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UniProtKB - P00367 (DHE3_HUMAN)

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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

GLUD1

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

Functioni

Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).By similarity

Catalytic activityi

L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.PROSITE-ProRule annotation

Enzyme regulationi

Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding site and activate the enzyme.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei147SubstrateBy similarity1
Binding sitei171SubstrateBy similarity1
Binding sitei176NADBy similarity1
Active sitei1831
Binding sitei252NADBy similarity1
Binding sitei266GTPBy similarity1
Binding sitei270GTPBy similarity1
Binding sitei319GTPBy similarity1
Binding sitei322GTPBy similarity1
Binding sitei438SubstrateBy similarity1
Binding sitei444NADBy similarity1
Binding sitei450ADPBy similarity1
Binding sitei516ADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi141 – 143NADBy similarity3

GO - Molecular functioni

  • ADP binding Source: BHF-UCL
  • ATP binding Source: UniProtKB-KW
  • glutamate dehydrogenase (NAD+) activity Source: UniProtKB
  • glutamate dehydrogenase [NAD(P)+] activity Source: BHF-UCL
  • GTP binding Source: BHF-UCL
  • identical protein binding Source: BHF-UCL
  • leucine binding Source: BHF-UCL
  • NAD+ binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cellular amino acid biosynthetic process Source: Reactome
  • glutamate biosynthetic process Source: BHF-UCL
  • glutamate catabolic process Source: UniProtKB
  • glutamine metabolic process Source: UniProtKB
  • positive regulation of insulin secretion Source: BHF-UCL
  • substantia nigra development Source: UniProtKB
  • tricarboxylic acid metabolic process Source: UniProtKB
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionOxidoreductase
LigandATP-binding, GTP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS07548-MONOMER
BRENDAi1.4.1.3 2681
ReactomeiR-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-70614 Amino acid synthesis and interconversion (transamination)
SABIO-RKiP00367
SIGNORiP00367

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
Short name:
GDH 1
Gene namesi
Name:GLUD1
Synonyms:GLUD
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 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000148672.8
HGNCiHGNC:4335 GLUD1
MIMi138130 gene
neXtProtiNX_P00367

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Familial hyperinsulinemic hypoglycemia 6 (HHF6)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionFamilial hyperinsulinemic hypoglycemia [MIM:256450], also referred to as congenital hyperinsulinism, nesidioblastosis, or persistent hyperinsulinemic hypoglycemia of infancy (PPHI), is the most common cause of persistent hypoglycemia in infancy and is due to defective negative feedback regulation of insulin secretion by low glucose levels. In HHF6 elevated oxidation rate of glutamate to alpha-ketoglutarate stimulates insulin secretion in the pancreatic beta cells, while they impair detoxification of ammonium in the liver.
See also OMIM:606762
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_016760270S → C in HHF6; diminished sensitivity to GTP. 1 Publication1
Natural variantiVAR_016761274R → C in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs56275071EnsemblClinVar.1
Natural variantiVAR_009270318R → K in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909736EnsemblClinVar.1
Natural variantiVAR_016762318R → T in HHF6; diminished sensitivity to GTP. 1 Publication1
Natural variantiVAR_016763319Y → C in HHF6. 1 Publication1
Natural variantiVAR_016764322R → C in HHF6; diminished sensitivity to GTP. 1 Publication1
Natural variantiVAR_016765322R → H in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs121909737EnsemblClinVar.1
Natural variantiVAR_009271349E → A in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909735EnsemblClinVar.1
Natural variantiVAR_008666498S → L in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909731EnsemblClinVar.1
Natural variantiVAR_008667499G → D in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909734EnsemblClinVar.1
Natural variantiVAR_008668499G → S in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909733EnsemblClinVar.1
Natural variantiVAR_008669501S → P in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909732EnsemblClinVar.1
Natural variantiVAR_008670507H → Y in HHF6; abolishes inhibition by ATP; no effect on activation by ADP. 3 PublicationsCorresponds to variant dbSNP:rs121909730EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi501S → A: Reduces activity and inhibition by GTP. 1 Publication1
Mutagenesisi507H → A: Strongly reduces inhibition by GTP. 1
Mutagenesisi516R → A: Abolishes activation by ADP. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2746
GeneReviewsiGLUD1
MalaCardsiGLUD1
MIMi606762 phenotype
OpenTargetsiENSG00000148672
Orphaneti35878 Hyperinsulinism-hyperammonemia syndrome
PharmGKBiPA28737

Chemistry databases

DrugBankiDB04137 Guanosine-5'-Triphosphate
DB00756 Hexachlorophene
DB00142 L-Glutamic Acid
DB00157 NADH

Polymorphism and mutation databases

BioMutaiGLUD1
DMDMi118541

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 53MitochondrionCombined sources2 PublicationsAdd BLAST53
ChainiPRO_000000720654 – 558Glutamate dehydrogenase 1, mitochondrialAdd BLAST505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei68N6-succinyllysineBy similarity1
Modified residuei79PhosphoserineBy similarity1
Modified residuei84N6-acetyllysine; alternateCombined sources1
Modified residuei84N6-succinyllysine; alternateBy similarity1
Modified residuei110N6-acetyllysine; alternateBy similarity1
Modified residuei110N6-succinyllysine; alternateBy similarity1
Modified residuei128PhosphoserineBy similarity1
Modified residuei135PhosphotyrosineBy similarity1
Modified residuei162N6-acetyllysine; alternateBy similarity1
Modified residuei162N6-succinyllysine; alternateBy similarity1
Modified residuei171N6-acetyllysineBy similarity1
Modified residuei172ADP-ribosylcysteine1 Publication1
Modified residuei183N6-acetyllysine; alternateBy similarity1
Modified residuei183N6-succinyllysine; alternateBy similarity1
Modified residuei187N6-acetyllysineBy similarity1
Modified residuei191N6-acetyllysine; alternateBy similarity1
Modified residuei191N6-succinyllysine; alternateBy similarity1
Modified residuei200N6-succinyllysineBy similarity1
Modified residuei211N6-acetyllysineBy similarity1
Modified residuei227PhosphoserineCombined sources1
Modified residuei326N6-acetyllysineBy similarity1
Modified residuei346N6-acetyllysine; alternateBy similarity1
Modified residuei346N6-succinyllysine; alternateBy similarity1
Modified residuei352N6-acetyllysine; alternateBy similarity1
Modified residuei352N6-succinyllysine; alternateBy similarity1
Modified residuei363N6-acetyllysine; alternateBy similarity1
Modified residuei363N6-succinyllysine; alternateBy similarity1
Modified residuei365N6-acetyllysine; alternateBy similarity1
Modified residuei365N6-succinyllysine; alternateBy similarity1
Modified residuei384PhosphoserineCombined sources1
Modified residuei386N6-acetyllysineBy similarity1
Modified residuei390N6-acetyllysine; alternateBy similarity1
Modified residuei390N6-succinyllysine; alternateBy similarity1
Modified residuei399N6-acetyllysineBy similarity1
Modified residuei410PhosphothreonineBy similarity1
Modified residuei415N6-acetyllysine; alternateBy similarity1
Modified residuei415N6-succinyllysine; alternateBy similarity1
Modified residuei457N6-acetyllysine; alternateBy similarity1
Modified residuei457N6-malonyllysine; alternateBy similarity1
Modified residuei457N6-succinyllysine; alternateBy similarity1
Modified residuei477N6-acetyllysine; alternateBy similarity1
Modified residuei477N6-succinyllysine; alternateBy similarity1
Modified residuei480N6-acetyllysine; alternateCombined sources1
Modified residuei480N6-succinyllysine; alternateBy similarity1
Modified residuei503N6-acetyllysine; alternateCombined sources1
Modified residuei503N6-malonyllysine; alternateBy similarity1
Modified residuei503N6-succinyllysine; alternateBy similarity1
Modified residuei512PhosphotyrosineCombined sources1
Modified residuei527N6-acetyllysine; alternateBy similarity1
Modified residuei527N6-malonyllysine; alternateBy similarity1
Modified residuei527N6-succinyllysine; alternateBy similarity1
Modified residuei545N6-acetyllysine; alternateBy similarity1
Modified residuei545N6-succinyllysine; alternateBy similarity1
Modified residuei548N6-acetyllysineBy similarity1

Post-translational modificationi

ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity (By similarity). Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

EPDiP00367
MaxQBiP00367
PaxDbiP00367
PeptideAtlasiP00367
PRIDEiP00367
ProteomicsDBi51236

2D gel databases

REPRODUCTION-2DPAGEiIPI00016801
SWISS-2DPAGEiP00367
UCD-2DPAGEiP00367

PTM databases

iPTMnetiP00367
PhosphoSitePlusiP00367
SwissPalmiP00367

Expressioni

Gene expression databases

BgeeiENSG00000148672
CleanExiHS_GLUD1
ExpressionAtlasiP00367 baseline and differential
GenevisibleiP00367 HS

Organism-specific databases

HPAiHPA042492
HPA044839
HPA061369

Interactioni

Subunit structurei

Homohexamer.

