Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O75223 (GGCT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. 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-glutamylcyclotransferase

EC=2.3.2.4
Alternative name(s):
Cytochrome c-releasing factor 21
Gene names
Name:GGCT
Synonyms:C7orf24, CRF21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.7

Catalytic activity

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

Subunit structure

Homodimer Probable. Ref.7 Ref.8

Induction

By geranylgeraniol. Ref.5

Sequence similarities

Belongs to the gamma-glutamylcyclotransferase family.

Biophysicochemical properties

Kinetic parameters:

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

Vmax=50.3 µmol/min/mg enzyme

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75223-1)

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.
Isoform 2 (identifier: O75223-2)

The sequence of this isoform differs from the canonical sequence as follows:
     97-114: QEGVKSGMYVVIEVKVAT → LFAWVQKKMVCRWSIKRS
     115-188: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O75223-3)

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.
Isoform 4 (identifier: O75223-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 188188Gamma-glutamylcyclotransferase
PRO_0000089580

Regions

Region19 – 224Substrate binding By similarity

Sites

Active site981Proton acceptor By similarity

Amino acid modifications

Modified residue1731Phosphoserine By similarity

Natural variations

Alternative sequence48 – 14194Missing in isoform 3.
VSP_046463
Alternative sequence97 – 18892QEGVK…ETQTL → WRKKRHTAFQNQGNHPCKHK TRMWDRDPKIPVQNLSLALC WQAQSGHGTCNRLFAWVQKK MVCRWSIKRS in isoform 4.
VSP_046464
Alternative sequence97 – 11418QEGVK…VKVAT → LFAWVQKKMVCRWSIKRS in isoform 2.
VSP_035599
Alternative sequence115 – 18874Missing in isoform 2.
VSP_035600

Experimental info

Mutagenesis231G → A: Marked decrease in catalytic efficiency. Ref.7
Mutagenesis981E → A or Q: Abolishes activity without altering structure. Ref.7
Mutagenesis1051Y → F: Marked decrease in catalytic efficiency and specific activity. Ref.7
Mutagenesis1251Y → F: Little or no change in reaction kinetics. Ref.7

Secondary structure

............................. 188
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1998. Version 1.
Checksum: 88B5C6F67F31C56C

FASTA18821,008
        10         20         30         40         50         60 
MANSGCKDVT GPDEESFLYF AYGSNLLTER IHLRNPSAAF FCVARLQDFK LDFGNSQGKT 

        70         80         90        100        110        120 
SQTWHGGIAT IFQSPGDEVW GVVWKMNKSN LNSLDEQEGV KSGMYVVIEV KVATQEGKEI 

       130        140        150        160        170        180 
TCRSYLMTNY ESAPPSPQYK KIICMGAKEN GLPLEYQEKL KAIEPNDYTG KVSEEIEDII 


KKGETQTL 

« Hide

Isoform 2 [UniParc].

Checksum: 45207EF9348A6A72
Show »

FASTA11412,943
Isoform 3 [UniParc].

Checksum: 8E15402CE6521BCC
Show »

FASTA9410,504
Isoform 4 [UniParc].

Checksum: D0D2773376F33287
Show »

FASTA16619,092

References

« Hide 'large scale' references
[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. 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 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5428.1. [O75223-1]
CCDS56474.1. [O75223-3]
CCDS56475.1. [O75223-2]
CCDS56476.1. [O75223-4]
RefSeqNP_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]
UniGeneHs.530024.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalO75223.
SMRO75223. Positions 15-183.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122486. 3 interactions.
IntActO75223. 4 interactions.
STRING9606.ENSP00000275428.

PTM databases

PhosphoSiteO75223.

2D gel databases

OGPO75223.

Proteomic databases

MaxQBO75223.
PaxDbO75223.
PeptideAtlasO75223.
PRIDEO75223.

Protocols and materials databases

DNASU79017.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000005374; ENSP00000005374; ENSG00000006625. [O75223-2]
ENST00000275428; ENSP00000275428; ENSG00000006625. [O75223-1]
ENST00000409144; ENSP00000386610; ENSG00000006625. [O75223-3]
ENST00000409390; ENSP00000387235; ENSG00000006625. [O75223-4]
GeneID79017.
KEGGhsa:79017.
UCSCuc003tba.3. human. [O75223-1]
uc003tbb.3. human. [O75223-2]
uc022abe.1. human.

Organism-specific databases

CTD79017.
GeneCardsGC07M030536.
HGNCHGNC:21705. GGCT.
HPAHPA020735.
HPA029914.
MIM137170. gene.
neXtProtNX_O75223.
PharmGKBPA162389392.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG87076.
HOGENOMHOG000008049.
HOVERGENHBG050922.
InParanoidO75223.
KOK00682.
OMAKKVICMG.
OrthoDBEOG7H1JNT.
PhylomeDBO75223.
TreeFamTF314378.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO75223.
BgeeO75223.
CleanExHS_GGCT.
GenevestigatorO75223.

Family and domain databases

Gene3D3.10.490.10. 1 hit.
InterProIPR013024. Butirosin_synth_BtrG-like.
IPR017939. G-Glutamylcylcotransferase.
[Graphical view]
PANTHERPTHR12935. PTHR12935. 1 hit.
SUPFAMSSF110857. SSF110857. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGGCT. human.
EvolutionaryTraceO75223.
GenomeRNAi79017.
NextBio67678.
PROO75223.
SOURCESearch...

Entry information

Entry nameGGCT_HUMAN
AccessionPrimary (citable) accession number: O75223
Secondary accession number(s): B2RDN0 expand/collapse secondary AC list , B8ZZN4, B8ZZR8, Q9BS37
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 104 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM