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UniProtKB - P48637 (GSHB_HUMAN)

UniProt

P48637 - GSHB_HUMAN

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Protein

Glutathione synthetase

Gene

GSS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Pathwayi: glutathione biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes glutathione from L-cysteine and L-glutamate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamate--cysteine ligase regulatory subunit (GCLM), Glutamate--cysteine ligase catalytic subunit (GCLC)
  2. Glutathione synthetase, Glutathione synthetase (GSS), Glutathione synthetase, Glutathione synthetase (HEL-S-64p)
This subpathway is part of the pathway glutathione biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutathione from L-cysteine and L-glutamate, the pathway glutathione biosynthesis and in Sulfur metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei125 – 1251Substrate
Metal bindingi144 – 1441Magnesium
Binding sitei144 – 1441ATP
Metal bindingi146 – 1461Magnesium
Binding sitei220 – 2201Substrate
Binding sitei305 – 3051ATP
Metal bindingi368 – 3681Magnesium
Binding sitei375 – 3751ATP
Binding sitei425 – 4251ATP
Binding sitei450 – 4501Substrate
Binding sitei452 – 4521ATP
Binding sitei458 – 4581ATP; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi364 – 37310ATP
Nucleotide bindingi398 – 4014ATP

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • glutathione binding Source: UniProtKB
  • glutathione synthase activity Source: Reactome
  • glycine binding Source: Ensembl
  • magnesium ion binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • aging Source: Ensembl
  • cellular amino acid metabolic process Source: ProtInc
  • glutathione biosynthetic process Source: Reactome
  • nervous system development Source: ProtInc
  • response to amino acid Source: Ensembl
  • response to cadmium ion Source: Ensembl
  • response to nutrient levels Source: Ensembl
  • response to oxidative stress Source: ProtInc
  • response to tumor necrosis factor Source: Ensembl
  • response to xenobiotic stimulus Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Glutathione biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS02174-MONOMER.
BRENDAi6.3.2.3. 2681.
ReactomeiR-HSA-174403. Glutathione synthesis and recycling.
R-HSA-5579006. Defective GSS causes Glutathione synthetase deficiency (GSS deficiency).
SABIO-RKP48637.
UniPathwayiUPA00142; UER00210.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione synthetase (EC:6.3.2.3)
Short name:
GSH synthetase
Short name:
GSH-S
Alternative name(s):
Glutathione synthase
Gene namesi
Name:GSS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:4624. GSS.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Glutathione synthetase deficiency (GSS deficiency)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSevere form characterized by an increased rate of hemolysis and defective function of the central nervous system.
See also OMIM:266130
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 261A → D in GSS deficiency.
Corresponds to variant rs759253242 [ dbSNP | Ensembl ].		VAR_003602
Natural varianti188 – 1881L → P in GSS deficiency; 100-fold reduction of activity.
VAR_003603
Natural varianti219 – 2191D → A in GSS deficiency.
VAR_003604
Natural varianti219 – 2191D → G in GSS deficiency. 1 Publication
Corresponds to variant rs28938472 [ dbSNP | Ensembl ].		VAR_003605
Natural varianti254 – 2541L → R in GSS deficiency.
VAR_003606
Natural varianti267 – 2671R → W in GSS deficiency. 1 Publication
Corresponds to variant rs121909308 [ dbSNP | Ensembl ].		VAR_003607
Natural varianti270 – 2701Y → C in GSS deficiency; 100-fold reduction of activity.
VAR_003608
Natural varianti270 – 2701Y → H in GSS deficiency; 100-fold reduction of activity.
VAR_003609
Natural varianti283 – 2831R → C in GSS deficiency; 10-fold reduction of activity. 1 Publication
Corresponds to variant rs121909309 [ dbSNP | Ensembl ].		VAR_003610
Natural varianti286 – 2861L → Q in GSS deficiency.
VAR_003611
Natural varianti330 – 3301R → C in GSS deficiency.
Corresponds to variant rs148640446 [ dbSNP | Ensembl ].		VAR_003612
Natural varianti464 – 4641G → V in GSS deficiency.
VAR_003613
Natural varianti469 – 4691D → E in GSS deficiency.
VAR_003614
Glutathione synthetase deficiency of erythrocytes (GLUSYNDE)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionMild form causing hemolytic anemia.
See also OMIM:231900

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

MalaCardsiGSS.
MIMi231900. phenotype.
266130. phenotype.
Orphaneti289846. Glutathione synthetase deficiency with 5-oxoprolinuria.
289849. Glutathione synthetase deficiency without 5-oxoprolinuria.
PharmGKBiPA29015.

Chemistry

DrugBankiDB06151. Acetylcysteine.
DB00143. Glutathione.
DB00145. Glycine.
DB00151. L-Cysteine.

Polymorphism and mutation databases

BioMutaiGSS.
DMDMi1346191.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 474473Glutathione synthetasePRO_0000211260Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei415 – 4151PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP48637.
PaxDbiP48637.
PeptideAtlasiP48637.
PRIDEiP48637.

2D gel databases

OGPiP48637.
REPRODUCTION-2DPAGEIPI00010706.

PTM databases

iPTMnetiP48637.
PhosphoSiteiP48637.

Expressioni

Gene expression databases

BgeeiENSG00000100983.
CleanExiHS_GSS.
ExpressionAtlasiP48637. baseline and differential.
GenevisibleiP48637. HS.

Organism-specific databases

HPAiHPA054508.
HPA059315.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TERF1P542742EBI-2969145,EBI-710997

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi109192. 27 interactions.
IntActiP48637. 3 interactions.
MINTiMINT-5001027.
STRINGi9606.ENSP00000216951.

Structurei

Secondary structure

1
474
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 94Combined sources
Helixi12 – 2817Combined sources
Beta strandi32 – 343Combined sources
Beta strandi43 – 475Combined sources
Beta strandi50 – 534Combined sources
Beta strandi56 – 583Combined sources
Helixi59 – 679Combined sources
Helixi69 – 8113Combined sources
Helixi83 – 919Combined sources
Helixi93 – 964Combined sources
Helixi98 – 11316Combined sources
Beta strandi119 – 13214Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi138 – 1469Combined sources
Helixi153 – 1586Combined sources
Helixi160 – 16910Combined sources
Helixi173 – 1764Combined sources
Helixi184 – 19916Combined sources
Beta strandi205 – 2095Combined sources
Helixi217 – 22812Combined sources
Turni229 – 2313Combined sources
Beta strandi234 – 2374Combined sources
Helixi239 – 2457Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi259 – 26810Combined sources
Helixi272 – 2743Combined sources
Helixi277 – 28812Combined sources
Beta strandi289 – 2957Combined sources
Helixi297 – 3015Combined sources
Helixi305 – 3106Combined sources
Helixi316 – 3205Combined sources
Helixi325 – 3339Combined sources
Beta strandi338 – 3403Combined sources
Beta strandi342 – 3443Combined sources
Helixi345 – 35612Combined sources
Helixi358 – 3603Combined sources
Beta strandi361 – 3666Combined sources
Beta strandi369 – 3713Combined sources
Helixi376 – 38611Combined sources
Helixi390 – 3945Combined sources
Beta strandi395 – 3995Combined sources
Beta strandi406 – 4116Combined sources
Beta strandi418 – 43518Combined sources
Beta strandi438 – 45316Combined sources
Turni461 – 4644Combined sources
Beta strandi467 – 4693Combined sources
Beta strandi472 – 4743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HGSX-ray2.10A1-474[»]
ProteinModelPortaliP48637.
SMRiP48637. Positions 3-474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48637.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 1514Substrate binding
Regioni214 – 2163Substrate binding
Regioni267 – 2704Substrate binding
Regioni461 – 4622Substrate binding

Sequence similaritiesi

Belongs to the eukaryotic GSH synthase family.Curated

Phylogenomic databases

eggNOGiKOG0021. Eukaryota.
ENOG410XPHH. LUCA.
GeneTreeiENSGT00390000013764.
HOGENOMiHOG000172641.
HOVERGENiHBG002458.
InParanoidiP48637.
KOiK01920.
OMAiYMPRQYS.
OrthoDBiEOG091G05V8.
PhylomeDBiP48637.
TreeFamiTF105187.

