P50440 (GATM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycine amidinotransferase, mitochondrial
EC=2.1.4.1

Alternative name(s):
L-arginine:glycine amidinotransferase
Transamidinase

Gene names

Name:	GATM
Synonyms:	AGAT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Arginine:glycine amidinotransferase deficiency (AGAT deficiency) [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. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the amidinotransferase family.
Biophysicochemical properties	Kinetic parameters: KM=2.0 µM for arginine Ref.7 Ref.15 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 component	Cytoplasm Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome creatine biosynthetic process Inferred from direct assay Ref.14. Source: MGI embryo development Inferred from electronic annotation. Source: Compara response to mercury ion Inferred from electronic annotation. Source: Compara response to nutrient Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from electronic annotation. Source: Compara response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara tissue regeneration Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial intermembrane space Inferred from direct assay Ref.14. Source: MGI
Molecular_function	glycine amidinotransferase activity Inferred from direct assay Ref.14. 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
Gatm	Q9D964	1	EBI-2552594,EBI-2552599	From 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 37

37

Mitochondrion By similarity

Chain

38 – 423

386

Glycine amidinotransferase, mitochondrial

PRO_0000001206

Sites

Active site

254

1

Active site

303

1

Active site

407

1

Amidino-cysteine intermediate Ref.8

Amino acid modifications

Modified residue

385

1

N6-acetyllysine Ref.13

Modified residue

417

1

Phosphothreonine By similarity

Natural variations

Alternative sequence

1 – 37

37

MLRVR…QRTFQ → MNILK in isoform 2.

VSP_000235

Alternative sequence

388 – 423

36

ITTIK…QSYLD → MYNK in isoform 3.

VSP_039871

Natural variant

110

1

Q → H. Ref.4
Corresponds to variant rs1288775 [ dbSNP | Ensembl ].

VAR_020305

Experimental info

Mutagenesis

170

1

D → N: Complete loss of activity. Ref.15

Mutagenesis

233

1

E → K: Complete loss of activity; when associated with S-407. Ref.15

Mutagenesis

254

1

D → N: Significantly reduced activity. Ref.15

Mutagenesis

303

1

H → V: Complete loss of activity. Ref.15

Mutagenesis

305

1

D → A: Complete loss of activity. Ref.15

Mutagenesis

322

1

R → E: Significantly reduced activity. Ref.15

Mutagenesis

355

1

S → A: Significantly reduced activity. Ref.15

Mutagenesis

407

1

C → S: Complete loss of activity; when associated with K-233. Ref.15

Mutagenesis

410

1

C → A: No effect on activity. Ref.15

Sequence conflict

98

1

N → I in BAG60595. Ref.3

Sequence conflict

246

1

T → I in BAG60595. Ref.3

Sequence conflict

384

1

E → G in BAG58060. Ref.3

Sequence conflict

395

1

I → V in BAG60595. Ref.3

Secondary structure

1

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423

Helix Strand Turn

Details...

Beta strand

70 – 73

4

Beta strand

75 – 80

6

Helix

93 – 96

4

Helix

101 – 103

3

Helix

104 – 110

7

Beta strand

113 – 115

3

Helix

117 – 136

20

Beta strand

140 – 142

3

Beta strand

152 – 154

3

Beta strand

159 – 161

3

Helix

168 – 171

4

Beta strand

172 – 176

5

Beta strand

178 – 181

4

Helix

187 – 189

3

Helix

192 – 195

4

Helix

197 – 205

9

Beta strand

209 – 212

4

Helix

220 – 222

3

Helix

232 – 240

9

Beta strand

248 – 250

3

Helix

255 – 257

3

Beta strand

258 – 261

4

Beta strand

264 – 267

4

Helix

275 – 285

11

Turn

286 – 288

3

Beta strand

290 – 293

4

Beta strand

296 – 298

3

Turn

305 – 307

3

Beta strand

308 – 312

5

Beta strand

315 – 318

4

Helix

327 – 332

6

Beta strand

336 – 338

3

Beta strand

352 – 354

3

Helix

356 – 360

5

Beta strand

363 – 366

4

Beta strand

369 – 373

5

Helix

377 – 385

9

Beta strand

389 – 393

5

Helix

396 – 399

4

Turn

400 – 402

3

Turn

405 – 408

4

Beta strand

409 – 415

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Mitochondrial) [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 5BEF7A8A039B70FB	FASTA	423	48,455
	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
	Isoform 2 (Cytoplasmic) [UniParc]. Checksum: DA7E75BB41D91528	FASTA	391	44,883
	10 20 30 40 50 60 MNILKSTQAA TASSRNSCAA DDKATEPLPK DCPVSSYNEW DPLEEVIVGR AENACVPPFT 70 80 90 100 110 120 IEVKANTYEK YWPFYQKQGG HYFPKDHLKK AVAEIEEMCN ILKTEGVTVR RPDPIDWSLK 130 140 150 160 170 180 YKTPDFESTG LYSAMPRDIL IVVGNEIIEA PMAWRSRFFE YRAYRSIIKD YFHRGAKWTT 190 200 210 220 230 240 APKPTMADEL YNQDYPIHSV EDRHKLAAQG KFVTTEFEPC FDAADFIRAG RDIFAQRSQV 250 260 270 280 290 300 TNYLGIEWMR RHLAPDYRVH IISFKDPNPM HIDATFNIIG PGIVLSNPDR PCHQIDLFKK 310 320 330 340 350 360 AGWTIITPPT PIIPDDHPLW MSSKWLSMNV LMLDEKRVMV DANEVPIQKM FEKLGITTIK 370 380 390 VNIRNANSLG GGFHCWTCDV RRRGTLQSYL D
	Isoform 3 [UniParc]. Checksum: 692D75D4BCD1B990	FASTA	391	44,943
	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 NVLMLDEKRV MVDANEVPIQ KMFEKLGMYN K

References

	« Hide 'large scale' referencesShow '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. , 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]	"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, MASS SPECTROMETRY.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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 AGAT DEFICIENCY.
+	Additional computationally mapped references.

Web resources

GeneReviews

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.

IPI

IPI00032103.
IPI00216279.
IPI00970843.

PIR

S41734.
S54161.

RefSeq

NP_001473.1. NM_001482.2.

UniGene

Hs.75335.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

DisProt

DP00099.

ProteinModelPortal

P50440.

ModBase

Search...

Protein-protein interaction databases

IntAct

P50440. 6 interactions.

STRING

9606.ENSP00000379895.

PTM databases

PhosphoSite

P50440.

Polymorphism databases

DMDM

1730201.

2D gel databases

REPRODUCTION-2DPAGE

IPI00032103.

Proteomic databases

PaxDb

P50440.

PRIDE

P50440.

Protocols and materials databases

DNASU

2628.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000396659; ENSP00000379895; ENSG00000171766.
ENST00000558336; ENSP00000454008; ENSG00000171766.

GeneID

2628.

KEGG

hsa:2628.

UCSC

uc001zvb.3. human.
uc010uev.1. human.

Organism-specific databases

CTD

2628.

GeneCards

GC15M045653.

HGNC

HGNC:4175. GATM.

HPA

HPA026077.

MIM

602360. gene.
612718. phenotype.

neXtProt

NX_P50440.

Orphanet

35704. Arginine:glycine amidinotransferase deficiency.

PharmGKB

PA28590.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1834.

HOGENOM

HOG000231593.

HOVERGEN

HBG002492.

InParanoid

P50440.

KO

K00613.

OMA

RPCHQID.

OrthoDB

EOG4C2H9H.

PhylomeDB

P50440.

Enzyme and pathway databases

BRENDA

2.1.4.1. 2681.

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00104; UER00579.

Gene expression databases

ArrayExpress

P50440.

Bgee

P50440.

CleanEx

HS_GATM.

Genevestigator

P50440.

GermOnline

ENSG00000171766. Homo sapiens.

Family and domain databases

InterPro

IPR003198. Amidino_trans.
[Graphical view]

Pfam

PF02274. Amidinotransf. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

GATM. human.

DrugBank

DB00148. Creatine.
DB00145. Glycine.
DB00129. L-Ornithine.

EvolutionaryTrace

P50440.

GenomeRNAi

2628.

NextBio

10353.

SOURCE

Search...

Entry information

Entry name

GATM_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 144 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.