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Protein

Gamma-glutamylaminecyclotransferase

Gene

GGACT

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

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
Complete GO annotation...

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 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:25100. GGACT.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

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

BgeeiQ9BVM4.
CleanExiHS_A2LD1.
ExpressionAtlasiQ9BVM4. baseline and differential.
GenevestigatoriQ9BVM4.

Organism-specific databases

HPAiHPA065320.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi124581. 1 interaction.
STRINGi9606.ENSP00000365426.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000010543.
HOGENOMiHOG000261862.
HOVERGENiHBG105481.
InParanoidiQ9BVM4.
OMAiVQCFVYS.
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

        10         20         30         40         50
MALVFVYGTL KRGQPNHRVL RDGAHGSAAF RARGRTLEPY PLVIAGEHNI
60 70 80 90 100
PWLLHLPGSG RLVEGEVYAV DERMLRFLDD FESCPALYQR TVLRVQLLED
110 120 130 140 150
RAPGAEEPPA PTAVQCFVYS RATFPPEWAQ LPHHDSYDSE GPHGLRYNPR

ENR
Length:153
Mass (Da):17,329
Last modified:February 29, 2004 - v2
Checksum:i1A01F350F761D208
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi124581. 1 interaction.
STRINGi9606.ENSP00000365426.

Polymorphism databases

DMDMi74752384.

Proteomic databases

MaxQBiQ9BVM4.
PaxDbiQ9BVM4.
PRIDEiQ9BVM4.

Protocols and materials databases

DNASUi87769.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi87769.
GeneCardsiGC13M101182.
HGNCiHGNC:25100. GGACT.
HPAiHPA065320.
MIMi613378. gene.
neXtProtiNX_Q9BVM4.
PharmGKBiPA164714645.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG242813.
GeneTreeiENSGT00390000010543.
HOGENOMiHOG000261862.
HOVERGENiHBG105481.
InParanoidiQ9BVM4.
OMAiVQCFVYS.
OrthoDBiEOG7TBC3D.
PhylomeDBiQ9BVM4.
TreeFamiTF323258.

Miscellaneous databases

EvolutionaryTraceiQ9BVM4.
GenomeRNAii87769.
NextBioi76214.
PROiQ9BVM4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BVM4.
CleanExiHS_A2LD1.
ExpressionAtlasiQ9BVM4. baseline and differential.
GenevestigatoriQ9BVM4.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2003) [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(2003) [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(2003) [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(2009) [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 25, 2008
Last sequence update: February 29, 2004
Last modified: March 3, 2015
This is version 98 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.