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UniProtKB - P50442 (GATM_RAT)

Entry version 136 (18 Sep 2019)
Sequence version 1 (01 Oct 1996)
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Protein

Glycine amidinotransferase, mitochondrial

Gene

Gatm

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. Also capable of catalyzing the synthesis of a range of neuroactive guanidino compounds by utilizing alternative amidine donors and acceptors for the transamidination reaction.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Two forms of the enzyme (denoted alpha and beta) with slightly different kinetic properties are present in cellular extracts. The molecular basis of the differences is unclear.
  1. KM=2.8 mM for arginine (alpha-transamidinase form)2 Publications
  2. KM=2.4 mM for arginine (beta-transamidinase form)2 Publications
  3. KM=3.0 mM for glycine (alpha-transamidinase form)2 Publications
  4. KM=3.1 mM for glycine (beta-transamidinase form)2 Publications
  5. KM=27.2 mM for 4-amino-butyrate (alpha-transamidinase form)2 Publications
  6. KM=24.9 mM for 4-amino-butyrate (beta-transamidinase form)2 Publications
  7. KM=23.0 mM for lysine (alpha-transamidinase form)2 Publications
  8. KM=23.5 mM for lysine (beta-transamidinase form)2 Publications
  9. KM=23.9 mM for 5-amino-valerate (alpha-transamidinase form)2 Publications
  10. KM=23.5 mM for 5-amino-valerate (beta-transamidinase form)2 Publications
  11. KM=57.4 mM for 3-amino-propanoate (alpha-transamidinase form)2 Publications
  12. KM=57.5 mM for 3-amino-propanoate (beta-transamidinase form)2 Publications
  13. KM=174 mM for ethanolamine (alpha-transamidinase form)2 Publications
  14. KM=171 mM for ethanolamine (beta-transamidinase form)2 Publications
  15. KM=392 mM for taurine (alpha-transamidinase form)2 Publications
  16. KM=450 mM for taurine (beta-transamidinase form)2 Publications
  1. Vmax=0.39 µmol/min/mg enzyme with L-arginine and glycine as substrates (alpha-transamidinase form)2 Publications
  2. Vmax=0.37 µmol/min/mg enzyme with L-arginine and glycine as substrates (beta-transamidinase form)2 Publications
  3. Vmax=39.8 µmol/h/mg enzyme with L-arginine and glycine as substrates (alpha-transamidinase form)2 Publications
  4. Vmax=27.0 µmol/h/mg enzyme with L-arginine and glycine as substrates (beta-transamidinase form)2 Publications
  5. Vmax=16.8 µmol/h/mg enzyme with L-arginine and 4-amino-butyrate as substrates (alpha-transamidinase form)2 Publications
  6. Vmax=11.8 µmol/h/mg enzyme with L-arginine and 4-amino-butyrate as substrates (beta-transamidinase form)2 Publications
  7. Vmax=12.0 µmol/h/µg enzyme with L-arginine and lysine as substrates (alpha-transamidinase form)2 Publications
  8. Vmax=10.1 µmol/h/µg enzyme with L-arginine and lysine as substrates (beta-transamidinase form)2 Publications
  9. Vmax=13.9 µmol/h/µg enzyme with L-arginine and 5-amino-valerate as substrates (alpha-transamidinase form)2 Publications
  10. Vmax=9.7 µmol/h/µg enzyme with L-arginine and 5-amino-valerate as substrates (beta-transamidinase form)2 Publications
  11. Vmax=10.8 µmol/h/µg enzyme with L-arginine and 3-amino-proponoate as substrates (alpha-transamidinase form)2 Publications
  12. Vmax=7.7 µmol/h/µg enzyme with L-arginine and 3-amino-proponoate as substrates (beta-transamidinase form)2 Publications
  13. Vmax=12.4 µmol/h/µg enzyme with L-arginine and ethanolamine as substrates (alpha-transamidinase form)2 Publications
  14. Vmax=9.4 µmol/h/µg enzyme with L-arginine and ethanolamine as substrates (beta-transamidinase form)2 Publications
  15. Vmax=2.8 µmol/h/µg enzyme with L-arginine and taurine as substrates (alpha-transamidinase form)2 Publications
  16. Vmax=2.1 µmol/h/µg enzyme with L-arginine and taurine as substrates (beta-transamidinase form)2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: creatine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes creatine from L-arginine and glycine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glycine amidinotransferase, mitochondrial (Gatm)
  2. Guanidinoacetate N-methyltransferase (Gamt), Guanidinoacetate N-methyltransferase (Gamt)
This subpathway is part of the pathway creatine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes creatine from L-arginine and glycine, the pathway creatine biosynthesis and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei254By similarity1
Active sitei303By similarity1
Active sitei407Amidino-cysteine intermediateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:MONOMER-7583

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.1.4.1 5301

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-71288 Creatine metabolism

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00104;UER00579

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glycine amidinotransferase, mitochondrial (EC:2.1.4.12 Publications)
Alternative name(s):
L-arginine:glycine amidinotransferase
Transamidinase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Gatm
Synonyms:Agat
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...RGDi		71090 Gatm

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 37MitochondrionAdd BLAST37
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000120838 – 423Glycine amidinotransferase, mitochondrialAdd BLAST386

