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P50440

- GATM_HUMAN

UniProt

P50440 - GATM_HUMAN

Protein

Glycine amidinotransferase, mitochondrial

Gene

GATM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central nervous system development. May be involved in the response to heart failure by elevating local creatine synthesis.3 Publications

    Catalytic activityi

    L-arginine + glycine = L-ornithine + guanidinoacetate.1 Publication

    Kineticsi

    1. KM=2.0 µM for arginine2 Publications
    2. KM=3.0 µM for glycine2 Publications

    Vmax=0.44 µmol/min/mg enzyme2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei254 – 2541
    Active sitei303 – 3031
    Active sitei407 – 4071Amidino-cysteine intermediate1 Publication

    GO - Molecular functioni

    1. glycine amidinotransferase activity Source: MGI
    2. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines Source: InterPro

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. creatine biosynthetic process Source: MGI
    3. creatine metabolic process Source: Reactome
    4. embryo development Source: Ensembl
    5. response to mercury ion Source: Ensembl
    6. response to nutrient Source: Ensembl
    7. response to oxidative stress Source: Ensembl
    8. response to peptide hormone Source: Ensembl
    9. small molecule metabolic process Source: Reactome
    10. tissue regeneration Source: Ensembl

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS10376-MONOMER.
    BRENDAi2.1.4.1. 2681.
    ReactomeiREACT_813. Creatine metabolism.
    UniPathwayiUPA00104; UER00579.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycine amidinotransferase, mitochondrial (EC:2.1.4.1)
    Alternative name(s):
    L-arginine:glycine amidinotransferase
    Transamidinase
    Gene namesi
    Name:GATM
    Synonyms:AGAT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:4175. GATM.

    Subcellular locationi

    Isoform 1 : Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side
    Note: Probably attached to the outer side of the inner membrane.

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial inner membrane Source: UniProtKB-SubCell
    3. mitochondrial intermembrane space Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Involvement in diseasei

    Cerebral creatine deficiency syndrome 3 (CCDS3) [MIM:612718]: An autosomal recessive disorder characterized by developmental delay/regression, mental retardation, severe disturbance of expressive and cognitive speech, and severe depletion of creatine/phosphocreatine in the brain. Most patients develop a myopathy characterized by muscle weakness and atrophy later in life.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti203 – 2031Y → S in CCDS3. 1 Publication
    VAR_069816

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi170 – 1701D → N: Complete loss of activity. 1 Publication
    Mutagenesisi233 – 2331E → K: Complete loss of activity; when associated with S-407. 1 Publication
    Mutagenesisi254 – 2541D → N: Significantly reduced activity. 1 Publication
    Mutagenesisi303 – 3031H → V: Complete loss of activity. 1 Publication
    Mutagenesisi305 – 3051D → A: Complete loss of activity. 1 Publication
    Mutagenesisi322 – 3221R → E: Significantly reduced activity. 1 Publication
    Mutagenesisi355 – 3551S → A: Significantly reduced activity. 1 Publication
    Mutagenesisi407 – 4071C → S: Complete loss of activity; when associated with K-233. 1 Publication
    Mutagenesisi410 – 4101C → A: No effect on activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi612718. phenotype.
    Orphaneti35704. Arginine:glycine amidinotransferase deficiency.
    PharmGKBiPA28590.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3737MitochondrionBy similarityAdd
    BLAST
    Chaini38 – 423386Glycine amidinotransferase, mitochondrialPRO_0000001206Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei385 – 3851N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP50440.
    PaxDbiP50440.
    PRIDEiP50440.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00032103.

    PTM databases

    PhosphoSiteiP50440.

    Expressioni

    Tissue specificityi

    Expressed in brain, heart, kidney, liver, lung, salivary gland and skeletal muscle tissue, with the highest expression in kidney. Biallelically expressed in placenta and fetal tissues.3 Publications

    Inductioni

    Expression is elevated in the myocardium during heart failure, and decreased in inter-uterine growth restriction (IUGR)-associated placenta.2 Publications

    Gene expression databases

    ArrayExpressiP50440.
    BgeeiP50440.
    CleanExiHS_GATM.
    GenevestigatoriP50440.

