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Q9UJ83

- HACL1_HUMAN

UniProt

Q9UJ83 - HACL1_HUMAN

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Protein
2-hydroxyacyl-CoA lyase 1
Gene
HACL1, HPCL, HPCL2, PHYH2, HSPC279
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Binds 1 magnesium ion per subunit.
Binds 1 thiamine pyrophosphate per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Thiamine pyrophosphate By similarity
Metal bindingi455 – 4551Magnesium By similarity
Metal bindingi482 – 4821Magnesium By similarity

GO - Molecular functioni

  1. carbon-carbon lyase activity Source: UniProtKB
  2. cofactor binding Source: UniProtKB
  3. identical protein binding Source: IntAct
  4. magnesium ion binding Source: InterPro
  5. receptor binding Source: UniProtKB
  6. thiamine pyrophosphate binding Source: UniProtKB

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. fatty acid alpha-oxidation Source: HGNC
  3. protein oligomerization Source: UniProtKB
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS05516-MONOMER.
ReactomeiREACT_17003. Alpha-oxidation of phytanate.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:HACL1
Synonyms:HPCL, HPCL2, PHYH2
ORF Names:HSPC279
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:17856. HACL1.

Subcellular locationi

GO - Cellular componenti

  1. peroxisomal matrix Source: Reactome
  2. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671172.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5785782-hydroxyacyl-CoA lyase 1
PRO_0000090816Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei351 – 3511N6-succinyllysine By similarity
Modified residuei358 – 3581N6-succinyllysine By similarity
Modified residuei365 – 3651N6-succinyllysine By similarity

Proteomic databases

MaxQBiQ9UJ83.
PaxDbiQ9UJ83.
PeptideAtlasiQ9UJ83.
PRIDEiQ9UJ83.

PTM databases

PhosphoSiteiQ9UJ83.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ9UJ83.
BgeeiQ9UJ83.
CleanExiHS_HACL1.
GenevestigatoriQ9UJ83.

Organism-specific databases

HPAiHPA035496.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-746580,EBI-746580

Protein-protein interaction databases

BioGridi117523. 6 interactions.
IntActiQ9UJ83. 3 interactions.
MINTiMINT-1444467.
STRINGi9606.ENSP00000323811.

Structurei

3D structure databases

ProteinModelPortaliQ9UJ83.
SMRiQ9UJ83. Positions 12-563.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni401 – 48686Thiamine pyrophosphate binding
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi576 – 5783Microbody targeting signal

Sequence similaritiesi

Belongs to the TPP enzyme family.

Phylogenomic databases

eggNOGiCOG0028.
HOGENOMiHOG000053808.
HOVERGENiHBG027302.
InParanoidiQ9UJ83.
KOiK12261.
OMAiHAEENIR.
PhylomeDBiQ9UJ83.
TreeFamiTF105690.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029035. 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]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UJ83-1) [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

MPDSNFAERS EEQVSGAKVI AQALKTQDVE YIFGIVGIPV TEIAIAAQQL    50
GIKYIGMRNE QAACYAASAI GYLTSRPGVC LVVSGPGLIH ALGGMANANM 100
NCWPLLVIGG SSERNQETMG AFQEFPQVEA CRLYTKFSAR PSSIEAIPFV 150
IEKAVRSSIY GRPGACYVDI PADFVNLQVN VNSIKYMERC MSPPISMAET 200
SAVCTAASVI RNAKQPLLII GKGAAYAHAE ESIKKLVEQY KLPFLPTPMG 250
KGVVPDNHPY CVGAARSRAL QFADVIVLFG ARLNWILHFG LPPRYQPDVK 300
FIQVDICAEE LGNNVKPAVT LLGNIHAVTK QLLEELDKTP WQYPPESKWW 350
KTLREKMKSN EAASKELASK KSLPMNYYTV FYHVQEQLPR DCFVVSEGAN 400
TMDIGRTVLQ NYLPRHRLDA GTFGTMGVGL GFAIAAAVVA KDRSPGQWII 450
CVEGDSAFGF SGMEVETICR YNLPIILLVV NNNGIYQGFD TDTWKEMLKF 500
QDATAVVPPM CLLPNSHYEQ VMTAFGGKGY FVQTPEELQK SLRQSLADTT 550
KPSLINIMIE PQATRKAQDF HWLTRSNM 578
Length:578
Mass (Da):63,729
Last modified:May 2, 2002 - v2
Checksum:iCF4F4B1A97025140
GO
Isoform 2 (identifier: Q9UJ83-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     77-103: Missing.

