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Q9UJ83 (HACL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
2-hydroxyacyl-CoA lyase 1

EC=4.1.-.-
Alternative name(s):
2-hydroxyphytanoyl-CoA lyase
Short name=2-HPCL
Phytanoyl-CoA 2-hydroxylase 2
Gene names
Name:HACL1
Synonyms:HPCL, HPCL2, PHYH2
ORF Names:HSPC279
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde.

Catalytic activity

2-hydroxyphytanoyl-CoA = pristanal + formyl-CoA.

Cofactor

Binds 1 magnesium ion per subunit.

Binds 1 thiamine pyrophosphate per subunit.

Pathway

Lipid metabolism; fatty acid metabolism.

Subunit structure

Homotetramer.

Subcellular location

Peroxisome.

Tissue specificity

Expressed in high levels in liver, also expressed in kidney, heart and skeletal muscle. Ref.1

Sequence similarities

Belongs to the TPP enzyme family.

Sequence caution

The sequence AAF28957.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-746580,EBI-746580

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UJ83-1)

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: Q9UJ83-2)

The sequence of this isoform differs from the canonical sequence as follows:
     77-103: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9UJ83-4)

The sequence of this isoform differs from the canonical sequence as follows:
     128-153: Missing.
     332-365: Missing.
Isoform 3 (identifier: Q9UJ83-3)

The sequence of this isoform differs from the canonical sequence as follows:
     104-185: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5785782-hydroxyacyl-CoA lyase 1
PRO_0000090816

Regions

Region401 – 48686Thiamine pyrophosphate binding
Motif576 – 5783Microbody targeting signal

Sites

Metal binding4551Magnesium By similarity
Metal binding4821Magnesium By similarity
Binding site601Thiamine pyrophosphate By similarity

Amino acid modifications

Modified residue3511N6-succinyllysine By similarity
Modified residue3581N6-succinyllysine By similarity
Modified residue3651N6-succinyllysine By similarity

Natural variations

Alternative sequence77 – 10327Missing in isoform 2.
VSP_054191
Alternative sequence104 – 18582Missing in isoform 3.
VSP_054192
Alternative sequence128 – 15326Missing in isoform 4.
VSP_054749
Alternative sequence332 – 36534Missing in isoform 4.
VSP_054750

Experimental info

Sequence conflict4471Q → H in CAB60200. Ref.1
Sequence conflict5431R → E in CAB60200. Ref.1

Sequences

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

Last modified May 2, 2002. Version 2.
Checksum: CF4F4B1A97025140

FASTA57863,729
        10         20         30         40         50         60 
MPDSNFAERS EEQVSGAKVI AQALKTQDVE YIFGIVGIPV TEIAIAAQQL GIKYIGMRNE 

        70         80         90        100        110        120 
QAACYAASAI GYLTSRPGVC LVVSGPGLIH ALGGMANANM NCWPLLVIGG SSERNQETMG 

       130        140        150        160        170        180 
AFQEFPQVEA CRLYTKFSAR PSSIEAIPFV IEKAVRSSIY GRPGACYVDI PADFVNLQVN 

       190        200        210        220        230        240 
VNSIKYMERC MSPPISMAET SAVCTAASVI RNAKQPLLII GKGAAYAHAE ESIKKLVEQY 

       250        260        270        280        290        300 
KLPFLPTPMG KGVVPDNHPY CVGAARSRAL QFADVIVLFG ARLNWILHFG LPPRYQPDVK 

       310        320        330        340        350        360 
FIQVDICAEE LGNNVKPAVT LLGNIHAVTK QLLEELDKTP WQYPPESKWW KTLREKMKSN 

       370        380        390        400        410        420 
EAASKELASK KSLPMNYYTV FYHVQEQLPR DCFVVSEGAN TMDIGRTVLQ NYLPRHRLDA 

       430        440        450        460        470        480 
GTFGTMGVGL GFAIAAAVVA KDRSPGQWII CVEGDSAFGF SGMEVETICR YNLPIILLVV 

       490        500        510        520        530        540 
NNNGIYQGFD TDTWKEMLKF QDATAVVPPM CLLPNSHYEQ VMTAFGGKGY FVQTPEELQK 

       550        560        570 
SLRQSLADTT KPSLINIMIE PQATRKAQDF HWLTRSNM 

« Hide

Isoform 2 [UniParc].

