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

Trifunctional enzyme subunit beta, mitochondrial

Gene

HADHB

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

Functioni

Catalytic activityi

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

Pathway:ifatty 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei138 – 1381Acyl-thioester intermediateBy similarity
Active sitei428 – 4281Proton acceptorPROSITE-ProRule annotation
Active sitei458 – 4581Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  • 3-hydroxyacyl-CoA dehydrogenase activity Source: ProtInc
  • acetyl-CoA C-acyltransferase activity Source: ProtInc
  • enoyl-CoA hydratase activity Source: ProtInc
  • long-chain-3-hydroxyacyl-CoA dehydrogenase activity Source: Ensembl
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

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_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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:4803. HADHB.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • mitochondrial envelope Source: ProtInc
  • mitochondrial inner membrane Source: UniProtKB
  • mitochondrial nucleoid Source: BHF-UCL
  • mitochondrial outer membrane Source: UniProtKB
  • 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)3 Publications

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

Disease descriptionThe 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.

See also OMIM:609015
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. 1 Publication
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.

Polymorphism and mutation databases

BioMutaiHADHB.
DMDMi116241345.

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; alternateBy similarity
Modified residuei188 – 1881N6-acetyllysine; alternate1 Publication
Modified residuei188 – 1881N6-succinyllysine; alternateBy similarity
Modified residuei190 – 1901N6-succinyllysineBy similarity
Modified residuei272 – 2721N6-succinyllysineBy similarity
Modified residuei291 – 2911N6-succinyllysineBy similarity
Modified residuei293 – 2931N6-acetyllysine; alternateBy similarity
Modified residuei293 – 2931N6-succinyllysine; alternateBy similarity
Modified residuei298 – 2981N6-acetyllysineBy similarity
Modified residuei332 – 3321N6-acetyllysine; alternateBy similarity
Modified residuei332 – 3321N6-succinyllysine; alternateBy similarity
Modified residuei348 – 3481N6-acetyllysineBy similarity
Modified residuei361 – 3611N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP55084.
PaxDbiP55084.
PRIDEiP55084.

2D gel databases

UCD-2DPAGEP55084.

PTM databases

PhosphoSiteiP55084.

Expressioni

Gene expression databases

BgeeiP55084.
CleanExiHS_HADHB.
ExpressionAtlasiP55084. baseline and differential.
GenevisibleiP55084. HS.

Organism-specific databases

HPAiHPA037539.
HPA037540.

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. 51 interactions.
IntActiP55084. 33 interactions.
MINTiMINT-1154861.
STRINGi9606.ENSP00000325136.

Structurei

3D structure databases

ProteinModelPortaliP55084.
SMRiP55084. Positions 52-470.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00760000119318.
HOGENOMiHOG000012240.
HOVERGENiHBG104782.
InParanoidiP55084.
KOiK07509.
OMAiMTAFPEP.
PhylomeDBiP55084.
TreeFamiTF315243.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
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. AlignAdd to basket

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

        10         20         30         40         50
MTILTYPFKN LPTASKWALR FSIRPLSCSS QLRAAPAVQT KTKKTLAKPN
60 70 80 90 100
IRNVVVVDGV RTPFLLSGTS YKDLMPHDLA RAALTGLLHR TSVPKEVVDY
110 120 130 140 150
IIFGTVIQEV KTSNVAREAA LGAGFSDKTP AHTVTMACIS ANQAMTTGVG
160 170 180 190 200
LIASGQCDVI VAGGVELMSD VPIRHSRKMR KLMLDLNKAK SMGQRLSLIS
210 220 230 240 250
KFRFNFLAPE LPAVSEFSTS ETMGHSADRL AAAFAVSRLE QDEYALRSHS
260 270 280 290 300
LAKKAQDEGL LSDVVPFKVP GKDTVTKDNG IRPSSLEQMA KLKPAFIKPY
310 320 330 340 350
GTVTAANSSF LTDGASAMLI MAEEKALAMG YKPKAYLRDF MYVSQDPKDQ
360 370 380 390 400
LLLGPTYATP KVLEKAGLTM NDIDAFEFHE AFSGQILANF KAMDSDWFAE
410 420 430 440 450
NYMGRKTKVG LPPLEKFNNW GGSLSLGHPF GATGCRLVMA AANRLRKEGG
460 470
QYGLVAACAA GGQGHAMIVE AYPK
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. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → MT in AAG39280 (Ref. 3) Curated
Sequence conflicti1 – 11M → MT in AAH14572 (PubMed:15489334).Curated
Sequence conflicti1 – 11M → MT in AAH17564 (PubMed:15489334).Curated
Sequence conflicti1 – 11M → MT in AAH30824 (PubMed:15489334).Curated
Sequence conflicti1 – 11M → MT in AAH66963 (PubMed:15489334).Curated

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. 1 Publication
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. 1 PublicationVSP_054426Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
XP_011531105.1. XM_011532803.1. [P55084-1]
XP_011531106.1. XM_011532804.1. [P55084-2]
UniGeneiHs.515848.

Genome annotation databases

EnsembliENST00000317799; ENSP00000325136; ENSG00000138029.
ENST00000545822; ENSP00000442665; ENSG00000138029. [P55084-2]
GeneIDi3032.
KEGGihsa:3032.
UCSCiuc002rgz.3. human. [P55084-1]
uc010ykv.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
XP_011531105.1. XM_011532803.1. [P55084-1]
XP_011531106.1. XM_011532804.1. [P55084-2]
UniGeneiHs.515848.

3D structure databases

ProteinModelPortaliP55084.
SMRiP55084. Positions 52-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109282. 51 interactions.
IntActiP55084. 33 interactions.
MINTiMINT-1154861.
STRINGi9606.ENSP00000325136.

PTM databases

PhosphoSiteiP55084.

Polymorphism and mutation databases

BioMutaiHADHB.
DMDMi116241345.

2D gel databases

UCD-2DPAGEP55084.

Proteomic databases

MaxQBiP55084.
PaxDbiP55084.
PRIDEiP55084.

Protocols and materials databases

DNASUi3032.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000317799; ENSP00000325136; ENSG00000138029.
ENST00000545822; ENSP00000442665; ENSG00000138029. [P55084-2]
GeneIDi3032.
KEGGihsa:3032.
UCSCiuc002rgz.3. human. [P55084-1]
uc010ykv.2. human.

Organism-specific databases

CTDi3032.
GeneCardsiGC02P026466.
HGNCiHGNC:4803. HADHB.
HPAiHPA037539.
HPA037540.
MIMi143450. gene.
609015. phenotype.
neXtProtiNX_P55084.
Orphaneti746. Mitochondrial trifunctional protein deficiency.
PharmGKBiPA29177.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00760000119318.
HOGENOMiHOG000012240.
HOVERGENiHBG104782.
InParanoidiP55084.
KOiK07509.
OMAiMTAFPEP.
PhylomeDBiP55084.
TreeFamiTF315243.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciMetaCyc:HS06436-MONOMER.
ReactomeiREACT_121006. Acyl chain remodeling of CL.
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

ChiTaRSiHADHB. human.
GeneWikiiHADHB.
GenomeRNAii3032.
NextBioi12002.
PROiP55084.
SOURCEiSearch...

Gene expression databases

BgeeiP55084.
CleanExiHS_HADHB.
ExpressionAtlasiP55084. baseline and differential.
GenevisibleiP55084. HS.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "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.
  16. "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.
  17. 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: July 22, 2015
This is version 155 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

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.