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Entry version 140 (07 Apr 2021)
Sequence version 1 (01 Nov 1999)
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Protein

Protein-glutamine gamma-glutamyltransferase 2

Gene

Tgm2

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

Calcium-dependent acyltransferase that catalyzes the formation of covalent bonds between peptide-bound glutamine and various primary amines, such as gamma-amino group of peptide-bound lysine, or mono- and polyamines, thereby producing cross-linked or aminated proteins, respectively (By similarity). Involved in many biological processes, such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification and apoptosis (By similarity). Acts as a protein-glutamine gamma-glutamyltransferase by mediating the cross-linking of proteins, such as ACO2, HSPB6, FN1, HMGB1, RAP1GDS1, SLC25A4/ANT1, SPP1 and WDR54 (PubMed:16341586, PubMed:29622788). Under physiological conditions, the protein cross-linking activity is inhibited by GTP; inhibition is relieved by Ca2+ in response to various stresses (By similarity). When secreted, catalyzes cross-linking of proteins of the extracellular matrix, such as FN1 and SPP1 resulting in the formation of scaffolds (By similarity). Plays a key role during apoptosis, both by (1) promoting the cross-linking of cytoskeletal proteins resulting in condensation of the cytoplasm, and by (2) mediating cross-linking proteins of the extracellular matrix, resulting in the irreversible formation of scaffolds that stabilize the integrity of the dying cells before their clearance by phagocytosis, thereby preventing the leakage of harmful intracellular components (By similarity). In addition to protein cross-linking, can use different monoamine substrates to catalyze a vast array of protein post-translational modifications: mediates aminylation of serotonin, dopamine, noradrenaline or histamine into glutamine residues of target proteins to generate protein serotonylation, dopaminylation, noradrenalinylation or histaminylation, respectively (By similarity). Mediates protein serotonylation of small GTPases during activation and aggregation of platelets, leading to constitutive activation of these GTPases (By similarity). Plays a key role in chromatin organization by mediating serotonylation and dopaminylation of histone H3 (By similarity). Catalyzes serotonylation of 'Gln-5' of histone H3 (H3Q5ser) during serotonergic neuron differentiation, thereby facilitating transcription (By similarity). Acts as a mediator of neurotransmission-independent role of nuclear dopamine in ventral tegmental area (VTA) neurons: catalyzes dopaminylation of 'Gln-5' of histone H3 (H3Q5dop), thereby regulating relapse-related transcriptional plasticity in the reward system (By similarity). Regulates vein remodeling by mediating serotonylation and subsequent inactivation of ATP2A2/SERCA2 (By similarity). Also acts as a protein deamidase by mediating the side chain deamidation of specific glutamine residues of proteins to glutamate (By similarity). Catalyzes specific deamidation of protein gliadin, a component of wheat gluten in the diet (By similarity). May also act as an isopeptidase cleaving the previously formed cross-links (By similarity). Also able to participate in signaling pathways independently of its acyltransferase activity: acts as a signal transducer in alpha-1 adrenergic receptor-mediated stimulation of phospholipase C-delta (PLCD) activity and is required for coupling alpha-1 adrenergic agonists to the stimulation of phosphoinositide lipid metabolism (PubMed:7911253, PubMed:12054611, PubMed:14970202). Activates alpha-1 adrenergic receptor signaling during pregnancy, promoting smooth muscle cell proliferation (PubMed:14970202).By similarity5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Acyltransferase activity is regulated by the binding of GTP and Ca2+: inactivated by GTP, which stabilizes its closed structure, thereby obstructing the accessibility of substrates to the active sites (PubMed:17179049). In contrast, Ca2+ acts as a cofactor by inducing conformational change to the active open form. In absence of Ca2+, Mg2+ may bind Ca2+-binding sites, promoting GTP-binding and subsequent inhibition of the acyltransferase activity (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei277PROSITE-ProRule annotation1 Publication1
Active sitei335PROSITE-ProRule annotation1
Active sitei358PROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi398CalciumBy similarity1
Metal bindingi400CalciumBy similarity1
Metal bindingi437CalciumBy similarity1
Metal bindingi447CalciumBy similarity1
Metal bindingi452CalciumBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei516Important for catalytic activityBy similarity1
Metal bindingi538CalciumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi476 – 483GTPBy similarity8
Nucleotide bindingi579 – 582GTPBy similarity4

<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

GO - Biological processi

<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 functionAcyltransferase, Hydrolase, Protease, Transferase
LigandCalcium, GTP-binding, Metal-binding, Nucleotide-binding

