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Protein

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Gene

PDHA1

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

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle.2 Publications

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.3 Publications

Cofactori

thiamine diphosphate2 Publications

Activity regulationi

Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation.3 Publications

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processCarbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle
LigandPyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS05573-MONOMER
BRENDAi1.2.4.1 2681
ReactomeiR-HSA-204174 Regulation of pyruvate dehydrogenase (PDH) complex
R-HSA-389661 Glyoxylate metabolism and glycine degradation
R-HSA-5362517 Signaling by Retinoic Acid
R-HSA-70268 Pyruvate metabolism
SABIO-RKiP08559
SIGNORiP08559

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (EC:1.2.4.1)
Alternative name(s):
PDHE1-A type I
Gene namesi
Name:PDHA1
Synonyms:PHE1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

EuPathDBiHostDB:ENSG00000131828.13
HGNCiHGNC:8806 PDHA1
MIMi300502 gene
neXtProtiNX_P08559

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

Pyruvate dehydrogenase E1-alpha deficiency (PDHAD)18 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.
See also OMIM:312170
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01023810R → P in PDHAD; affects mitochondrial import of precursor protein. 1 PublicationCorresponds to variant dbSNP:rs137853257EnsemblClinVar.1
Natural variantiVAR_00494972R → C in PDHAD. 2 PublicationsCorresponds to variant dbSNP:rs863224148EnsemblClinVar.1
Natural variantiVAR_004950113H → D in PDHAD. 1 Publication1
Natural variantiVAR_004951162G → R in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs866868610Ensembl.1
Natural variantiVAR_004952167V → M in PDHAD. 1 Publication1
Natural variantiVAR_004953199A → T in PDHAD. 1 Publication1
Natural variantiVAR_004954205F → L in PDHAD. 2 PublicationsCorresponds to variant dbSNP:rs137853254EnsemblClinVar.1
Natural variantiVAR_004955210M → V in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs794727843EnsemblClinVar.1
Natural variantiVAR_004956217P → L in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs1131691792Ensembl.1
Natural variantiVAR_004957231T → A in PDHAD. 1 Publication1
Natural variantiVAR_021053243Y → N in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs137853255EnsemblClinVar.1
Natural variantiVAR_004958258D → A in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs137853253EnsemblClinVar.1
Natural variantiVAR_004959263R → G in PDHAD. 4 PublicationsCorresponds to variant dbSNP:rs137853259EnsemblClinVar.1
Natural variantiVAR_004960263R → Q in PDHAD. 1 Publication1
Natural variantiVAR_021055288R → H in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs137853258EnsemblClinVar.1
Natural variantiVAR_004961292H → L in PDHAD. 1 Publication1
Natural variantiVAR_004962302R → C in PDHAD; loss of activity; common mutation. 4 PublicationsCorresponds to variant dbSNP:rs137853252EnsemblClinVar.1
Natural variantiVAR_004963302R → H in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs1064794149Ensembl.1
Natural variantiVAR_020908305E → EDSYRTRE in PDHAD. 1 Publication1
Natural variantiVAR_020909307I → IPPHSYRTREEI in PDHAD. 1 Publication1
Natural variantiVAR_004964311Missing in PDHAD. 2 Publications1
Natural variantiVAR_004965313Missing in PDHAD. 1 Publication1
Natural variantiVAR_021056315D → N in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs137853256EnsemblClinVar.1
Natural variantiVAR_004966378R → H in PDHAD. 3 PublicationsCorresponds to variant dbSNP:rs137853250Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi232S → A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300. 1 Publication1
Mutagenesisi293S → A: Reduces enzyme activity. Abolishes inactivation by phosphorylation; when associated with A-232 and A-300. 2 Publications1
Mutagenesisi293S → E: Interferes with substrate binding. 2 Publications1
Mutagenesisi300S → A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293. 1 Publication1

Keywords - Diseasei

Disease mutation, Leigh syndrome, Primary mitochondrial disease

Organism-specific databases

DisGeNETi5160
MalaCardsiPDHA1
MIMi312170 phenotype
OpenTargetsiENSG00000131828
Orphaneti70474 Leigh syndrome with cardiomyopathy
79243 Pyruvate dehydrogenase E1-alpha deficiency
PharmGKBiPA33150

Chemistry databases

DrugBankiDB00157 NADH

Polymorphism and mutation databases

BioMutaiPDHA1
DMDMi129063

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 30Mitochondrion1 PublicationAdd BLAST30
ChainiPRO_000002044031 – 390Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrialAdd BLAST360

