLEA...QMITPLVTKG → VRPPEVPHGS...TVEGRGGQIA

Note: No experimental confirmation available.

Show »
Length:269
Mass (Da):29,377
Checksum:iD04624287AE534A8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81P → T Rare polymorphism with no effect on activity. 1 Publication
VAR_071775
Natural varianti20 – 201W → S in CCDS2. 2 Publications
VAR_058102
Natural varianti27 – 271Y → H Polymorphism with no effect on activity. 1 Publication
VAR_071776
Natural varianti45 – 451W → R in CCDS2; loss of activity. 2 Publications
VAR_071777
Natural varianti50 – 501M → L in CCDS2; retains no significant activity. 2 Publications
VAR_058103
Natural varianti51 – 511H → P in CCDS2; retains no significant activity. 3 Publications
VAR_058104
Natural varianti54 – 541A → P in CCDS2; loss of activity. 2 Publications
VAR_058105
Natural varianti68 – 681G → C in CCDS2; retains no significant activity. 1 Publication
VAR_071778
Natural varianti75 – 751A → V in CCDS2; retains no significant activity. 1 Publication
VAR_071779
Natural varianti78 – 781V → E in CCDS2. 1 Publication
VAR_071780
Natural varianti110 – 1101V → F in CCDS2; retains no significant activity. 1 Publication
VAR_071781
Natural varianti135 – 1351D → N in CCDS2. 1 Publication
VAR_071782
Natural varianti147 – 1471H → Y in CCDS2; retains no significant activity. 1 Publication
VAR_071783
Natural varianti159 – 1591L → P in CCDS2; loss of activity. 1 Publication
VAR_071784
Natural varianti164 – 1641G → D in CCDS2. 1 Publication
VAR_071785
Natural varianti166 – 1661L → P in CCDS2; loss of activity. 2 Publications
VAR_071786
Natural varianti169 – 1691C → R in CCDS2. 1 Publication
VAR_071787
Natural varianti169 – 1691C → Y in CCDS2; retains no significant activity. 2 Publications
VAR_058106
Natural varianti197 – 1971L → P in CCDS2; loss of activity. 3 Publications
VAR_058107
Natural varianti208 – 2081R → P in CCDS2; retains no significant activity. 1 Publication
VAR_071788
Natural varianti209 – 2091T → M.1 Publication
Corresponds to variant rs17851582 [ dbSNP | Ensembl ].
VAR_025723

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei191 – 23646ETQVP…LVTKG → VRPPEVPHGSPGSDLGWGWE GAAGATLLPGEGPFLTPWVG WTVLVHLEIKVLCLAQWLPG AVAQVYNPSTVEGRGGQIA in isoform 2. 1 PublicationVSP_042722Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49878 mRNA. Translation: CAA90035.1.
AF010248, AF010246, AF010247 Genomic DNA. Translation: AAD04781.1.
AF188893 Genomic DNA. Translation: AAF01461.1.
BT007034 mRNA. Translation: AAP35682.1.
AK289465 mRNA. Translation: BAF82154.1.
AC005329 Genomic DNA. Translation: AAC27668.1.
CH471139 Genomic DNA. Translation: EAW69505.1.
BC016760 mRNA. Translation: AAH16760.1.
BC017936 mRNA. Translation: AAH17936.1.
CCDSiCCDS12064.1. [Q14353-1]
CCDS45897.1. [Q14353-2]
PIRiS62732.
RefSeqiNP_000147.1. NM_000156.5. [Q14353-1]
NP_620279.1. NM_138924.2. [Q14353-2]
UniGeneiHs.81131.

Genome annotation databases

EnsembliENST00000252288; ENSP00000252288; ENSG00000130005. [Q14353-1]
ENST00000447102; ENSP00000403536; ENSG00000130005. [Q14353-2]
GeneIDi2593.
KEGGihsa:2593.
UCSCiuc002lsj.4. human. [Q14353-1]
uc002lsk.4. human. [Q14353-2]

Polymorphism databases

DMDMi2498404.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49878 mRNA. Translation: CAA90035.1 .
AF010248 , AF010246 , AF010247 Genomic DNA. Translation: AAD04781.1 .
AF188893 Genomic DNA. Translation: AAF01461.1 .
BT007034 mRNA. Translation: AAP35682.1 .
AK289465 mRNA. Translation: BAF82154.1 .
AC005329 Genomic DNA. Translation: AAC27668.1 .
CH471139 Genomic DNA. Translation: EAW69505.1 .
BC016760 mRNA. Translation: AAH16760.1 .
BC017936 mRNA. Translation: AAH17936.1 .
CCDSi CCDS12064.1. [Q14353-1 ]
CCDS45897.1. [Q14353-2 ]
PIRi S62732.
RefSeqi NP_000147.1. NM_000156.5. [Q14353-1 ]
NP_620279.1. NM_138924.2. [Q14353-2 ]
UniGenei Hs.81131.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ORH X-ray 1.86 A/B/C/D 1-236 [» ]
ProteinModelPortali Q14353.
SMRi Q14353. Positions 7-236.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108865. 7 interactions.
IntActi Q14353. 2 interactions.
STRINGi 9606.ENSP00000403536.

Chemistry

DrugBanki DB00148. Creatine.
DB00536. Guanidine.

PTM databases

PhosphoSitei Q14353.

Polymorphism databases

DMDMi 2498404.

2D gel databases

OGPi Q14353.

Proteomic databases

MaxQBi Q14353.
PaxDbi Q14353.
PeptideAtlasi Q14353.
PRIDEi Q14353.

