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Protein

2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial

Gene

BCKDHA

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

Functioni

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activityi

3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi206Potassium1
Metal bindingi211Potassium1
Metal bindingi212Potassium1

GO - Molecular functioni

  • 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Source: ProtInc
  • alpha-ketoacid dehydrogenase activity Source: HGNC
  • carboxy-lyase activity Source: HGNC
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • branched-chain amino acid catabolic process Source: HGNC
  • glyoxylate metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, Potassium, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12005.
ZFISH:MONOMER-12005.
ReactomeiR-HSA-389661. Glyoxylate metabolism and glycine degradation.
R-HSA-70895. Branched-chain amino acid catabolism.
SABIO-RKP12694.
SIGNORiP12694.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial (EC:1.2.4.4)
Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
Short name:
BCKDE1A
Short name:
BCKDH E1-alpha
Gene namesi
Name:BCKDHA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:986. BCKDHA.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial alpha-ketoglutarate dehydrogenase complex Source: HGNC
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Maple syrup urine disease 1A (MSUD1A)9 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA metabolic disorder due to an enzyme defect in the catabolic pathway of the branched-chain amino acids leucine, isoleucine, and valine. Accumulation of these 3 amino acids and their corresponding keto acids leads to encephalopathy and progressive neurodegeneration. Clinical features include mental and physical retardation, feeding problems, and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine. If untreated, maple syrup urine disease can lead to seizures, coma, and death. The disease is often classified by its pattern of signs and symptoms. The most common and severe form of the disease is the classic type, which becomes apparent soon after birth. Variant forms of the disorder become apparent later in infancy or childhood and are typically milder, but they still involve developmental delay and other medical problems if not treated.
See also OMIM:248600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004968159R → W in MSUD1A. 1 PublicationCorresponds to variant rs769688327dbSNPEnsembl.1
Natural variantiVAR_004969190Q → K in MSUD1A. 1 Publication1
Natural variantiVAR_069748211T → M in MSUD1A. 1 PublicationCorresponds to variant rs398123503dbSNPEnsembl.1
Natural variantiVAR_069749220A → V in MSUD1A. 1 PublicationCorresponds to variant rs375785084dbSNPEnsembl.1
Natural variantiVAR_004970253A → T in MSUD1A. 1 PublicationCorresponds to variant rs199599175dbSNPEnsembl.1
Natural variantiVAR_015101290G → R in MSUD1A. 1 PublicationCorresponds to variant rs137852871dbSNPEnsembl.1
Natural variantiVAR_004971326I → T in MSUD1A. 1 Publication1
Natural variantiVAR_069750346R → C in MSUD1A. 1 PublicationCorresponds to variant rs182923857dbSNPEnsembl.1
Natural variantiVAR_069751403P → PKP in MSUD1A. 1
Natural variantiVAR_015102409F → C in MSUD1A. 1 PublicationCorresponds to variant rs137852872dbSNPEnsembl.1
Natural variantiVAR_004972413Y → C in MSUD1A. 1 Publication1
Natural variantiVAR_069752427 – 428LA → P in MSUD1A. 1 Publication2
Natural variantiVAR_004973438Y → N in MSUD1A; impedes assembly of the E1 component. 5 PublicationsCorresponds to variant rs137852870dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Maple syrup urine disease

Organism-specific databases

DisGeNETi593.
MalaCardsiBCKDHA.
MIMi248600. phenotype.
OpenTargetsiENSG00000248098.
Orphaneti268145. Classic maple syrup urine disease.
268162. Intermediate maple syrup urine disease.
268173. Intermittent maple syrup urine disease.
268184. Thiamine-responsive maple syrup urine disease.
PharmGKBiPA25297.

Polymorphism and mutation databases

BioMutaiBCKDHA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 45Mitochondrion1 PublicationAdd BLAST45
ChainiPRO_000002046546 – 4452-oxoisovalerate dehydrogenase subunit alpha, mitochondrialAdd BLAST400

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei337PhosphoserineBy similarity1
Modified residuei338PhosphothreonineBy similarity1
Modified residuei339PhosphoserineBy similarity1
Modified residuei347PhosphoserineBy similarity1
Modified residuei356N6-acetyllysine; alternateBy similarity1
Modified residuei356N6-succinyllysine; alternateBy similarity1
Modified residuei380N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP12694.
MaxQBiP12694.
PaxDbiP12694.
PeptideAtlasiP12694.
PRIDEiP12694.

PTM databases

iPTMnetiP12694.
PhosphoSitePlusiP12694.

Expressioni

Gene expression databases

BgeeiENSG00000248098.
CleanExiHS_BCKDHA.
ExpressionAtlasiP12694. baseline and differential.
GenevisibleiP12694. HS.

Organism-specific databases

HPAiHPA036640.

Interactioni

Subunit structurei

Heterotetramer of alpha and beta chains.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BCKDHBP2195314EBI-1029053,EBI-1029067

Protein-protein interaction databases

BioGridi107065. 24 interactors.
DIPiDIP-6146N.
IntActiP12694. 8 interactors.
MINTiMINT-271818.
STRINGi9606.ENSP00000269980.

Structurei

Secondary structure

1445
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi61 – 64Combined sources4
Beta strandi88 – 90Combined sources3
Helixi91 – 93Combined sources3
Helixi99 – 124Combined sources26
Beta strandi127 – 129Combined sources3
Turni135 – 137Combined sources3
Helixi138 – 146Combined sources9
Beta strandi152 – 155Combined sources4
Helixi161 – 166Combined sources6
Helixi171 – 179Combined sources9
Turni185 – 188Combined sources4
Turni198 – 201Combined sources4
Turni209 – 211Combined sources3
Helixi212 – 226Combined sources15
Beta strandi232 – 237Combined sources6
Helixi240 – 242Combined sources3
Helixi244 – 255Combined sources12
Beta strandi260 – 266Combined sources7
Beta strandi268 – 270Combined sources3
Helixi275 – 277Combined sources3
Beta strandi280 – 282Combined sources3
Helixi285 – 287Combined sources3
Helixi289 – 291Combined sources3
Beta strandi294 – 299Combined sources6
Helixi303 – 320Combined sources18
Beta strandi324 – 329Combined sources6
Helixi342 – 344Combined sources3
Helixi351 – 357Combined sources7
Helixi360 – 368Combined sources9
Turni369 – 372Combined sources4
Helixi376 – 399Combined sources24
Helixi405 – 408Combined sources4
Turni409 – 411Combined sources3
Beta strandi412 – 415Combined sources4
Helixi418 – 434Combined sources17
Helixi435 – 437Combined sources3
Helixi440 – 442Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DTWX-ray2.70A46-445[»]
1OLSX-ray1.85A46-445[»]
1OLUX-ray1.90A46-445[»]
1OLXX-ray2.25A46-445[»]
1U5BX-ray1.83A46-445[»]
1V11X-ray1.95A46-445[»]
1V16X-ray1.90A46-445[»]
1V1MX-ray2.00A46-445[»]
1V1RX-ray1.80A46-445[»]
1WCIX-ray1.84A46-445[»]
1X7WX-ray1.73A46-445[»]
1X7XX-ray2.10A46-445[»]
1X7YX-ray1.57A46-445[»]
1X7ZX-ray1.72A46-445[»]
1X80X-ray2.00A46-445[»]
2BEUX-ray1.89A46-445[»]
2BEVX-ray1.80A46-445[»]
2BEWX-ray1.79A46-445[»]
2BFBX-ray1.77A46-445[»]
2BFCX-ray1.64A46-445[»]
2BFDX-ray1.39A46-445[»]
2BFEX-ray1.69A46-445[»]
2BFFX-ray1.46A46-445[»]
2J9FX-ray1.88A/C46-445[»]
ProteinModelPortaliP12694.
SMRiP12694.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12694.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni157 – 159Thiamine pyrophosphate binding3

Sequence similaritiesi

Belongs to the BCKDHA family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1182. Eukaryota.
COG1071. LUCA.
GeneTreeiENSGT00530000063174.
HOGENOMiHOG000281337.
HOVERGENiHBG002459.
InParanoidiP12694.
KOiK00166.
OrthoDBiEOG091G073F.
PhylomeDBiP12694.
TreeFamiTF300863.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 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: P12694-1) [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
MAVAIAAARV WRLNRGLSQA ALLLLRQPGA RGLARSHPPR QQQQFSSLDD
60 70 80 90 100
KPQFPGASAE FIDKLEFIQP NVISGIPIYR VMDRQGQIIN PSEDPHLPKE
110 120 130 140 150
KVLKLYKSMT LLNTMDRILY ESQRQGRISF YMTNYGEEGT HVGSAAALDN
160 170 180 190 200
TDLVFGQYRE AGVLMYRDYP LELFMAQCYG NISDLGKGRQ MPVHYGCKER
210 220 230 240 250
HFVTISSPLA TQIPQAVGAA YAAKRANANR VVICYFGEGA ASEGDAHAGF
260 270 280 290 300
NFAATLECPI IFFCRNNGYA ISTPTSEQYR GDGIAARGPG YGIMSIRVDG
310 320 330 340 350
NDVFAVYNAT KEARRRAVAE NQPFLIEAMT YRIGHHSTSD DSSAYRSVDE
360 370 380 390 400
VNYWDKQDHP ISRLRHYLLS QGWWDEEQEK AWRKQSRRKV MEAFEQAERK
410 420 430 440
PKPNPNLLFS DVYQEMPAQL RKQQESLARH LQTYGEHYPL DHFDK
Length:445
Mass (Da):50,471
Last modified:June 1, 1994 - v2
Checksum:i2B4DD658924DB0C3
GO
Isoform 2 (identifier: P12694-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-40: Missing.
     331-331: Y → YSSSPILPPDPHSREPTLTWGPLPLC

