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O75223

- GGCT_HUMAN

UniProt

O75223 - GGCT_HUMAN

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Protein
Gamma-glutamylcyclotransferase
Gene
GGCT, C7orf24, CRF21
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and may play a significant role in glutathione homeostasis. Induces release of cytochrome c from mitochondria with resultant induction of apoptosis.2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=2.0 mM for gamma-glutamyl-L-alanine

Vmax=50.3 µmol/min/mg enzyme

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei98 – 981Proton acceptor By similarity

GO - Molecular functioni

  1. gamma-glutamylcyclotransferase activity Source: UniProtKB
  2. protein homodimerization activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. glutathione biosynthetic process Source: Reactome
  2. glutathione derivative biosynthetic process Source: Reactome
  3. release of cytochrome c from mitochondria Source: UniProtKB
  4. small molecule metabolic process Source: Reactome
  5. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_6960. Glutathione synthesis and recycling.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamylcyclotransferase (EC:2.3.2.4)
Alternative name(s):
Cytochrome c-releasing factor 21
Gene namesi
Name:GGCT
Synonyms:C7orf24, CRF21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:21705. GGCT.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231G → A: Marked decrease in catalytic efficiency. 1 Publication
Mutagenesisi98 – 981E → A or Q: Abolishes activity without altering structure. 1 Publication
Mutagenesisi105 – 1051Y → F: Marked decrease in catalytic efficiency and specific activity. 1 Publication
Mutagenesisi125 – 1251Y → F: Little or no change in reaction kinetics. 1 Publication

Organism-specific databases

PharmGKBiPA162389392.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Gamma-glutamylcyclotransferase
PRO_0000089580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei173 – 1731Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75223.
PaxDbiO75223.
PeptideAtlasiO75223.
PRIDEiO75223.

2D gel databases

OGPiO75223.

PTM databases

PhosphoSiteiO75223.

Expressioni

Inductioni

By geranylgeraniol.1 Publication

Gene expression databases

ArrayExpressiO75223.
BgeeiO75223.
CleanExiHS_GGCT.
GenevestigatoriO75223.

Organism-specific databases

HPAiHPA020735.
HPA029914.

Interactioni

Subunit structurei

Homodimer Inferred.2 Publications

Protein-protein interaction databases

BioGridi122486. 3 interactions.
IntActiO75223. 4 interactions.
STRINGi9606.ENSP00000275428.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 216
Helixi24 – 263
Helixi28 – 347
Beta strandi39 – 5618
Turni62 – 643
Beta strandi68 – 8720
Helixi88 – 903
Helixi91 – 977
Helixi100 – 1023
Beta strandi106 – 1149
Beta strandi119 – 1268
Beta strandi128 – 1325
Helixi137 – 14913
Helixi154 – 1618
Helixi174 – 1818

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I5TX-ray2.01A/B2-188[»]
2PN7X-ray2.41A/B1-188[»]
2Q53X-ray2.01A/B2-188[»]
2RBHX-ray2.10A/B1-188[»]
3CRYX-ray1.70A/B1-188[»]
ProteinModelPortaliO75223.
SMRiO75223. Positions 15-183.

Miscellaneous databases

EvolutionaryTraceiO75223.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 224Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG87076.
HOGENOMiHOG000008049.
HOVERGENiHBG050922.
InParanoidiO75223.
KOiK00682.
OMAiKKVICMG.
OrthoDBiEOG7H1JNT.
PhylomeDBiO75223.
TreeFamiTF314378.

Family and domain databases

Gene3Di3.10.490.10. 1 hit.
InterProiIPR013024. Butirosin_synth_BtrG-like.
IPR017939. G-Glutamylcylcotransferase.
[Graphical view]
PANTHERiPTHR12935. PTHR12935. 1 hit.
SUPFAMiSSF110857. SSF110857. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75223-1) [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

MANSGCKDVT GPDEESFLYF AYGSNLLTER IHLRNPSAAF FCVARLQDFK    50
LDFGNSQGKT SQTWHGGIAT IFQSPGDEVW GVVWKMNKSN LNSLDEQEGV 100
KSGMYVVIEV KVATQEGKEI TCRSYLMTNY ESAPPSPQYK KIICMGAKEN 150
GLPLEYQEKL KAIEPNDYTG KVSEEIEDII KKGETQTL 188
Length:188
Mass (Da):21,008
Last modified:November 1, 1998 - v1
Checksum:i88B5C6F67F31C56C
GO
Isoform 2 (identifier: O75223-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     97-114: QEGVKSGMYVVIEVKVAT → LFAWVQKKMVCRWSIKRS
     115-188: Missing.

Note: No experimental confirmation available.

Show »
Length:114
Mass (Da):12,943
Checksum:i45207EF9348A6A72
GO
Isoform 3 (identifier: O75223-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     48-141: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:94
Mass (Da):10,504
Checksum:i8E15402CE6521BCC
GO
Isoform 4 (identifier: O75223-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     97-188: QEGVKSGMYV...IIKKGETQTL → WRKKRHTAFQ...MVCRWSIKRS

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:166
Mass (Da):19,092
Checksum:iD0D2773376F33287
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei48 – 14194Missing in isoform 3.
VSP_046463Add
BLAST
Alternative sequencei97 – 18892QEGVK…ETQTL → WRKKRHTAFQNQGNHPCKHK TRMWDRDPKIPVQNLSLALC WQAQSGHGTCNRLFAWVQKK MVCRWSIKRS in isoform 4.
VSP_046464Add
BLAST
Alternative sequencei97 – 11418QEGVK…VKVAT → LFAWVQKKMVCRWSIKRS in isoform 2.
VSP_035599Add
BLAST
Alternative sequencei115 – 18874Missing in isoform 2.
VSP_035600Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK315608 mRNA. Translation: BAG37977.1.
AC005154 Genomic DNA. No translation available.
CH471073 Genomic DNA. Translation: EAW93950.1.
CH471073 Genomic DNA. Translation: EAW93952.1.
CH471073 Genomic DNA. Translation: EAW93953.1.
BC000625 mRNA. Translation: AAH00625.1.
BC005356 mRNA. Translation: AAH05356.1.
BC013937 mRNA. Translation: AAH13937.1.
BC019243 mRNA. Translation: AAH19243.1.
CCDSiCCDS5428.1. [O75223-1]
CCDS56474.1. [O75223-3]
CCDS56475.1. [O75223-2]
CCDS56476.1. [O75223-4]
RefSeqiNP_001186744.1. NM_001199815.1. [O75223-4]
NP_001186745.1. NM_001199816.1. [O75223-2]
NP_001186746.1. NM_001199817.1. [O75223-3]
NP_076956.1. NM_024051.3. [O75223-1]
UniGeneiHs.530024.

Genome annotation databases

EnsembliENST00000005374; ENSP00000005374; ENSG00000006625. [O75223-2]
ENST00000275428; ENSP00000275428; ENSG00000006625. [O75223-1]
ENST00000409144; ENSP00000386610; ENSG00000006625. [O75223-3]
ENST00000409390; ENSP00000387235; ENSG00000006625. [O75223-4]
GeneIDi79017.
KEGGihsa:79017.
UCSCiuc003tba.3. human. [O75223-1]
uc003tbb.3. human. [O75223-2]
uc022abe.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK315608 mRNA. Translation: BAG37977.1 .
AC005154 Genomic DNA. No translation available.
CH471073 Genomic DNA. Translation: EAW93950.1 .
CH471073 Genomic DNA. Translation: EAW93952.1 .
CH471073 Genomic DNA. Translation: EAW93953.1 .
BC000625 mRNA. Translation: AAH00625.1 .
BC005356 mRNA. Translation: AAH05356.1 .
BC013937 mRNA. Translation: AAH13937.1 .
BC019243 mRNA. Translation: AAH19243.1 .
CCDSi CCDS5428.1. [O75223-1 ]
CCDS56474.1. [O75223-3 ]
CCDS56475.1. [O75223-2 ]
CCDS56476.1. [O75223-4 ]
RefSeqi NP_001186744.1. NM_001199815.1. [O75223-4 ]
NP_001186745.1. NM_001199816.1. [O75223-2 ]
NP_001186746.1. NM_001199817.1. [O75223-3 ]
NP_076956.1. NM_024051.3. [O75223-1 ]
UniGenei Hs.530024.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I5T X-ray 2.01 A/B 2-188 [» ]
2PN7 X-ray 2.41 A/B 1-188 [» ]
2Q53 X-ray 2.01 A/B 2-188 [» ]
2RBH X-ray 2.10 A/B 1-188 [» ]
3CRY X-ray 1.70 A/B 1-188 [» ]
ProteinModelPortali O75223.
SMRi O75223. Positions 15-183.
ModBasei Search...

