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Protein

Gamma-glutamyltransferase 5

Gene

GGT5

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

Functioni

Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4).

Catalytic activityi

A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.
Glutathione + H2O = L-cysteinylglycine + L-glutamate.
Leukotriene C4 + H2O = leukotriene D4 + L-glutamate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101GlutamateBy similarity
Active sitei388 – 3881NucleophileBy similarity
Binding sitei406 – 4061GlutamateBy similarity
Binding sitei427 – 4271GlutamateBy similarity

GO - Molecular functioni

  1. gamma-glutamyltransferase activity Source: UniProtKB
  2. glutathione hydrolase activity Source: UniProtKB-EC

GO - Biological processi

  1. arachidonic acid metabolic process Source: Reactome
  2. cellular amino acid metabolic process Source: ProtInc
  3. glutathione biosynthetic process Source: UniProtKB-KW
  4. glutathione metabolic process Source: UniProtKB
  5. inflammatory response Source: Ensembl
  6. leukotriene biosynthetic process Source: UniProtKB
  7. leukotriene metabolic process Source: Reactome
  8. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Hydrolase, Protease, Transferase

Keywords - Biological processi

Glutathione biosynthesis, Leukotriene biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:HS01949-MONOMER.
ReactomeiREACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_228214. Aflatoxin activation and detoxification.
REACT_6960. Glutathione synthesis and recycling.
UniPathwayiUPA00204.
UPA00880.

Protein family/group databases

MEROPSiT03.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyltransferase 5 (EC:2.3.2.2)
Short name:
GGT 5
Alternative name(s):
Gamma-glutamyl transpeptidase-related enzyme
Short name:
GGT-rel
Gamma-glutamyltransferase-like activity 1
Gamma-glutamyltranspeptidase 5
Glutathione hydrolase 5 (EC:3.4.19.13)
Leukotriene-C4 hydrolase (EC:3.4.19.14)
Cleaved into the following 2 chains:
Gene namesi
Name:GGT5
Synonyms:GGTLA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:4260. GGT5.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence Analysis
Transmembranei9 – 2921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini30 – 586557ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. anchored component of external side of plasma membrane Source: UniProtKB
  2. integral component of membrane Source: ProtInc
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162389442.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 387387Gamma-glutamyltransferase 5 heavy chainBy similarityPRO_0000011072Add
BLAST
Chaini388 – 586199Gamma-glutamyltransferase 5 light chainBy similarityPRO_0000011073Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi535 – 5351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi550 – 5501N-linked (GlcNAc...)1 Publication

Post-translational modificationi

Cleaved by autocatalysis into a large and a small subunit.By similarity

Keywords - PTMi

Glycoprotein, Zymogen

Proteomic databases

MaxQBiP36269.
PaxDbiP36269.
PRIDEiP36269.

PTM databases

PhosphoSiteiP36269.

Expressioni

Gene expression databases

BgeeiP36269.
CleanExiHS_GGT5.
ExpressionAtlasiP36269. baseline and differential.
GenevestigatoriP36269.

Organism-specific databases

HPAiCAB032489.
HPA008121.

Interactioni

Subunit structurei

Heterodimer composed of the light and heavy chains. The active site is located in the light chain (By similarity).By similarity

Protein-protein interaction databases

STRINGi9606.ENSP00000381340.

Structurei

3D structure databases

ProteinModelPortaliP36269.
SMRiP36269. Positions 38-586.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni469 – 4702Glutamate bindingBy similarity

Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0405.
GeneTreeiENSGT00550000074591.
HOGENOMiHOG000175620.
HOVERGENiHBG005835.
InParanoidiP36269.
KOiK18592.
OMAiICTSVMN.
OrthoDBiEOG7V7665.
PhylomeDBiP36269.
TreeFamiTF313608.

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]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P36269-1) [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
MARGYGATVS LVLLGLGLAL AVIVLAVVLS RHQAPCGPQA FAHAAVAADS
60 70 80 90 100
KVCSDIGRAI LQQQGSPVDA TIAALVCTSV VNPQSMGLGG GVIFTIYNVT
110 120 130 140 150
TGKVEVINAR ETVPASHAPS LLDQCAQALP LGTGAQWIGV PGELRGYAEA
160 170 180 190 200
HRRHGRLPWA QLFQPTIALL RGGHVVAPVL SRFLHNSILR PSLQASTLRQ
210 220 230 240 250
LFFNGTEPLR PQDPLPWPAL ATTLETVATE GVEVFYTGRL GQMLVEDIAK
260 270 280 290 300
EGSQLTLQDL AKFQPEVVDA LEVPLGDYTL YSPPPPAGGA ILSFILNVLR
310 320 330 340 350
GFNFSTESMA RPEGRVNVYH HLVETLKFAK GQRWRLGDPR SHPKLQNASR
360 370 380 390 400
DLLGETLAQL IRQQIDGRGD HQLSHYSLAE AWGHGTGTSH VSVLGEDGSA
410 420 430 440 450
VAATSTINTP FGAMVYSPRT GIILNNELLD LCERCPRGSG TTPSPVSGDR
460 470 480 490 500
VGGAPGRCWP PVPGERSPSS MVPSILINKA QGSKLVIGGA GGELIISAVA
510 520 530 540 550
QAIMSKLWLG FDLRAAIAAP ILHVNSKGCV EYEPNFSQEV QRGLQDRGQN
560 570 580
QTQRPFFLNV VQAVSQEGAC VYAVSDLRKS GEAAGY
Length:586
Mass (Da):62,261
Last modified:October 17, 2006 - v2
Checksum:iEE37B3CE516F5788
GO
Isoform 2 (identifier: P36269-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     101-132: Missing.

Note: No experimental confirmation available.

Show »
Length:554
Mass (Da):58,992
Checksum:i86001882BE5A0D10
GO
Isoform 3 (identifier: P36269-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     445-445: P → PA

Note: No experimental confirmation available.

Show »
Length:587
Mass (Da):62,332
Checksum:iC7F2285F9FFF1A22
GO

Sequence cautioni

The sequence CAB55910.1 differs from that shown. Reason: Frameshift at position 446. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti408 – 4081N → Y in CAB55910. (PubMed:17974005)Curated
Sequence conflicti437 – 4371R → W in AAA58503. (PubMed:1676842)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111L → I.
Corresponds to variant rs5760274 [ dbSNP | Ensembl ].
VAR_028006
Natural varianti330 – 3301K → R.2 Publications
Corresponds to variant rs2275984 [ dbSNP | Ensembl ].
VAR_028007
Natural varianti332 – 3321Q → H.
Corresponds to variant rs6004105 [ dbSNP | Ensembl ].
VAR_028008
Natural varianti475 – 4751I → V.
Corresponds to variant rs7288201 [ dbSNP | Ensembl ].
VAR_024455

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei101 – 13232Missing in isoform 2. 1 PublicationVSP_008146Add
BLAST
Alternative sequencei445 – 4451P → PA in isoform 3. 1 PublicationVSP_043470

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64099 mRNA. Translation: AAA58503.1.
AL117414 mRNA. Translation: CAB55910.1. Frameshift.
BT009808 mRNA. Translation: AAP88810.1.
CT841518 mRNA. Translation: CAJ86448.1.
AK292006 mRNA. Translation: BAF84695.1.
AP000353 Genomic DNA. No translation available.
AP000354 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW59643.1.
BC011362 mRNA. Translation: AAH11362.1.
BC073999 mRNA. Translation: AAH73999.1.
CCDSiCCDS13825.1. [P36269-1]
CCDS42989.1. [P36269-2]
CCDS42990.1. [P36269-3]
PIRiA41125.
T17220.
RefSeqiNP_001093251.1. NM_001099781.2. [P36269-3]
NP_001093252.1. NM_001099782.2. [P36269-2]
NP_001289393.1. NM_001302464.1.
NP_001289394.1. NM_001302465.1.
NP_004112.2. NM_004121.3. [P36269-1]
UniGeneiHs.437156.

Genome annotation databases

EnsembliENST00000263112; ENSP00000263112; ENSG00000099998. [P36269-2]
ENST00000327365; ENSP00000330080; ENSG00000099998. [P36269-1]
ENST00000398292; ENSP00000381340; ENSG00000099998. [P36269-3]
GeneIDi2687.
KEGGihsa:2687.
UCSCiuc002zzo.4. human. [P36269-1]
uc002zzp.4. human. [P36269-3]
uc002zzq.4. human. [P36269-2]

Polymorphism databases

DMDMi116242493.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64099 mRNA. Translation: AAA58503.1.
AL117414 mRNA. Translation: CAB55910.1. Frameshift.
BT009808 mRNA. Translation: AAP88810.1.
CT841518 mRNA. Translation: CAJ86448.1.
AK292006 mRNA. Translation: BAF84695.1.
AP000353 Genomic DNA. No translation available.
AP000354 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW59643.1.
BC011362 mRNA. Translation: AAH11362.1.
BC073999 mRNA. Translation: AAH73999.1.
CCDSiCCDS13825.1. [P36269-1]
CCDS42989.1. [P36269-2]
CCDS42990.1. [P36269-3]
PIRiA41125.
T17220.
RefSeqiNP_001093251.1. NM_001099781.2. [P36269-3]
NP_001093252.1. NM_001099782.2. [P36269-2]
NP_001289393.1. NM_001302464.1.
NP_001289394.1. NM_001302465.1.
NP_004112.2. NM_004121.3. [P36269-1]
UniGeneiHs.437156.

3D structure databases

ProteinModelPortaliP36269.
SMRiP36269. Positions 38-586.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000381340.

Protein family/group databases

MEROPSiT03.002.

PTM databases

PhosphoSiteiP36269.

Polymorphism databases

DMDMi116242493.

Proteomic databases

MaxQBiP36269.
PaxDbiP36269.
PRIDEiP36269.

Protocols and materials databases

DNASUi2687.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263112; ENSP00000263112; ENSG00000099998. [P36269-2]
ENST00000327365; ENSP00000330080; ENSG00000099998. [P36269-1]
ENST00000398292; ENSP00000381340; ENSG00000099998. [P36269-3]
GeneIDi2687.
KEGGihsa:2687.
UCSCiuc002zzo.4. human. [P36269-1]
uc002zzp.4. human. [P36269-3]
uc002zzq.4. human. [P36269-2]

Organism-specific databases

CTDi2687.
GeneCardsiGC22M024615.
H-InvDBHIX0138942.
HGNCiHGNC:4260. GGT5.
HPAiCAB032489.
HPA008121.
MIMi137168. gene.
neXtProtiNX_P36269.
PharmGKBiPA162389442.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0405.
GeneTreeiENSGT00550000074591.
HOGENOMiHOG000175620.
HOVERGENiHBG005835.
InParanoidiP36269.
KOiK18592.
OMAiICTSVMN.
OrthoDBiEOG7V7665.
PhylomeDBiP36269.
TreeFamiTF313608.

Enzyme and pathway databases

UniPathwayiUPA00204.
UPA00880.
BioCyciMetaCyc:HS01949-MONOMER.
ReactomeiREACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_228214. Aflatoxin activation and detoxification.
REACT_6960. Glutathione synthesis and recycling.

Miscellaneous databases

GeneWikiiGGTLA1.
GenomeRNAii2687.
NextBioi10606.
PROiP36269.
SOURCEiSearch...

Gene expression databases

BgeeiP36269.
CleanExiHS_GGT5.
ExpressionAtlasiP36269. baseline and differential.
GenevestigatoriP36269.

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. "Identification of a human gamma-glutamyl cleaving enzyme related to, but distinct from, gamma-glutamyl transpeptidase."
    Heisterkamp N., Rajpert-De Meyts E., Uribe L., Forman H.J., Groffen J.
    Proc. Natl. Acad. Sci. U.S.A. 88:6303-6307(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-330.
    Tissue: Placenta.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Small intestine.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal kidney.
  6. "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], VARIANT ARG-330.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 3).
    Tissue: Brain and PNS.
  9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-550.
    Tissue: Liver.

Entry informationi

Entry nameiGGT5_HUMAN
AccessioniPrimary (citable) accession number: P36269
Secondary accession number(s): Q53XM9
, Q6GMP0, Q96FC1, Q9UFM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 17, 2006
Last modified: January 7, 2015
This is version 146 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

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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

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.