Note: No experimental confirmation available.
Show »
Length:448
Mass (Da):50,790
Checksum:i25C9E70619832776
GO

Sequence cautioni

The sequence AAB59549 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3V → G in AAB20222 (PubMed:2060625).Curated1
Sequence conflicti3V → G in AAB19268 (PubMed:2060625).Curated1
Sequence conflicti36S → A in AAB59549 (PubMed:2914958).Curated1
Sequence conflicti248A → D in AAA35590 (PubMed:3224821).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03436039P → H.Corresponds to variant rs34589432dbSNPEnsembl.1
Natural variantiVAR_034361151T → M.Corresponds to variant rs34442879dbSNPEnsembl.1
Natural variantiVAR_004968159R → W in MSUD1A. 1 PublicationCorresponds to variant rs769688327dbSNPEnsembl.1
Natural variantiVAR_004969190Q → K in MSUD1A. 1 Publication1
Natural variantiVAR_069748211T → M in MSUD1A. 1 PublicationCorresponds to variant rs398123503dbSNPEnsembl.1
Natural variantiVAR_069749220A → V in MSUD1A. 1 PublicationCorresponds to variant rs375785084dbSNPEnsembl.1
Natural variantiVAR_004970253A → T in MSUD1A. 1 PublicationCorresponds to variant rs199599175dbSNPEnsembl.1
Natural variantiVAR_015101290G → R in MSUD1A. 1 PublicationCorresponds to variant rs137852871dbSNPEnsembl.1
Natural variantiVAR_004971326I → T in MSUD1A. 1 Publication1
Natural variantiVAR_069750346R → C in MSUD1A. 1 PublicationCorresponds to variant rs182923857dbSNPEnsembl.1
Natural variantiVAR_069751403P → PKP in MSUD1A. 1
Natural variantiVAR_015102409F → C in MSUD1A. 1 PublicationCorresponds to variant rs137852872dbSNPEnsembl.1
Natural variantiVAR_004972413Y → C in MSUD1A. 1 Publication1
Natural variantiVAR_069752427 – 428LA → P in MSUD1A. 1 Publication2
Natural variantiVAR_004973438Y → N in MSUD1A; impedes assembly of the E1 component. 5 PublicationsCorresponds to variant rs137852870dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05615619 – 40Missing in isoform 2. 1 PublicationAdd BLAST22
Alternative sequenceiVSP_056157331Y → YSSSPILPPDPHSREPTLTW GPLPLC in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14093 mRNA. Translation: CAA78475.1.
AK298188 mRNA. Translation: BAG60459.1.
AC011462 Genomic DNA. No translation available.
BC007878 mRNA. Translation: AAH07878.1.
BC008933 mRNA. Translation: AAH08933.1.
BC023983 mRNA. Translation: AAH23983.1.
J04474 mRNA. Translation: AAB59549.1. Different initiation.
AH003771 Genomic DNA. Translation: AAB20222.2.
AH003707 Genomic DNA. Translation: AAB19268.2.
M22221 mRNA. Translation: AAA35590.1.
CCDSiCCDS12581.1. [P12694-1]
PIRiS27156. DEHUXA.
RefSeqiNP_000700.1. NM_000709.3. [P12694-1]
NP_001158255.1. NM_001164783.1.
UniGeneiHs.433307.

Genome annotation databases

EnsembliENST00000269980; ENSP00000269980; ENSG00000248098. [P12694-1]
ENST00000457836; ENSP00000416000; ENSG00000248098. [P12694-2]
GeneIDi593.
KEGGihsa:593.
UCSCiuc002oqq.4. human. [P12694-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14093 mRNA. Translation: CAA78475.1.
AK298188 mRNA. Translation: BAG60459.1.
AC011462 Genomic DNA. No translation available.
BC007878 mRNA. Translation: AAH07878.1.
BC008933 mRNA. Translation: AAH08933.1.
BC023983 mRNA. Translation: AAH23983.1.
J04474 mRNA. Translation: AAB59549.1. Different initiation.
AH003771 Genomic DNA. Translation: AAB20222.2.
AH003707 Genomic DNA. Translation: AAB19268.2.
M22221 mRNA. Translation: AAA35590.1.
CCDSiCCDS12581.1. [P12694-1]
PIRiS27156. DEHUXA.
RefSeqiNP_000700.1. NM_000709.3. [P12694-1]
NP_001158255.1. NM_001164783.1.
UniGeneiHs.433307.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DTWX-ray2.70A46-445[»]
1OLSX-ray1.85A46-445[»]
1OLUX-ray1.90A46-445[»]
1OLXX-ray2.25A46-445[»]
1U5BX-ray1.83A46-445[»]
1V11X-ray1.95A46-445[»]
1V16X-ray1.90A46-445[»]
1V1MX-ray2.00A46-445[»]
1V1RX-ray1.80A46-445[»]
1WCIX-ray1.84A46-445[»]
1X7WX-ray1.73A46-445[»]
1X7XX-ray2.10A46-445[»]
1X7YX-ray1.57A46-445[»]
1X7ZX-ray1.72A46-445[»]
1X80X-ray2.00A46-445[»]
2BEUX-ray1.89A46-445[»]
2BEVX-ray1.80A46-445[»]
2BEWX-ray1.79A46-445[»]
2BFBX-ray1.77A46-445[»]
2BFCX-ray1.64A46-445[»]
2BFDX-ray1.39A46-445[»]
2BFEX-ray1.69A46-445[»]
2BFFX-ray1.46A46-445[»]
2J9FX-ray1.88A/C46-445[»]
ProteinModelPortaliP12694.
SMRiP12694.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107065. 24 interactors.
DIPiDIP-6146N.
IntActiP12694. 8 interactors.
MINTiMINT-271818.
STRINGi9606.ENSP00000269980.

PTM databases

iPTMnetiP12694.
PhosphoSitePlusiP12694.

Polymorphism and mutation databases

BioMutaiBCKDHA.

Proteomic databases

EPDiP12694.
MaxQBiP12694.
PaxDbiP12694.
PeptideAtlasiP12694.
PRIDEiP12694.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269980; ENSP00000269980; ENSG00000248098. [P12694-1]
ENST00000457836; ENSP00000416000; ENSG00000248098. [P12694-2]
GeneIDi593.
KEGGihsa:593.
UCSCiuc002oqq.4. human. [P12694-1]

Organism-specific databases

CTDi593.
DisGeNETi593.
GeneCardsiBCKDHA.
GeneReviewsiBCKDHA.
HGNCiHGNC:986. BCKDHA.
HPAiHPA036640.
MalaCardsiBCKDHA.
MIMi248600. phenotype.
608348. gene.
neXtProtiNX_P12694.
OpenTargetsiENSG00000248098.
Orphaneti268145. Classic maple syrup urine disease.
268162. Intermediate maple syrup urine disease.
268173. Intermittent maple syrup urine disease.
268184. Thiamine-responsive maple syrup urine disease.
PharmGKBiPA25297.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1182. Eukaryota.
COG1071. LUCA.
GeneTreeiENSGT00530000063174.
HOGENOMiHOG000281337.
HOVERGENiHBG002459.
InParanoidiP12694.
KOiK00166.
OrthoDBiEOG091G073F.
PhylomeDBiP12694.
TreeFamiTF300863.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12005.
ZFISH:MONOMER-12005.
ReactomeiR-HSA-389661. Glyoxylate metabolism and glycine degradation.
R-HSA-70895. Branched-chain amino acid catabolism.
SABIO-RKP12694.
SIGNORiP12694.

Miscellaneous databases

EvolutionaryTraceiP12694.
GeneWikiiBCKDHA.
GenomeRNAii593.
PROiP12694.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000248098.
CleanExiHS_BCKDHA.
ExpressionAtlasiP12694. baseline and differential.
GenevisibleiP12694. HS.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiODBA_HUMAN
AccessioniPrimary (citable) accession number: P12694
Secondary accession number(s): B4DP47
, E7EW46, Q16034, Q16472
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: June 1, 1994
Last modified: November 30, 2016
This is version 200 of the entry and version 2 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

Bound potassium ions stabilize the protein structure.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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

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.