Protein-protein interaction databases

BioGridi 122486. 3 interactions.
IntActi O75223. 4 interactions.
STRINGi 9606.ENSP00000275428.

PTM databases

PhosphoSitei O75223.

2D gel databases

OGPi O75223.

Proteomic databases

MaxQBi O75223.
PaxDbi O75223.
PeptideAtlasi O75223.
PRIDEi O75223.

Protocols and materials databases

DNASUi 79017.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000005374 ; ENSP00000005374 ; ENSG00000006625 . [O75223-2 ]
ENST00000275428 ; ENSP00000275428 ; ENSG00000006625 . [O75223-1 ]
ENST00000409144 ; ENSP00000386610 ; ENSG00000006625 . [O75223-3 ]
ENST00000409390 ; ENSP00000387235 ; ENSG00000006625 . [O75223-4 ]
GeneIDi 79017.
KEGGi hsa:79017.
UCSCi uc003tba.3. human. [O75223-1 ]
uc003tbb.3. human. [O75223-2 ]
uc022abe.1. human.

Organism-specific databases

CTDi 79017.
GeneCardsi GC07M030536.
HGNCi HGNC:21705. GGCT.
HPAi HPA020735.
HPA029914.
MIMi 137170. gene.
neXtProti NX_O75223.
PharmGKBi PA162389392.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG87076.
HOGENOMi HOG000008049.
HOVERGENi HBG050922.
InParanoidi O75223.
KOi K00682.
OMAi KKVICMG.
OrthoDBi EOG7H1JNT.
PhylomeDBi O75223.
TreeFami TF314378.

Enzyme and pathway databases

Reactomei REACT_6960. Glutathione synthesis and recycling.

Miscellaneous databases

ChiTaRSi GGCT. human.
EvolutionaryTracei O75223.
GenomeRNAii 79017.
NextBioi 67678.
PROi O75223.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75223.
Bgeei O75223.
CleanExi HS_GGCT.
Genevestigatori O75223.

Family and domain databases

Gene3Di 3.10.490.10. 1 hit.
InterProi IPR013024. Butirosin_synth_BtrG-like.
IPR017939. G-Glutamylcylcotransferase.
[Graphical view ]
PANTHERi PTHR12935. PTHR12935. 1 hit.
SUPFAMi SSF110857. SSF110857. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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: Skeletal muscle.
  2. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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] (ISOFORMS 1 AND 2).
    Tissue: Kidney, Lung, Skin and Urinary bladder.
  5. "A novel 21-kDa cytochrome c-releasing factor is generated upon treatment of human leukemia U937 cells with geranylgeraniol."
    Masuda Y., Maeda S., Watanabe A., Sano Y., Aiuchi T., Nakajo S., Itabe H., Nakaya K.
    Biochem. Biophys. Res. Commun. 346:454-460(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INDUCTION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "The identification and structural characterization of C7orf24 as gamma-glutamyl cyclotransferase: an essential enzyme in the gamma-glutamyl cycle."
    Oakley A.J., Yamada T., Liu D., Coggan M., Clark A.G., Board P.G.
    J. Biol. Chem. 283:22031-22042(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLY-23; GLU-98; TYR-105 AND TYR-125.
  8. "Crystal structure of Homo sapiens protein LOC79017."
    Bae E., Bingman C.A., Aceti D.J., Phillips G.N. Jr.
    Proteins 70:588-591(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 2-188, SUBUNIT.

Entry informationi

Entry nameiGGCT_HUMAN
AccessioniPrimary (citable) accession number: O75223
Secondary accession number(s): B2RDN0
, B8ZZN4, B8ZZR8, Q9BS37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: November 1, 1998
Last modified: September 3, 2014
This is version 105 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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