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Protein

Gamma-glutamyltransferase light chain 2

Gene

GGTLC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei37 – 371NucleophileBy similarity
Binding sitei55 – 551GlutamateBy similarity
Binding sitei76 – 761GlutamateBy similarity

GO - Molecular functioni

  • gamma-glutamyltransferase activity Source: UniProtKB

GO - Biological processi

  • glutathione metabolic process Source: UniProtKB
  • leukotriene biosynthetic process Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyltransferase light chain 2
Alternative name(s):
Gamma-glutamyltransferase-like protein 4
Gene namesi
Name:GGTLC2
Synonyms:GGTL4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:18596. GGTLC2.

Subcellular locationi

GO - Cellular componenti

  • anchored component of external side of plasma membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162389523.

Polymorphism and mutation databases

BioMutaiGGTLC2.
DMDMi294862536.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Gamma-glutamyltransferase light chain 2PRO_0000205982Add
BLAST

Proteomic databases

PaxDbiQ14390.
PeptideAtlasiQ14390.
PRIDEiQ14390.

PTM databases

iPTMnetiQ14390.

Expressioni

Tissue specificityi

Placenta and sigmoid tissues.

Gene expression databases

BgeeiQ14390.
CleanExiHS_GGTLC2.
ExpressionAtlasiQ14390. baseline and differential.
GenevisibleiQ14390. HS.

Organism-specific databases

HPAiHPA045635.
HPA047534.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000419751.

Structurei

3D structure databases

ProteinModelPortaliQ14390.
SMRiQ14390. Positions 1-31, 37-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 1082Glutamate bindingBy similarity

Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Phylogenomic databases

eggNOGiKOG2410. Eukaryota.
COG0405. LUCA.
GeneTreeiENSGT00550000074591.
HOGENOMiHOG000074069.
HOVERGENiHBG051730.
InParanoidiQ14390.
OrthoDBiEOG7V7665.
PhylomeDBiQ14390.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q14390-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSEFFAAQL RAQISDDTTH PISYYKPEFY TPVDGGTAHL SVVAEDGSAV
60 70 80 90 100
SATSTINLYF GSKVRSPVSE ILFNDEMDDF SSPNITNEFG VPPSPANFIQ
110 120 130 140 150
PGKQPLSSMC PTIMVGQDGQ PPSHADHTPM PQAIIYNLWF GYDVKRAVEE
160 170 180 190 200
PRLHNQLLPN VTTVERNIDQ AVTAALETRH HHTQIASTFI AVVQAIVRTA
210
GGWAAASDSR KGGEPAGY
Length:218
Mass (Da):23,661
Last modified:April 20, 2010 - v4
Checksum:i66AD78A639C74E36
GO

Sequence cautioni

The sequence BAA20001.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAA67421.1 differs from that shown.Contains an unspliced intron inserted in position 120.Curated
The sequence CAA67421.1 differs from that shown. Reason: Frameshift at position 217. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81A → R in CAA67421 (PubMed:8830654).Curated
Sequence conflicti214 – 2141E → V in CAA67421 (PubMed:8830654).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti70 – 701E → G.2 Publications
Corresponds to variant rs2904923 [ dbSNP | Ensembl ].
VAR_035113
Natural varianti75 – 751D → N.
Corresponds to variant rs2330126 [ dbSNP | Ensembl ].
VAR_055836

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98922 mRNA. Translation: CAA67421.1. Sequence problems.
D87002 Genomic DNA. Translation: BAA20001.1. Sequence problems.
AC002308 Genomic DNA. No translation available.
BC069534 mRNA. Translation: AAH69534.1.
EL736203 mRNA. No translation available.
CCDSiCCDS13802.2.
PIRiS74240.
RefSeqiNP_001269808.1. NM_001282879.1.
NP_954578.2. NM_199127.2.
UniGeneiHs.450000.
Hs.632765.

Genome annotation databases

EnsembliENST00000480559; ENSP00000419751; ENSG00000100121.
GeneIDi91227.
KEGGihsa:91227.
UCSCiuc010gtt.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98922 mRNA. Translation: CAA67421.1. Sequence problems.
D87002 Genomic DNA. Translation: BAA20001.1. Sequence problems.
AC002308 Genomic DNA. No translation available.
BC069534 mRNA. Translation: AAH69534.1.
EL736203 mRNA. No translation available.
CCDSiCCDS13802.2.
PIRiS74240.
RefSeqiNP_001269808.1. NM_001282879.1.
NP_954578.2. NM_199127.2.
UniGeneiHs.450000.
Hs.632765.

3D structure databases

ProteinModelPortaliQ14390.
SMRiQ14390. Positions 1-31, 37-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000419751.

PTM databases

iPTMnetiQ14390.

Polymorphism and mutation databases

BioMutaiGGTLC2.
DMDMi294862536.

Proteomic databases

PaxDbiQ14390.
PeptideAtlasiQ14390.
PRIDEiQ14390.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000480559; ENSP00000419751; ENSG00000100121.
GeneIDi91227.
KEGGihsa:91227.
UCSCiuc010gtt.3. human.

Organism-specific databases

CTDi91227.
GeneCardsiGGTLC2.
H-InvDBHIX0041180.
HGNCiHGNC:18596. GGTLC2.
HPAiHPA045635.
HPA047534.
MIMi612339. gene.
neXtProtiNX_Q14390.
PharmGKBiPA162389523.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2410. Eukaryota.
COG0405. LUCA.
GeneTreeiENSGT00550000074591.
HOGENOMiHOG000074069.
HOVERGENiHBG051730.
InParanoidiQ14390.
OrthoDBiEOG7V7665.
PhylomeDBiQ14390.

Miscellaneous databases

GenomeRNAii91227.
PROiQ14390.
SOURCEiSearch...

Gene expression databases

BgeeiQ14390.
CleanExiHS_GGTLC2.
ExpressionAtlasiQ14390. baseline and differential.
GenevisibleiQ14390. HS.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a novel type (III) of human gamma-glutamyltransferase truncated mRNA."
    Leh L., Courtey C., Gerardin P., Wellman M., Siest G., Visvikis A.
    FEBS Lett. 394:258-262(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-70.
    Tissue: Placenta.
  2. "One-megabase sequence analysis of the human immunoglobulin lambda gene locus."
    Kawasaki K., Minoshima S., Nakato E., Shibuya K., Shintani A., Schmeits J.L., Wang J., Shimizu N.
    Genome Res. 7:250-261(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    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], VARIANT GLY-70.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-212.
  6. Cited for: NOMENCLATURE.

Entry informationi

Entry nameiGGTL2_HUMAN
AccessioniPrimary (citable) accession number: Q14390
Secondary accession number(s): A1A516
, A2VCM9, Q5NV76, Q6ISH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: April 20, 2010
Last modified: July 6, 2016
This is version 123 of the entry and version 4 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

Miscellaneous

Corresponds to the light chain of other gamma-glutamyltransferase family members. Has no catalytic activity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.