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei46PhosphoserineBy similarity1
Modified residuei49PhosphoserineBy similarity1
Modified residuei385N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P50442

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P50442

PRoteomics IDEntifications database

More...PRIDEi		P50442

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P50442

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P50442

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in the kidney and pancreas, especially in the proximal tubules of the kidney, and alpha cells of the pancreatic islets (at protein level). Moderately expressed in liver hepatocytes (at protein level). Expressed in the kidney, pancreas, liver, colon, ileum, jejunum, heart and skeletal muscle. In reproductive tissues, expressed in the testis, epididymis, ovary, oviduct and uterus. Expressed throughout the brain in neurons, astrocytes and oligodendrocytes. In E12.5 embryos, it is expressed in the middle part of the somites, hepatic primordium and wall of the dorsal aorta. Expressed in E15.5 embryos in isolated cells throughout the central nervous system, skeletal muscles, gonad primordia, caudal somites, liver and pancreas, but not in the choroid plexus, root ganglia or kidney. Expressed in skeletal muscle, kidney, pancreas, central nervous system, liver and intestine epithelial cells, but not in epidermis, dermis, olfactory epithelium, trachea, lung, stomach or heart in E18.5 embryos.5 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed throughout embryogenesis. Expression in the colon and small intestine is highest in newborns and declines with age. Expression in the kidney increases with age.2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is induced by growth hormone and repressed by dietary intake of creatine.3 Publications

Gene expression databases

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P50442 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000000181

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P50442

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P50442

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the amidinotransferase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IFBR Eukaryota
ENOG410Y45M LUCA

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P50442

KEGG Orthology (KO)

More...KOi		K00613

Database of Orthologous Groups

More...OrthoDBi		636718at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P50442

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR033195 AmidinoTrfase

The PANTHER Classification System

More...PANTHERi		PTHR10488 PTHR10488, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P50442-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLRVRCLRGG SRGAEAVHYI GSRLGGSLTG WVQRTFQSTQ AATASSQNSC 
        60         70         80         90        100
AAEDKATHPL PKDCPVSSYN EWDPLEEVIV GRAENACVPP FTVEVKANTY 
       110        120        130        140        150
EKYWPFYQKN GGLYFPKDHL KKAVAEVEEM CNILSMEGVT VKRPDPIDWS 
       160        170        180        190        200
LKYKTPDFES TGLYSAMPRD ILMVVGNEII EAPMAWRSRF FEYRAYRSII 
       210        220        230        240        250
KDYFHRGAKW TTAPKPTMAD ELYDQDYPIH SVEDRHKLAA QGKFVTTEFE 
       260        270        280        290        300
PCFDAADFIR AGRDIFAQRS QVTNYLGIEW MRRHLAPDYR VHIISFKDPN 
       310        320        330        340        350
PMHIDATFNI IGPGLVLSNP DRPCHQIDLF KKAGWTIVTP PTPVIPDDHP 
       360        370        380        390        400
LWMSSKWLSM NVLMLDEKRV MVDANEVPIQ KMFEKLGIST IKVNIRNANS 
       410        420 
LGGGFHCWTC DVRRRGTLQS YFD
Length:423
Mass (Da):48,242
Last modified:October 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i442D7FBA4984DEA0
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A140TA89A0A140TA89_RAT
Glycine amidinotransferase, mitocho...
Gatm
462Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U07971 mRNA Translation: AAA21250.1
BC081785 mRNA Translation: AAH81785.1
AY625271 mRNA Translation: AAT39897.1

Protein sequence database of the Protein Information Resource

More...PIRi		A54140

NCBI Reference Sequences

More...RefSeqi		NP_112293.1, NM_031031.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		81660

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:81660

UCSC genome browser

More...UCSCi		RGD:71090 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07971 mRNA Translation: AAA21250.1
BC081785 mRNA Translation: AAH81785.1
AY625271 mRNA Translation: AAT39897.1
PIRiA54140
RefSeqiNP_112293.1, NM_031031.2

3D structure databases

SMRiP50442
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000181

Chemistry databases

BindingDBiP50442

PTM databases

iPTMnetiP50442
PhosphoSitePlusiP50442

Proteomic databases

jPOSTiP50442
PaxDbiP50442
PRIDEiP50442

Genome annotation databases

GeneIDi81660
KEGGirno:81660
UCSCiRGD:71090 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2628
RGDi71090 Gatm

Phylogenomic databases

eggNOGiENOG410IFBR Eukaryota
ENOG410Y45M LUCA
InParanoidiP50442
KOiK00613
OrthoDBi636718at2759
PhylomeDBiP50442

Enzyme and pathway databases

UniPathwayiUPA00104;UER00579
BioCyciMetaCyc:MONOMER-7583
BRENDAi2.1.4.1 5301
ReactomeiR-RNO-71288 Creatine metabolism

Miscellaneous databases

Protein Ontology

More...PROi		PR:P50442

Gene expression databases

GenevisibleiP50442 RN

Family and domain databases

InterProiView protein in InterPro
IPR033195 AmidinoTrfase
PANTHERiPTHR10488 PTHR10488, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGATM_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P50442
Secondary accession number(s): Q6ITZ7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 18, 2019
This is version 136 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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