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P19157

- GSTP1_MOUSE

UniProt

P19157 - GSTP1_MOUSE

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Protein

Glutathione S-transferase P 1

Gene

Gstp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can metabolize 1-chloro-2,4-dinitrobenzene. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81Glutathione
Binding sitei14 – 141Glutathione
Binding sitei39 – 391Glutathione
Binding sitei45 – 451Glutathione

GO - Molecular functioni

  1. drug binding Source: BHF-UCL
  2. glutathione transferase activity Source: MGI
  3. JUN kinase binding Source: BHF-UCL
  4. kinase regulator activity Source: BHF-UCL

GO - Biological processi

  1. cellular response to cell-matrix adhesion Source: BHF-UCL
  2. cellular response to epidermal growth factor stimulus Source: BHF-UCL
  3. cellular response to glucocorticoid stimulus Source: BHF-UCL
  4. cellular response to insulin stimulus Source: BHF-UCL
  5. cellular response to lipopolysaccharide Source: BHF-UCL
  6. common myeloid progenitor cell proliferation Source: BHF-UCL
  7. glutathione metabolic process Source: MGI
  8. negative regulation of acute inflammatory response Source: BHF-UCL
  9. negative regulation of apoptotic process Source: BHF-UCL
  10. negative regulation of biosynthetic process Source: BHF-UCL
  11. negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  12. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  13. negative regulation of fibroblast proliferation Source: BHF-UCL
  14. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
  15. negative regulation of interleukin-1 beta production Source: BHF-UCL
  16. negative regulation of JUN kinase activity Source: BHF-UCL
  17. negative regulation of leukocyte proliferation Source: BHF-UCL
  18. negative regulation of MAP kinase activity Source: BHF-UCL
  19. negative regulation of monocyte chemotactic protein-1 production Source: BHF-UCL
  20. negative regulation of neutrophil aggregation Source: BHF-UCL
  21. negative regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  22. negative regulation of peroxidase activity Source: BHF-UCL
  23. negative regulation of stress-activated MAPK cascade Source: BHF-UCL
  24. negative regulation of tumor necrosis factor production Source: BHF-UCL
  25. oligodendrocyte development Source: BHF-UCL
  26. organ regeneration Source: BHF-UCL
  27. positive regulation of superoxide anion generation Source: BHF-UCL
  28. regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  29. regulation of stress-activated MAPK cascade Source: BHF-UCL
  30. response to amino acid Source: BHF-UCL
  31. response to estradiol Source: BHF-UCL
  32. response to ethanol Source: BHF-UCL
  33. response to L-ascorbic acid Source: BHF-UCL
  34. response to nutrient levels Source: BHF-UCL
  35. response to reactive oxygen species Source: BHF-UCL
  36. response to toxic substance Source: BHF-UCL
  37. xenobiotic metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.
REACT_215316. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase P 1 (EC:2.5.1.18)
Short name:
Gst P1
Alternative name(s):
GST YF-YF
GST class-pi
GST-piB
Preadipocyte growth factor
Gene namesi
Name:Gstp1
Synonyms:Gstpib
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:95865. Gstp1.

Subcellular locationi

Cytoplasm By similarity. Mitochondrion By similarity. Nucleus By similarity
Note: The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization.By similarity

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: BHF-UCL
  3. intracellular Source: BHF-UCL
  4. mitochondrion Source: UniProtKB-KW
  5. nucleus Source: BHF-UCL
  6. plasma membrane Source: BHF-UCL
  7. protein complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 210209Glutathione S-transferase P 1PRO_0000185903Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41Phosphotyrosine; by EGFRBy similarity
Modified residuei103 – 1031N6-succinyllysine1 Publication
Modified residuei116 – 1161N6-succinyllysine1 Publication
Modified residuei128 – 1281N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP19157.
PaxDbiP19157.
PRIDEiP19157.

2D gel databases

REPRODUCTION-2DPAGEP19157.
SWISS-2DPAGEP19157.

PTM databases

PhosphoSiteiP19157.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiP19157.
CleanExiMM_GSTP1.
GenevestigatoriP19157.

Interactioni

Subunit structurei

Homodimer. Interacts with CDK5 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Prdx6O087092EBI-2309446,EBI-444895

Protein-protein interaction databases

BioGridi200101. 2 interactions.
IntActiP19157. 5 interactions.
MINTiMINT-1869068.
STRINGi10090.ENSMUSP00000047790.

Structurei

Secondary structure

1
210
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85
Beta strandi10 – 123
Helixi13 – 153
Helixi16 – 249
Beta strandi29 – 335
Helixi36 – 405
Beta strandi42 – 443
Helixi45 – 473
Beta strandi49 – 513
Beta strandi55 – 584
Beta strandi61 – 655
Helixi66 – 7712
Helixi84 – 11027
Helixi112 – 13524
Helixi138 – 1403
Beta strandi144 – 1485
Helixi151 – 16616
Turni168 – 1736
Helixi175 – 18612
Helixi188 – 1958
Helixi197 – 2004
Beta strandi204 – 2085

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BAYX-ray2.00A/B2-210[»]
1GLPX-ray1.90A/B2-210[»]
1GLQX-ray1.80A/B2-210[»]
1GSYX-ray2.44A/B2-210[»]
1GTIX-ray3.00A/B/C/D/E/F2-210[»]
2GLRX-ray2.20A/B2-210[»]
2OA7X-ray2.20A/B2-210[»]
2OACX-ray2.20A/B2-210[»]
2OADX-ray2.50A/B2-210[»]
3O76X-ray1.77A/B2-210[»]
ProteinModelPortaliP19157.
SMRiP19157. Positions 2-210.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19157.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8180GST N-terminalAdd
BLAST
Domaini83 – 204122GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 532Glutathione binding
Regioni65 – 662Glutathione binding

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG05174.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115733.
HOVERGENiHBG108324.
InParanoidiP19157.
KOiK00799.
OMAiLRCKYAT.
OrthoDBiEOG7KH9M3.
PhylomeDBiP19157.
TreeFamiTF105321.

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.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01268. GSTRNSFRASEP.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P19157 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPYTIVYFP VRGRCEAMRM LLADQGQSWK EEVVTIDTWM QGLLKPTCLY
60 70 80 90 100
GQLPKFEDGD LTLYQSNAIL RHLGRSLGLY GKNQREAAQM DMVNDGVEDL
110 120 130 140 150
RGKYVTLIYT NYENGKNDYV KALPGHLKPF ETLLSQNQGG KAFIVGDQIS
160 170 180 190 200
FADYNLLDLL LIHQVLAPGC LDNFPLLSAY VARLSARPKI KAFLSSPEHV
210
NRPINGNGKQ
Length:210
Mass (Da):23,609
Last modified:January 23, 2007 - v2
Checksum:iDAC7762F4E34FF27
GO

Mass spectrometryi

Molecular mass is 23478.8±2 Da from positions 2 - 210. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53451 mRNA. Translation: CAA37529.1.
X76143 Genomic DNA. No translation available.
U15654 Genomic DNA. Translation: AAA64837.1.
D30687 mRNA. Translation: BAA06349.1.
BC002048 mRNA. Translation: AAH02048.1.
BC061109 mRNA. Translation: AAH61109.1.
AK079144 mRNA. Translation: BAC37560.1.
CCDSiCCDS29411.1.
PIRiS12709. B55140.
RefSeqiNP_038569.1. NM_013541.1.
UniGeneiMm.299292.

Genome annotation databases

EnsembliENSMUST00000169613; ENSMUSP00000129565; ENSMUSG00000060803.
ENSMUST00000180480; ENSMUSP00000138073; ENSMUSG00000097830.
GeneIDi14870.
KEGGimmu:14870.
UCSCiuc008fyf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53451 mRNA. Translation: CAA37529.1 .
X76143 Genomic DNA. No translation available.
U15654 Genomic DNA. Translation: AAA64837.1 .
D30687 mRNA. Translation: BAA06349.1 .
BC002048 mRNA. Translation: AAH02048.1 .
BC061109 mRNA. Translation: AAH61109.1 .
AK079144 mRNA. Translation: BAC37560.1 .
CCDSi CCDS29411.1.
PIRi S12709. B55140.
RefSeqi NP_038569.1. NM_013541.1.
UniGenei Mm.299292.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BAY X-ray 2.00 A/B 2-210 [» ]
1GLP X-ray 1.90 A/B 2-210 [» ]
1GLQ X-ray 1.80 A/B 2-210 [» ]
1GSY X-ray 2.44 A/B 2-210 [» ]
1GTI X-ray 3.00 A/B/C/D/E/F 2-210 [» ]
2GLR X-ray 2.20 A/B 2-210 [» ]
2OA7 X-ray 2.20 A/B 2-210 [» ]
2OAC X-ray 2.20 A/B 2-210 [» ]
2OAD X-ray 2.50 A/B 2-210 [» ]
3O76 X-ray 1.77 A/B 2-210 [» ]
ProteinModelPortali P19157.
SMRi P19157. Positions 2-210.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200101. 2 interactions.
IntActi P19157. 5 interactions.
MINTi MINT-1869068.
STRINGi 10090.ENSMUSP00000047790.

PTM databases

PhosphoSitei P19157.

2D gel databases

REPRODUCTION-2DPAGE P19157.
SWISS-2DPAGE P19157.

Proteomic databases

MaxQBi P19157.
PaxDbi P19157.
PRIDEi P19157.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000169613 ; ENSMUSP00000129565 ; ENSMUSG00000060803 .
ENSMUST00000180480 ; ENSMUSP00000138073 ; ENSMUSG00000097830 .
GeneIDi 14870.
KEGGi mmu:14870.
UCSCi uc008fyf.1. mouse.

Organism-specific databases

CTDi 2950.
MGIi MGI:95865. Gstp1.

Phylogenomic databases

eggNOGi NOG05174.
GeneTreei ENSGT00550000074559.
HOGENOMi HOG000115733.
HOVERGENi HBG108324.
InParanoidi P19157.
KOi K00799.
OMAi LRCKYAT.
OrthoDBi EOG7KH9M3.
PhylomeDBi P19157.
TreeFami TF105321.

Enzyme and pathway databases

Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.
REACT_215316. Glutathione conjugation.

Miscellaneous databases

EvolutionaryTracei P19157.
NextBioi 287133.
PROi P19157.
SOURCEi Search...

Gene expression databases

Bgeei P19157.
CleanExi MM_GSTP1.
Genevestigatori P19157.

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.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01268. GSTRNSFRASEP.
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

« Hide 'large scale' publications
  1. "A cDNA sequence coding a class pi glutathione S-transferase of mouse."
    Hatayama I., Satoh K., Sato K.
    Nucleic Acids Res. 18:4606-4606(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Liver.
  2. "Isolation and characterization of two mouse PI class glutathione S-transferase genes."
    Bammler T.K., Smith C.A.D., Wolf R.C.
    Biochem. J. 298:385-390(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Two murine GSTpi genes are arranged in tandem and are differentially expressed."
    Xu X., Stambrook P.J.
    J. Biol. Chem. 269:30268-30273(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
    Tissue: Liver.
  4. "Molecular cloning of mouse preadipocyte growth factor."
    Kawada T., Aoki N., Kamei Y., Sugimoto E.
    Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "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].
  6. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12; 56-71; 122-141 AND 192-209, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  7. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-210.
    Strain: C57BL/6J.
    Tissue: Embryo.
  8. "Purification, mass spectrometric characterization, and covalent modification of murine glutathione S-transferases."
    Mitchell A.E., Morin D., Lame M.W., Jones A.D.
    Chem. Res. Toxicol. 8:1054-1062(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MASS SPECTROMETRY.
    Strain: CD-1.
    Tissue: Liver.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-103 AND LYS-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Molecular structure at 1.8 A of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors."
    Garcia-Saez I., Parraga A., Phillips M.F., Mantle T.J., Coll M.
    J. Mol. Biol. 237:298-314(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOGS.
  11. "The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-310B region."
    Vega M.C., Walsh S.B., Mantle T.J., Coll M.
    J. Biol. Chem. 273:2844-2850(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Entry informationi

Entry nameiGSTP1_MOUSE
AccessioniPrimary (citable) accession number: P19157
Secondary accession number(s): Q8BNY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3