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Protein

Peroxisomal bifunctional enzyme

Gene

EHHADH

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

Functioni

Catalytic activityi

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

Enzyme regulationi

Enzyme activity enhanced by acetylation.1 Publication

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei101Substrate; via amide nitrogenBy similarity1
Sitei104Important for catalytic activityBy similarity1
Sitei124Important for catalytic activityBy similarity1

GO - Molecular functioni

  • 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB
  • dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-EC
  • enoyl-CoA hydratase activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • long-chain-enoyl-CoA hydratase activity Source: Reactome
  • receptor binding Source: UniProtKB

GO - Biological processi

  • cellular lipid metabolic process Source: Reactome
  • fatty acid beta-oxidation Source: UniProtKB
  • internal protein amino acid acetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS03720-MONOMER.
ZFISH:HS03720-MONOMER.
ReactomeiR-HSA-390918. Peroxisomal lipid metabolism.
SABIO-RKQ08426.
UniPathwayiUPA00659.

Chemistry databases

SwissLipidsiSLP:000000543.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal bifunctional enzyme
Short name:
PBE
Short name:
PBFE
Including the following 2 domains:
Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase (EC:4.2.1.17, EC:5.3.3.8)
3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
Gene namesi
Name:EHHADH
Synonyms:ECHD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:3247. EHHADH.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • mitochondrion Source: Ensembl
  • peroxisomal matrix Source: Reactome
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Involvement in diseasei

Fanconi renotubular syndrome 3 (FRTS3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease due to a generalized dysfunction of the proximal kidney tubule resulting in decreased solute and water reabsorption. Patients have polydipsia and polyuria with phosphaturia, glycosuria and aminoaciduria. They may develop hypophosphatemic rickets or osteomalacia, acidosis and a tendency toward dehydration. Some eventually develop renal insufficiency.
See also OMIM:615605
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0709493E → K in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells. 1 PublicationCorresponds to variant rs398124646dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi165K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584. 1 Publication1
Mutagenesisi171K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584. 1 Publication1
Mutagenesisi346K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584. 1 Publication1
Mutagenesisi584K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi1962.
51807.
MalaCardsiEHHADH.
MIMi615605. phenotype.
OpenTargetsiENSG00000113790.
Orphaneti300. Bifunctional enzyme deficiency.
3337. Primary Fanconi syndrome.
PharmGKBiPA27682.

Polymorphism and mutation databases

BioMutaiEHHADH.
DMDMi223590229.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001092471 – 723Peroxisomal bifunctional enzymeAdd BLAST723

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38N6-succinyllysineBy similarity1
Modified residuei165N6-acetyllysine; alternate1 Publication1
Modified residuei165N6-succinyllysine; alternateBy similarity1
Modified residuei171N6-acetyllysine1 Publication1
Modified residuei219N6-acetyllysine; alternateBy similarity1
Modified residuei219N6-succinyllysine; alternateBy similarity1
Modified residuei250N6-acetyllysineBy similarity1
Modified residuei280N6-succinyllysineBy similarity1
Modified residuei290N6-succinyllysineBy similarity1
Modified residuei346N6-acetyllysine1 Publication1
Modified residuei350N6-acetyllysineBy similarity1
Modified residuei464N6-acetyllysineBy similarity1
Modified residuei532N6-succinyllysineBy similarity1
Modified residuei548PhosphothreonineCombined sources1
Modified residuei577N6-succinyllysineBy similarity1
Modified residuei584N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei584N6-succinyllysine; alternateBy similarity1
Modified residuei591N6-acetyllysine; alternateBy similarity1
Modified residuei591N6-succinyllysine; alternateBy similarity1
Modified residuei710N6-acetyllysine; alternateBy similarity1
Modified residuei710N6-succinyllysine; alternateBy similarity1
Modified residuei718PhosphoserineCombined sources1
Modified residuei722N6-succinyllysineBy similarity1

Post-translational modificationi

Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TSA) or with nicotinamide (NAM) with highest increase on Lys-346. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ08426.
MaxQBiQ08426.
PaxDbiQ08426.
PeptideAtlasiQ08426.
PRIDEiQ08426.

