SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O15217

- GSTA4_HUMAN

UniProt

O15217 - GSTA4_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Glutathione S-transferase A4
Gene
GSTA4
Organism
Homo sapiens (Human)
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. This isozyme has a high catalytic efficiency with 4-hydroxyalkenals such as 4-hydroxynonenal (4-HNE).2 Publications

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91Glutathione
Binding sitei212 – 2121Substrate

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB
  2. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. glutathione derivative biosynthetic process Source: Reactome
  2. glutathione metabolic process Source: UniProtKB
  3. small molecule metabolic process Source: Reactome
  4. xenobiotic metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_6926. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase A4 (EC:2.5.1.18)
Alternative name(s):
GST class-alpha member 4
Glutathione S-transferase A4-4
Gene namesi
Name:GSTA4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:4629. GSTA4.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91Y → F: Reduces catalytic activity 70-fold. 1 Publication
Mutagenesisi212 – 2121Y → A, F or S: Strongly reduced activity towards 4-hydroxynon-2-enal and 1-chloro-2,4-dinitrobenzene. 1 Publication

Organism-specific databases

PharmGKBiPA29019.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Glutathione S-transferase A4
PRO_0000185786Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO15217.
PaxDbiO15217.
PRIDEiO15217.

PTM databases

PhosphoSiteiO15217.

Expressioni

Tissue specificityi

Expressed at a high level in brain, placenta, and skeletal muscle and much lower in lung and liver.

Gene expression databases

ArrayExpressiO15217.
BgeeiO15217.
CleanExiHS_GSTA4.
GenevestigatoriO15217.

Organism-specific databases

HPAiHPA048934.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi109196. 3 interactions.
MINTiMINT-1466182.
STRINGi9606.ENSP00000359998.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94
Turni14 – 163
Helixi17 – 259
Beta strandi31 – 344
Helixi38 – 469
Beta strandi57 – 604
Beta strandi63 – 675
Helixi68 – 7811
Helixi86 – 10823
Helixi109 – 1113
Helixi114 – 13118
Helixi133 – 14210
Beta strandi146 – 1494
Helixi155 – 17016
Turni172 – 1776
Helixi179 – 18911
Helixi192 – 1987
Beta strandi199 – 2035
Helixi210 – 22011

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GULX-ray2.70A/B/C/D/E/F/G/H1-222[»]
1GUMX-ray3.00A/B/C/D/E/F/G/H1-222[»]
3IK7X-ray1.97A/B/C/D1-222[»]
ProteinModelPortaliO15217.
SMRiO15217. Positions 2-222.

Miscellaneous databases

EvolutionaryTraceiO15217.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8381GST N-terminal
Add
BLAST
Domaini85 – 208124GST C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 552Glutathione binding
Regioni67 – 682Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Alpha family.

Phylogenomic databases

eggNOGiNOG266414.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiO15217.
KOiK00799.
OMAiIIMHPFL.
OrthoDBiEOG79CZ0K.
PhylomeDBiO15217.
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.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15217-1 [UniParc]FASTAAdd to Basket

« Hide

MAARPKLHYP NGRGRMESVR WVLAAAGVEF DEEFLETKEQ LYKLQDGNHL    50
LFQQVPMVEI DGMKLVQTRS ILHYIADKHN LFGKNLKERT LIDMYVEGTL 100
DLLELLIMHP FLKPDDQQKE VVNMAQKAII RYFPVFEKIL RGHGQSFLVG 150
NQLSLADVIL LQTILALEEK IPNILSAFPF LQEYTVKLSN IPTIKRFLEP 200
GSKKKPPPDE IYVRTVYNIF RP 222
Length:222
Mass (Da):25,704
Last modified:January 1, 1998 - v1
Checksum:i1BD98B41E413BB4E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001L → P.1 Publication
Corresponds to variant rs45551133 [ dbSNP | Ensembl ].
VAR_022210
Natural varianti163 – 1631T → A.1 Publication
Corresponds to variant rs4147617 [ dbSNP | Ensembl ].
VAR_022211

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13047 mRNA. Translation: CAA73482.1.
AF020918 mRNA. Translation: AAD04711.1.
AF025887 mRNA. Translation: AAC39695.1.
AF125271 mRNA. Translation: AAD27704.1.
AF125272 mRNA. Translation: AAD27705.1.
AF125273 mRNA. Translation: AAD27706.1.
AF050059
, AF050054, AF050055, AF050056, AF050057, AF050058 Genomic DNA. Translation: AAC72706.1.
AY878121 Genomic DNA. Translation: AAW56075.1.
AK315369 mRNA. Translation: BAG37762.1.
AL121969, AL162581 Genomic DNA. Translation: CAI42451.1.
AL162581, AL121969 Genomic DNA. Translation: CAI19517.1.
CH471081 Genomic DNA. Translation: EAX04394.1.
BC015523 mRNA. Translation: AAH15523.1.
CCDSiCCDS4948.1.
RefSeqiNP_001503.1. NM_001512.3.
XP_005249092.1. XM_005249035.1.
UniGeneiHs.485557.