Family and domain databases

Gene3Di1.10.1080.10. 2 hits.
3.30.1490.50. 1 hit.
3.30.1490.80. 2 hits.
3.40.50.1760. 1 hit.
InterProiIPR004887. 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]
PANTHERiPTHR11130. PTHR11130. 1 hit.
PfamiPF03917. GSH_synth_ATP. 1 hit.
PF03199. GSH_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001558. GSHase. 1 hit.
SUPFAMiSSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01986. glut_syn_euk. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P48637-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MATNWGSLLQ DKQQLEELAR QAVDRALAEG VLLRTSQEPT SSEVVSYAPF 
        60         70         80         90        100
TLFPSLVPSA LLEQAYAVQM DFNLLVDAVS QNAAFLEQTL SSTIKQDDFT 
       110        120        130        140        150
ARLFDIHKQV LKEGIAQTVF LGLNRSDYMF QRSADGSPAL KQIEINTISA 
       160        170        180        190        200
SFGGLASRTP AVHRHVLSVL SKTKEAGKIL SNNPSKGLAL GIAKAWELYG 
       210        220        230        240        250
SPNALVLLIA QEKERNIFDQ RAIENELLAR NIHVIRRTFE DISEKGSLDQ 
       260        270        280        290        300
DRRLFVDGQE IAVVYFRDGY MPRQYSLQNW EARLLLERSH AAKCPDIATQ 
       310        320        330        340        350
LAGTKKVQQE LSRPGMLEML LPGQPEAVAR LRATFAGLYS LDVGEEGDQA 
       360        370        380        390        400
IAEALAAPSR FVLKPQREGG GNNLYGEEMV QALKQLKDSE ERASYILMEK 
       410        420        430        440        450
IEPEPFENCL LRPGSPARVV QCISELGIFG VYVRQEKTLV MNKHVGHLLR 
       460        470 
TKAIEHADGG VAAGVAVLDN PYPV
Length:474
Mass (Da):52,385
Last modified:February 1, 1996 - v1
Checksum:i3C25EF7072EFE058
GO
Isoform 2 (identifier: P48637-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:363
Mass (Da):40,349
Checksum:i931DA0F137EE1634
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 261A → D in GSS deficiency.
Corresponds to variant rs759253242 [ dbSNP | Ensembl ].		VAR_003602
Natural varianti188 – 1881L → P in GSS deficiency; 100-fold reduction of activity.
VAR_003603
Natural varianti219 – 2191D → A in GSS deficiency.
VAR_003604
Natural varianti219 – 2191D → G in GSS deficiency. 1 Publication
Corresponds to variant rs28938472 [ dbSNP | Ensembl ].		VAR_003605
Natural varianti236 – 2361R → Q.1 Publication
Corresponds to variant rs34239729 [ dbSNP | Ensembl ].		VAR_025047
Natural varianti254 – 2541L → R in GSS deficiency.
VAR_003606
Natural varianti267 – 2671R → W in GSS deficiency. 1 Publication
Corresponds to variant rs121909308 [ dbSNP | Ensembl ].		VAR_003607
Natural varianti270 – 2701Y → C in GSS deficiency; 100-fold reduction of activity.
VAR_003608
Natural varianti270 – 2701Y → H in GSS deficiency; 100-fold reduction of activity.
VAR_003609
Natural varianti283 – 2831R → C in GSS deficiency; 10-fold reduction of activity. 1 Publication
Corresponds to variant rs121909309 [ dbSNP | Ensembl ].		VAR_003610
Natural varianti286 – 2861L → Q in GSS deficiency.
VAR_003611
Natural varianti330 – 3301R → C in GSS deficiency.
Corresponds to variant rs148640446 [ dbSNP | Ensembl ].		VAR_003612
Natural varianti437 – 4371K → E.2 Publications
Corresponds to variant rs34852238 [ dbSNP | Ensembl ].		VAR_025048
Natural varianti464 – 4641G → V in GSS deficiency.
VAR_003613
Natural varianti469 – 4691D → E in GSS deficiency.
VAR_003614

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei93 – 203111Missing in isoform 2. 1 PublicationVSP_047617Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13245.1. [P48637-1]
PIRiS56748.
RefSeqiNP_000169.1. NM_000178.3. [P48637-1]
NP_001309423.1. NM_001322494.1. [P48637-1]
NP_001309424.1. NM_001322495.1. [P48637-1]
UniGeneiHs.82327.

Genome annotation databases

EnsembliENST00000216951; ENSP00000216951; ENSG00000100983. [P48637-1]
ENST00000451957; ENSP00000407517; ENSG00000100983. [P48637-2]
GeneIDi2937.
KEGGihsa:2937.
UCSCiuc010zuo.3. human. [P48637-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13245.1. [P48637-1]
PIRiS56748.
RefSeqiNP_000169.1. NM_000178.3. [P48637-1]
NP_001309423.1. NM_001322494.1. [P48637-1]
NP_001309424.1. NM_001322495.1. [P48637-1]
UniGeneiHs.82327.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HGSX-ray2.10A1-474[»]
ProteinModelPortaliP48637.
SMRiP48637. Positions 3-474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109192. 27 interactions.
IntActiP48637. 3 interactions.
MINTiMINT-5001027.
STRINGi9606.ENSP00000216951.

Chemistry

DrugBankiDB06151. Acetylcysteine.
DB00143. Glutathione.
DB00145. Glycine.
DB00151. L-Cysteine.

PTM databases

iPTMnetiP48637.
PhosphoSiteiP48637.

Polymorphism and mutation databases

BioMutaiGSS.
DMDMi1346191.

2D gel databases

OGPiP48637.
REPRODUCTION-2DPAGEIPI00010706.

Proteomic databases

EPDiP48637.
PaxDbiP48637.
PeptideAtlasiP48637.
PRIDEiP48637.

Protocols and materials databases

DNASUi2937.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216951; ENSP00000216951; ENSG00000100983. [P48637-1]
ENST00000451957; ENSP00000407517; ENSG00000100983. [P48637-2]
GeneIDi2937.
KEGGihsa:2937.
UCSCiuc010zuo.3. human. [P48637-1]

Organism-specific databases

CTDi2937.
GeneCardsiGSS.
HGNCiHGNC:4624. GSS.
HPAiHPA054508.
HPA059315.
MalaCardsiGSS.
MIMi231900. phenotype.
266130. phenotype.
601002. gene.
neXtProtiNX_P48637.
Orphaneti289846. Glutathione synthetase deficiency with 5-oxoprolinuria.
289849. Glutathione synthetase deficiency without 5-oxoprolinuria.
PharmGKBiPA29015.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0021. Eukaryota.
ENOG410XPHH. LUCA.
GeneTreeiENSGT00390000013764.
HOGENOMiHOG000172641.
HOVERGENiHBG002458.
InParanoidiP48637.
KOiK01920.
OMAiYMPRQYS.
OrthoDBiEOG091G05V8.
PhylomeDBiP48637.
TreeFamiTF105187.

Enzyme and pathway databases

UniPathwayiUPA00142; UER00210.
BioCyciMetaCyc:HS02174-MONOMER.
BRENDAi6.3.2.3. 2681.
ReactomeiR-HSA-174403. Glutathione synthesis and recycling.
R-HSA-5579006. Defective GSS causes Glutathione synthetase deficiency (GSS deficiency).
SABIO-RKP48637.

Miscellaneous databases

ChiTaRSiGSS. human.
EvolutionaryTraceiP48637.
GenomeRNAii2937.
PROiP48637.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100983.
CleanExiHS_GSS.
ExpressionAtlasiP48637. baseline and differential.
GenevisibleiP48637. HS.

Family and domain databases

Gene3Di1.10.1080.10. 2 hits.
3.30.1490.50. 1 hit.
3.30.1490.80. 2 hits.
3.40.50.1760. 1 hit.
InterProiIPR004887. 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]
PANTHERiPTHR11130. PTHR11130. 1 hit.
PfamiPF03917. GSH_synth_ATP. 1 hit.
PF03199. GSH_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001558. GSHase. 1 hit.
SUPFAMiSSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01986. glut_syn_euk. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGSHB_HUMAN
AccessioniPrimary (citable) accession number: P48637
Secondary accession number(s): B2R697
, B6F210, E1P5P9, Q4TTD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 7, 2016
This is version 170 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

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 one 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.