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Q9UJ14 (GGT7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-glutamyltransferase 7

Short name=GGT 7
EC=2.3.2.2
Alternative name(s):
Gamma-glutamyltransferase-like 3
Gamma-glutamyltransferase-like 5
Gamma-glutamyltranspeptidase 7
Glutathione hydrolase 7
EC=3.4.19.13
Gene names
Name:GGT7
Synonyms:GGTL3, GGTL5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length662 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves glutathione conjugates By similarity.

Catalytic activity

A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.

Glutathione + H2O = L-cysteinylglycine + L-glutamate.

Pathway

Sulfur metabolism; glutathione metabolism.

Subunit structure

Heterodimer composed of the light and heavy chains. The active site is located in the light chain By similarity. Isoform 3 interacts with FAM57A. Ref.1

Subcellular location

Membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

Widely expressed, but at low level, except in the airway epithelial cells. Detected in brain, heart, kidney, liver, lung, spleen, testis and trachea.

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

Sequence caution

The sequence BAC03394.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UJ14-1)

Also known as: a;

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.
Note: Gene prediction confirmed by EST data.
Isoform 2 (identifier: Q9UJ14-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: Missing.
     273-289: ARALAEQLPPNMSERFR → GQWGLGIWERHEVDGEG
     290-662: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9UJ14-5)

Also known as: GGTL3B; B;

The sequence of this isoform differs from the canonical sequence as follows:
     226-251: PGLLVGVPGMVKGLHEAHQLYGRLPW → VGTLVRRESSGESLFIALLLTQALIC
     252-662: Missing.
Isoform 4 (identifier: Q9UJ14-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-283: Missing.
     369-425: HLVLSPPPPH...LALASRLGDP → DLSPGSQGPP...QTRVSPPSEK
     426-662: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Gamma-glutamyltransferase 7 heavy chain By similarity
PRO_0000011066
Chain473 – 662190Gamma-glutamyltransferase 7 light chain By similarity
PRO_0000011067

Regions

Topological domain1 – 106106Cytoplasmic Potential
Transmembrane107 – 12721Helical; Signal-anchor for type II membrane protein; Potential
Topological domain128 – 662535Extracellular Potential

Amino acid modifications

Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2671N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Glycosylation3941N-linked (GlcNAc...) Potential
Glycosylation4521N-linked (GlcNAc...) Potential
Glycosylation5191N-linked (GlcNAc...) Potential
Glycosylation5231N-linked (GlcNAc...) Potential
Glycosylation5861N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 283283Missing in isoform 4.
VSP_008133
Alternative sequence1 – 7676Missing in isoform 2.
VSP_008134
Alternative sequence226 – 25126PGLLV…GRLPW → VGTLVRRESSGESLFIALLL TQALIC in isoform 3.
VSP_008136
Alternative sequence252 – 662411Missing in isoform 3.
VSP_008137
Alternative sequence273 – 28917ARALA…SERFR → GQWGLGIWERHEVDGEG in isoform 2.
VSP_008138
Alternative sequence290 – 662373Missing in isoform 2.
VSP_008139
Alternative sequence369 – 42557HLVLS…RLGDP → DLSPGSQGPPSGEASQSMAT SFWPRDSSPFHRRETKAVSY LGSQLLKQTRVSPPSEK in isoform 4.
VSP_008140
Alternative sequence426 – 662237Missing in isoform 4.
VSP_008141

Experimental info

Sequence conflict51N → K in AAN15928. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (a) [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: 29DDBC719CADD195

FASTA66270,467
        10         20         30         40         50         60 
MAAENEASQE SALGAYSPVD YMSITSFPRL PEDEPAPAAP LRGRKDEDAF LGDPDTDPDS 

        70         80         90        100        110        120 
FLKSARLQRL PSSSSEMGSQ DGSPLRETRK DPFSAAAAEC SCRQDGLTVI VTACLTFATG 

       130        140        150        160        170        180 
VTVALVMQIY FGDPQIFQQG AVVTDAARCT SLGIEVLSKQ GSSVDAAVAA ALCLGIVAPH 

       190        200        210        220        230        240 
SSGLGGGGVM LVHDIRRNES HLIDFRESAP GALREETLQR SWETKPGLLV GVPGMVKGLH 

       250        260        270        280        290        300 
EAHQLYGRLP WSQVLAFAAA VAQDGFNVTH DLARALAEQL PPNMSERFRE TFLPSGRPPL 

       310        320        330        340        350        360 
PGSLLHRPDL AEVLDVLGTS GPAAFYAGGN LTLEMVAEAQ HAGGVITEED FSNYSALVEK 