Checksum: E4CCA8D486BE14FB
Show »

FASTA55161,064
Isoform 4 [UniParc].

Checksum: C8ED2E77A6246C04
Show »

FASTA51856,660
Isoform 3 [UniParc].

Checksum: BACFA0F55B8007A1
Show »

FASTA49654,724

References

« Hide 'large scale' references
[1]"Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine hydrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during alpha-oxidation of 3-methyl-branched fatty acids."
Foulon V., Antonenkov V.D., Croes K., Waelkens E., Mannaerts G.P., Van Veldhoven P.P., Casteels M.
Proc. Natl. Acad. Sci. U.S.A. 96:10039-10044(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Umbilical cord blood.
[3]"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 2 AND 3).
Tissue: Mammary gland and Testis.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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).
Tissue: Lung.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ131753 mRNA. Translation: CAB60200.1.
AF161397 mRNA. Translation: AAF28957.1. Different initiation.
AK301546 mRNA. Translation: BAG63043.1.
AK301990 mRNA. Translation: BAG63397.1.
AC027129 Genomic DNA. No translation available.
BC001627 mRNA. Translation: AAH01627.1.
CCDSCCDS2627.1.
RefSeqNP_001271342.1. NM_001284413.1. [Q9UJ83-2]
NP_001271344.1. NM_001284415.1. [Q9UJ83-4]
NP_001271345.1. NM_001284416.1. [Q9UJ83-3]
NP_036392.2. NM_012260.3. [Q9UJ83-1]
UniGeneHs.63290.

3D structure databases

ProteinModelPortalQ9UJ83.
SMRQ9UJ83. Positions 12-563.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117523. 6 interactions.
IntActQ9UJ83. 3 interactions.
MINTMINT-1444467.
STRING9606.ENSP00000323811.

PTM databases

PhosphoSiteQ9UJ83.

Polymorphism databases

DMDM20455027.

Proteomic databases

MaxQBQ9UJ83.
PaxDbQ9UJ83.
PeptideAtlasQ9UJ83.
PRIDEQ9UJ83.

Protocols and materials databases

DNASU26061.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321169; ENSP00000323811; ENSG00000131373.
ENST00000451445; ENSP00000403656; ENSG00000131373.
ENST00000456194; ENSP00000390699; ENSG00000131373.
ENST00000457447; ENSP00000404883; ENSG00000131373.
GeneID26061.
KEGGhsa:26061.
UCSCuc003caf.3. human. [Q9UJ83-1]

Organism-specific databases

CTD26061.
GeneCardsGC03M015602.
HGNCHGNC:17856. HACL1.
HPAHPA035496.
MIM604300. gene.
neXtProtNX_Q9UJ83.
PharmGKBPA142671172.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0028.
HOGENOMHOG000053808.
HOVERGENHBG027302.
InParanoidQ9UJ83.
KOK12261.
OMAHAEENIR.
PhylomeDBQ9UJ83.
TreeFamTF105690.

Enzyme and pathway databases

BioCycMetaCyc:HS05516-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00199.

Gene expression databases

ArrayExpressQ9UJ83.
BgeeQ9UJ83.
CleanExHS_HACL1.
GenevestigatorQ9UJ83.

Family and domain databases

Gene3D3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
ProtoNetSearch...

Other

ChiTaRSHACL1. human.
GenomeRNAi26061.
NextBio35475725.
PROQ9UJ83.
SOURCESearch...

Entry information

Entry nameHACL1_HUMAN
AccessionPrimary (citable) accession number: Q9UJ83
Secondary accession number(s): B4DWI1 expand/collapse secondary AC list , B4DXI5, E9PEN4, Q9BV42, Q9P0A2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 2, 2002
Last modified: July 9, 2014
This is version 118 of the entry and version 2 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 chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM