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P55084 (ECHB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trifunctional enzyme subunit beta, mitochondrial
Alternative name(s):
TP-beta

Including the following 1 domains:

  1. 3-ketoacyl-CoA thiolase
    EC=2.3.1.16
    Alternative name(s):
    Acetyl-CoA acyltransferase
    Beta-ketothiolase
Gene names
Name:HADHB
ORF Names:MSTP029
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. Ref.8

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits. Interacts with RSAD2/viperin. Ref.10 Ref.13

Subcellular location

Mitochondrion. Mitochondrion inner membrane. Mitochondrion outer membrane. Endoplasmic reticulum Ref.13.

Involvement in disease

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.

Sequence similarities

Belongs to the thiolase family.

Sequence caution

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

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
Mitochondrion
Mitochondrion inner membrane
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcardiolipin acyl-chain remodeling

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

fatty acid beta-oxidation

Traceable author statement. Source: Reactome

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.13. Source: UniProtKB

mitochondrial envelope

Traceable author statement PubMed 1550553. Source: ProtInc

mitochondrial fatty acid beta-oxidation multienzyme complex

Inferred from electronic annotation. Source: Ensembl

mitochondrial inner membrane

Inferred from direct assay Ref.13. Source: UniProtKB

mitochondrial nucleoid

Inferred from direct assay PubMed 18063578. Source: BHF-UCL

mitochondrial outer membrane

Inferred from direct assay Ref.13. Source: UniProtKB

mitochondrion

Non-traceable author statement Ref.8. Source: UniProtKB

   Molecular_function3-hydroxyacyl-CoA dehydrogenase activity

Traceable author statement PubMed 1550553. Source: ProtInc

NAD binding

Inferred from electronic annotation. Source: Ensembl

acetyl-CoA C-acyltransferase activity

Traceable author statement Ref.1. Source: ProtInc

enoyl-CoA hydratase activity

Traceable author statement PubMed 1550553. Source: ProtInc

fatty-acyl-CoA binding

Inferred from electronic annotation. Source: Ensembl

long-chain-3-hydroxyacyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: Ensembl

long-chain-enoyl-CoA hydratase activity

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GABARAPL1Q9H0R84EBI-356635,EBI-746969

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P55084-1)

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.
Isoform 2 (identifier: P55084-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAP → MTLVSGWLLYGWII
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion Ref.7
Chain34 – 474441Trifunctional enzyme subunit beta, mitochondrial
PRO_0000034080

Sites

Active site1381Acyl-thioester intermediate By similarity
Active site4281Proton acceptor By similarity
Active site4581Proton acceptor By similarity

Amino acid modifications

Modified residue721N6-acetyllysine; alternate Ref.11
Modified residue721N6-succinyllysine; alternate By similarity
Modified residue1881N6-acetyllysine; alternate Ref.11
Modified residue1881N6-succinyllysine; alternate By similarity
Modified residue1901N6-succinyllysine By similarity
Modified residue2721N6-succinyllysine By similarity
Modified residue2911N6-succinyllysine By similarity
Modified residue2931N6-acetyllysine; alternate By similarity
Modified residue2931N6-succinyllysine; alternate By similarity
Modified residue2981N6-acetyllysine By similarity
Modified residue3321N6-acetyllysine; alternate By similarity
Modified residue3321N6-succinyllysine; alternate By similarity
Modified residue3481N6-acetyllysine By similarity
Modified residue3611N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 3636MTILT…LRAAP → MTLVSGWLLYGWII in isoform 2.
VSP_054426
Natural variant591G → D in TFP deficiency. Ref.15
VAR_021128
Natural variant611R → C in TFP deficiency. Ref.15
VAR_021129
Natural variant611R → H in TFP deficiency. Ref.14 Ref.15
VAR_007493
Natural variant1171R → G in TFP deficiency. Ref.15
VAR_021130
Natural variant1191A → V in a breast cancer sample; somatic mutation. Ref.16
VAR_035705
Natural variant1211L → P in TFP deficiency. Ref.15
VAR_021131
Natural variant1331T → P in TFP deficiency. Ref.15
VAR_021132
Natural variant2091P → S. Ref.6
Corresponds to variant rs17851200 [ dbSNP | Ensembl ].
VAR_028231
Natural variant2421D → G in TFP deficiency. Ref.15
VAR_021133
Natural variant2471R → H in TFP deficiency. Ref.14 Ref.15
VAR_007494
Natural variant259 – 27012Missing in TFP deficiency.
VAR_021134
Natural variant2631D → G in TFP deficiency. Ref.14 Ref.15
VAR_007495
Natural variant2771K → R.
Corresponds to variant rs57969630 [ dbSNP | Ensembl ].
VAR_061897
Natural variant2801G → D in TFP deficiency. Ref.15
VAR_021135
Natural variant2941P → L in TFP deficiency. Ref.15
VAR_021136
Natural variant2941P → R in TFP deficiency. Ref.15
VAR_021137
Natural variant3011G → S in TFP deficiency. Ref.15
VAR_021138
Natural variant4441R → K in TFP deficiency. Ref.2 Ref.15
VAR_017409

