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Q6Y1H2

- HACD2_HUMAN

UniProt

Q6Y1H2 - HACD2_HUMAN

Protein

Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2

Gene

PTPLB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Responsible for the dehydration step in very long-chain fatty acid (VLCFA) synthesis.1 Publication

    Catalytic activityi

    A very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain trans-2,3-dehydroacyl-CoA + H2O.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei176 – 1761By similarity
    Active sitei183 – 1831By similarity

    GO - Molecular functioni

    1. lyase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2 (EC:4.2.1.134)
    Alternative name(s):
    3-hydroxyacyl-CoA dehydratase 2
    Short name:
    HACD2
    Protein-tyrosine phosphatase-like member B
    Gene namesi
    Name:PTPLB
    Synonyms:HACD2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9640. PTPLB.

    Subcellular locationi

    Endoplasmic reticulum membrane 2 Publications; Multi-pass membrane protein 2 Publications

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33983.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 254253Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2PRO_0000349319Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    MaxQBiQ6Y1H2.
    PaxDbiQ6Y1H2.
    PRIDEiQ6Y1H2.

    PTM databases

    PhosphoSiteiQ6Y1H2.

    Expressioni

    Tissue specificityi

    Highly expressed in testis, spleen, prostate, colon and heart, followed by moderate expression in thymus, ovary, small intestine, peripheral blood leukocytes, liver, skeletal muscle and pancreas. Weakly detected in kidney, placenta, brain and lung.2 Publications

    Gene expression databases

    ArrayExpressiQ6Y1H2.
    BgeeiQ6Y1H2.
    CleanExiHS_PTPLB.
    GenevestigatoriQ6Y1H2.

    Organism-specific databases

    HPAiCAB019282.

    Interactioni

    Subunit structurei

    Interacts with the condensation enzymes of the ELOVL family. Interacts with BCAP31.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCAP31P515724EBI-530257,EBI-77683

    Protein-protein interaction databases

    BioGridi128393. 3 interactions.
    IntActiQ6Y1H2. 1 interaction.
    STRINGi9606.ENSP00000373153.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6Y1H2.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 4140CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini61 – 7919LumenalSequence AnalysisAdd
    BLAST
    Topological domaini98 – 10710CytoplasmicSequence Analysis
    Topological domaini126 – 1305LumenalSequence Analysis
    Topological domaini147 – 16923CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini188 – 21730LumenalSequence AnalysisAdd
    BLAST
    Topological domaini236 – 25419CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei42 – 6019HelicalSequence AnalysisAdd
    BLAST
    Transmembranei80 – 9718HelicalSequence AnalysisAdd
    BLAST
    Transmembranei108 – 12518HelicalSequence AnalysisAdd
    BLAST
    Transmembranei131 – 14616HelicalSequence AnalysisAdd
    BLAST
    Transmembranei170 – 18718HelicalSequence AnalysisAdd
    BLAST
    Transmembranei218 – 23518HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi12 – 187Poly-Gly

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5198.
    HOGENOMiHOG000190538.
    HOVERGENiHBG057518.
    InParanoidiQ6Y1H2.
    KOiK10703.
    OMAiVREVQSE.
    OrthoDBiEOG7X6M18.
    PhylomeDBiQ6Y1H2.
    TreeFamiTF313326.

    Family and domain databases

    InterProiIPR007482. Tyr_Pase-like_PTPLA.
    [Graphical view]
    PANTHERiPTHR11035. PTHR11035. 1 hit.
    PfamiPF04387. PTPLA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q6Y1H2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVAATAAA KGNGGGGGRA GAGDASGTRK KKGPGPLATA YLVIYNVVMT    50
    AGWLVIAVGL VRAYLAKGSY HSLYYSIEKP LKFFQTGALL EILHCAIGIV 100
    PSSVVLTSFQ VMSRVFLIWA VTHSVKEVQS EDSVLLFVIA WTITEIIRYS 150
    FYTFSLLNHL PYLIKWARYT LFIVLYPMGV SGELLTIYAA LPFVRQAGLY 200
    SISLPNKYNF SFDYYAFLIL IMISYIPIFP QLYFHMIHQR RKILSHTEEH 250
    KKFE 254
    Length:254
    Mass (Da):28,368
    Last modified:July 5, 2004 - v1
    Checksum:i6B301176C696899E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY191814 mRNA. Translation: AAP20101.1.
    AK289983 mRNA. Translation: BAF82672.1.
    AC020631 Genomic DNA. No translation available.
    AC023165 Genomic DNA. No translation available.
    AC025571 Genomic DNA. No translation available.
    AC084039 Genomic DNA. No translation available.
    BC049369 mRNA. Translation: AAH49369.1.
    BC060839 mRNA. Translation: AAH60839.1.
    CCDSiCCDS46895.1.
    RefSeqiNP_940684.1. NM_198402.3.
    UniGeneiHs.705480.

    Genome annotation databases

    EnsembliENST00000383657; ENSP00000373153; ENSG00000206527.
    GeneIDi201562.
    KEGGihsa:201562.
    UCSCiuc003egj.2. human.

    Polymorphism databases

    DMDMi74738322.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY191814 mRNA. Translation: AAP20101.1 .
    AK289983 mRNA. Translation: BAF82672.1 .
    AC020631 Genomic DNA. No translation available.
    AC023165 Genomic DNA. No translation available.
    AC025571 Genomic DNA. No translation available.
    AC084039 Genomic DNA. No translation available.
    BC049369 mRNA. Translation: AAH49369.1 .
    BC060839 mRNA. Translation: AAH60839.1 .
    CCDSi CCDS46895.1.
    RefSeqi NP_940684.1. NM_198402.3.
    UniGenei Hs.705480.

    3D structure databases

    ProteinModelPortali Q6Y1H2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128393. 3 interactions.
    IntActi Q6Y1H2. 1 interaction.
    STRINGi 9606.ENSP00000373153.

    PTM databases

    PhosphoSitei Q6Y1H2.

    Polymorphism databases

    DMDMi 74738322.

    Proteomic databases

    MaxQBi Q6Y1H2.
    PaxDbi Q6Y1H2.
    PRIDEi Q6Y1H2.

    Protocols and materials databases

    DNASUi 201562.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000383657 ; ENSP00000373153 ; ENSG00000206527 .
    GeneIDi 201562.
    KEGGi hsa:201562.
    UCSCi uc003egj.2. human.

    Organism-specific databases

    CTDi 201562.
    GeneCardsi GC03M123209.
    HGNCi HGNC:9640. PTPLB.
    HPAi CAB019282.
    neXtProti NX_Q6Y1H2.
    PharmGKBi PA33983.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5198.
    HOGENOMi HOG000190538.
    HOVERGENi HBG057518.
    InParanoidi Q6Y1H2.
    KOi K10703.
    OMAi VREVQSE.
    OrthoDBi EOG7X6M18.
    PhylomeDBi Q6Y1H2.
    TreeFami TF313326.

    Miscellaneous databases

    GenomeRNAii 201562.
    NextBioi 90164.
    PROi Q6Y1H2.

    Gene expression databases

    ArrayExpressi Q6Y1H2.
    Bgeei Q6Y1H2.
    CleanExi HS_PTPLB.
    Genevestigatori Q6Y1H2.

    Family and domain databases

    InterProi IPR007482. Tyr_Pase-like_PTPLA.
    [Graphical view ]
    PANTHERi PTHR11035. PTHR11035. 1 hit.
    Pfami PF04387. PTPLA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The yeast split-ubiquitin membrane protein two-hybrid screen identifies BAP31 as a regulator of the turnover of endoplasmic reticulum-associated protein tyrosine phosphatase-like B."
      Wang B., Pelletier J., Massaad M.J., Herscovics A., Shore G.C.
      Mol. Cell. Biol. 24:2767-2778(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH BCAP31.
    2. "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].
    3. "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].
    4. "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].
      Tissue: Brain and Testis.
    5. "Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved in very long-chain fatty acid synthesis."
      Ikeda M., Kanao Y., Yamanaka M., Sakuraba H., Mizutani Y., Igarashi Y., Kihara A.
      FEBS Lett. 582:2435-2440(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INTERACTION WITH ELOVL FAMILY.
    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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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 nameiHACD2_HUMAN
    AccessioniPrimary (citable) accession number: Q6Y1H2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 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

    Miscellaneous

    Turns over rapidly through degradation by the proteasome system.

    Caution

    Shares some similarity with tyrosine phosphatase proteins but it has probably no phosphatase activity.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3