Note: No experimental confirmation available.

Show »
Length:551
Mass (Da):61,064
Checksum:iE4CCA8D486BE14FB
GO
Isoform 4 (identifier: Q9UJ83-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     128-153: Missing.
     332-365: Missing.

Show »
Length:518
Mass (Da):56,660
Checksum:iC8ED2E77A6246C04
GO
Isoform 3 (identifier: Q9UJ83-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     104-185: Missing.

Note: No experimental confirmation available.

Show »
Length:496
Mass (Da):54,724
Checksum:iBACFA0F55B8007A1
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei77 – 10327Missing in isoform 2.
VSP_054191Add
BLAST
Alternative sequencei104 – 18582Missing in isoform 3.
VSP_054192Add
BLAST
Alternative sequencei128 – 15326Missing in isoform 4.
VSP_054749Add
BLAST
Alternative sequencei332 – 36534Missing in isoform 4.
VSP_054750Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti447 – 4471Q → H in CAB60200. 1 Publication
Sequence conflicti543 – 5431R → E in CAB60200. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2627.1. [Q9UJ83-1]
CCDS68360.1. [Q9UJ83-2]
CCDS68361.1. [Q9UJ83-3]
CCDS68362.1. [Q9UJ83-4]
RefSeqiNP_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]
UniGeneiHs.63290.

Genome annotation databases

EnsembliENST00000321169; ENSP00000323811; ENSG00000131373.
ENST00000451445; ENSP00000403656; ENSG00000131373.
ENST00000456194; ENSP00000390699; ENSG00000131373.
ENST00000457447; ENSP00000404883; ENSG00000131373.
GeneIDi26061.
KEGGihsa:26061.
UCSCiuc003caf.3. human. [Q9UJ83-1]

Polymorphism databases

DMDMi20455027.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2627.1. [Q9UJ83-1 ]
CCDS68360.1. [Q9UJ83-2 ]
CCDS68361.1. [Q9UJ83-3 ]
CCDS68362.1. [Q9UJ83-4 ]
RefSeqi NP_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 ]
UniGenei Hs.63290.

3D structure databases

ProteinModelPortali Q9UJ83.
SMRi Q9UJ83. Positions 12-563.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117523. 6 interactions.
IntActi Q9UJ83. 3 interactions.
MINTi MINT-1444467.
STRINGi 9606.ENSP00000323811.

PTM databases

PhosphoSitei Q9UJ83.

Polymorphism databases

DMDMi 20455027.

Proteomic databases

MaxQBi Q9UJ83.
PaxDbi Q9UJ83.
PeptideAtlasi Q9UJ83.
PRIDEi Q9UJ83.

Protocols and materials databases

DNASUi 26061.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000321169 ; ENSP00000323811 ; ENSG00000131373 .
ENST00000451445 ; ENSP00000403656 ; ENSG00000131373 .
ENST00000456194 ; ENSP00000390699 ; ENSG00000131373 .
ENST00000457447 ; ENSP00000404883 ; ENSG00000131373 .
GeneIDi 26061.
KEGGi hsa:26061.
UCSCi uc003caf.3. human. [Q9UJ83-1 ]

Organism-specific databases

CTDi 26061.
GeneCardsi GC03M015602.
HGNCi HGNC:17856. HACL1.
HPAi HPA035496.
MIMi 604300. gene.
neXtProti NX_Q9UJ83.
PharmGKBi PA142671172.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0028.
HOGENOMi HOG000053808.
HOVERGENi HBG027302.
InParanoidi Q9UJ83.
KOi K12261.
OMAi HAEENIR.
PhylomeDBi Q9UJ83.
TreeFami TF105690.

Enzyme and pathway databases

UniPathwayi UPA00199 .
BioCyci MetaCyc:HS05516-MONOMER.
Reactomei REACT_17003. Alpha-oxidation of phytanate.

Miscellaneous databases

ChiTaRSi HACL1. human.
GenomeRNAii 26061.
NextBioi 35475725.
PROi Q9UJ83.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UJ83.
Bgeei Q9UJ83.
CleanExi HS_HACL1.
Genevestigatori Q9UJ83.

Family and domain databases

Gene3Di 3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProi IPR029035. 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 ]
Pfami PF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view ]
SUPFAMi SSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHACL1_HUMAN
AccessioniPrimary (citable) accession number: Q9UJ83
Secondary accession number(s): B4DWI1
, B4DXI5, E9PEN4, Q9BV42, Q9P0A2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 2, 2002
Last modified: September 3, 2014
This is version 119 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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