Experimental info

Sequence conflict11M → MT in AAG39280. Ref.3
Sequence conflict11M → MT in AAH14572. Ref.6
Sequence conflict11M → MT in AAH17564. Ref.6
Sequence conflict11M → MT in AAH30824. Ref.6
Sequence conflict11M → MT in AAH66963. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: A7B41C37BEC1E6AD

FASTA47451,294
        10         20         30         40         50         60 
MTILTYPFKN LPTASKWALR FSIRPLSCSS QLRAAPAVQT KTKKTLAKPN IRNVVVVDGV 

        70         80         90        100        110        120 
RTPFLLSGTS YKDLMPHDLA RAALTGLLHR TSVPKEVVDY IIFGTVIQEV KTSNVAREAA 

       130        140        150        160        170        180 
LGAGFSDKTP AHTVTMACIS ANQAMTTGVG LIASGQCDVI VAGGVELMSD VPIRHSRKMR 

       190        200        210        220        230        240 
KLMLDLNKAK SMGQRLSLIS KFRFNFLAPE LPAVSEFSTS ETMGHSADRL AAAFAVSRLE 

       250        260        270        280        290        300 
QDEYALRSHS LAKKAQDEGL LSDVVPFKVP GKDTVTKDNG IRPSSLEQMA KLKPAFIKPY 

       310        320        330        340        350        360 
GTVTAANSSF LTDGASAMLI MAEEKALAMG YKPKAYLRDF MYVSQDPKDQ LLLGPTYATP 

       370        380        390        400        410        420 
KVLEKAGLTM NDIDAFEFHE AFSGQILANF KAMDSDWFAE NYMGRKTKVG LPPLEKFNNW 

       430        440        450        460        470 
GGSLSLGHPF GATGCRLVMA AANRLRKEGG QYGLVAACAA GGQGHAMIVE AYPK 

« Hide

Isoform 2 [UniParc].

Checksum: 3633B6AE6528FC78
Show »

FASTA45248,880

References

« Hide 'large scale' references
[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]Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., Liu L.S., Ding J.F. expand/collapse author list , Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-119.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1722.1.
PIRJC2109.
RefSeqNP_000174.1. NM_000183.2. [P55084-1]
NP_001268441.1. NM_001281512.1.
NP_001268442.1. NM_001281513.1. [P55084-2]
UniGeneHs.515848.

3D structure databases

ProteinModelPortalP55084.
SMRP55084. Positions 56-471.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109282. 42 interactions.
IntActP55084. 32 interactions.
MINTMINT-1154861.
STRING9606.ENSP00000325136.

PTM databases

PhosphoSiteP55084.

Polymorphism databases

DMDM116241345.

2D gel databases

UCD-2DPAGEP55084.

Proteomic databases

MaxQBP55084.
PaxDbP55084.
PRIDEP55084.

Protocols and materials databases

DNASU3032.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317799; ENSP00000325136; ENSG00000138029.
ENST00000545822; ENSP00000442665; ENSG00000138029.
GeneID3032.
KEGGhsa:3032.
UCSCuc002rgz.3. human. [P55084-1]

Organism-specific databases

CTD3032.
GeneCardsGC02P026466.
HGNCHGNC:4803. HADHB.
HPAHPA037539.
MIM143450. gene.
609015. phenotype.
neXtProtNX_P55084.
Orphanet746. Mitochondrial trifunctional protein deficiency.
PharmGKBPA29177.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0183.
HOGENOMHOG000012240.
HOVERGENHBG104782.
InParanoidP55084.
KOK07509.
OMAMHNISRE.
PhylomeDBP55084.
TreeFamTF315243.

Enzyme and pathway databases

BioCycMetaCyc:HS06436-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00659.

Gene expression databases

ArrayExpressP55084.
BgeeP55084.
CleanExHS_HADHB.
GenevestigatorP55084.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
InterProIPR002155. 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]
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
SUPFAMSSF53901. SSF53901. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHADHB. human.
GeneWikiHADHB.
GenomeRNAi3032.
NextBio12002.
PROP55084.
SOURCESearch...

Entry information

Entry nameECHB_HUMAN
AccessionPrimary (citable) accession number: P55084
Secondary accession number(s): B2RB16 expand/collapse secondary AC list , B4E2W0, O14969, Q53TA6, Q96C77, Q9H3F5, Q9T2V8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM