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Q9BVM4 (GGACT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-glutamylaminecyclotransferase

Short name=GGACT
EC=2.3.2.4
Alternative name(s):
AIG2-like domain-containing protein 1
Gamma-glutamylamine cyclotransferase
Gene names
Name:GGACT
Synonyms:A2LD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Catalytic activity

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

Subunit structure

Monomer. Ref.5

Sequence similarities

Belongs to the gamma-glutamylcyclotransferase family.

Sequence caution

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 153153Gamma-glutamylaminecyclotransferase
PRO_0000320203

Regions

Region7 – 104Substrate binding

Sites

Active site821Proton acceptor Ref.5

Experimental info

Mutagenesis821E → A or Q: Loss of activity. Ref.5

Secondary structure

.......................... 153
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BVM4 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 1A01F350F761D208

FASTA15317,329
        10         20         30         40         50         60 
MALVFVYGTL KRGQPNHRVL RDGAHGSAAF RARGRTLEPY PLVIAGEHNI PWLLHLPGSG 

        70         80         90        100        110        120 
RLVEGEVYAV DERMLRFLDD FESCPALYQR TVLRVQLLED RAPGAEEPPA PTAVQCFVYS 

       130        140        150 
RATFPPEWAQ LPHHDSYDSE GPHGLRYNPR ENR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS45066.1.
RefSeqNP_001182016.1. NM_001195087.1.
NP_149101.1. NM_033110.2.
XP_005254140.1. XM_005254083.1.
UniGeneHs.350868.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3JUBX-ray1.20A1-153[»]
3JUCX-ray1.20A1-153[»]
3JUDX-ray0.98A1-153[»]
ProteinModelPortalQ9BVM4.
SMRQ9BVM4. Positions 1-151.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000365426.

Polymorphism databases

DMDM74752384.

Proteomic databases

MaxQBQ9BVM4.
PaxDbQ9BVM4.
PRIDEQ9BVM4.

Protocols and materials databases

DNASU87769.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376250; ENSP00000365426; ENSG00000134864.
ENST00000455100; ENSP00000410449; ENSG00000134864.
GeneID87769.
KEGGhsa:87769.
UCSCuc001voq.2. human.

Organism-specific databases

CTD87769.
GeneCardsGC13M101182.
HGNCHGNC:25100. GGACT.
MIM613378. gene.
neXtProtNX_Q9BVM4.
PharmGKBPA164714645.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242813.
HOGENOMHOG000261862.
HOVERGENHBG105481.
InParanoidQ9BVM4.
OMACFVYSTA.
OrthoDBEOG7TBC3D.
PhylomeDBQ9BVM4.
TreeFamTF323258.

Gene expression databases

ArrayExpressQ9BVM4.
BgeeQ9BVM4.
CleanExHS_A2LD1.
GenevestigatorQ9BVM4.

Family and domain databases

Gene3D3.10.490.10. 1 hit.
InterProIPR009288. AIG2-like.
IPR013024. Butirosin_synth_BtrG-like.
[Graphical view]
PfamPF06094. AIG2. 1 hit.
[Graphical view]
SUPFAMSSF110857. SSF110857. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9BVM4.
GenomeRNAi87769.
NextBio76214.
PROQ9BVM4.
SOURCESearch...

Entry information

Entry nameGGACT_HUMAN
AccessionPrimary (citable) accession number: Q9BVM4
Secondary accession number(s): B3KTN1, Q9BT41
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2004
Last modified: July 9, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Uncharacterized protein families (UPF)

List of uncharacterized protein family (UPF) entries

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM