Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

DLAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

Catalytic activityi

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateNote: Binds 2 lipoyl cofactors covalently.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei620 – 6201Sequence Analysis
Active sitei624 – 6241Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB

GO - Biological processi

  1. cellular metabolic process Source: Reactome
  2. glucose metabolic process Source: UniProtKB-KW
  3. pyruvate metabolic process Source: Reactome
  4. regulation of acetyl-CoA biosynthetic process from pyruvate Source: Reactome
  5. small molecule metabolic process Source: Reactome
  6. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciMetaCyc:HS07688-MONOMER.
BRENDAi2.3.1.12. 2681.
ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_2071. Pyruvate metabolism.
REACT_267785. Signaling by Retinoic Acid.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
Alternative name(s):
70 kDa mitochondrial autoantigen of primary biliary cirrhosis
Short name:
PBC
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
M2 antigen complex 70 kDa subunit
Pyruvate dehydrogenase complex component E2
Short name:
PDC-E2
Short name:
PDCE2
Gene namesi
Name:DLAT
Synonyms:DLTA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:2896. DLAT.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrial pyruvate dehydrogenase complex Source: UniProtKB
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Primary biliary cirrhosis is a chronic, progressive cholestatic liver disease characterized by the presence of antimitochondrial autoantibodies in patients' serum. It manifests with inflammatory obliteration of intra-hepatic bile duct, leading to liver cell damage and cirrhosis. Patients with primary biliary cirrhosis show autoantibodies against the E2 component of pyruvate dehydrogenase complex.

Pyruvate dehydrogenase E2 deficiency (PDHE2 deficiency)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionPyruvate dehydrogenase (PDH) deficiency is a major cause of primary lactic acidosis and neurological dysfunction in infancy and early childhood. In this form of PDH deficiency episodic dystonia is the major neurological manifestation, with other more common features of pyruvate dehydrogenase deficiency, such as hypotonia and ataxia, being less prominent.

See also OMIM:245348

Organism-specific databases

MIMi245348. phenotype.
Orphaneti79244. Pyruvate dehydrogenase E2 deficiency.
PharmGKBiPA27350.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8686MitochondrionAdd
BLAST
Chaini87 – 647561Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000020479Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei132 – 1321N6-lipoyllysinePROSITE-ProRule annotation1 Publication
Modified residuei259 – 2591N6-lipoyllysinePROSITE-ProRule annotation1 Publication
Modified residuei466 – 4661N6-acetyllysine1 Publication
Modified residuei473 – 4731N6-succinyllysineBy similarity
Modified residuei547 – 5471N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP10515.
PaxDbiP10515.
PRIDEiP10515.

PTM databases

PhosphoSiteiP10515.

Expressioni

Gene expression databases

BgeeiP10515.
CleanExiHS_DLAT.
ExpressionAtlasiP10515. baseline and differential.
GenevestigatoriP10515.

Organism-specific databases

HPAiCAB003782.
HPA040786.

Interactioni

Subunit structurei

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. Interacts with PDK2 and PDK3.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDHBP111777EBI-2959723,EBI-1035872

Protein-protein interaction databases

BioGridi108081. 26 interactions.
DIPiDIP-29496N.
IntActiP10515. 8 interactions.
MINTiMINT-3007324.
STRINGi9606.ENSP00000280346.

Structurei

Secondary structure

1
647
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi92 – 954Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi105 – 1106Combined sources
Beta strandi123 – 1297Combined sources
Beta strandi134 – 1385Combined sources
Beta strandi140 – 1478Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi162 – 1687Combined sources
Helixi170 – 1778Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi218 – 2225Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi232 – 2387Combined sources
Beta strandi251 – 2566Combined sources
Beta strandi261 – 2655Combined sources
Beta strandi270 – 2778Combined sources
Beta strandi283 – 2853Combined sources
Beta strandi289 – 2979Combined sources
Helixi301 – 3033Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FYCNMR-A212-315[»]
1Y8NX-ray2.60B212-319[»]
1Y8OX-ray2.48B212-319[»]
1Y8PX-ray2.63B212-319[»]
2DNENMR-A92-186[»]
2PNRX-ray2.50C/G212-319[»]
2Q8IX-ray2.60B212-319[»]
3B8Kelectron microscopy8.80A409-647[»]
3CRKX-ray2.30C/D214-300[»]
3CRLX-ray2.61C/D214-300[»]
ProteinModelPortaliP10515.
SMRiP10515. Positions 92-182, 214-306, 355-398, 409-647.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10515.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 16777Lipoyl-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini218 – 29477Lipoyl-binding 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni358 – 38932E3-binding siteBy similarityAdd
BLAST
Regioni417 – 647231CatalyticBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 2 lipoyl-binding domains.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
HOVERGENiHBG005063.
InParanoidiP10515.
KOiK00627.
OMAiATMEFES.
PhylomeDBiP10515.
TreeFamiTF106145.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10515-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWRVCARRAQ NVAPWAGLEA RWTALQEVPG TPRVTSRSGP APARRNSVTT
60 70 80 90 100
GYGGVRALCG WTPSSGATPR NRLLLQLLGS PGRRYYSLPP HQKVPLPSLS
110 120 130 140 150
PTMQAGTIAR WEKKEGDKIN EGDLIAEVET DKATVGFESL EECYMAKILV
160 170 180 190 200
AEGTRDVPIG AIICITVGKP EDIEAFKNYT LDSSAAPTPQ AAPAPTPAAT
210 220 230 240 250
ASPPTPSAQA PGSSYPPHMQ VLLPALSPTM TMGTVQRWEK KVGEKLSEGD
260 270 280 290 300
LLAEIETDKA TIGFEVQEEG YLAKILVPEG TRDVPLGTPL CIIVEKEADI
310 320 330 340 350
SAFADYRPTE VTDLKPQVPP PTPPPVAAVP PTPQPLAPTP SAPCPATPAG
360 370 380 390 400
PKGRVFVSPL AKKLAVEKGI DLTQVKGTGP DGRITKKDID SFVPSKVAPA
410 420 430 440 450
PAAVVPPTGP GMAPVPTGVF TDIPISNIRR VIAQRLMQSK QTIPHYYLSI
460 470 480 490 500
DVNMGEVLLV RKELNKILEG RSKISVNDFI IKASALACLK VPEANSSWMD
510 520 530 540 550
TVIRQNHVVD VSVAVSTPAG LITPIVFNAH IKGVETIAND VVSLATKARE
560 570 580 590 600
GKLQPHEFQG GTFTISNLGM FGIKNFSAII NPPQACILAI GASEDKLVPA
610 620 630 640
DNEKGFDVAS MMSVTLSCDH RVVDGAVGAQ WLAEFRKYLE KPITMLL
Length:647
Mass (Da):68,997
Last modified:November 24, 2008 - v3
Checksum:iDD93A8E666E377C2
GO

Sequence cautioni

The sequence AAA62253.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence AAA62253.1 differs from that shown. Reason: Frameshift at positions 449, 451 and 455. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121E → K in CAA68787 (PubMed:3191998).Curated
Sequence conflicti342 – 3421A → T in AAA62253 (PubMed:3174635).Curated
Sequence conflicti358 – 3581S → D in AAA62253 (PubMed:3174635).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431A → V.1 Publication
Corresponds to variant rs2303436 [ dbSNP | Ensembl ].
VAR_047410
Natural varianti98 – 981S → F.
Corresponds to variant rs537057 [ dbSNP | Ensembl ].
VAR_047411
Natural varianti99 – 991L → F.
Corresponds to variant rs537060 [ dbSNP | Ensembl ].
VAR_047412
Natural varianti209 – 2091Q → R.
Corresponds to variant rs11553595 [ dbSNP | Ensembl ].
VAR_047413
Natural varianti313 – 3131D → V.
Corresponds to variant rs11553592 [ dbSNP | Ensembl ].
VAR_047414
Natural varianti318 – 3181V → A.1 Publication
Corresponds to variant rs627441 [ dbSNP | Ensembl ].
VAR_047415
Natural varianti451 – 4511D → N.1 Publication
Corresponds to variant rs10891314 [ dbSNP | Ensembl ].
VAR_047416

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK223596 mRNA. Translation: BAD97316.1.
AP000907 Genomic DNA. No translation available.
J03866 mRNA. Translation: AAA62253.1. Sequence problems.
Y00978 mRNA. Translation: CAA68787.1.
CCDSiCCDS8354.1.
PIRiA40497.
RefSeqiNP_001922.2. NM_001931.4.
UniGeneiHs.335551.

Genome annotation databases

EnsembliENST00000280346; ENSP00000280346; ENSG00000150768.
GeneIDi1737.
KEGGihsa:1737.
UCSCiuc001pmo.3. human.

Polymorphism databases

DMDMi215274207.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK223596 mRNA. Translation: BAD97316.1.
AP000907 Genomic DNA. No translation available.
J03866 mRNA. Translation: AAA62253.1. Sequence problems.
Y00978 mRNA. Translation: CAA68787.1.
CCDSiCCDS8354.1.
PIRiA40497.
RefSeqiNP_001922.2. NM_001931.4.
UniGeneiHs.335551.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FYCNMR-A212-315[»]
1Y8NX-ray2.60B212-319[»]
1Y8OX-ray2.48B212-319[»]
1Y8PX-ray2.63B212-319[»]
2DNENMR-A92-186[»]
2PNRX-ray2.50C/G212-319[»]
2Q8IX-ray2.60B212-319[»]
3B8Kelectron microscopy8.80A409-647[»]
3CRKX-ray2.30C/D214-300[»]
3CRLX-ray2.61C/D214-300[»]
ProteinModelPortaliP10515.
SMRiP10515. Positions 92-182, 214-306, 355-398, 409-647.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108081. 26 interactions.
DIPiDIP-29496N.
IntActiP10515. 8 interactions.
MINTiMINT-3007324.
STRINGi9606.ENSP00000280346.

PTM databases

PhosphoSiteiP10515.

Polymorphism databases

DMDMi215274207.

Proteomic databases

MaxQBiP10515.
PaxDbiP10515.
PRIDEiP10515.

Protocols and materials databases

DNASUi1737.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000280346; ENSP00000280346; ENSG00000150768.
GeneIDi1737.
KEGGihsa:1737.
UCSCiuc001pmo.3. human.

Organism-specific databases

CTDi1737.
GeneCardsiGC11P111895.
HGNCiHGNC:2896. DLAT.
HPAiCAB003782.
HPA040786.
MIMi245348. phenotype.
608770. gene.
neXtProtiNX_P10515.
Orphaneti79244. Pyruvate dehydrogenase E2 deficiency.
PharmGKBiPA27350.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
HOVERGENiHBG005063.
InParanoidiP10515.
KOiK00627.
OMAiATMEFES.
PhylomeDBiP10515.
TreeFamiTF106145.

Enzyme and pathway databases

BioCyciMetaCyc:HS07688-MONOMER.
BRENDAi2.3.1.12. 2681.
ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_2071. Pyruvate metabolism.
REACT_267785. Signaling by Retinoic Acid.

Miscellaneous databases

ChiTaRSiDLAT. human.
EvolutionaryTraceiP10515.
GeneWikiiDihydrolipoyl_transacetylase.
GenomeRNAii1737.
NextBioi7043.
PROiP10515.
SOURCEiSearch...

Gene expression databases

BgeeiP10515.
CleanExiHS_DLAT.
ExpressionAtlasiP10515. baseline and differential.
GenevestigatoriP10515.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-43; ALA-318 AND ASN-451.
    Tissue: Kidney.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Primary structure of the human M2 mitochondrial autoantigen of primary biliary cirrhosis: dihydrolipoamide acetyltransferase."
    Coppel R.L., McNeilage L.J., Surh C.D., van de Water J., Spithill T.W., Whittingham S., Gershwin M.E.
    Proc. Natl. Acad. Sci. U.S.A. 85:7317-7321(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-647.
    Tissue: Placenta.
  4. "Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex."
    Thekkumkara T.J., Ho L., Wexler I.D., Pon G., Liu T., Patel M.S.
    FEBS Lett. 240:45-48(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 73-647, LIPOYLATION AT LYS-132 AND LYS-259.
    Tissue: Liver.
  5. "Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components."
    Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.
    J. Biol. Chem. 279:6921-6933(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-466, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Three-dimensional structure of the major autoantigen in primary biliary cirrhosis."
    Howard M.J., Fuller C., Broadhurst R.W., Perham R.N., Tang J.G., Quinn J., Diamond A.G., Yeaman S.J.
    Gastroenterology 115:139-146(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 214-315.
  9. "Clinical and genetic spectrum of pyruvate dehydrogenase deficiency: dihydrolipoamide acetyltransferase (E2) deficiency."
    Head R.A., Brown R.M., Zolkipli Z., Shahdadpuri R., King M.D., Clayton P.T., Brown G.K.
    Ann. Neurol. 58:234-241(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PDHE2 DEFICIENCY.
  10. "Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex."
    Kato M., Chuang J.L., Tso S.C., Wynn R.M., Chuang D.T.
    EMBO J. 24:1763-1774(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 212-319 IN COMPLEX WITH PDK3.
  11. "Solution structure of RSGI RUH-058, a lipoyl domain of human 2-oxoacid dehydrogenase."
    RIKEN structural genomics initiative (RSGI)
    Submitted (SEP-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 92-186.
  12. "Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications."
    Devedjiev Y., Steussy C.N., Vassylyev D.G.
    J. Mol. Biol. 370:407-416(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 212-319 IN COMPLEX WITH PDK3.
  13. "Distinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicol."
    Kato M., Li J., Chuang J.L., Chuang D.T.
    Structure 15:992-1004(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 212-319 IN COMPLEX WITH PDK3.
  14. "Structural and functional insights into the molecular mechanisms responsible for the regulation of pyruvate dehydrogenase kinase 2."
    Green T., Grigorian A., Klyuyeva A., Tuganova A., Luo M., Popov K.M.
    J. Biol. Chem. 283:15789-15798(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 214-300 IN COMPLEX WITH PDK2.

Entry informationi

Entry nameiODP2_HUMAN
AccessioniPrimary (citable) accession number: P10515
Secondary accession number(s): Q16783, Q53EP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 30, 1989
Last sequence update: November 24, 2008
Last modified: March 31, 2015
This is version 183 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

External Data

Dasty 3

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 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.