PTM databases

iPTMnetiQ08426.
PhosphoSitePlusiQ08426.

Expressioni

Tissue specificityi

Liver and kidney. Strongly expressed in the terminal segments of the proximal tubule. Lower amounts seen in the brain.2 Publications

Gene expression databases

BgeeiENSG00000113790.
CleanExiHS_EHHADH.
ExpressionAtlasiQ08426. baseline and differential.
GenevisibleiQ08426. HS.

Organism-specific databases

HPAiHPA036401.
HPA042021.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTG1P632613EBI-2339219,EBI-351292
BHLHE40O145033EBI-2339219,EBI-711810
CBSP355203EBI-2339219,EBI-740135
CCDC102BA1A4H13EBI-2339219,EBI-10171570
DESP176615EBI-2339219,EBI-1055572
FUNDC1Q8IVP53EBI-2339219,EBI-3059266
KCTD6Q8NC693EBI-2339219,EBI-2511344
KCTD9Q7L2733EBI-2339219,EBI-4397613
KRTAP10-7P604093EBI-2339219,EBI-10172290
LZTS2Q9BRK43EBI-2339219,EBI-741037
MID1O153445EBI-2339219,EBI-2340316
NECAB2H3BTW23EBI-2339219,EBI-10172876
PNMA1Q8ND903EBI-2339219,EBI-302345
PS1TP5BP1Q1KLZ03EBI-2339219,EBI-9978131
SSNA1O438053EBI-2339219,EBI-2515299
SSX2IPQ9Y2D83EBI-2339219,EBI-2212028
TNIP1Q150253EBI-2339219,EBI-357849
TPP2P291443EBI-2339219,EBI-1044672
TRAF1Q130773EBI-2339219,EBI-359224
TRIM27P143735EBI-2339219,EBI-719493
TRIM41Q8WV445EBI-2339219,EBI-725997
TRIM54Q9BYV23EBI-2339219,EBI-2130429
ZBTB9Q96C005EBI-2339219,EBI-395708

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108282. 29 interactors.
IntActiQ08426. 51 interactors.
STRINGi9606.ENSP00000231887.

Structurei

3D structure databases

ProteinModelPortaliQ08426.
SMRiQ08426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 282Enoyl-CoA hydratase / isomeraseAdd BLAST282
Regioni283 – 5723-hydroxyacyl-CoA dehydrogenaseAdd BLAST290

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi721 – 723Microbody targeting signal3

Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

Phylogenomic databases

eggNOGiKOG1683. Eukaryota.
COG1024. LUCA.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261347.
HOVERGENiHBG104990.
InParanoidiQ08426.
KOiK07514.
OMAiFMYLQKS.
OrthoDBiEOG091G082G.
PhylomeDBiQ08426.
TreeFamiTF316708.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q08426-1) [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
MAEYTRLHNA LALIRLRNPP VNAISTTLLR DIKEGLQKAV IDHTIKAIVI
60 70 80 90 100
CGAEGKFSAG ADIRGFSAPR TFGLTLGHVV DEIQRNEKPV VAAIQGMAFG
110 120 130 140 150
GGLELALGCH YRIAHAEAQV GLPEVTLGLL PGARGTQLLP RLTGVPAALD
160 170 180 190 200
LITSGRRILA DEALKLGILD KVVNSDPVEE AIRFAQRVSD QPLESRRLCN
210 220 230 240 250
KPIQSLPNMD SIFSEALLKM RRQHPGCLAQ EACVRAVQAA VQYPYEVGIK
260 270 280 290 300
KEEELFLYLL QSGQARALQY AFFAERKANK WSTPSGASWK TASARPVSSV
310 320 330 340 350
GVVGLGTMGR GIVISFARAR IPVIAVDSDK NQLATANKMI TSVLEKEASK
360 370 380 390 400
MQQSGHPWSG PKPRLTSSVK ELGGVDLVIE AVFEEMSLKK QVFAELSAVC
410 420 430 440 450
KPEAFLCTNT SALDVDEIAS STDRPHLVIG THFFSPAHVM KLLEVIPSQY
460 470 480 490 500
SSPTTIATVM NLSKKIKKIG VVVGNCFGFV GNRMLNPYYN QAYFLLEEGS
510 520 530 540 550
KPEEVDQVLE EFGFKMGPFR VSDLAGLDVG WKSRKGQGLT GPTLLPGTPA
560 570 580 590 600
RKRGNRRYCP IPDVLCELGR FGQKTGKGWY QYDKPLGRIH KPDPWLSKFL
610 620 630 640 650
SRYRKTHHIE PRTISQDEIL ERCLYSLINE AFRILGEGIA ASPEHIDVVY
660 670 680 690 700
LHGYGWPRHK GGPMFYASTV GLPTVLEKLQ KYYRQNPDIP QLEPSDYLKK
710 720
LASQGNPPLK EWQSLAGSPS SKL
Length:723
Mass (Da):79,495
Last modified:February 10, 2009 - v3
Checksum:iFC3B44B030A7BCBD
GO
Isoform 2 (identifier: Q08426-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: Missing.

