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Protein
Submitted name:

GSTM3 protein

Gene

GSTM3

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

  1. glutathione transferase activity Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

TransferaseImported

Names & Taxonomyi

Protein namesi
Submitted name:
GSTM3 proteinImported
Submitted name:
Glutathione S-transferase M3 (Brain)Imported
Submitted name:
cDNA, FLJ93985, Homo sapiens glutathione S-transferase M3 (brain) (GSTM3), mRNAImported
Gene namesi
Name:GSTM3Imported
ORF Names:hCG_40244Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

GO - Cellular componenti

  1. sperm fibrous sheath Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29024.

Structurei

3D structure databases

ProteinModelPortaliQ6FGJ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GST superfamily.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074559.
HOVERGENiHBG106842.
KOiK00799.
OMAiMSCESSM.

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.

Q6FGJ9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSCESSMVLG YWDIRGLAHA IRLLLEFTDT SYEEKRYTCG EAPDYDRSQW
60 70 80 90 100
LDVKFKLDLD FPNLPYLLDG KNKITQSNAI LRYIARKHNM CGETEEEKIR
110 120 130 140 150
VDIIENQVMD FRTQLIRLCY SSDHEKLKPQ YLEELPGQLK QFSMFLGKFS
160 170 180 190 200
WFAGEKLTFV DFLTYDILDQ NRIFDPKCLD EFPNLKAFMC RFEALEKIAA
210 220
YLQSDQFCKM PINNKMAQWG NKPVC
Length:225
Mass (Da):26,560
Last modified:May 10, 2005 - v1
Checksum:i79093161ECEF5396
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU136188 Genomic DNA. Translation: ABV02583.1.
AK313444 mRNA. Translation: BAG36233.1.
CR542108 mRNA. Translation: CAG46905.1.
CH471122 Genomic DNA. Translation: EAW56409.1.
RefSeqiNP_000840.2. NM_000849.4.
UniGeneiHs.2006.

Genome annotation databases

GeneIDi2947.
KEGGihsa:2947.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU136188 Genomic DNA. Translation: ABV02583.1.
AK313444 mRNA. Translation: BAG36233.1.
CR542108 mRNA. Translation: CAG46905.1.
CH471122 Genomic DNA. Translation: EAW56409.1.
RefSeqiNP_000840.2. NM_000849.4.
UniGeneiHs.2006.

3D structure databases

ProteinModelPortaliQ6FGJ9.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

DNASUi2947.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2947.
KEGGihsa:2947.

Organism-specific databases

CTDi2947.
PharmGKBiPA29024.

Phylogenomic databases

GeneTreeiENSGT00550000074559.
HOVERGENiHBG106842.
KOiK00799.
OMAiMSCESSM.

Miscellaneous databases

GenomeRNAii2947.
NextBioi11678.

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]
ProtoNetiSearch...

Publicationsi

  1. "The sequence of the human genome."
    Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
    , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
    Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  3. Cited for: NUCLEOTIDE SEQUENCE.
  4. Cited for: NUCLEOTIDE SEQUENCE.
  5. "NEDO functional analysis of protein and research application project."
    Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., Isogai T.
    Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: AmygdalaImported.

Entry informationi

Entry nameiQ6FGJ9_HUMAN
AccessioniPrimary (citable) accession number: Q6FGJ9
Entry historyi
Integrated into UniProtKB/TrEMBL: May 10, 2005
Last sequence update: May 10, 2005
Last modified: February 4, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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.

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.