    Organism-specific databases

    HPAiHPA026077.

    Interactioni

    Subunit structurei

    Homodimer. There is an equilibrium between the monomeric and dimeric forms, shifted towards the side of the monomer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GatmQ9D9641EBI-2552594,EBI-2552599From a different organism.

    Protein-protein interaction databases

    BioGridi108898. 2 interactions.
    IntActiP50440. 7 interactions.
    STRINGi9606.ENSP00000379895.

    Structurei

    Secondary structure

    1
    423
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi70 – 734
    Beta strandi75 – 806
    Helixi93 – 964
    Helixi101 – 1033
    Helixi104 – 1107
    Beta strandi113 – 1153
    Helixi117 – 13620
    Beta strandi140 – 1423
    Beta strandi152 – 1543
    Beta strandi159 – 1613
    Helixi168 – 1714
    Beta strandi172 – 1765
    Beta strandi178 – 1814
    Helixi187 – 1893
    Helixi192 – 1954
    Helixi197 – 2059
    Beta strandi209 – 2124
    Helixi220 – 2223
    Helixi232 – 2409
    Beta strandi248 – 2503
    Helixi255 – 2573
    Beta strandi258 – 2614
    Beta strandi264 – 2674
    Helixi275 – 28511
    Turni286 – 2883
    Beta strandi290 – 2934
    Beta strandi296 – 2983
    Turni305 – 3073
    Beta strandi308 – 3125
    Beta strandi315 – 3184
    Helixi327 – 3326
    Beta strandi336 – 3383
    Beta strandi352 – 3543
    Helixi356 – 3605
    Beta strandi363 – 3664
    Beta strandi369 – 3735
    Helixi377 – 3859
    Beta strandi389 – 3935
    Helixi396 – 3994
    Turni400 – 4023
    Turni405 – 4084
    Beta strandi409 – 4157

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JDWX-ray1.90A1-423[»]
    1JDXX-ray2.40A38-423[»]
    2JDWX-ray2.10A1-423[»]
    2JDXX-ray2.90A38-423[»]
    3JDWX-ray2.40A1-423[»]
    4JDWX-ray2.50A1-423[»]
    5JDWX-ray2.60A38-423[»]
    6JDWX-ray2.50A38-423[»]
    7JDWX-ray2.37A38-423[»]
    8JDWX-ray2.30A38-423[»]
    9JDWX-ray2.50A38-423[»]
    DisProtiDP00099.
    ProteinModelPortaliP50440.
    SMRiP50440. Positions 64-423.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50440.

    Family & Domainsi

    Domaini

    One chain folds into a compact single domain composed of repeating units, five beta-beta-alpha-beta modules, which surround the central active site.

    Sequence similaritiesi

    Belongs to the amidinotransferase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1834.
    HOGENOMiHOG000231593.
    HOVERGENiHBG002492.
    InParanoidiP50440.
    KOiK00613.
    OMAiRPCHQID.
    OrthoDBiEOG712TW4.
    PhylomeDBiP50440.
    TreeFamiTF300256.

    Family and domain databases

    InterProiIPR003198. Amidino_trans.
    [Graphical view]
    PfamiPF02274. Amidinotransf. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P50440-1) [UniParc]FASTAAdd to Basket