Show »
Length:627
Mass (Da):69,154
Checksum:iF1F1A30F0E89ED98
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti117E → D in AAA53289 (PubMed:8188243).Curated1
Sequence conflicti656 – 657WP → CA in AAA53289 (PubMed:8188243).Curated2
Sequence conflicti656 – 657WP → CA in AAB19482 (PubMed:15489334).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0709493E → K in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells. 1 PublicationCorresponds to variant rs398124646dbSNPEnsembl.1
Natural variantiVAR_05432940V → G.1 PublicationCorresponds to variant rs1062551dbSNPEnsembl.1
Natural variantiVAR_05433041I → R.1 PublicationCorresponds to variant rs1062552dbSNPEnsembl.1
Natural variantiVAR_04713275T → I.1 PublicationCorresponds to variant rs1062553dbSNPEnsembl.1
Natural variantiVAR_047133274A → T.1 PublicationCorresponds to variant rs2302819dbSNPEnsembl.1
Natural variantiVAR_054331325A → G.1 PublicationCorresponds to variant rs1062555dbSNPEnsembl.1
Natural variantiVAR_054332598K → T.2 PublicationsCorresponds to variant rs1042437dbSNPEnsembl.1
Natural variantiVAR_047134606T → P.2 PublicationsCorresponds to variant rs1042438dbSNPEnsembl.1
Natural variantiVAR_047135685Q → K.Corresponds to variant rs11919970dbSNPEnsembl.1
Natural variantiVAR_047136715L → S.Corresponds to variant rs11927618dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0428111 – 96Missing in isoform 2. 1 PublicationAdd BLAST96

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07077 mRNA. Translation: AAA53289.1.
AJ427345
, AJ427346, AJ427347, AJ427348, AJ427349, AJ427350, AJ427351 Genomic DNA. Translation: CAD22483.1.
AK291798 mRNA. Translation: BAF84487.1.
AK223460 mRNA. Translation: BAD97180.1.
AK301521 mRNA. Translation: BAG63025.1.
AC007934 Genomic DNA. No translation available.
AC128680 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78229.1.
CH471052 Genomic DNA. Translation: EAW78230.1.
BC038948 mRNA. Translation: AAH38948.1.
BC110460 mRNA. Translation: AAI10461.1.
S50245 mRNA. Translation: AAB19482.1.
CCDSiCCDS33901.1. [Q08426-1]
CCDS54694.1. [Q08426-2]
PIRiA49613.
RefSeqiNP_001159887.1. NM_001166415.1. [Q08426-2]
NP_001957.2. NM_001966.3. [Q08426-1]
UniGeneiHs.429879.

