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Protein

Gamma-glutamylaminecyclotransferase

Gene

Ggact

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei82 – 821Proton acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:2385008. Ggact.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 149149Gamma-glutamylaminecyclotransferasePRO_0000320204Add
BLAST

Proteomic databases

EPDiQ923B0.
MaxQBiQ923B0.
PaxDbiQ923B0.
PRIDEiQ923B0.

Expressioni

Gene expression databases

BgeeiQ923B0.
ExpressionAtlasiQ923B0. baseline and differential.
GenevisibleiQ923B0. MM.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiQ923B0. 2 interactions.
MINTiMINT-4122860.
STRINGi10090.ENSMUSP00000037278.

Structurei

Secondary structure

1
149
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Beta strandi11 – 133Combined sources
Turni15 – 173Combined sources
Helixi18 – 214Combined 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 – 10012Combined sources
Beta strandi108 – 11811Combined sources
Helixi122 – 1265Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VKBX-ray1.90A1-149[»]
2KL2NMR-A1-149[»]
ProteinModelPortaliQ923B0.
SMRiQ923B0. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ923B0.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4450. Eukaryota.
ENOG4111N8W. LUCA.
GeneTreeiENSGT00390000010543.
HOGENOMiHOG000261862.
HOVERGENiHBG105481.
InParanoidiQ923B0.
KOiK19761.
OMAiRIQVVEW.
OrthoDBiEOG7TBC3D.
TreeFamiTF323258.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q923B0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAHIFVYGTL KRGQPNHKVM LDHSHGLAAF RGRGCTVESF PLVIAGEHNI
60 70 80 90 100
PWLLYLPGKG HCVTGEIYEV DEQMLRFLDD FEDCPSMYQR TALQVQVLEW
110 120 130 140
EGDGDPGDSV QCFVYTTATY APEWLFLPYH ESYDSEGPHG LRYNPRENR
Length:149
Mass (Da):17,080
Last modified:December 1, 2001 - v1
Checksum:i0FB86B86AF2AB46B
GO
Isoform 2 (identifier: Q923B0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     66-79: EIYEVDEQMLRFLD → NWKGGHICHCRWIH
     80-149: Missing.

Note: No experimental confirmation available.
Show »
Length:79
Mass (Da):8,866
Checksum:i1F4CCF7BBE385459
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei66 – 7914EIYEV…LRFLD → NWKGGHICHCRWIH in isoform 2. 1 PublicationVSP_031641Add
BLAST
Alternative sequencei80 – 14970Missing in isoform 2. 1 PublicationVSP_031642Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050251 mRNA. Translation: BAC34147.1.
BC006662 mRNA. Translation: AAH06662.1.
BC080839 mRNA. Translation: AAH80839.1.
CCDSiCCDS27351.1. [Q923B0-1]
RefSeqiNP_663441.1. NM_145466.2. [Q923B0-1]
XP_006518983.1. XM_006518920.1. [Q923B0-1]
UniGeneiMm.379358.

Genome annotation databases

EnsembliENSMUST00000038075; ENSMUSP00000037278; ENSMUSG00000041625. [Q923B0-1]
ENSMUST00000110679; ENSMUSP00000135487; ENSMUSG00000041625. [Q923B0-2]
GeneIDi223267.
KEGGimmu:223267.
UCSCiuc011zqm.1. mouse. [Q923B0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050251 mRNA. Translation: BAC34147.1.
BC006662 mRNA. Translation: AAH06662.1.
BC080839 mRNA. Translation: AAH80839.1.
CCDSiCCDS27351.1. [Q923B0-1]
RefSeqiNP_663441.1. NM_145466.2. [Q923B0-1]
XP_006518983.1. XM_006518920.1. [Q923B0-1]
UniGeneiMm.379358.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VKBX-ray1.90A1-149[»]
2KL2NMR-A1-149[»]
ProteinModelPortaliQ923B0.
SMRiQ923B0. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ923B0. 2 interactions.
MINTiMINT-4122860.
STRINGi10090.ENSMUSP00000037278.

Proteomic databases

EPDiQ923B0.
MaxQBiQ923B0.
PaxDbiQ923B0.
PRIDEiQ923B0.

Protocols and materials databases

DNASUi223267.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038075; ENSMUSP00000037278; ENSMUSG00000041625. [Q923B0-1]
ENSMUST00000110679; ENSMUSP00000135487; ENSMUSG00000041625. [Q923B0-2]
GeneIDi223267.
KEGGimmu:223267.
UCSCiuc011zqm.1. mouse. [Q923B0-1]

Organism-specific databases

CTDi87769.
MGIiMGI:2385008. Ggact.

Phylogenomic databases

eggNOGiKOG4450. Eukaryota.
ENOG4111N8W. LUCA.
GeneTreeiENSGT00390000010543.
HOGENOMiHOG000261862.
HOVERGENiHBG105481.
InParanoidiQ923B0.
KOiK19761.
OMAiRIQVVEW.
OrthoDBiEOG7TBC3D.
TreeFamiTF323258.

Miscellaneous databases

EvolutionaryTraceiQ923B0.
NextBioi376683.
PROiQ923B0.
SOURCEiSearch...

Gene expression databases

BgeeiQ923B0.
ExpressionAtlasiQ923B0. baseline and differential.
GenevisibleiQ923B0. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: Czech II.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney and Liver.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT.
  5. "Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites."
    Serrano P., Pedrini B., Geralt M., Jaudzems K., Mohanty B., Horst R., Herrmann T., Elsliger M.A., Wilson I.A., Wuthrich K.
    Acta Crystallogr. F 66:1393-1405(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiGGACT_MOUSE
AccessioniPrimary (citable) accession number: Q923B0
Secondary accession number(s): Q66JP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 1, 2001
Last modified: March 16, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.