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P48637 (GSHB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione synthetase
Short name=GSH synthetase
Short name=GSH-S
EC=6.3.2.3
Alternative name(s):
Glutathione synthase
Gene names
Name:GSS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.

Cofactor

Binds 1 magnesium ion per subunit. Ref.13

Pathway

Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.

Subunit structure

Homodimer. Ref.13

Involvement in disease

Glutathione synthetase deficiency (GSS deficiency) [MIM:266130]: Severe form characterized by an increased rate of hemolysis and defective function of the central nervous system.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Glutathione synthetase deficiency of erythrocytes (GLUSYNDE) [MIM:231900]: Mild form causing hemolytic anemia.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the eukaryotic GSH synthase family.

Ontologies

Keywords
   Biological processGlutathione biosynthesis
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Hereditary hemolytic anemia
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

glutathione derivative biosynthetic process

Traceable author statement. Source: Reactome

nervous system development

Traceable author statement Ref.14. Source: ProtInc

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Traceable author statement PubMed 465367. Source: ProtInc

response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from direct assay Ref.13. Source: UniProtKB

glutathione binding

Inferred from direct assay Ref.13. Source: UniProtKB

glutathione synthase activity

Traceable author statement. Source: Reactome

glycine binding

Inferred from electronic annotation. Source: Ensembl

magnesium ion binding

Inferred from direct assay Ref.13. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.13. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P48637-1)

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: P48637-2)

The sequence of this isoform differs from the canonical sequence as follows:
     93-203: Missing.
Note: Detected in colon, kidney, lung, liver, placenta, peripheral blood and uterus, but not in heart, skeletal muscle and spleen.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 474473Glutathione synthetase
PRO_0000211260

Regions

Nucleotide binding364 – 37310ATP
Nucleotide binding398 – 4014ATP
Region148 – 1514Substrate binding
Region214 – 2163Substrate binding
Region267 – 2704Substrate binding
Region461 – 4622Substrate binding

Sites

Metal binding1441Magnesium
Metal binding1461Magnesium
Metal binding3681Magnesium
Binding site1251Substrate
Binding site1441ATP
Binding site2201Substrate
Binding site3051ATP
Binding site3751ATP
Binding site4251ATP
Binding site4501Substrate
Binding site4521ATP
Binding site4581ATP; via carbonyl oxygen

Amino acid modifications

Modified residue21N-acetylalanine Ref.10

Natural variations

Alternative sequence93 – 203111Missing in isoform 2.
VSP_047617
Natural variant261A → D in GSS deficiency.
VAR_003602
Natural variant1881L → P in GSS deficiency; 100-fold reduction of activity.
VAR_003603
Natural variant2191D → A in GSS deficiency.
VAR_003604
Natural variant2191D → G in GSS deficiency. Ref.14
Corresponds to variant rs28938472 [ dbSNP | Ensembl ].
VAR_003605
Natural variant2361R → Q. Ref.5
Corresponds to variant rs34239729 [ dbSNP | Ensembl ].
VAR_025047
Natural variant2541L → R in GSS deficiency.
VAR_003606
Natural variant2671R → W in GSS deficiency. Ref.14
VAR_003607
Natural variant2701Y → C in GSS deficiency; 100-fold reduction of activity.
VAR_003608
Natural variant2701Y → H in GSS deficiency; 100-fold reduction of activity.
VAR_003609
Natural variant2831R → C in GSS deficiency; 10-fold reduction of activity. Ref.14
VAR_003610
Natural variant2861L → Q in GSS deficiency.
VAR_003611
Natural variant3301R → C in GSS deficiency.
Corresponds to variant rs148640446 [ dbSNP | Ensembl ].
VAR_003612
Natural variant4371K → E. Ref.4 Ref.5
Corresponds to variant rs34852238 [ dbSNP | Ensembl ].
VAR_025048
Natural variant4641G → V in GSS deficiency.
VAR_003613
Natural variant4691D → E in GSS deficiency.
VAR_003614

Secondary structure

1 ......................................................................................... 474
Helix Strand Turn

Details...

Sequences

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

Last modified February 1, 1996. Version 1.
Checksum: 3C25EF7072EFE058

FASTA47452,385
        10         20         30         40         50         60 
MATNWGSLLQ DKQQLEELAR QAVDRALAEG VLLRTSQEPT SSEVVSYAPF TLFPSLVPSA 

        70         80         90        100        110        120 
LLEQAYAVQM DFNLLVDAVS QNAAFLEQTL SSTIKQDDFT ARLFDIHKQV LKEGIAQTVF 

       130        140        150        160        170        180 
LGLNRSDYMF QRSADGSPAL KQIEINTISA SFGGLASRTP AVHRHVLSVL SKTKEAGKIL 

       190        200        210        220        230        240 
SNNPSKGLAL GIAKAWELYG SPNALVLLIA QEKERNIFDQ RAIENELLAR NIHVIRRTFE 

       250        260        270        280        290        300 
DISEKGSLDQ DRRLFVDGQE IAVVYFRDGY MPRQYSLQNW EARLLLERSH AAKCPDIATQ 

       310        320        330        340        350        360 
LAGTKKVQQE LSRPGMLEML LPGQPEAVAR LRATFAGLYS LDVGEEGDQA IAEALAAPSR 

       370        380        390        400        410        420 
FVLKPQREGG GNNLYGEEMV QALKQLKDSE ERASYILMEK IEPEPFENCL LRPGSPARVV 

       430        440        450        460        470 
QCISELGIFG VYVRQEKTLV MNKHVGHLLR TKAIEHADGG VAAGVAVLDN PYPV

« Hide

Isoform 2 [UniParc].

Checksum: 931DA0F137EE1634
Show »

FASTA36340,349

References

« Hide 'large scale' references
[1]"Sequencing and expression of a cDNA for human glutathione synthetase."
Gali R.R., Board P.G.
Biochem. J. 310:353-358(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Alternative RNA splicing in expression of the glutathione synthetase gene in human cells."
Uchida M., Sugaya M., Kanamaru T., Hisatomi H.
Mol. Biol. Rep. 37:2105-2109(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]Shi Z.-Z., Galang R.L., Habib G.M., Lebovitz R.M., Lieberman M.W.
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Kidney.
[4]"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), VARIANT GLU-437.
Tissue: Substantia nigra.
[5]NIEHS SNPs program
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-236 AND GLU-437.
[6]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM 1).
Tissue: Lung.
[9]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 26-34; 113-125; 142-158; 222-230; 254-267; 274-283; 294-305; 419-434 AND 453-474, MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
[11]"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].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Molecular basis of glutathione synthetase deficiency and a rare gene permutation event."
Polekhina G., Board P.G., Gali R.R., Rossjohn J., Parker M.W.
EMBO J. 18:3204-3213(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-474 IN COMPLEX WITH ADP AND GLUTATHIONE, COFACTOR, SUBUNIT.
[14]"Mutations in the glutathione synthetase gene cause 5-oxoprolinuria."
Shi Z.-Z., Habib G.M., Rhead W.J., Gahl W.A., He X., Sazer S., Lieberman M.W.
Nat. Genet. 14:361-365(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSS DEFICIENCY GLY-219; TRP-267 AND CYS-283.
[15]"Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction."
Dahl N., Pigg M., Ristoff E., Gali R., Carlsson B., Mannervik B., Larsson A., Board P.
Hum. Mol. Genet. 6:1147-1152(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSS DEFICIENCY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42531 mRNA. Translation: AAA69492.1.
AB459500 mRNA. Translation: BAG75452.1.
U34683 mRNA. Translation: AAB62390.1.
AK312492 mRNA. Translation: BAG35394.1.
DQ074975 Genomic DNA. Translation: AAY57328.1.
AL133324 Genomic DNA. Translation: CAB93423.1.
CH471077 Genomic DNA. Translation: EAW76239.1.
CH471077 Genomic DNA. Translation: EAW76240.1.
BC007927 mRNA. Translation: AAH07927.1.
PIRS56748.
RefSeqNP_000169.1. NM_000178.2.
XP_005260462.1. XM_005260405.1.
XP_005260463.1. XM_005260406.1.
UniGeneHs.82327.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HGSX-ray2.10A1-474[»]
ProteinModelPortalP48637.
SMRP48637. Positions 3-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109192. 5 interactions.
IntActP48637. 2 interactions.
MINTMINT-5001027.
STRING9606.ENSP00000216951.

Chemistry

DrugBankDB00143. Glutathione.
DB00145. Glycine.
DB00151. L-Cysteine.

PTM databases

PhosphoSiteP48637.

Polymorphism databases

DMDM1346191.

2D gel databases

OGPP48637.
REPRODUCTION-2DPAGEIPI00010706.

Proteomic databases

PaxDbP48637.
PeptideAtlasP48637.
PRIDEP48637.

Protocols and materials databases

DNASU2937.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216951; ENSP00000216951; ENSG00000100983.
ENST00000451957; ENSP00000407517; ENSG00000100983.
GeneID2937.
KEGGhsa:2937.
UCSCuc010zuo.2. human.

Organism-specific databases

CTD2937.
GeneCardsGC20M033517.
HGNCHGNC:4624. GSS.
HPAHPA051186.
HPA054508.
MIM231900. phenotype.
266130. phenotype.
601002. gene.
neXtProtNX_P48637.
Orphanet289846. Glutathione synthetase deficiency with 5-oxoprolinuria.
289849. Glutathione synthetase deficiency without 5-oxoprolinuria.
PharmGKBPA29015.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG329040.
HOGENOMHOG000172641.
HOVERGENHBG002458.
InParanoidP48637.
KOK01920.
OMAFENCLLR.
OrthoDBEOG757CXD.
PhylomeDBP48637.
TreeFamTF105187.

Enzyme and pathway databases

BioCycMetaCyc:HS02174-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP48637.
UniPathwayUPA00142; UER00210.

Gene expression databases

ArrayExpressP48637.
BgeeP48637.
CleanExHS_GSS.
GenevestigatorP48637.

Family and domain databases

Gene3D1.10.1080.10. 2 hits.
3.30.1490.50. 1 hit.
3.30.1490.80. 2 hits.
3.40.50.1760. 1 hit.
InterProIPR004887. Glutathione_synth_subst-bd_euk.
IPR014042. Glutathione_synthase_a-hlx_euk.
IPR014709. Glutathione_synthase_dom.
IPR005615. Glutathione_synthase_euk.
IPR014049. Glutathione_synthase_N_euk.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PANTHERPTHR11130. PTHR11130. 1 hit.
PfamPF03917. GSH_synth_ATP. 1 hit.
PF03199. GSH_synthase. 1 hit.
[Graphical view]
PIRSFPIRSF001558. GSHase. 1 hit.
SUPFAMSSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR01986. glut_syn_euk. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGSS. human.
EvolutionaryTraceP48637.
GenomeRNAi2937.
NextBio11639.
PROP48637.
SOURCESearch...

Entry information

Entry nameGSHB_HUMAN
AccessionPrimary (citable) accession number: P48637
Secondary accession number(s): B2R697 expand/collapse secondary AC list , B6F210, E1P5P9, Q4TTD9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 146 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

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