GO - Molecular functioni

  • identical protein binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi109008, 43 interactors
IntActiP00367, 47 interactors
MINTiP00367
STRINGi9606.ENSP00000277865

Structurei

Secondary structure

1558
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi66 – 90Combined sources25
Helixi91 – 93Combined sources3
Helixi95 – 97Combined sources3
Helixi99 – 102Combined sources4
Helixi104 – 109Combined sources6
Beta strandi113 – 123Combined sources11
Beta strandi125 – 127Combined sources3
Beta strandi129 – 138Combined sources10
Beta strandi142 – 152Combined sources11
Helixi158 – 174Combined sources17
Beta strandi180 – 186Combined sources7
Helixi190 – 192Combined sources3
Helixi195 – 211Combined sources17
Turni217 – 219Combined sources3
Beta strandi220 – 223Combined sources4
Helixi230 – 242Combined sources13
Turni243 – 247Combined sources5
Helixi251 – 253Combined sources3
Helixi260 – 262Combined sources3
Helixi271 – 284Combined sources14
Helixi287 – 293Combined sources7
Beta strandi298 – 300Combined sources3
Beta strandi303 – 307Combined sources5
Helixi311 – 322Combined sources12
Beta strandi326 – 331Combined sources6
Helixi345 – 354Combined sources10
Beta strandi355 – 358Combined sources4
Turni371 – 373Combined sources3
Beta strandi377 – 381Combined sources5
Beta strandi383 – 386Combined sources4
Turni390 – 392Combined sources3
Helixi393 – 395Combined sources3
Beta strandi399 – 402Combined sources4
Beta strandi405 – 407Combined sources3
Helixi411 – 419Combined sources9
Beta strandi423 – 425Combined sources3
Helixi427 – 430Combined sources4
Helixi433 – 447Combined sources15
Turni451 – 455Combined sources5
Helixi456 – 475Combined sources20
Turni476 – 479Combined sources4
Beta strandi481 – 484Combined sources4
Helixi491 – 498Combined sources8
Helixi502 – 527Combined sources26
Helixi534 – 551Combined sources18

3D structure databases

ProteinModelPortaliP00367
SMRiP00367
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00367

Family & Domainsi

Sequence similaritiesi

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2250 Eukaryota
COG0334 LUCA
GeneTreeiENSGT00390000000854
HOGENOMiHOG000243801
HOVERGENiHBG005479
InParanoidiP00367
KOiK00261
OMAiPCFAAFP
OrthoDBiEOG091G0KMT
PhylomeDBiP00367
TreeFamiTF313945

Family and domain databases

CDDicd01076 NAD_bind_1_Glu_DH, 1 hit
InterProiView protein in InterPro
IPR006095 Glu/Leu/Phe/Val_DH
IPR033524 Glu/Leu/Phe/Val_DH_AS
IPR006096 Glu/Leu/Phe/Val_DH_C
IPR006097 Glu/Leu/Phe/Val_DH_dimer_dom
IPR036291 NAD(P)-bd_dom_sf
IPR033922 NAD_bind_Glu_DH
PfamiView protein in Pfam
PF00208 ELFV_dehydrog, 1 hit
PF02812 ELFV_dehydrog_N, 1 hit
PRINTSiPR00082 GLFDHDRGNASE
SMARTiView protein in SMART
SM00839 ELFV_dehydrog, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00074 GLFV_DEHYDROGENASE, 1 hit

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P00367-1) [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
MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLALAAR 
        60         70         80         90        100
RHYSEAVADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN 
       110        120        130        140        150
RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI 
       160        170        180        190        200
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK 
       210        220        230        240        250
ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN 
       260        270        280        290        300
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG 
       310        320        330        340        350
DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED 
       360        370        380        390        400
FKLQHGSILG FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI 
       410        420        430        440        450
IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS 
       460        470        480        490        500
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDRISGA 
       510        520        530        540        550
SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY 

NEAGVTFT
Length:558
Mass (Da):61,398
Last modified:January 1, 1990 - v2
Checksum:iA7319A840F57FBB2
GO
Isoform 2 (identifier: P00367-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-167: Missing.

Note: No experimental confirmation available.
Show »
Length:391
Mass (Da):42,950
Checksum:i8A493E2898605460
GO
Isoform 3 (identifier: P00367-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MYRYLGEALLLSRAGP → MTCPCDNASSVFLGFC
     17-149: Missing.

Note: No experimental confirmation available.
Show »
Length:425
Mass (Da):46,575
Checksum:i2637B3023F58A7C4
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_016760270S → C in HHF6; diminished sensitivity to GTP. 1 Publication1
Natural variantiVAR_016761274R → C in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs56275071EnsemblClinVar.1
Natural variantiVAR_009270318R → K in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909736EnsemblClinVar.1
Natural variantiVAR_016762318R → T in HHF6; diminished sensitivity to GTP. 1 Publication1
Natural variantiVAR_016763319Y → C in HHF6. 1 Publication1
Natural variantiVAR_016764322R → C in HHF6; diminished sensitivity to GTP. 1 Publication1
Natural variantiVAR_016765322R → H in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs121909737EnsemblClinVar.1
Natural variantiVAR_009271349E → A in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909735EnsemblClinVar.1
Natural variantiVAR_008666498S → L in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909731EnsemblClinVar.1
Natural variantiVAR_008667499G → D in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909734EnsemblClinVar.1
Natural variantiVAR_008668499G → S in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909733EnsemblClinVar.1
Natural variantiVAR_008669501S → P in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909732EnsemblClinVar.1
Natural variantiVAR_008670507H → Y in HHF6; abolishes inhibition by ATP; no effect on activation by ADP. 3 PublicationsCorresponds to variant dbSNP:rs121909730EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0562441 – 167Missing in isoform 2. 1 PublicationAdd BLAST167
Alternative sequenceiVSP_0565231 – 16MYRYL…SRAGP → MTCPCDNASSVFLGFC in isoform 3. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_05652417 – 149Missing in isoform 3. 1 PublicationAdd BLAST133

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07674 mRNA Translation: CAA30521.1
M20867 mRNA Translation: AAA52526.1
M37154 mRNA Translation: AAA52525.1
X07769 mRNA Translation: CAA30598.1
J03248 mRNA Translation: AAA52523.1
X66300
, X66301, X66302, X66303, X66304, X66305, X66306, X66307, X66308, X66309, X66311, X66312 Genomic DNA Translation: CAA46994.2
AK122685 mRNA Translation: BAG53667.1
AK294685 mRNA Translation: BAG57846.1
AL136982 Genomic DNA Translation: CAI17120.1
CH471142 Genomic DNA Translation: EAW80300.1
CH471142 Genomic DNA Translation: EAW80302.1
BC040132 mRNA Translation: AAH40132.1
BC112946 mRNA Translation: AAI12947.1
X67491 Genomic DNA Translation: CAA47830.1
CCDSiCCDS7382.1 [P00367-1]
PIRiA28208 DEHUE
I37424
S29331
S60192
RefSeqiNP_001305829.1, NM_001318900.1 [P00367-3]
NP_001305830.1, NM_001318901.1 [P00367-2]
NP_001305831.1, NM_001318902.1 [P00367-2]
NP_001305833.1, NM_001318904.1 [P00367-2]
NP_001305834.1, NM_001318905.1 [P00367-2]
NP_001305835.1, NM_001318906.1 [P00367-2]
NP_005262.1, NM_005271.4 [P00367-1]
UniGeneiHs.500409
Hs.731740

Genome annotation databases

EnsembliENST00000277865; ENSP00000277865; ENSG00000148672 [P00367-1]
GeneIDi2746
KEGGihsa:2746
UCSCiuc001keh.4 human [P00367-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiDHE3_HUMAN
AccessioniPrimary (citable) accession number: P00367
Secondary accession number(s): B3KV55, B4DGN5, Q5TBU3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: July 18, 2018
This is version 209 of the entry and version 2 of the sequence. See 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 10
    Human chromosome 10: 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

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