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P08587

- TGM2_CAVCU

UniProt

P08587 - TGM2_CAVCU

Protein

Protein-glutamine gamma-glutamyltransferase 2

Gene

TGM2

Organism
Cavia cutleri (Guinea pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.

    Catalytic activityi

    Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.PROSITE-ProRule annotation

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei277 – 2771PROSITE-ProRule annotation
    Active sitei335 – 3351PROSITE-ProRule annotation
    Active sitei358 – 3581PROSITE-ProRule annotation
    Metal bindingi398 – 3981CalciumBy similarity
    Metal bindingi400 – 4001CalciumBy similarity
    Metal bindingi446 – 4461CalciumBy similarity
    Metal bindingi451 – 4511CalciumBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB-EC
    4. transaminase activity Source: MGI

    GO - Biological processi

    1. peptide cross-linking Source: InterPro

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-glutamine gamma-glutamyltransferase 2 (EC:2.3.2.13)
    Alternative name(s):
    Tissue transglutaminase
    Transglutaminase C
    Short name:
    TG(C)
    Short name:
    TGC
    Short name:
    TGase C
    Transglutaminase-2
    Short name:
    TGase-2
    Gene namesi
    Name:TGM2
    OrganismiCavia cutleri (Guinea pig)
    Taxonomic identifieri10144 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 690689Protein-glutamine gamma-glutamyltransferase 2PRO_0000213706Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei467 – 4671N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    IntActiP08587. 6 interactions.
    MINTiMINT-1522105.

    Structurei

    3D structure databases

    ProteinModelPortaliP08587.
    SMRiP08587. Positions 15-690.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG004342.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    3.90.260.10. 1 hit.
    InterProiIPR023608. Gln_gamma-glutamylTfrase_euk.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002931. Transglutaminase-like.
    IPR008958. Transglutaminase_C.
    IPR013808. Transglutaminase_CS.
    IPR001102. Transglutaminase_N.
    [Graphical view]
    PANTHERiPTHR11590. PTHR11590. 1 hit.
    PfamiPF00927. Transglut_C. 2 hits.
    PF01841. Transglut_core. 1 hit.
    PF00868. Transglut_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
    SMARTiSM00460. TGc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49309. SSF49309. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08587-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEDLILERC DLQLEVNGRD HRTADLCRER LVLRRGQPFW LTLHFEGRGY    50
    EAGVDTLTFN AVTGPDPSEE AGTMARFSLS SAVEGGTWSA SAVDQQDSTV 100
    SLLLSTPADA PIGLYRLSLE ASTGYQGSSF VLGHFILLYN PRCPADAVYM 150
    DSDQERQEYV LTQQGFIYQG SAKFINGIPW NFGQFEDGIL DICLMLLDTN 200
    PKFLKNAGQD CSRRSRPVYV GRVVSAMVNC NDDQGVLQGR WDNNYSDGVS 250
    PMSWIGSVDI LRRWKDYGCQ RVKYGQCWVF AAVACTVLRC LGIPTRVVTN 300
    FNSAHDQNSN LLIEYFRNES GEIEGNKSEM IWNFHCWVES WMTRPDLEPG 350
    YEGWQALDPT PQEKSEGTYC CGPVPVRAIK EGHLNVKYDA PFVFAEVNAD 400
    VVNWIRQKDG SLRKSINHLV VGLKISTKSV GRDEREDITH TYKYPEGSEE 450
    EREAFVRANH LNKLATKEEA QEETGVAMRI RVGQNMTMGS DFDIFAYITN 500
    GTAESHECQL LLCARIVSYN GVLGPVCSTN DLLNLTLDPF SENSIPLHIL 550
    YEKYGDYLTE SNLIKVRGLL IEPAANSYVL AERDIYLENP EIKIRVLGEP 600
    KQNRKLIAEV SLKNPLPVPL LGCIFTVEGA GLTKDQKSVE VPDPVEAGEQ 650
    AKVRVDLLPT EVGLHKLVVN FECDKLKAVK GYRNVIIGPA 690
    Length:690
    Mass (Da):77,141
    Last modified:January 23, 2007 - v4
    Checksum:i047223D38DBEA4A4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 32AE → EA AA sequence (PubMed:5543674)Curated
    Sequence conflicti292 – 2921G → A in BAA00068. 1 PublicationCurated
    Sequence conflicti336 – 35419CWVES…GYEGW → SLLGGVVDDQAGPGAWVRGV in BAA00068. 1 PublicationCuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19646 mRNA. Translation: AAA37056.1.
    D00114 mRNA. Translation: BAA00068.1.
    PIRiA29996.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19646 mRNA. Translation: AAA37056.1 .
    D00114 mRNA. Translation: BAA00068.1 .
    PIRi A29996.

    3D structure databases

    ProteinModelPortali P08587.
    SMRi P08587. Positions 15-690.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08587. 6 interactions.
    MINTi MINT-1522105.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG004342.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    3.90.260.10. 1 hit.
    InterProi IPR023608. Gln_gamma-glutamylTfrase_euk.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002931. Transglutaminase-like.
    IPR008958. Transglutaminase_C.
    IPR013808. Transglutaminase_CS.
    IPR001102. Transglutaminase_N.
    [Graphical view ]
    PANTHERi PTHR11590. PTHR11590. 1 hit.
    Pfami PF00927. Transglut_C. 2 hits.
    PF01841. Transglut_core. 1 hit.
    PF00868. Transglut_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000459. TGM_EBP42. 1 hit.
    SMARTi SM00460. TGc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49309. SSF49309. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS00547. TRANSGLUTAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Amino acid sequence of guinea pig liver transglutaminase from its cDNA sequence."
      Ikura K., Nasu T.-A., Yokota H., Tsuchiya Y., Sasaki R., Chiba H.
      Biochemistry 27:2898-2905(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Structural properties of guinea pig liver transglutaminase."
      Connellan J.M., Chung S.I., Whetzel N.K., Bradley L.M., Folk J.E.
      J. Biol. Chem. 246:1093-1098(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-5.
      Tissue: Liver.
    3. "Determination of amino- and carboxyl-terminal sequences of guinea pig liver transglutaminase: evidence for amino-terminal processing."
      Ikura K., Yokota H., Sasaki R., Chiba H.
      Biochemistry 28:2344-2348(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-8 AND 684-690, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Liver.
    4. "Cloning of cDNA coding for guinea pig liver transglutaminase."
      Ikura K., Nasu T.-A., Yokota H., Sasaki R., Chiba H.
      Agric. Biol. Chem. 51:957-961(1987)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 189-632.
      Tissue: Liver.

    Entry informationi

    Entry nameiTGM2_CAVCU
    AccessioniPrimary (citable) accession number: P08587
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 108 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3