    Also known as: Mitochondrial

    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

    MLRVRCLRGG SRGAEAVHYI GSRLGRTLTG WVQRTFQSTQ AATASSRNSC    50
    AADDKATEPL PKDCPVSSYN EWDPLEEVIV GRAENACVPP FTIEVKANTY 100
    EKYWPFYQKQ GGHYFPKDHL KKAVAEIEEM CNILKTEGVT VRRPDPIDWS 150
    LKYKTPDFES TGLYSAMPRD ILIVVGNEII EAPMAWRSRF FEYRAYRSII 200
    KDYFHRGAKW TTAPKPTMAD ELYNQDYPIH SVEDRHKLAA QGKFVTTEFE 250
    PCFDAADFIR AGRDIFAQRS QVTNYLGIEW MRRHLAPDYR VHIISFKDPN 300
    PMHIDATFNI IGPGIVLSNP DRPCHQIDLF KKAGWTIITP PTPIIPDDHP 350
    LWMSSKWLSM NVLMLDEKRV MVDANEVPIQ KMFEKLGITT IKVNIRNANS 400
    LGGGFHCWTC DVRRRGTLQS YLD 423
    Length:423
    Mass (Da):48,455
    Last modified:October 1, 1996 - v1
    Checksum:i5BEF7A8A039B70FB
    GO
    Isoform 2 (identifier: P50440-2) [UniParc]FASTAAdd to Basket

    Also known as: Cytoplasmic

    The sequence of this isoform differs from the canonical sequence as follows:
         1-37: MLRVRCLRGGSRGAEAVHYIGSRLGRTLTGWVQRTFQ → MNILK

    Show »
    Length:391
    Mass (Da):44,883
    Checksum:iDA7E75BB41D91528
    GO
    Isoform 3 (identifier: P50440-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         388-423: ITTIKVNIRNANSLGGGFHCWTCDVRRRGTLQSYLD → MYNK

    Show »
    Length:391
    Mass (Da):44,943
    Checksum:i692D75D4BCD1B990
    GO

    Sequence cautioni

    The sequence BAG60595.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 981N → I in BAG60595. (PubMed:14702039)Curated
    Sequence conflicti246 – 2461T → I in BAG60595. (PubMed:14702039)Curated
    Sequence conflicti384 – 3841E → G in BAG58060. (PubMed:14702039)Curated
    Sequence conflicti395 – 3951I → V in BAG60595. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti110 – 1101Q → H.1 Publication
    Corresponds to variant rs1288775 [ dbSNP | Ensembl ].
    VAR_020305
    Natural varianti203 – 2031Y → S in CCDS3. 1 Publication
    VAR_069816

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3737MLRVR…QRTFQ → MNILK in isoform 2. 1 PublicationVSP_000235Add
    BLAST
    Alternative sequencei388 – 42336ITTIK…QSYLD → MYNK in isoform 3. 1 PublicationVSP_039871Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S68805 mRNA. Translation: AAB29892.1.
    X86401 mRNA. Translation: CAA60153.1.
    AK294995 mRNA. Translation: BAG58060.1.
    AK298350 mRNA. Translation: BAG60595.1. Different initiation.
    AK223585 mRNA. Translation: BAD97305.1.
    AC025580 Genomic DNA. No translation available.
    BC004141 mRNA. Translation: AAH04141.1.
    CCDSiCCDS10122.1. [P50440-1]
    PIRiS41734.
    S54161.
    RefSeqiNP_001473.1. NM_001482.2. [P50440-1]
    UniGeneiHs.75335.

    Genome annotation databases

    EnsembliENST00000396659; ENSP00000379895; ENSG00000171766. [P50440-1]
    ENST00000558336; ENSP00000454008; ENSG00000171766. [P50440-3]
    GeneIDi2628.
    KEGGihsa:2628.
    UCSCiuc001zvb.3. human. [P50440-1]
    uc010uev.1. human. [P50440-3]

    Polymorphism databases

    DMDMi1730201.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S68805 mRNA. Translation: AAB29892.1 .
    X86401 mRNA. Translation: CAA60153.1 .
    AK294995 mRNA. Translation: BAG58060.1 .
    AK298350 mRNA. Translation: BAG60595.1 . Different initiation.
    AK223585 mRNA. Translation: BAD97305.1 .
    AC025580 Genomic DNA. No translation available.
    BC004141 mRNA. Translation: AAH04141.1 .
    CCDSi CCDS10122.1. [P50440-1 ]
    PIRi S41734.
    S54161.
    RefSeqi NP_001473.1. NM_001482.2. [P50440-1 ]
    UniGenei Hs.75335.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JDW X-ray 1.90 A 1-423 [» ]
    1JDX X-ray 2.40 A 38-423 [» ]
    2JDW X-ray 2.10 A 1-423 [» ]
    2JDX X-ray 2.90 A 38-423 [» ]
    3JDW X-ray 2.40 A 1-423 [» ]
    4JDW X-ray 2.50 A 1-423 [» ]
    5JDW X-ray 2.60 A 38-423 [» ]
    6JDW X-ray 2.50 A 38-423 [» ]
    7JDW X-ray 2.37 A 38-423 [» ]
    8JDW X-ray 2.30 A 38-423 [» ]
    9JDW X-ray 2.50 A 38-423 [» ]
    DisProti DP00099.
    ProteinModelPortali P50440.
    SMRi P50440. Positions 64-423.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108898. 2 interactions.
    IntActi P50440. 7 interactions.
    STRINGi 9606.ENSP00000379895.

    Chemistry

    DrugBanki DB00145. Glycine.
    DB00129. L-Ornithine.

    PTM databases

    PhosphoSitei P50440.

    Polymorphism databases

    DMDMi 1730201.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00032103.

    Proteomic databases

    MaxQBi P50440.
    PaxDbi P50440.
    PRIDEi P50440.

    Protocols and materials databases

    DNASUi 2628.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000396659 ; ENSP00000379895 ; ENSG00000171766 . [P50440-1 ]
    ENST00000558336 ; ENSP00000454008 ; ENSG00000171766 . [P50440-3 ]
    GeneIDi 2628.
    KEGGi hsa:2628.
    UCSCi uc001zvb.3. human. [P50440-1 ]
    uc010uev.1. human. [P50440-3 ]

    Organism-specific databases

    CTDi 2628.
    GeneCardsi GC15M045653.
    GeneReviewsi GATM.
    HGNCi HGNC:4175. GATM.
    HPAi HPA026077.
    MIMi 602360. gene.
    612718. phenotype.
    neXtProti NX_P50440.
    Orphaneti 35704. Arginine:glycine amidinotransferase deficiency.
    PharmGKBi PA28590.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1834.
    HOGENOMi HOG000231593.
    HOVERGENi HBG002492.
    InParanoidi P50440.
    KOi K00613.
    OMAi RPCHQID.
    OrthoDBi EOG712TW4.
    PhylomeDBi P50440.
    TreeFami TF300256.

    Enzyme and pathway databases

    UniPathwayi UPA00104 ; UER00579 .
    BioCyci MetaCyc:HS10376-MONOMER.
    BRENDAi 2.1.4.1. 2681.
    Reactomei REACT_813. Creatine metabolism.

    Miscellaneous databases

    ChiTaRSi GATM. human.
    EvolutionaryTracei P50440.
    GeneWikii GATM_(gene).
    GenomeRNAii 2628.
    NextBioi 10353.
    PROi P50440.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50440.
    Bgeei P50440.
    CleanExi HS_GATM.
    Genevestigatori P50440.

