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Q9BVM4

- GGACT_HUMAN

UniProt

Q9BVM4 - GGACT_HUMAN

Protein

Gamma-glutamylaminecyclotransferase

Gene

GGACT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Contributes to degradation of proteins cross-linked by transglutaminases. Degrades the cross-link between a lysine and a glutamic acid residue from two proteins that have been cross-linked by transglutaminases. Catalyzes the formation of 5-oxoproline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L-gamma-glutamyl-alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine.1 Publication

    Catalytic activityi

    (Gamma-L-glutamyl)-L-amino acid = 5-oxoproline + L-amino acid.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei82 – 821Proton acceptor1 Publication

    GO - Molecular functioni

    1. gamma-glutamylcyclotransferase activity Source: UniProtKB

    GO - Biological processi

    1. cellular modified amino acid catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-glutamylaminecyclotransferase (EC:2.3.2.4)
    Short name:
    GGACT
    Alternative name(s):
    AIG2-like domain-containing protein 1
    Gamma-glutamylamine cyclotransferase
    Gene namesi
    Name:GGACT
    Synonyms:A2LD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:25100. GGACT.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi82 – 821E → A or Q: Loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA164714645.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 153153Gamma-glutamylaminecyclotransferasePRO_0000320203Add
    BLAST

    Proteomic databases

    MaxQBiQ9BVM4.
    PaxDbiQ9BVM4.
    PRIDEiQ9BVM4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BVM4.
    BgeeiQ9BVM4.
    CleanExiHS_A2LD1.
    GenevestigatoriQ9BVM4.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi9606.ENSP00000365426.

    Structurei

    Secondary structure

    1
    153
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Helixi17 – 204
    Helixi23 – 253
    Beta strandi28 – 3811
    Beta strandi42 – 454
    Turni46 – 494
    Beta strandi50 – 556
    Beta strandi59 – 613
    Beta strandi64 – 707
    Helixi72 – 8110
    Turni82 – 865
    Beta strandi89 – 9810
    Beta strandi113 – 1219
    Helixi126 – 1305

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3JUBX-ray1.20A1-153[»]
    3JUCX-ray1.20A1-153[»]
    3JUDX-ray0.98A1-153[»]
    ProteinModelPortaliQ9BVM4.
    SMRiQ9BVM4. Positions 1-151.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BVM4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 104Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG242813.
    HOGENOMiHOG000261862.
    HOVERGENiHBG105481.
    InParanoidiQ9BVM4.
    OMAiCFVYSTA.
    OrthoDBiEOG7TBC3D.
    PhylomeDBiQ9BVM4.
    TreeFamiTF323258.

    Family and domain databases

    Gene3Di3.10.490.10. 1 hit.
    InterProiIPR009288. AIG2-like.
    IPR013024. Butirosin_synth_BtrG-like.
    [Graphical view]
    PfamiPF06094. AIG2. 1 hit.
    [Graphical view]
    SUPFAMiSSF110857. SSF110857. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9BVM4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALVFVYGTL KRGQPNHRVL RDGAHGSAAF RARGRTLEPY PLVIAGEHNI    50
    PWLLHLPGSG RLVEGEVYAV DERMLRFLDD FESCPALYQR TVLRVQLLED 100
    RAPGAEEPPA PTAVQCFVYS RATFPPEWAQ LPHHDSYDSE GPHGLRYNPR 150
    ENR 153
    Length:153
    Mass (Da):17,329
    Last modified:March 1, 2004 - v2
    Checksum:i1A01F350F761D208
    GO

    Sequence cautioni

    The sequence AAH04360.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK095850 mRNA. Translation: BAG53143.1.
    AL136526 Genomic DNA. Translation: CAI39558.1.
    CH471085 Genomic DNA. Translation: EAX09037.1.
    BC001077 mRNA. Translation: AAH01077.2.
    BC004360 mRNA. Translation: AAH04360.1. Different initiation.
    CCDSiCCDS45066.1.
    RefSeqiNP_001182016.1. NM_001195087.1.
    NP_149101.1. NM_033110.2.
    XP_005254140.1. XM_005254083.1.
    UniGeneiHs.350868.

    Genome annotation databases

    EnsembliENST00000376250; ENSP00000365426; ENSG00000134864.
    ENST00000455100; ENSP00000410449; ENSG00000134864.
    GeneIDi87769.
    KEGGihsa:87769.
    UCSCiuc001voq.2. human.

    Polymorphism databases

    DMDMi74752384.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK095850 mRNA. Translation: BAG53143.1 .
    AL136526 Genomic DNA. Translation: CAI39558.1 .
    CH471085 Genomic DNA. Translation: EAX09037.1 .
    BC001077 mRNA. Translation: AAH01077.2 .
    BC004360 mRNA. Translation: AAH04360.1 . Different initiation.
    CCDSi CCDS45066.1.
    RefSeqi NP_001182016.1. NM_001195087.1.
    NP_149101.1. NM_033110.2.
    XP_005254140.1. XM_005254083.1.
    UniGenei Hs.350868.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3JUB X-ray 1.20 A 1-153 [» ]
    3JUC X-ray 1.20 A 1-153 [» ]
    3JUD X-ray 0.98 A 1-153 [» ]
    ProteinModelPortali Q9BVM4.
    SMRi Q9BVM4. Positions 1-151.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000365426.

    Polymorphism databases

    DMDMi 74752384.

    Proteomic databases

    MaxQBi Q9BVM4.
    PaxDbi Q9BVM4.
    PRIDEi Q9BVM4.

    Protocols and materials databases

    DNASUi 87769.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376250 ; ENSP00000365426 ; ENSG00000134864 .
    ENST00000455100 ; ENSP00000410449 ; ENSG00000134864 .
    GeneIDi 87769.
    KEGGi hsa:87769.
    UCSCi uc001voq.2. human.

    Organism-specific databases

    CTDi 87769.
    GeneCardsi GC13M101182.
    HGNCi HGNC:25100. GGACT.
    MIMi 613378. gene.
    neXtProti NX_Q9BVM4.
    PharmGKBi PA164714645.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG242813.
    HOGENOMi HOG000261862.
    HOVERGENi HBG105481.
    InParanoidi Q9BVM4.
    OMAi CFVYSTA.
    OrthoDBi EOG7TBC3D.
    PhylomeDBi Q9BVM4.
    TreeFami TF323258.

    Miscellaneous databases

    EvolutionaryTracei Q9BVM4.
    GenomeRNAii 87769.
    NextBioi 76214.
    PROi Q9BVM4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BVM4.
    Bgeei Q9BVM4.
    CleanExi HS_A2LD1.
    Genevestigatori Q9BVM4.

    Family and domain databases

    Gene3Di 3.10.490.10. 1 hit.
    InterProi IPR009288. AIG2-like.
    IPR013024. Butirosin_synth_BtrG-like.
    [Graphical view ]
    Pfami PF06094. AIG2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF110857. SSF110857. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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].
    2. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Tissue: Lung.
    5. "Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism."
      Oakley A.J., Coggan M., Board P.G.
      J. Biol. Chem. 285:9642-9648(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) IN COMPLEX WITH 5-OXOPROLINE AND NITRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLU-82.

    Entry informationi

    Entry nameiGGACT_HUMAN
    AccessioniPrimary (citable) accession number: Q9BVM4
    Secondary accession number(s): B3KTN1, Q9BT41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: March 1, 2004
    Last modified: October 1, 2014
    This is version 93 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families
    5. Uncharacterized protein families (UPF)
      List of uncharacterized protein family (UPF) entries

    External Data

    Dasty 3