<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%5Fand%5Ftaxonomy%5Fsection">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:
Protein-glutamine gamma-glutamyltransferase 2Curated (EC:2.3.2.131 Publication)
Alternative name(s):
Isopeptidase TGM2Curated (EC:3.4.-.-By similarity)
Protein G alpha(h)1 Publication
Short name:
Protein G(h)1 Publication
Protein-glutamine deamidase TGM2Curated (EC:3.5.1.44By similarity)
Protein-glutamine dopaminyltransferase TGM2Curated (EC:2.3.1.-By similarity)
Protein-glutamine histaminyltransferase TGM2Curated (EC:2.3.1.-By similarity)
Protein-glutamine noradrenalinyltransferase TGM2Curated (EC:2.3.1.-By similarity)
Protein-glutamine serotonyltransferase TGM2Curated (EC:2.3.1.-By similarity)
Tissue transglutaminase1 Publication
Short name:
tTG1 Publication
Short name:
tTgaseBy similarity
Transglutaminase II1 Publication
Short name:
TGase II1 Publication
Transglutaminase-21 Publication
Short name:
TGase 21 Publication
Short name:
TGase-21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Tgm2Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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: Chromosome 3
  • UP000234681 Componentsi: Chromosome 3, Unassembled WGS sequence

Organism-specific databases

Rat genome database

More...
RGDi
621081, Tgm2

<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

Keywords - Cellular componenti

Cell membrane, Chromosome, Cytoplasm, Extracellular matrix, Membrane, Mitochondrion, Nucleus, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi277C → S: Abolished protein-glutamine gamma-glutamyltransferase activity without affecting alpha-1 adrenergic receptor signaling. 1 Publication1
Mutagenesisi579R → A: Destabilizes the compact conformation in presence of GTP. 1 Publication1

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004524732 – 686Protein-glutamine gamma-glutamyltransferase 2Add BLAST685

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 residuei2N-acetylalanineBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi230 ↔ 370AlternateBy similarity
Disulfide bondi370 ↔ 371AlternateBy similarity
Modified residuei468N6-acetyllysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki632Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Disulfide bond formation inactivates the calcium-dependent acyltransferase activity. Cys-370 can form disulfide bonds with both Cys-230 and Cys-371: formation of a disulfide bond between Cys-230 and Cys-370 facilitates formation of the disulfide between Cy-370 and Cys-371, which promotes inactivation of the acyltransferase activity. May also form interchain disulfids between Cys-230 and Cys-370. Ca2+ protects against disulfide bond formation and inactivation.By similarity
Auto-transglutaminated: Forms covalent cross-links mediated by transglutaminase between Gln-632 and the epsilon-amino group of a lysine residue of itself or HMGB1, forming homopolymers and heteropolymers, respectively.By similarity
S-nitrosylated, leading to its inactivate the acyltransferase activity.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, S-nitrosylation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q9WVJ6

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6P6R6

<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 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

By retinoic acid (PubMed:11073883). Up-regulated during pregnancy (PubMed:14970202).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000012956, Expressed in lung and 21 other tissues

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (By similarity).

Interacts with phospholipase C; promoting alpha-1 adrenergic receptor signaling (By similarity).

Interacts with PLCD1 (PubMed:12054611).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q6P6R6

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000018328

<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
Q9WVJ6

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QUSX, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT01010000222350