    Family and domain databases

    InterProi IPR003198. Amidino_trans.
    [Graphical view ]
    Pfami PF02274. Amidinotransf. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The amino acid sequences of human and pig L-arginine:glycine amidinotransferase."
      Humm A., Huber R., Mann K.
      FEBS Lett. 339:101-107(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Kidney.
    2. "Characterization of the human cDNA with partial homology with the gamma subunit of sodium potassium ATPase of rat, mouse, rabbit and sheep."
      Austruy E., Belley L., Millasot P., Junien C., Jeanpierre C.
      Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Kidney.
    3. "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] (ISOFORMS 1 AND 3).
      Tissue: Brain and Kidney.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-110.
      Tissue: Kidney.
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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).
      Tissue: Muscle.
    7. "The purification and characterization of human kidney L-arginine:glycine amidinotransferase."
      Gross M.D., Eggen M.A., Simon A.M., Van Pilsum J.F.
      Arch. Biochem. Biophys. 251:747-755(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    8. "Recombinant expression and isolation of human L-arginine:glycine amidinotransferase and identification of its active-site cysteine residue."
      Humm A., Fritsche E., Mann K., Goehl U., Huber R.
      Biochem. J. 322:771-776(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE CYS-407.
    9. "Structure and reaction mechanism of L-arginine:glycine amidinotransferase."
      Humm A., Fritsche E., Steinbacher S.
      Biol. Chem. 378:193-197(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    10. "Myocardial expression of the arginine:glycine amidinotransferase gene is elevated in heart failure and normalized after recovery: potential implications for local creatine synthesis."
      Cullen M.E., Yuen A.H., Felkin L.E., Smolenski R.T., Hall J.L., Grindle S., Miller L.W., Birks E.J., Yacoub M.H., Barton P.J.
      Circulation 114:I16-I20(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    11. "Unbalanced placental expression of imprinted genes in human intrauterine growth restriction."
      McMinn J., Wei M., Schupf N., Cusmai J., Johnson E.B., Smith A.C., Weksberg R., Thaker H.M., Tycko B.
      Placenta 27:540-549(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    12. Cited for: FUNCTION, TISSUE SPECIFICITY.
    13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "l-arginine:glycine amidinotransferase (AGAT) deficiency: clinical presentation and response to treatment in two patients with a novel mutation."
      Edvardson S., Korman S.H., Livne A., Shaag A., Saada A., Nalbandian R., Allouche-Arnon H., Gomori J.M., Katz-Brull R.
      Mol. Genet. Metab. 101:228-232(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CCDS3.
    15. "Developmental progress and creatine restoration upon long-term creatine supplementation of a patient with arginine:glycine amidinotransferase deficiency."
      Ndika J.D., Johnston K., Barkovich J.A., Wirt M.D., O'Neill P., Betsalel O.T., Jakobs C., Salomons G.S.
      Mol. Genet. Metab. 106:48-54(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CCDS3.
    16. "Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis."
      Humm A., Fritsche E., Steinbacher S., Huber R.
      EMBO J. 16:3373-3385(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 38-423.
      Tissue: Kidney.
    17. "Substrate binding and catalysis by L-arginine:glycine amidinotransferase -- a mutagenesis and crystallographic study."
      Fritsche E., Humm A., Huber R.
      Eur. J. Biochem. 247:483-490(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF MUTANTS ASN-170; ASN-254 AND SER-407, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, MUTAGENESIS OF ASP-170; GLU-233; ASP-254; HIS-303; ASP-305; ARG-322; SER-355; CYS-407 AND CYS-410.
    18. "The ligand-induced structural changes of human L-arginine:glycine amidinotransferase. A mutational and crystallographic study."
      Fritsche E., Humm A., Huber R.
      J. Biol. Chem. 274:3026-3032(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 38-423.
    19. "Arginine:glycine amidinotransferase deficiency: the third inborn error of creatine metabolism in humans."
      Item C.B., Stockler-Ipsiroglu S., Stromberger C., Muhl A., Alessandri M.G., Bianchi M.C., Tosetti M., Fornai F., Cioni G.
      Am. J. Hum. Genet. 69:1127-1133(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CCDS3.
    20. "Creatine deficiency syndrome. A treatable myopathy due to arginine-glycine amidinotransferase (AGAT) deficiency."
      Nouioua S., Cheillan D., Zaouidi S., Salomons G.S., Amedjout N., Kessaci F., Boulahdour N., Hamadouche T., Tazir M.
      Neuromuscul. Disord. 23:670-674(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CCDS3 SER-203.

    Entry informationi

    Entry nameiGATM_HUMAN
    AccessioniPrimary (citable) accession number: P50440
    Secondary accession number(s): B4DH99, B4DPI3, Q53EQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 156 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 15
      Human chromosome 15: 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