Protocols and materials databases

DNASUi 2593.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252288 ; ENSP00000252288 ; ENSG00000130005 . [Q14353-1 ]
ENST00000447102 ; ENSP00000403536 ; ENSG00000130005 . [Q14353-2 ]
GeneIDi 2593.
KEGGi hsa:2593.
UCSCi uc002lsj.4. human. [Q14353-1 ]
uc002lsk.4. human. [Q14353-2 ]

Organism-specific databases

CTDi 2593.
GeneCardsi GC19M001397.
GeneReviewsi GAMT.
H-InvDB HIX0030201.
HGNCi HGNC:4136. GAMT.
HPAi HPA051806.
MIMi 601240. gene.
612736. phenotype.
neXtProti NX_Q14353.
Orphaneti 382. Guanidinoacetate methyltransferase deficiency.
PharmGKBi PA28549.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG235457.
GeneTreei ENSGT00390000018061.
HOGENOMi HOG000010290.
HOVERGENi HBG005801.
InParanoidi Q14353.
KOi K00542.
OMAi RYYAFPQ.
OrthoDBi EOG75QR4S.
PhylomeDBi Q14353.
TreeFami TF328555.

Enzyme and pathway databases

UniPathwayi UPA00104 ; UER00580 .
BioCyci MetaCyc:HS05327-MONOMER.
BRENDAi 2.1.1.2. 2681.
Reactomei REACT_813. Creatine metabolism.

Miscellaneous databases

EvolutionaryTracei Q14353.
GeneWikii Guanidinoacetate_N-methyltransferase.
GenomeRNAii 2593.
NextBioi 10257.
PROi Q14353.
SOURCEi Search...

Gene expression databases

Bgeei Q14353.
CleanExi HS_GAMT.
ExpressionAtlasi Q14353. baseline and differential.
Genevestigatori Q14353.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR016550. GuanidinoAc_N-MeTrfase.
IPR026480. RMT2_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PIRSFi PIRSF009285. GAMT. 1 hit.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51559. SAM_RMT2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of human guanidinoacetate N-methyltransferase cDNA."
    Isbrandt D., von Figura K.
    Biochim. Biophys. Acta 1264:265-267(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "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."
    Jenne D.E., Olsen A.S., Zimmer M.
    Biochem. Biophys. Res. Commun. 238:723-727(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Gene structure of human guanidinoacetate N-methyltransferase."
    Isbrandt D., Schmidt A.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    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.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Cerebellum.
  6. "The DNA sequence and biology of human chromosome 19."
    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.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-209.
    Tissue: Lymph and Skeletal muscle.
  9. "Guanidinoacetate methyltransferase deficiency: the first inborn error of creatine metabolism in man."
    Stoeckler S., Isbrandt D., Hanefeld F., Schmidt B., von Figura K.
    Am. J. Hum. Genet. 58:914-922(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INVOLVEMENT IN CCDS2.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "The crystal structure of human guanidinoacetate N-methyltransferase with SAH."
    Structural genomics consortium (SGC)
    Submitted (MAR-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.
  13. "Creatine depletion in a new case with AGAT deficiency: clinical and genetic study in a large pedigree."
    Battini R., Leuzzi V., Carducci C., Tosetti M., Bianchi M.C., Item C.B., Stoeckler-Ipsiroglu S., Cioni G.
    Mol. Genet. Metab. 77:326-331(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CCDS2 PRO-197.
  14. Cited for: VARIANTS CCDS2 SER-20; PRO-51 AND PRO-54.
  15. "Guanidinoacetate methyltransferase deficiency identified in adults and a child with mental retardation."
    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.
    Am. J. Med. Genet. A 133:122-127(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CCDS2 SER-20 AND TYR-169.
  16. "A mutation on exon 6 of guanidinoacetate methyltransferase (GAMT) gene supports a different function for isoform a and b of GAMT enzyme."
    Leuzzi V., Carducci C., Carducci C., Matricardi M., Bianchi M.C., Di Sabato M.L., Artiola C., Antonozzi I.
    Mol. Genet. Metab. 87:88-90(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CCDS2 PRO-197.
  17. Cited for: VARIANT CCDS2 PRO-51.
  18. Cited for: VARIANT CCDS2 LEU-50.
  19. "Successful treatment of a guanidinoacetate methyltransferase deficient patient: findings with relevance to treatment strategy and pathophysiology."
    Verbruggen K.T., Sijens P.E., Schulze A., Lunsing R.J., Jakobs C., Salomons G.S., van Spronsen F.J.
    Mol. Genet. Metab. 91:294-296(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CCDS2 PRO-166.
  20. "Guanidinoacetate methyltransferase (GAMT) deficiency: late onset of movement disorder and preserved expressive language."
    O'Rourke D.J., Ryan S., Salomons G., Jakobs C., Monavari A., King M.D.
    Dev. Med. Child. Neurol. 51:404-407(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CCDS2 ASN-135.
  21. "Biochemical, molecular, and clinical diagnoses of patients with cerebral creatine deficiency syndromes."
    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.
    Mol. Genet. Metab. 109:260-268(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CCDS2 ARG-45; GLU-78; ASP-164 AND ARG-169.
  22. "Thirteen new patients with guanidinoacetate methyltransferase deficiency and functional characterization of nineteen novel missense variants in the GAMT gene."
    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.
    Hum. Mutat. 35:462-469(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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.

Entry informationi

Entry nameiGAMT_HUMAN
AccessioniPrimary (citable) accession number: Q14353
Secondary accession number(s): A8K0A0, Q53Y34, Q8WVJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

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