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_013435_1_0_1

Identification of Orthologs from Complete Genome Data

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OMAi
IKSVPWN

Database of Orthologous Groups

More...
OrthoDBi
297055at2759

TreeFam database of animal gene trees

More...
TreeFami
TF324278

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 3 hits
3.90.260.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013783, Ig-like_fold
IPR014756, Ig_E-set
IPR038765, Papain-like_cys_pep_sf
IPR002931, Transglutaminase-like
IPR036985, Transglutaminase-like_sf
IPR023608, Transglutaminase_animal
IPR013808, Transglutaminase_AS
IPR008958, Transglutaminase_C
IPR036238, Transglutaminase_C_sf
IPR001102, Transglutaminase_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00927, Transglut_C, 2 hits
PF01841, Transglut_core, 1 hit
PF00868, Transglut_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000459, TGM_EBP42, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00460, TGc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49309, SSF49309, 2 hits
SSF54001, SSF54001, 1 hit
SSF81296, SSF81296, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00547, TRANSGLUTAMINASES, 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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q9WVJ6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEELNLERC DLEIQANGRD HHTADLCQQK LVLRRGQRFR LTLYFEGRGY
60 70 80 90 100
EASVDRLTFG AVTGPDPSEE AGTKARFSLS DDVEEGSWSA SVLDQQDNVL
110 120 130 140 150
SLQLCTPANA PVGQYRLSLE TSTGYQGSSF MLGHFILLFN AWCPADDVYL
160 170 180 190 200
DSEAERREYV LTQQGFIYQG SVKFIKSVPW NFGQFEDGIL DACLMLLDVN
210 220 230 240 250
PKFLKDRSRD CSRRSSPIYV GRVVSGMVNC NDDQGVLLGR WDNNYGDGIS
260 270 280 290 300
PMAWIGSVDI LRRWKEHGCQ QVKYGQCWVF AAVACTVLRC LGIPTRVVTN
310 320 330 340 350
YNSAHDQNSN LLIEYFRNEY GELESNKSEM IWNFHCWVES WMTRPDLQPG
360 370 380 390 400
YEGWQAIDPT PQEKSEGTYC CGPVSVRAIK EGDLSTKYDA SFVFAEVNAD
410 420 430 440 450
VVDWIRQSDG SVLKSINNSL VVGQKISTKS VGRDDREDIT YTYKYPEGSP
460 470 480 490 500
EEREVFTRAN HLNKLAEKEE TGVAMRIRVG DGMSLGNDFD VFAHIGNDTS
510 520 530 540 550
ESRECRLLLC ARTVSYNGVL GPECGTEDIN LTLDPYSENS IPLRILYEKY
560 570 580 590 600
SGCLTESNLI KVRGLLVEPA ANSYLLAERD LYLENPEIKI RILGEPKQNR
610 620 630 640 650
KLVAEVSLKN PLSDSLYDCV FTVEGAGLTK EQKSVEVSDP VPAGDAVKVR
660 670 680
VDLFPTDIGL HKLVVNFQCD KLKSVKGYRN IIIGPA
Length:686
Mass (Da):76,935
Last modified:November 1, 1999 - 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:i4CD3D377FA86EC1A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti29Q → E in AAH62062 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AABR07054457 Genomic DNA No translation available.
AF106325 mRNA Translation: AAD42046.1
CH474005 Genomic DNA Translation: EDL96658.1
BC062062 mRNA Translation: AAH62062.1

NCBI Reference Sequences

More...
RefSeqi
NP_062259.2, NM_019386.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000018328; ENSRNOP00000018328; ENSRNOG00000012956

Database of genes from NCBI RefSeq genomes

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GeneIDi
56083

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:56083

UCSC genome browser

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UCSCi
RGD:621081, 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
AABR07054457 Genomic DNA No translation available.
AF106325 mRNA Translation: AAD42046.1
CH474005 Genomic DNA Translation: EDL96658.1
BC062062 mRNA Translation: AAH62062.1
RefSeqiNP_062259.2, NM_019386.2

3D structure databases

SMRiQ9WVJ6
ModBaseiSearch...

Protein-protein interaction databases

CORUMiQ6P6R6
STRINGi10116.ENSRNOP00000018328

PTM databases

iPTMnetiQ6P6R6

Proteomic databases

PRIDEiQ9WVJ6

Genome annotation databases

EnsembliENSRNOT00000018328; ENSRNOP00000018328; ENSRNOG00000012956
GeneIDi56083
KEGGirno:56083
UCSCiRGD:621081, rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
7052
RGDi621081, Tgm2

Phylogenomic databases

eggNOGiENOG502QUSX, Eukaryota
GeneTreeiENSGT01010000222350
HOGENOMiCLU_013435_1_0_1
OMAiIKSVPWN
OrthoDBi297055at2759
TreeFamiTF324278

Gene expression databases

BgeeiENSRNOG00000012956, Expressed in lung and 21 other tissues

Family and domain databases

Gene3Di2.60.40.10, 3 hits
3.90.260.10, 1 hit
InterProiView protein in InterPro
IPR013783, Ig-like_fold
IPR014756, Ig_E-set
IPR038765, Papain-like_cys_pep_sf
IPR002931, Transglutaminase-like
IPR036985, Transglutaminase-like_sf
IPR023608, Transglutaminase_animal
IPR013808, Transglutaminase_AS
IPR008958, Transglutaminase_C
IPR036238, Transglutaminase_C_sf
IPR001102, Transglutaminase_N
PfamiView protein in Pfam
PF00927, Transglut_C, 2 hits
PF01841, Transglut_core, 1 hit
PF00868, Transglut_N, 1 hit
PIRSFiPIRSF000459, TGM_EBP42, 1 hit
SMARTiView protein in SMART
SM00460, TGc, 1 hit
SUPFAMiSSF49309, SSF49309, 2 hits
SSF54001, SSF54001, 1 hit
SSF81296, SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS00547, TRANSGLUTAMINASES, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiTGM2_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: Q9WVJ6
Secondary accession number(s): Q6P6R6
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 7, 2021
Last sequence update: November 1, 1999
Last modified: April 7, 2021
This is version 140 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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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