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Protein

Glycine amidinotransferase, mitochondrial

Gene

GATM

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

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. response to mercury ion Source: Ensembl
  5. response to nutrient Source: Ensembl
  6. response to oxidative stress Source: Ensembl
  7. response to peptide hormone Source: Ensembl
  8. small molecule metabolic process Source: Reactome
  9. tissue regeneration Source: Ensembl
Complete GO annotation...

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: UniProtKB
  2. mitochondrial inner membrane Source: UniProtKB-SubCell
  3. mitochondrial intermembrane space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Cerebral creatine deficiency syndrome 35 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:612718
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti203 – 2031Y → S in CCDS3. 1 Publication
VAR_069816
Natural varianti413 – 4131R → Q in CCDS3. 1 Publication
VAR_071789
Natural varianti413 – 4131R → W in CCDS3. 1 Publication
VAR_071790

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 residuei46 – 461Phosphoserine1 Publication
Modified residuei49 – 491Phosphoserine1 Publication
Modified residuei385 – 3851N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

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

BgeeiP50440.
CleanExiHS_GATM.
ExpressionAtlasiP50440. baseline and differential.
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 – 734Combined sources
Beta strandi75 – 806Combined sources
Helixi93 – 964Combined sources
Helixi101 – 1033Combined sources
Helixi104 – 1107Combined sources
Beta strandi113 – 1153Combined sources
Helixi117 – 13620Combined sources
Beta strandi140 – 1423Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi159 – 1613Combined sources
Helixi168 – 1714Combined sources
Beta strandi172 – 1765Combined sources
Beta strandi178 – 1814Combined sources
Helixi187 – 1893Combined sources
Helixi192 – 1954Combined sources
Helixi197 – 2059Combined sources
Beta strandi209 – 2124Combined sources
Helixi220 – 2223Combined sources
Helixi232 – 2409Combined sources
Beta strandi248 – 2503Combined sources
Helixi255 – 2573Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi264 – 2674Combined sources
Helixi275 – 28511Combined sources
Turni286 – 2883Combined sources
Beta strandi290 – 2934Combined sources
Beta strandi296 – 2983Combined sources
Turni305 – 3073Combined sources
Beta strandi308 – 3125Combined sources
Beta strandi315 – 3184Combined sources
Helixi327 – 3326Combined sources
Beta strandi336 – 3383Combined sources
Beta strandi352 – 3543Combined sources
Helixi356 – 3605Combined sources
Beta strandi363 – 3664Combined sources
Beta strandi369 – 3735Combined sources
Helixi377 – 3859Combined sources
Beta strandi389 – 3935Combined sources
Helixi396 – 3994Combined sources
Turni400 – 4023Combined sources
Turni405 – 4084Combined sources
Beta strandi409 – 4157Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000011613.
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. AlignAdd to basket

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

        10         20         30         40         50
MLRVRCLRGG SRGAEAVHYI GSRLGRTLTG WVQRTFQSTQ AATASSRNSC
60 70 80 90 100
AADDKATEPL PKDCPVSSYN EWDPLEEVIV GRAENACVPP FTIEVKANTY
110 120 130 140 150
EKYWPFYQKQ GGHYFPKDHL KKAVAEIEEM CNILKTEGVT VRRPDPIDWS
160 170 180 190 200
LKYKTPDFES TGLYSAMPRD ILIVVGNEII EAPMAWRSRF FEYRAYRSII
210 220 230 240 250
KDYFHRGAKW TTAPKPTMAD ELYNQDYPIH SVEDRHKLAA QGKFVTTEFE
260 270 280 290 300
PCFDAADFIR AGRDIFAQRS QVTNYLGIEW MRRHLAPDYR VHIISFKDPN
310 320 330 340 350
PMHIDATFNI IGPGIVLSNP DRPCHQIDLF KKAGWTIITP PTPIIPDDHP
360 370 380 390 400
LWMSSKWLSM NVLMLDEKRV MVDANEVPIQ KMFEKLGITT IKVNIRNANS
410 420
LGGGFHCWTC DVRRRGTLQS YLD
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.Curated

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
Natural varianti413 – 4131R → Q in CCDS3. 1 Publication
VAR_071789
Natural varianti413 – 4131R → W in CCDS3. 1 Publication
VAR_071790

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:
EMBLi
GenBanki
DDBJi
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.560354.
Hs.729565.
Hs.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:
EMBLi
GenBanki
DDBJi
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.560354.
Hs.729565.
Hs.75335.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Chemistry

DrugBankiDB00145. Glycine.
DB00129. L-Ornithine.

PTM databases

PhosphoSiteiP50440.

Polymorphism databases

DMDMi1730201.

2D gel databases

REPRODUCTION-2DPAGEIPI00032103.

Proteomic databases

MaxQBiP50440.
PaxDbiP50440.
PRIDEiP50440.

Protocols and materials databases

DNASUi2628.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi2628.
GeneCardsiGC15M045653.
GeneReviewsiGATM.
HGNCiHGNC:4175. GATM.
HPAiHPA026077.
MIMi602360. gene.
612718. phenotype.
neXtProtiNX_P50440.
Orphaneti35704. Arginine:glycine amidinotransferase deficiency.
PharmGKBiPA28590.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1834.
GeneTreeiENSGT00390000011613.
HOGENOMiHOG000231593.
HOVERGENiHBG002492.
InParanoidiP50440.
KOiK00613.
OMAiRPCHQID.
OrthoDBiEOG712TW4.
PhylomeDBiP50440.
TreeFamiTF300256.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiGATM. human.
EvolutionaryTraceiP50440.
GeneWikiiGATM_(gene).
GenomeRNAii2628.
NextBioi10353.
PROiP50440.
SOURCEiSearch...

Gene expression databases

BgeeiP50440.
CleanExiHS_GATM.
ExpressionAtlasiP50440. baseline and differential.
GenevestigatoriP50440.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  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 CCDS3 GLN-413 AND TRP-413.
  22. "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: March 4, 2015
This is version 159 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.