Genome annotation databases

EnsembliENST00000370959; ENSP00000359998; ENSG00000170899.
ENST00000370963; ENSP00000360002; ENSG00000170899.
GeneIDi2941.
KEGGihsa:2941.
UCSCiuc003pbd.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13047 mRNA. Translation: CAA73482.1 .
AF020918 mRNA. Translation: AAD04711.1 .
AF025887 mRNA. Translation: AAC39695.1 .
AF125271 mRNA. Translation: AAD27704.1 .
AF125272 mRNA. Translation: AAD27705.1 .
AF125273 mRNA. Translation: AAD27706.1 .
AF050059
, AF050054 , AF050055 , AF050056 , AF050057 , AF050058 Genomic DNA. Translation: AAC72706.1 .
AY878121 Genomic DNA. Translation: AAW56075.1 .
AK315369 mRNA. Translation: BAG37762.1 .
AL121969 , AL162581 Genomic DNA. Translation: CAI42451.1 .
AL162581 , AL121969 Genomic DNA. Translation: CAI19517.1 .
CH471081 Genomic DNA. Translation: EAX04394.1 .
BC015523 mRNA. Translation: AAH15523.1 .
CCDSi CCDS4948.1.
RefSeqi NP_001503.1. NM_001512.3.
XP_005249092.1. XM_005249035.1.
UniGenei Hs.485557.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GUL X-ray 2.70 A/B/C/D/E/F/G/H 1-222 [» ]
1GUM X-ray 3.00 A/B/C/D/E/F/G/H 1-222 [» ]
3IK7 X-ray 1.97 A/B/C/D 1-222 [» ]
ProteinModelPortali O15217.
SMRi O15217. Positions 2-222.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109196. 3 interactions.
MINTi MINT-1466182.
STRINGi 9606.ENSP00000359998.

Chemistry

ChEMBLi CHEMBL4933.
DrugBanki DB00143. Glutathione.

PTM databases

PhosphoSitei O15217.

Proteomic databases

MaxQBi O15217.
PaxDbi O15217.
PRIDEi O15217.

Protocols and materials databases

DNASUi 2941.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370959 ; ENSP00000359998 ; ENSG00000170899 .
ENST00000370963 ; ENSP00000360002 ; ENSG00000170899 .
GeneIDi 2941.
KEGGi hsa:2941.
UCSCi uc003pbd.3. human.

Organism-specific databases

CTDi 2941.
GeneCardsi GC06M052842.
HGNCi HGNC:4629. GSTA4.
HPAi HPA048934.
MIMi 605450. gene.
neXtProti NX_O15217.
PharmGKBi PA29019.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG266414.
HOGENOMi HOG000115734.
HOVERGENi HBG053749.
InParanoidi O15217.
KOi K00799.
OMAi IIMHPFL.
OrthoDBi EOG79CZ0K.
PhylomeDBi O15217.
TreeFami TF105321.

Enzyme and pathway databases

Reactomei REACT_6926. Glutathione conjugation.

Miscellaneous databases

EvolutionaryTracei O15217.
GeneWikii GSTA4.
GenomeRNAii 2941.
NextBioi 11655.
PROi O15217.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15217.
Bgeei O15217.
CleanExi HS_GSTA4.
Genevestigatori O15217.

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.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01266. GSTRNSFRASEA.
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. "Human glutathione transferase A4-4: an alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation."
    Hubatsch I., Ridderstrom M., Mannervik B.
    Biochem. J. 330:175-179(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4."
    Board P.G.
    Biochem. J. 330:827-831(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Identification of a novel human glutathione S-transferase using bioinformatics."
    Liu S., Stoesz S.P., Pickett C.B.
    Arch. Biochem. Biophys. 352:306-313(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The 4-HNE metabolizing GST isozyme hGSTA4-4 is expressed in human heart, pancreas, and skeletal muscle."
    Piper J.T., Awasthi Y.C.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart, Pancreas and Skeletal muscle.
  5. "Genomic organization, 5'-flanking region and chromosomal localization of the human glutathione transferase A4 gene."
    Desmots F., Rauch C., Henry C., Guillouzo A., Morel F.
    Biochem. J. 336:437-442(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. NIEHS SNPs program
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-100 AND ALA-163.
  7. "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].
    Tissue: Cerebellum.
  8. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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].
    Tissue: Uterus.
  11. "Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products."
    Bruns C.M., Hubatsch I., Ridderstroem M., Mannervik B., Tainer J.A.
    J. Mol. Biol. 288:427-439(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH 2-IODOBENZYL GLUTATHIONE, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF TYR-212, SUBUNIT.
  12. "Substrate specificity combined with stereopromiscuity in glutathione transferase A4-4-dependent metabolism of 4-hydroxynonenal."
    Balogh L.M., Le Trong I., Kripps K.A., Shireman L.M., Stenkamp R.E., Zhang W., Mannervik B., Atkins W.M.
    Biochemistry 49:1541-1548(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF TYR-9.

Entry informationi

Entry nameiGSTA4_HUMAN
AccessioniPrimary (citable) accession number: O15217
Secondary accession number(s): B2RD15
, Q5T7Q8, Q9BX18, Q9H414
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 138 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi