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Q9UJ83

- HACL1_HUMAN

UniProt

Q9UJ83 - HACL1_HUMAN

Protein

2-hydroxyacyl-CoA lyase 1

Gene

HACL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (02 May 2002)
      Previous versions | rss
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    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 pyrophosphateBy similarity
    Metal bindingi455 – 4551MagnesiumBy similarity
    Metal bindingi482 – 4821MagnesiumBy 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

    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

    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 1PRO_0000090816Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei351 – 3511N6-succinyllysineBy similarity
    Modified residuei358 – 3581N6-succinyllysineBy similarity
    Modified residuei365 – 3651N6-succinyllysineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Motif

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

    Sequence similaritiesi

    Belongs to the TPP enzyme family.Curated

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti447 – 4471Q → H in CAB60200. (PubMed:10468558)Curated
    Sequence conflicti543 – 5431R → E in CAB60200. (PubMed:10468558)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei77 – 10327Missing in isoform 2. 1 PublicationVSP_054191Add
    BLAST
    Alternative sequencei104 – 18582Missing in isoform 3. 1 PublicationVSP_054192Add
    BLAST
    Alternative sequencei128 – 15326Missing in isoform 4. CuratedVSP_054749Add
    BLAST
    Alternative sequencei332 – 36534Missing in isoform 4. CuratedVSP_054750Add
    BLAST

    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. [Q9UJ83-1]
    ENST00000451445; ENSP00000403656; ENSG00000131373. [Q9UJ83-3]
    ENST00000456194; ENSP00000390699; ENSG00000131373. [Q9UJ83-2]
    ENST00000457447; ENSP00000404883; ENSG00000131373. [Q9UJ83-4]
    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 . [Q9UJ83-1 ]
    ENST00000451445 ; ENSP00000403656 ; ENSG00000131373 . [Q9UJ83-3 ]
    ENST00000456194 ; ENSP00000390699 ; ENSG00000131373 . [Q9UJ83-2 ]
    ENST00000457447 ; ENSP00000404883 ; ENSG00000131373 . [Q9UJ83-4 ]
    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

    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: October 1, 2014
    This is version 120 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