       370        380        390        400        410        420 
PVCGVYRGHL VLSPPPPHTG PALISALNIL EGFNLTSLVS REQALHWVAE TLKIALALAS 

       430        440        450        460        470        480 
RLGDPVYDST ITESMDDMLS KVEAAYLRGH INDSQAAPAP LLPVYELDGA PTAAQVLIMG 

       490        500        510        520        530        540 
PDDFIVAMVS SLNQPFGSGL ITPSGILLNS QMLDFSWPNR TANHSAPSLE NSVQPGKRPL 

       550        560        570        580        590        600 
SFLLPTVVRP AEGLCGTYLA LGANGAARGL SGLTQVLLNV LTLNRNLSDS LARGRLHPDL 

       610        620        630        640        650        660 
QSNLLQVDSE FTEEEIEFLE ARGHHVEKVD VLSWVHGSRR TNNFIIAVKD PRSPDAAGAT 


IL 

« Hide

Isoform 2 [UniParc].

Checksum: 830752C08248C1DA
Show »

FASTA21322,494
Isoform 3 (GGTL3B) (B) [UniParc].

Checksum: 3A8BBC5A2B81311C
Show »

FASTA25126,578
Isoform 4 [UniParc].

Checksum: 15B48378E9DCA3A5
Show »

FASTA14215,236

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of CT120, a novel membrane-associated gene involved in amino acid transport and glutathione metabolism."
He X.H., Di Y., Li J., Xie Y., Tang Y., Zhang F., Wei L., Zhang Y., Qin W.X., Huo K., Li Y., Wan D.F., Gu J.R.
Biochem. Biophys. Res. Commun. 297:528-536(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH FAM57A.
[2]"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] (ISOFORM 2).
Tissue: Spleen.
[3]"Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones."
Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O.
DNA Res. 10:49-57(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Spleen.
[4]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The human gamma-glutamyltransferase gene family."
Heisterkamp N., Groffen J., Warburton D., Sneddon T.P.
Hum. Genet. 123:321-332(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY138815 mRNA. Translation: AAN15928.1.
AK097100 mRNA. Translation: BAC04950.1.
AK090413 mRNA. Translation: BAC03394.1. Different initiation.
AL049709 Genomic DNA. Translation: CAB61787.2.
CCDSCCDS13242.2. [Q9UJ14-1]
RefSeqNP_821158.2. NM_178026.2. [Q9UJ14-1]
UniGeneHs.433738.

3D structure databases

ProteinModelPortalQ9UJ14.
SMRQ9UJ14. Positions 133-655.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108953. 2 interactions.
IntActQ9UJ14. 1 interaction.
STRING9606.ENSP00000338964.

Protein family/group databases

MEROPST03.017.

PTM databases

PhosphoSiteQ9UJ14.

Polymorphism databases

DMDM152031612.

Proteomic databases

MaxQBQ9UJ14.
PaxDbQ9UJ14.
PRIDEQ9UJ14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336431; ENSP00000338964; ENSG00000131067. [Q9UJ14-1]
GeneID2686.
KEGGhsa:2686.
UCSCuc002xay.3. human. [Q9UJ14-1]
uc002xba.1. human. [Q9UJ14-5]

Organism-specific databases

CTD2686.
GeneCardsGC20M033435.
H-InvDBHIX0203047.
HGNCHGNC:4259. GGT7.
HPAHPA013204.
MIM612342. gene.
neXtProtNX_Q9UJ14.
PharmGKBPA28669.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0405.
HOGENOMHOG000231793.
HOVERGENHBG039468.
InParanoidQ9UJ14.
KOK00681.
OMAMLVHDIR.
OrthoDBEOG7DNNTR.
PhylomeDBQ9UJ14.
TreeFamTF333329.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00204.

Gene expression databases

ArrayExpressQ9UJ14.
BgeeQ9UJ14.
CleanExHS_GGT7.
GenevestigatorQ9UJ14.

Family and domain databases

InterProIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERPTHR11686. PTHR11686. 1 hit.
PfamPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSPR01210. GGTRANSPTASE.
SUPFAMSSF56235. SSF56235. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGGT7. human.
GeneWikiGGTL3.
GenomeRNAi2686.
NextBio10602.
PROQ9UJ14.
SOURCESearch...

Entry information

Entry nameGGT7_HUMAN
AccessionPrimary (citable) accession number: Q9UJ14
Secondary accession number(s): Q8N899 expand/collapse secondary AC list , Q8NF66, Q9BYP5, Q9BYP6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: July 10, 2007
Last modified: July 9, 2014
This is version 115 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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM