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P55084

- ECHB_HUMAN

UniProt

P55084 - ECHB_HUMAN

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Protein

Trifunctional enzyme subunit beta, mitochondrial

Gene
HADHB, MSTP029
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei138 – 1381Acyl-thioester intermediate By similarity
Active sitei428 – 4281Proton acceptor By similarity
Active sitei458 – 4581Proton acceptor By similarity

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: ProtInc
  2. acetyl-CoA C-acyltransferase activity Source: ProtInc
  3. enoyl-CoA hydratase activity Source: ProtInc
  4. fatty-acyl-CoA binding Source: Ensembl
  5. long-chain-3-hydroxyacyl-CoA dehydrogenase activity Source: Ensembl
  6. long-chain-enoyl-CoA hydratase activity Source: Ensembl
  7. NAD binding Source: Ensembl
  8. poly(A) RNA binding Source: UniProtKB
  9. protein binding Source: UniProtKB

GO - Biological processi

  1. cardiolipin acyl-chain remodeling Source: Reactome
  2. cellular lipid metabolic process Source: Reactome
  3. fatty acid beta-oxidation Source: Reactome
  4. glycerophospholipid biosynthetic process Source: Reactome
  5. phospholipid metabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS06436-MONOMER.
ReactomeiREACT_121006. Acyl chain remodeling of CL.
REACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
REACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_2025. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
REACT_2108. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Trifunctional enzyme subunit beta, mitochondrial
Alternative name(s):
TP-beta
Including the following 1 domains:
3-ketoacyl-CoA thiolase (EC:2.3.1.16)
Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Gene namesi
Name:HADHB
ORF Names:MSTP029
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:4803. HADHB.

Subcellular locationi

Mitochondrion. Mitochondrion inner membrane. Mitochondrion outer membrane. Endoplasmic reticulum 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. mitochondrial envelope Source: ProtInc
  4. mitochondrial fatty acid beta-oxidation multienzyme complex Source: Ensembl
  5. mitochondrial inner membrane Source: UniProtKB
  6. mitochondrial nucleoid Source: BHF-UCL
  7. mitochondrial outer membrane Source: UniProtKB
  8. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion outer membrane

Pathology & Biotechi

Involvement in diseasei

Trifunctional protein deficiency (TFP deficiency) [MIM:609015]: The clinical manifestations are very variable and include hypoglycemia, cardiomyopathy and sudden death. Phenotypes with mainly hepatic and neuromyopathic involvement can also be distinguished. Biochemically, TFP deficiency is defined by the loss of all three enzyme activities of the TFP complex.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591G → D in TFP deficiency. 1 Publication
VAR_021128
Natural varianti61 – 611R → C in TFP deficiency. 1 Publication
VAR_021129
Natural varianti61 – 611R → H in TFP deficiency. 2 Publications
VAR_007493
Natural varianti117 – 1171R → G in TFP deficiency. 1 Publication
VAR_021130
Natural varianti121 – 1211L → P in TFP deficiency. 1 Publication
VAR_021131
Natural varianti133 – 1331T → P in TFP deficiency. 1 Publication
VAR_021132
Natural varianti242 – 2421D → G in TFP deficiency. 1 Publication
VAR_021133
Natural varianti247 – 2471R → H in TFP deficiency. 2 Publications
VAR_007494
Natural varianti259 – 27012Missing in TFP deficiency.
VAR_021134Add
BLAST
Natural varianti263 – 2631D → G in TFP deficiency. 2 Publications
VAR_007495
Natural varianti280 – 2801G → D in TFP deficiency. 1 Publication
VAR_021135
Natural varianti294 – 2941P → L in TFP deficiency. 1 Publication
VAR_021136
Natural varianti294 – 2941P → R in TFP deficiency. 1 Publication
VAR_021137
Natural varianti301 – 3011G → S in TFP deficiency. 1 Publication
VAR_021138
Natural varianti444 – 4441R → K in TFP deficiency. 2 Publications
VAR_017409

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi609015. phenotype.
Orphaneti746. Mitochondrial trifunctional protein deficiency.
PharmGKBiPA29177.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333Mitochondrion1 PublicationAdd
BLAST
Chaini34 – 474441Trifunctional enzyme subunit beta, mitochondrialPRO_0000034080Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721N6-acetyllysine; alternate1 Publication
Modified residuei72 – 721N6-succinyllysine; alternate By similarity
Modified residuei188 – 1881N6-acetyllysine; alternate1 Publication
Modified residuei188 – 1881N6-succinyllysine; alternate By similarity
Modified residuei190 – 1901N6-succinyllysine By similarity
Modified residuei272 – 2721N6-succinyllysine By similarity
Modified residuei291 – 2911N6-succinyllysine By similarity
Modified residuei293 – 2931N6-acetyllysine; alternate By similarity
Modified residuei293 – 2931N6-succinyllysine; alternate By similarity
Modified residuei298 – 2981N6-acetyllysine By similarity
Modified residuei332 – 3321N6-acetyllysine; alternate By similarity
Modified residuei332 – 3321N6-succinyllysine; alternate By similarity
Modified residuei348 – 3481N6-acetyllysine By similarity
Modified residuei361 – 3611N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP55084.
PaxDbiP55084.
PRIDEiP55084.

2D gel databases

UCD-2DPAGEP55084.

PTM databases

PhosphoSiteiP55084.

Expressioni

Gene expression databases

ArrayExpressiP55084.
BgeeiP55084.
CleanExiHS_HADHB.
GenevestigatoriP55084.

Organism-specific databases

HPAiHPA037539.

Interactioni

Subunit structurei

Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits. Interacts with RSAD2/viperin.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GABARAPL1Q9H0R84EBI-356635,EBI-746969

Protein-protein interaction databases

BioGridi109282. 41 interactions.
IntActiP55084. 33 interactions.
MINTiMINT-1154861.
STRINGi9606.ENSP00000325136.

Structurei

3D structure databases

ProteinModelPortaliP55084.
SMRiP55084. Positions 56-471.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0183.
HOGENOMiHOG000012240.
HOVERGENiHBG104782.
InParanoidiP55084.
KOiK07509.
OMAiMHNISRE.
PhylomeDBiP55084.
TreeFamiTF315243.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

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. Align

Isoform 1 (identifier: P55084-1) [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

MTILTYPFKN LPTASKWALR FSIRPLSCSS QLRAAPAVQT KTKKTLAKPN    50
IRNVVVVDGV RTPFLLSGTS YKDLMPHDLA RAALTGLLHR TSVPKEVVDY 100
IIFGTVIQEV KTSNVAREAA LGAGFSDKTP AHTVTMACIS ANQAMTTGVG 150
LIASGQCDVI VAGGVELMSD VPIRHSRKMR KLMLDLNKAK SMGQRLSLIS 200
KFRFNFLAPE LPAVSEFSTS ETMGHSADRL AAAFAVSRLE QDEYALRSHS 250
LAKKAQDEGL LSDVVPFKVP GKDTVTKDNG IRPSSLEQMA KLKPAFIKPY 300
GTVTAANSSF LTDGASAMLI MAEEKALAMG YKPKAYLRDF MYVSQDPKDQ 350
LLLGPTYATP KVLEKAGLTM NDIDAFEFHE AFSGQILANF KAMDSDWFAE 400
NYMGRKTKVG LPPLEKFNNW GGSLSLGHPF GATGCRLVMA AANRLRKEGG 450
QYGLVAACAA GGQGHAMIVE AYPK 474
Length:474
Mass (Da):51,294
Last modified:October 17, 2006 - v3
Checksum:iA7B41C37BEC1E6AD
GO
Isoform 2 (identifier: P55084-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAP → MTLVSGWLLYGWII

Note: No experimental confirmation available.

Show »
Length:452
Mass (Da):48,880
Checksum:i3633B6AE6528FC78
GO

Sequence cautioni

The sequence BAA22061.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591G → D in TFP deficiency. 1 Publication
VAR_021128
Natural varianti61 – 611R → C in TFP deficiency. 1 Publication
VAR_021129
Natural varianti61 – 611R → H in TFP deficiency. 2 Publications
VAR_007493
Natural varianti117 – 1171R → G in TFP deficiency. 1 Publication
VAR_021130
Natural varianti119 – 1191A → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035705
Natural varianti121 – 1211L → P in TFP deficiency. 1 Publication
VAR_021131
Natural varianti133 – 1331T → P in TFP deficiency. 1 Publication
VAR_021132
Natural varianti209 – 2091P → S.1 Publication
Corresponds to variant rs17851200 [ dbSNP | Ensembl ].
VAR_028231
Natural varianti242 – 2421D → G in TFP deficiency. 1 Publication
VAR_021133
Natural varianti247 – 2471R → H in TFP deficiency. 2 Publications
VAR_007494
Natural varianti259 – 27012Missing in TFP deficiency.
VAR_021134Add
BLAST
Natural varianti263 – 2631D → G in TFP deficiency. 2 Publications
VAR_007495
Natural varianti277 – 2771K → R.
Corresponds to variant rs57969630 [ dbSNP | Ensembl ].
VAR_061897
Natural varianti280 – 2801G → D in TFP deficiency. 1 Publication
VAR_021135
Natural varianti294 – 2941P → L in TFP deficiency. 1 Publication
VAR_021136
Natural varianti294 – 2941P → R in TFP deficiency. 1 Publication
VAR_021137
Natural varianti301 – 3011G → S in TFP deficiency. 1 Publication
VAR_021138
Natural varianti444 – 4441R → K in TFP deficiency. 2 Publications
VAR_017409

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MTILT…LRAAP → MTLVSGWLLYGWII in isoform 2. VSP_054426Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → MT in AAG39280. 1 Publication
Sequence conflicti1 – 11M → MT in AAH14572. 1 Publication
Sequence conflicti1 – 11M → MT in AAH17564. 1 Publication
Sequence conflicti1 – 11M → MT in AAH30824. 1 Publication
Sequence conflicti1 – 11M → MT in AAH66963. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16481 mRNA. Translation: BAA03942.1.
D86850 Genomic DNA. Translation: BAA22061.1. Sequence problems.
AF113209 mRNA. Translation: AAG39280.1.
AK304455 mRNA. Translation: BAG65272.1.
AK314455 mRNA. Translation: BAG37063.1.
AC010896 Genomic DNA. Translation: AAY14644.1.
BC014572 mRNA. Translation: AAH14572.1.
BC017564 mRNA. Translation: AAH17564.1.
BC030824 mRNA. Translation: AAH30824.1.
BC066963 mRNA. Translation: AAH66963.1.
CCDSiCCDS1722.1. [P55084-1]
CCDS62872.1. [P55084-2]
PIRiJC2109.
RefSeqiNP_000174.1. NM_000183.2. [P55084-1]
NP_001268441.1. NM_001281512.1.
NP_001268442.1. NM_001281513.1. [P55084-2]
UniGeneiHs.515848.

Genome annotation databases

EnsembliENST00000317799; ENSP00000325136; ENSG00000138029.
ENST00000545822; ENSP00000442665; ENSG00000138029.
GeneIDi3032.
KEGGihsa:3032.
UCSCiuc002rgz.3. human. [P55084-1]

Polymorphism databases

DMDMi116241345.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16481 mRNA. Translation: BAA03942.1 .
D86850 Genomic DNA. Translation: BAA22061.1 . Sequence problems.
AF113209 mRNA. Translation: AAG39280.1 .
AK304455 mRNA. Translation: BAG65272.1 .
AK314455 mRNA. Translation: BAG37063.1 .
AC010896 Genomic DNA. Translation: AAY14644.1 .
BC014572 mRNA. Translation: AAH14572.1 .
BC017564 mRNA. Translation: AAH17564.1 .
BC030824 mRNA. Translation: AAH30824.1 .
BC066963 mRNA. Translation: AAH66963.1 .
CCDSi CCDS1722.1. [P55084-1 ]
CCDS62872.1. [P55084-2 ]
PIRi JC2109.
RefSeqi NP_000174.1. NM_000183.2. [P55084-1 ]
NP_001268441.1. NM_001281512.1.
NP_001268442.1. NM_001281513.1. [P55084-2 ]
UniGenei Hs.515848.

3D structure databases

ProteinModelPortali P55084.
SMRi P55084. Positions 56-471.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109282. 41 interactions.
IntActi P55084. 33 interactions.
MINTi MINT-1154861.
STRINGi 9606.ENSP00000325136.

PTM databases

PhosphoSitei P55084.

Polymorphism databases

DMDMi 116241345.

2D gel databases

UCD-2DPAGE P55084.

Proteomic databases

MaxQBi P55084.
PaxDbi P55084.
PRIDEi P55084.

Protocols and materials databases

DNASUi 3032.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000317799 ; ENSP00000325136 ; ENSG00000138029 .
ENST00000545822 ; ENSP00000442665 ; ENSG00000138029 .
GeneIDi 3032.
KEGGi hsa:3032.
UCSCi uc002rgz.3. human. [P55084-1 ]

Organism-specific databases

CTDi 3032.
GeneCardsi GC02P026466.
HGNCi HGNC:4803. HADHB.
HPAi HPA037539.
MIMi 143450. gene.
609015. phenotype.
neXtProti NX_P55084.
Orphaneti 746. Mitochondrial trifunctional protein deficiency.
PharmGKBi PA29177.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0183.
HOGENOMi HOG000012240.
HOVERGENi HBG104782.
InParanoidi P55084.
KOi K07509.
OMAi MHNISRE.
PhylomeDBi P55084.
TreeFami TF315243.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci MetaCyc:HS06436-MONOMER.
Reactomei REACT_121006. Acyl chain remodeling of CL.
REACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
REACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_2025. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
REACT_2108. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.

Miscellaneous databases

ChiTaRSi HADHB. human.
GeneWikii HADHB.
GenomeRNAii 3032.
NextBioi 12002.
PROi P55084.
SOURCEi Search...

Gene expression databases

ArrayExpressi P55084.
Bgeei P55084.
CleanExi HS_HADHB.
Genevestigatori P55084.

Family and domain databases

Gene3Di 3.40.47.10. 4 hits.
InterProi IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view ]
Pfami PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53901. SSF53901. 2 hits.
TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEi PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein."
    Kamijo T., Aoyama T., Komiyama A., Hashimoto T.
    Biochem. Biophys. Res. Commun. 199:818-825(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Genomic and mutational analysis of the mitochondrial trifunctional protein beta-subunit (HADHB) gene in patients with trifunctional protein deficiency."
    Orii K.E., Aoyama T., Wakui K., Fukushima Y., Miyajima H., Yamaguchi S., Orii T., Kondo N., Hashimoto T.
    Hum. Mol. Genet. 6:1215-1224(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TFP DEFICIENCY LYS-444.
    Tissue: Blood.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Heart.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Stomach and Tongue.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-209.
    Tissue: Colon, Hypothalamus, Skeletal muscle and Urinary bladder.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-52.
    Tissue: Platelet.
  8. "The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA thiolase."
    Middleton B.
    Biochem. Soc. Trans. 22:427-431(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 48-63, CATALYTIC ACTIVITY.
    Tissue: Liver.
  9. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
    Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
    Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 62-72 AND 96-111.
    Tissue: Adipocyte.
  10. "Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients."
    Kamijo T., Wanders R.J., Saudubray J.-M., Aoyama T., Komiyama A., Hashimoto T.
    J. Clin. Invest. 93:1740-1747(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  11. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-72 AND LYS-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Human cytomegalovirus directly induces the antiviral protein viperin to enhance infectivity."
    Seo J.Y., Yaneva R., Hinson E.R., Cresswell P.
    Science 332:1093-1097(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH RSAD2.
  14. "Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both alpha- and beta-subunits."
    Ushikubo S., Aoyama T., Kamijo T., Wanders R.J.A., Rinaldo P., Vockley J., Hashimoto T.
    Am. J. Hum. Genet. 58:979-988(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TFP DEFICIENCY HIS-61; HIS-247 AND GLY-263.
  15. "Molecular and phenotypic heterogeneity in mitochondrial trifunctional protein deficiency due to beta-subunit mutations."
    Spiekerkoetter U., Sun B., Khuchua Z., Bennett M.J., Strauss A.W.
    Hum. Mutat. 21:598-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TFP DEFICIENCY ASP-59; CYS-61; HIS-61; GLY-117; PRO-121; PRO-133; GLY-242; HIS-247; 259-GLY--PRO-270 DEL; GLY-263; ASP-280; ARG-294; LEU-294; SER-301 AND LYS-444.
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-119.

Entry informationi

Entry nameiECHB_HUMAN
AccessioniPrimary (citable) accession number: P55084
Secondary accession number(s): B2RB16
, B4E2W0, O14969, Q53TA6, Q96C77, Q9H3F5, Q9T2V8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 146 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

External Data

Dasty 3

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