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Q00285

- GSTMU_CRILO

UniProt

Q00285 - GSTMU_CRILO

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Protein

Glutathione S-transferase Y1

Gene
N/A
Organism
Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161SubstrateBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Y1 (EC:2.5.1.18)
Alternative name(s):
Chain 3
GST class-mu
OrganismiCricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster)
Taxonomic identifieri10030 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Glutathione S-transferase Y1PRO_0000185835Add
BLAST

Proteomic databases

PRIDEiQ00285.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliQ00285.
SMRiQ00285. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8887GST N-terminalAdd
BLAST
Domaini90 – 208119GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 82Glutathione bindingBy similarity
Regioni46 – 505Glutathione bindingBy similarity
Regioni59 – 602Glutathione bindingBy similarity
Regioni72 – 732Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Mu family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

HOVERGENiHBG106842.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01267. GSTRNSFRASEM.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q00285-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPMILGYWNV RGLTNPIRLL LEYTDSSYEE KKYTMGDAPD SDRSQWLNEK
60 70 80 90 100
FKLGLDFPNL PYLIDGSHKI TQSNAILRYI ARKHNLCGET EEERIRVDIV
110 120 130 140 150
ENQAMDTRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKMYSE FLGKRPWFAG
160 170 180 190 200
DKVTLCGFLA YDVLDQYQMF EPKCLDPFPN LKDFLARFEG LKKISAYMKT
210
SRFLRRPIFS KMAQWSNK
Length:218
Mass (Da):25,819
Last modified:January 23, 2007 - v2
Checksum:i0498A5629DA2DA70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57489 mRNA. Translation: CAA40726.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57489 mRNA. Translation: CAA40726.1 .

3D structure databases

ProteinModelPortali Q00285.
SMRi Q00285. Positions 2-218.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q00285.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG106842.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01267. GSTRNSFRASEM.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Coamplification of mu class glutathione S-transferase genes and an adenylate deaminase gene in coformycin-resistant Chinese hamster fibroblasts."
    de Saint Vincent B.R., Hyrien O., Debatisse M., Buttin G.
    Eur. J. Biochem. 193:19-24(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiGSTMU_CRILO
AccessioniPrimary (citable) accession number: Q00285
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3