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Q14353

- GAMT_HUMAN

UniProt

Q14353 - GAMT_HUMAN

Protein

Guanidinoacetate N-methyltransferase

Gene

GAMT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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

    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.6 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 varianti50 – 501M → L in CCDS2. 1 Publication
    VAR_058103
    Natural varianti51 – 511H → P in CCDS2. 1 Publication
    VAR_058104
    Natural varianti54 – 541A → P in CCDS2. 1 Publication
    VAR_058105
    Natural varianti169 – 1691C → Y in CCDS2. 1 Publication
    VAR_058106
    Natural varianti197 – 1971L → P in CCDS2; unknown pathological significance. 2 Publications
    VAR_058107

    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.
    GenevestigatoriQ14353.

    Organism-specific databases

    HPAiHPA051806.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi108865. 6 interactions.
    IntActiQ14353. 2 interactions.
    STRINGi9606.ENSP00000403536.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MSAPSATPIF APGENCSPAW GAAPAAYDAA DTHLRILGKP VMERWETPYM    50
    HALAAAASSK GGRVLEVGFG MAIAASKVQE APIDEHWIIE CNDGVFQRLR 100
    DWAPRQTHKV IPLKGLWEDV APTLPDGHFD GILYDTYPLS EETWHTHQFN 150
    FIKNHAFRLL KPGGVLTYCN LTSWGELMKS KYSDITIMFE ETQVPALLEA 200
    GFRRENIRTE VMALVPPADC RYYAFPQMIT PLVTKG 236
    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 varianti20 – 201W → S in CCDS2. 2 Publications
    VAR_058102
    Natural varianti50 – 501M → L in CCDS2. 1 Publication
    VAR_058103
    Natural varianti51 – 511H → P in CCDS2. 1 Publication
    VAR_058104
    Natural varianti54 – 541A → P in CCDS2. 1 Publication
    VAR_058105
    Natural varianti169 – 1691C → Y in CCDS2. 1 Publication
    VAR_058106
    Natural varianti197 – 1971L → P in CCDS2; unknown pathological significance. 2 Publications
    VAR_058107
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 6 interactions.
    IntActi Q14353. 2 interactions.
    STRINGi 9606.ENSP00000403536.

    Chemistry

    DrugBanki DB00148. Creatine.

    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.
    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.
    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

    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 LEU-50.

    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: October 1, 2014
    This is version 143 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

    Dasty 3