Genome annotation databases

EnsembliENST00000231887; ENSP00000231887; ENSG00000113790. [Q08426-1]
ENST00000456310; ENSP00000387746; ENSG00000113790. [Q08426-2]
GeneIDi1962.
KEGGihsa:1962.
UCSCiuc003fpf.3. human. [Q08426-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07077 mRNA. Translation: AAA53289.1.
AJ427345
, AJ427346, AJ427347, AJ427348, AJ427349, AJ427350, AJ427351 Genomic DNA. Translation: CAD22483.1.
AK291798 mRNA. Translation: BAF84487.1.
AK223460 mRNA. Translation: BAD97180.1.
AK301521 mRNA. Translation: BAG63025.1.
AC007934 Genomic DNA. No translation available.
AC128680 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78229.1.
CH471052 Genomic DNA. Translation: EAW78230.1.
BC038948 mRNA. Translation: AAH38948.1.
BC110460 mRNA. Translation: AAI10461.1.
S50245 mRNA. Translation: AAB19482.1.
CCDSiCCDS33901.1. [Q08426-1]
CCDS54694.1. [Q08426-2]
PIRiA49613.
RefSeqiNP_001159887.1. NM_001166415.1. [Q08426-2]
NP_001957.2. NM_001966.3. [Q08426-1]
UniGeneiHs.429879.

3D structure databases

ProteinModelPortaliQ08426.
SMRiQ08426.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108282. 29 interactors.
IntActiQ08426. 51 interactors.
STRINGi9606.ENSP00000231887.

Chemistry databases

SwissLipidsiSLP:000000543.

PTM databases

iPTMnetiQ08426.
PhosphoSitePlusiQ08426.

Polymorphism and mutation databases

BioMutaiEHHADH.
DMDMi223590229.

Proteomic databases

EPDiQ08426.
MaxQBiQ08426.
PaxDbiQ08426.
PeptideAtlasiQ08426.
PRIDEiQ08426.

Protocols and materials databases

DNASUi1962.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000231887; ENSP00000231887; ENSG00000113790. [Q08426-1]
ENST00000456310; ENSP00000387746; ENSG00000113790. [Q08426-2]
GeneIDi1962.
KEGGihsa:1962.
UCSCiuc003fpf.3. human. [Q08426-1]

Organism-specific databases

CTDi1962.
DisGeNETi1962.
51807.
GeneCardsiEHHADH.
HGNCiHGNC:3247. EHHADH.
HPAiHPA036401.
HPA042021.
MalaCardsiEHHADH.
MIMi607037. gene.
615605. phenotype.
neXtProtiNX_Q08426.
OpenTargetsiENSG00000113790.
Orphaneti300. Bifunctional enzyme deficiency.
3337. Primary Fanconi syndrome.
PharmGKBiPA27682.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1683. Eukaryota.
COG1024. LUCA.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261347.
HOVERGENiHBG104990.
InParanoidiQ08426.
KOiK07514.
OMAiFMYLQKS.
OrthoDBiEOG091G082G.
PhylomeDBiQ08426.
TreeFamiTF316708.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciMetaCyc:HS03720-MONOMER.
ZFISH:HS03720-MONOMER.
ReactomeiR-HSA-390918. Peroxisomal lipid metabolism.
SABIO-RKQ08426.

Miscellaneous databases

GenomeRNAii1962.
PROiQ08426.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113790.
CleanExiHS_EHHADH.
ExpressionAtlasiQ08426. baseline and differential.
GenevisibleiQ08426. HS.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiECHP_HUMAN
AccessioniPrimary (citable) accession number: Q08426
Secondary accession number(s): A8K6Y3
, B4DWG3, D3DNU0, Q58EZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: February 10, 2009
Last modified: November 30, 2016
This is version 172 of the entry and version 3 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

Miscellaneous

Absent in patients suffering with peroxisomal disorders such as Zellweger syndrome, neonatal adrenoleukodystrophy and infantile Refsum disease.

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. 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.