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei63N6-acetyllysine; alternateBy similarity1
Modified residuei63N6-succinyllysine; alternateBy similarity1
Modified residuei232Phosphoserine; by PDK1Combined sources1 Publication1
Modified residuei244N6-acetyllysine; alternateBy similarity1
Modified residuei244N6-succinyllysine; alternateBy similarity1
Modified residuei277N6-succinyllysineBy similarity1
Modified residuei293Phosphoserine; by PDK1, PDK2, PDK3 and PDK43 Publications1
Modified residuei295PhosphoserineBy similarity1
Modified residuei300Phosphoserine; by PDK1, PDK2, PDK3 and PDK42 Publications1
Modified residuei301PhosphotyrosineBy similarity1
Modified residuei313N6-acetyllysine; alternateBy similarity1
Modified residuei313N6-succinyllysine; alternateBy similarity1
Modified residuei321N6-acetyllysineCombined sources1
Modified residuei336N6-acetyllysineBy similarity1
Modified residuei385N6-succinyllysineBy similarity1

Post-translational modificationi

Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation.3 Publications
Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP08559
MaxQBiP08559
PeptideAtlasiP08559
PRIDEiP08559
ProteomicsDBi52117
52118 [P08559-2]
52119 [P08559-3]
52120 [P08559-4]
TopDownProteomicsiP08559-3 [P08559-3]
P08559-4 [P08559-4]

2D gel databases

REPRODUCTION-2DPAGEiIPI00306301
UCD-2DPAGEiP08559

PTM databases

iPTMnetiP08559
PhosphoSitePlusiP08559
SwissPalmiP08559

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000131828 Expressed in 232 organ(s), highest expression level in heart left ventricle
CleanExiHS_PDHA1
ExpressionAtlasiP08559 baseline and differential
GenevisibleiP08559 HS

Organism-specific databases

HPAiHPA047487
HPA047864
HPA063053

Interactioni

Subunit structurei

Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules.3 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi111186, 307 interactors
ComplexPortaliCPX-376 Pyruvate dehydrogenase E1 heterotetramer
CORUMiP08559
DIPiDIP-37652N
IntActiP08559, 259 interactors
MINTiP08559

Structurei

Secondary structure

1390
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP08559
SMRiP08559
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08559

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00530000063174
HOGENOMiHOG000281336
HOVERGENiHBG001863
InParanoidiP08559
KOiK00161
OMAiRRFEDKC
OrthoDBiEOG091G0966
PhylomeDBiP08559
TreeFamiTF300742

Family and domain databases

InterProiView protein in InterPro
IPR001017 DH_E1
IPR017597 Pyrv_DH_E1_asu_subgrp-y
IPR029061 THDP-binding
PfamiView protein in Pfam
PF00676 E1_dh, 1 hit
SUPFAMiSSF52518 SSF52518, 1 hit
TIGRFAMsiTIGR03182 PDH_E1_alph_y, 1 hit

Sequences (4+)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 5 potential isoforms that are computationally mapped.iShow all

Isoform 1 (identifier: P08559-1) [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
MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP
60 70 80 90 100
PVTTVLTRED GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC
110 120 130 140 150
CVGLEAGINP TDHLITAYRA HGFTFTRGLS VREILAELTG RKGGCAKGKG
160 170 180 190 200
GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA CKYNGKDEVC LTLYGDGAAN
210 220 230 240 250
QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST DYYKRGDFIP
260 270 280 290 300
GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS
310 320 330 340 350
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA
360 370 380 390
QFATADPEPP LEELGYHIYS SDPPFEVRGA NQWIKFKSVS
Length:390
Mass (Da):43,296
Last modified:May 1, 1992 - v3
Checksum:i4D685BBE44A92D4B
GO
Isoform 2 (identifier: P08559-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     96-96: G → GQFLLPLT

Note: No experimental confirmation available.
Show »
Length:397
Mass (Da):44,109
Checksum:i4BE156001F9994A5
GO
Isoform 3 (identifier: P08559-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     170-200: Missing.

Note: No experimental confirmation available.
Show »
Length:359
Mass (Da):40,188
Checksum:i7E94F39FC1293065
GO
Isoform 4 (identifier: P08559-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: P → PRHGLATLPSLVSISRLKQSSHLGLPKCWDYSHSLKTRQ

Show »
Length:428
Mass (Da):47,580
Checksum:i14FE765CFF2C7120
GO

Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5JPU1Q5JPU1_HUMAN
Pyruvate dehydrogenase E1 component...
PDHA1
205Annotation score:
Q5JPU0Q5JPU0_HUMAN
Pyruvate dehydrogenase E1 component...
PDHA1
180Annotation score:
Q5JPT9Q5JPT9_HUMAN
Pyruvate dehydrogenase E1 component...
PDHA1
203Annotation score:
Q5JPU2Q5JPU2_HUMAN
Pyruvate dehydrogenase E1 component...
PDHA1
121Annotation score:
Q5JPU3Q5JPU3_HUMAN
Pyruvate dehydrogenase E1 component...
PDHA1
109Annotation score:

Sequence cautioni

The sequence AAA60055 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB59581 differs from that shown. Reason: Frameshift at positions 106 and 175.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti278G → E in BAG35194 (PubMed:14702039).Curated1
Sequence conflicti301Y → S in AAD23857 (PubMed:10077682).Curated1
Sequence conflicti306E → D in AAD23857 (PubMed:10077682).Curated1
Sequence conflicti349A → P in AAA60055 (PubMed:2828359).Curated1
Sequence conflicti354T → A in AAA60055 (PubMed:2828359).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01023810R → P in PDHAD; affects mitochondrial import of precursor protein. 1 PublicationCorresponds to variant dbSNP:rs137853257EnsemblClinVar.1
Natural variantiVAR_00494972R → C in PDHAD. 2 PublicationsCorresponds to variant dbSNP:rs863224148EnsemblClinVar.1
Natural variantiVAR_004950113H → D in PDHAD. 1 Publication1
Natural variantiVAR_069381136A → T Probable disease-associated mutation found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate. 1 PublicationCorresponds to variant dbSNP:rs138727886EnsemblClinVar.1
Natural variantiVAR_004951162G → R in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs866868610Ensembl.1
Natural variantiVAR_004952167V → M in PDHAD. 1 Publication1
Natural variantiVAR_004953199A → T in PDHAD. 1 Publication1
Natural variantiVAR_004954205F → L in PDHAD. 2 PublicationsCorresponds to variant dbSNP:rs137853254EnsemblClinVar.1
Natural variantiVAR_004955210M → V in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs794727843EnsemblClinVar.1
Natural variantiVAR_004956217P → L in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs1131691792Ensembl.1
Natural variantiVAR_004957231T → A in PDHAD. 1 Publication1
Natural variantiVAR_021053243Y → N in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs137853255EnsemblClinVar.1
Natural variantiVAR_004958258D → A in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs137853253EnsemblClinVar.1
Natural variantiVAR_004959263R → G in PDHAD. 4 PublicationsCorresponds to variant dbSNP:rs137853259EnsemblClinVar.1
Natural variantiVAR_004960263R → Q in PDHAD. 1 Publication1
Natural variantiVAR_021054282M → L3 PublicationsCorresponds to variant dbSNP:rs2229137EnsemblClinVar.1
Natural variantiVAR_021055288R → H in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs137853258EnsemblClinVar.1
Natural variantiVAR_004961292H → L in PDHAD. 1 Publication1
Natural variantiVAR_004962302R → C in PDHAD; loss of activity; common mutation. 4 PublicationsCorresponds to variant dbSNP:rs137853252EnsemblClinVar.1
Natural variantiVAR_004963302R → H in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs1064794149Ensembl.1
Natural variantiVAR_020908305E → EDSYRTRE in PDHAD. 1 Publication1
Natural variantiVAR_020909307I → IPPHSYRTREEI in PDHAD. 1 Publication1
Natural variantiVAR_004964311Missing in PDHAD. 2 Publications1
Natural variantiVAR_004965313Missing in PDHAD. 1 Publication1
Natural variantiVAR_021056315D → N in PDHAD. 1 PublicationCorresponds to variant dbSNP:rs137853256EnsemblClinVar.1
Natural variantiVAR_050436333E → D. Corresponds to variant dbSNP:rs2228067EnsemblClinVar.1
Natural variantiVAR_004966378R → H in PDHAD. 3 PublicationsCorresponds to variant dbSNP:rs137853250Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04336319P → PRHGLATLPSLVSISRLKQS SHLGLPKCWDYSHSLKTRQ in isoform 4. 2 Publications1
Alternative sequenceiVSP_04256996G → GQFLLPLT in isoform 2. 1 Publication1
Alternative sequenceiVSP_042570170 – 200Missing in isoform 3. 1 PublicationAdd BLAST31

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90084 Genomic DNA Translation: BAA14121.1
M24848 mRNA Translation: AAA36533.1
X52709 mRNA Translation: CAA36933.1
X52710 mRNA Translation: CAA36934.1
M27257
, M29155, M29156, M29157, M29158, M29159, M29160, M29161, M29162, M29163, M29164 Genomic DNA Translation: AAA60051.1
L13318 mRNA Translation: AAA60227.1
J03503 mRNA Translation: AAA60055.1 Different initiation.
J03575 mRNA Translation: AAA60050.1
L48690 mRNA Translation: AAB59581.1 Frameshift.
EF590117 mRNA Translation: ABQ59099.1
AK293250 mRNA Translation: BAH11476.1
AK296457 mRNA Translation: BAH12361.1
AK312263 mRNA Translation: BAG35194.1
AK296341 mRNA Translation: BAH12323.1
AK222740 mRNA Translation: BAD96460.1
AL732326 Genomic DNA No translation available.
CH471074 Genomic DNA Translation: EAW98960.1
BC002406 mRNA Translation: AAH02406.1
AF125053 Genomic DNA Translation: AAD23841.1
AF125054 Genomic DNA Translation: AAD23842.1
AF125055 Genomic DNA Translation: AAD23843.1
AF125056 Genomic DNA Translation: AAD23844.1
AF125057 Genomic DNA Translation: AAD23845.1
AF125058 Genomic DNA Translation: AAD23846.1
AF125059 Genomic DNA Translation: AAD23847.1
AF125060 Genomic DNA Translation: AAD23848.1
AF125061 Genomic DNA Translation: AAD23849.1
AF125062 Genomic DNA Translation: AAD23850.1
AF125063 Genomic DNA Translation: AAD23851.1
AF125064 Genomic DNA Translation: AAD23852.1
AF125065 Genomic DNA Translation: AAD23853.1
AF125066 Genomic DNA Translation: AAD23854.1
AF125067 Genomic DNA Translation: AAD23855.1
AF125068 Genomic DNA Translation: AAD23856.1
AF125069 Genomic DNA Translation: AAD23857.1
AF125070 Genomic DNA Translation: AAD23858.1
AF125071 Genomic DNA Translation: AAD23859.1
AF125072 Genomic DNA Translation: AAD23860.1
AF125073 Genomic DNA Translation: AAD23861.1
AF125074 Genomic DNA Translation: AAD23862.1
AF125075 Genomic DNA Translation: AAD23863.1
AF125076 Genomic DNA Translation: AAD23864.1
AF125078 Genomic DNA Translation: AAD23866.1
AF125079 Genomic DNA Translation: AAD23867.1
AF125080 Genomic DNA Translation: AAD23868.1
AF125081 Genomic DNA Translation: AAD23869.1
AF125082 Genomic DNA Translation: AAD23870.1
AF125083 Genomic DNA Translation: AAD23871.1
AF125084 Genomic DNA Translation: AAD23872.1
AF125085 Genomic DNA Translation: AAD23873.1
AF125086 Genomic DNA Translation: AAD23874.1
AF125087 Genomic DNA Translation: AAD23875.1
AF125088 Genomic DNA Translation: AAD23876.1
CCDSiCCDS14192.1 [P08559-1]
CCDS55380.1 [P08559-4]
CCDS55381.1 [P08559-2]
CCDS55382.1 [P08559-3]
PIRiJQ0770 DEHUPA
RefSeqiNP_000275.1, NM_000284.3 [P08559-1]
NP_001166925.1, NM_001173454.1 [P08559-4]
NP_001166926.1, NM_001173455.1 [P08559-2]
NP_001166927.1, NM_001173456.1 [P08559-3]
UniGeneiHs.530331

Genome annotation databases

EnsembliENST00000379806; ENSP00000369134; ENSG00000131828 [P08559-4]
ENST00000422285; ENSP00000394382; ENSG00000131828 [P08559-1]
ENST00000540249; ENSP00000440761; ENSG00000131828 [P08559-3]
ENST00000545074; ENSP00000438550; ENSG00000131828 [P08559-2]
GeneIDi5160
KEGGihsa:5160
UCSCiuc004czg.5 human [P08559-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiODPA_HUMAN
AccessioniPrimary (citable) accession number: P08559
Secondary accession number(s): A5YVE9
, B2R5P7, B7Z3T7, B7Z3X5, Q53H41, Q5JPT8, Q9NP12, Q9UBJ8, Q9UBU0, Q9UNG4, Q9UNG5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 1, 1992
Last modified: September 12, 2018
This is version 223 of the entry and version 3 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
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Main funding by: National Institutes of Health

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