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P50440 (GATM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycine amidinotransferase, mitochondrial

EC=2.1.4.1
Alternative name(s):
L-arginine:glycine amidinotransferase
Transamidinase
Gene names
Name:GATM
Synonyms:AGAT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11 Ref.12

Catalytic activity

L-arginine + glycine = L-ornithine + guanidinoacetate. Ref.7

Pathway

Amine and polyamine biosynthesis; creatine biosynthesis; creatine from L-arginine and glycine: step 1/2.

Subunit structure

Homodimer. There is an equilibrium between the monomeric and dimeric forms, shifted towards the side of the monomer. Ref.7

Subcellular location

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

Isoform 2: Cytoplasm.

Tissue specificity

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. Ref.10 Ref.11 Ref.12

Induction

Expression is elevated in the myocardium during heart failure, and decreased in inter-uterine growth restriction (IUGR)-associated placenta. Ref.10 Ref.11

Domain

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15 Ref.19 Ref.20

Sequence similarities

Belongs to the amidinotransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=2.0 µM for arginine Ref.7 Ref.17

KM=3.0 µM for glycine

Vmax=0.44 µmol/min/mg enzyme

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   Molecular functionTransferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

creatine biosynthetic process

Inferred from direct assay Ref.16. Source: MGI

creatine metabolic process

Traceable author statement. Source: Reactome

embryo development

Inferred from electronic annotation. Source: Ensembl

response to mercury ion

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

tissue regeneration

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial intermembrane space

Inferred from direct assay Ref.16. Source: MGI

   Molecular_functionglycine amidinotransferase activity

Inferred from direct assay Ref.16. Source: MGI

hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GatmQ9D9641EBI-2552594,EBI-2552599From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P50440-1)

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.
Isoform 2 (identifier: P50440-2)

Also known as: Cytoplasmic;

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MLRVRCLRGGSRGAEAVHYIGSRLGRTLTGWVQRTFQ → MNILK
Isoform 3 (identifier: P50440-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Mitochondrion By similarity
Chain38 – 423386Glycine amidinotransferase, mitochondrial
PRO_0000001206

Sites

Active site2541
Active site3031
Active site4071Amidino-cysteine intermediate Ref.8

Amino acid modifications

Modified residue3851N6-acetyllysine Ref.13

Natural variations

Alternative sequence1 – 3737MLRVR…QRTFQ → MNILK in isoform 2.
VSP_000235
Alternative sequence388 – 42336ITTIK…QSYLD → MYNK in isoform 3.
VSP_039871
Natural variant1101Q → H. Ref.4
Corresponds to variant rs1288775 [ dbSNP | Ensembl ].
VAR_020305
Natural variant2031Y → S in CCDS3. Ref.20
VAR_069816

Experimental info

Mutagenesis1701D → N: Complete loss of activity. Ref.17
Mutagenesis2331E → K: Complete loss of activity; when associated with S-407. Ref.17
Mutagenesis2541D → N: Significantly reduced activity. Ref.17
Mutagenesis3031H → V: Complete loss of activity. Ref.17
Mutagenesis3051D → A: Complete loss of activity. Ref.17
Mutagenesis3221R → E: Significantly reduced activity. Ref.17
Mutagenesis3551S → A: Significantly reduced activity. Ref.17
Mutagenesis4071C → S: Complete loss of activity; when associated with K-233. Ref.17
Mutagenesis4101C → A: No effect on activity. Ref.17
Sequence conflict981N → I in BAG60595. Ref.3
Sequence conflict2461T → I in BAG60595. Ref.3
Sequence conflict3841E → G in BAG58060. Ref.3
Sequence conflict3951I → V in BAG60595. Ref.3

Secondary structure

.............................................................................. 423
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Mitochondrial) [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 5BEF7A8A039B70FB

FASTA42348,455
        10         20         30         40         50         60 
MLRVRCLRGG SRGAEAVHYI GSRLGRTLTG WVQRTFQSTQ AATASSRNSC AADDKATEPL 

        70         80         90        100        110        120 
PKDCPVSSYN EWDPLEEVIV GRAENACVPP FTIEVKANTY EKYWPFYQKQ GGHYFPKDHL 

       130        140        150        160        170        180 
KKAVAEIEEM CNILKTEGVT VRRPDPIDWS LKYKTPDFES TGLYSAMPRD ILIVVGNEII 

       190        200        210        220        230        240 
EAPMAWRSRF FEYRAYRSII KDYFHRGAKW TTAPKPTMAD ELYNQDYPIH SVEDRHKLAA 

       250        260        270        280        290        300 
QGKFVTTEFE PCFDAADFIR AGRDIFAQRS QVTNYLGIEW MRRHLAPDYR VHIISFKDPN 

       310        320        330        340        350        360 
PMHIDATFNI IGPGIVLSNP DRPCHQIDLF KKAGWTIITP PTPIIPDDHP LWMSSKWLSM 

       370        380        390        400        410        420 
NVLMLDEKRV MVDANEVPIQ KMFEKLGITT IKVNIRNANS LGGGFHCWTC DVRRRGTLQS 


YLD 

« Hide

Isoform 2 (Cytoplasmic) [UniParc].

Checksum: DA7E75BB41D91528
Show »

FASTA39144,883
Isoform 3 [UniParc].

Checksum: 692D75D4BCD1B990
Show »

FASTA39144,943

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Limited evolutionary conservation of imprinting in the human placenta."
Monk D., Arnaud P., Apostolidou S., Hills F.A., Kelsey G., Stanier P., Feil R., Moore G.E.
Proc. Natl. Acad. Sci. U.S.A. 103:6623-6628(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS41734.
S54161.
RefSeqNP_001473.1. NM_001482.2.
UniGeneHs.75335.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
DisProtDP00099.
ProteinModelPortalP50440.
SMRP50440. Positions 64-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108898. 2 interactions.
IntActP50440. 7 interactions.
STRING9606.ENSP00000379895.

Chemistry

DrugBankDB00148. Creatine.
DB00145. Glycine.
DB00129. L-Ornithine.

PTM databases

PhosphoSiteP50440.

Polymorphism databases

DMDM1730201.

2D gel databases

REPRODUCTION-2DPAGEIPI00032103.

Proteomic databases

PaxDbP50440.
PRIDEP50440.

Protocols and materials databases

DNASU2628.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000396659; ENSP00000379895; ENSG00000171766. [P50440-1]
ENST00000558336; ENSP00000454008; ENSG00000171766. [P50440-3]
GeneID2628.
KEGGhsa:2628.
UCSCuc001zvb.3. human. [P50440-1]
uc010uev.1. human. [P50440-3]

Organism-specific databases

CTD2628.
GeneCardsGC15M045653.
HGNCHGNC:4175. GATM.
HPAHPA026077.
MIM602360. gene.
612718. phenotype.
neXtProtNX_P50440.
Orphanet35704. Arginine:glycine amidinotransferase deficiency.
PharmGKBPA28590.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1834.
HOGENOMHOG000231593.
HOVERGENHBG002492.
InParanoidP50440.
KOK00613.
OMARPCHQID.
OrthoDBEOG712TW4.
PhylomeDBP50440.
TreeFamTF300256.

Enzyme and pathway databases

BRENDA2.1.4.1. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00104; UER00579.

Gene expression databases

ArrayExpressP50440.
BgeeP50440.
CleanExHS_GATM.
GenevestigatorP50440.

Family and domain databases

InterProIPR003198. Amidino_trans.
[Graphical view]
PfamPF02274. Amidinotransf. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGATM. human.
EvolutionaryTraceP50440.
GeneWikiGATM_(gene).
GenomeRNAi2628.
NextBio10353.
PROP50440.
SOURCESearch...

Entry information

Entry nameGATM_HUMAN
AccessionPrimary (citable) accession number: P50440
Secondary accession number(s): B4DH99, B4DPI3, Q53EQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM