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Q15102

- PA1B3_HUMAN

UniProt

Q15102 - PA1B3_HUMAN

Protein

Platelet-activating factor acetylhydrolase IB subunit gamma

Gene

PAFAH1B3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Inactivates paf by removing the acetyl group at the sn-2 position. This is a catalytic subunit. Plays an important role during the development of brain.

    Catalytic activityi

    1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei47 – 471By similarity
    Active sitei192 – 1921By similarity
    Active sitei195 – 1951By similarity

    GO - Molecular functioni

    1. 1-alkyl-2-acetylglycerophosphocholine esterase activity Source: UniProtKB-EC
    2. protein binding Source: IntAct

    GO - Biological processi

    1. brain development Source: Ensembl
    2. lipid catabolic process Source: UniProtKB-KW
    3. lipid metabolic process Source: ProtInc
    4. nervous system development Source: ProtInc
    5. spermatogenesis Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet-activating factor acetylhydrolase IB subunit gamma (EC:3.1.1.47)
    Alternative name(s):
    PAF acetylhydrolase 29 kDa subunit
    Short name:
    PAF-AH 29 kDa subunit
    PAF-AH subunit gamma
    Short name:
    PAFAH subunit gamma
    Gene namesi
    Name:PAFAH1B3
    Synonyms:PAFAHG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:8576. PAFAH1B3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32907.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 231230Platelet-activating factor acetylhydrolase IB subunit gammaPRO_0000058155Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ15102.
    PaxDbiQ15102.
    PeptideAtlasiQ15102.
    PRIDEiQ15102.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00014808.

    PTM databases

    PhosphoSiteiQ15102.

    Expressioni

    Tissue specificityi

    In the adult, expressed in brain, skeletal muscle, kidney, thymus, spleen, colon, testis, ovary and peripheral blood leukocytes. In the fetus, highest expression occurs in brain.

    Gene expression databases

    ArrayExpressiQ15102.
    BgeeiQ15102.
    CleanExiHS_PAFAH1B3.
    GenevestigatoriQ15102.

    Organism-specific databases

    HPAiHPA035639.

    Interactioni

    Subunit structurei

    Cytosolic PAF-AH IB is formed of three subunits of 45 kDa (alpha), 30 kDa (beta) and 29 kDa (gamma). The catalytic activity of the enzyme resides in the beta and gamma subunits, whereas the alpha subunit has regulatory activity. Trimer formation is not essential for the catalytic activity.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LNX1Q8TBB12EBI-711522,EBI-739832

    Protein-protein interaction databases

    BioGridi111087. 41 interactions.
    IntActiQ15102. 32 interactions.
    MINTiMINT-1368260.
    STRINGi9606.ENSP00000262890.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15102.
    SMRiQ15102. Positions 5-207.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG69837.
    HOGENOMiHOG000232143.
    HOVERGENiHBG053477.
    InParanoidiQ15102.
    KOiK16795.
    OMAiFAPLHCL.
    OrthoDBiEOG7HB5BS.
    PhylomeDBiQ15102.
    TreeFamiTF323955.

    Family and domain databases

    Gene3Di3.40.50.1110. 1 hit.
    InterProiIPR013831. SGNH_hydro-type_esterase_dom.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q15102-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGEENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ    50
    LMHQCEIWRE LFSPLHALNF GIGGDGTQHV LWRLENGELE HIRPKIVVVW 100
    VGTNNHGHTA EQVTGGIKAI VQLVNERQPQ ARVVVLGLLP RGQHPNPLRE 150
    KNRQVNELVR AALAGHPRAH FLDADPGFVH SDGTISHHDM YDYLHLSRLG 200
    YTPVCRALHS LLLRLLAQDQ GQGAPLLEPA P 231
    Length:231
    Mass (Da):25,734
    Last modified:November 1, 1996 - v1
    Checksum:i58A4CB8E7076AE23
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti214 – 2141R → G.
    Corresponds to variant rs1043818 [ dbSNP | Ensembl ].
    VAR_051261

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63391 mRNA. Translation: BAA09706.1.
    CR407626 mRNA. Translation: CAG28554.1.
    AC006486 Genomic DNA. Translation: AAD11989.1.
    CH471126 Genomic DNA. Translation: EAW57122.1.
    BC003016 mRNA. Translation: AAH03016.1.
    BC007863 mRNA. Translation: AAH07863.1.
    CCDSiCCDS12602.1.
    PIRiJC4246.
    RefSeqiNP_001139411.1. NM_001145939.1.
    NP_001139412.1. NM_001145940.1.
    NP_002564.1. NM_002573.3.
    UniGeneiHs.466831.

    Genome annotation databases

    EnsembliENST00000262890; ENSP00000262890; ENSG00000079462.
    ENST00000538771; ENSP00000444935; ENSG00000079462.
    GeneIDi5050.
    KEGGihsa:5050.
    UCSCiuc002otg.2. human.

    Polymorphism databases

    DMDMi3024344.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63391 mRNA. Translation: BAA09706.1 .
    CR407626 mRNA. Translation: CAG28554.1 .
    AC006486 Genomic DNA. Translation: AAD11989.1 .
    CH471126 Genomic DNA. Translation: EAW57122.1 .
    BC003016 mRNA. Translation: AAH03016.1 .
    BC007863 mRNA. Translation: AAH07863.1 .
    CCDSi CCDS12602.1.
    PIRi JC4246.
    RefSeqi NP_001139411.1. NM_001145939.1.
    NP_001139412.1. NM_001145940.1.
    NP_002564.1. NM_002573.3.
    UniGenei Hs.466831.

    3D structure databases

    ProteinModelPortali Q15102.
    SMRi Q15102. Positions 5-207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111087. 41 interactions.
    IntActi Q15102. 32 interactions.
    MINTi MINT-1368260.
    STRINGi 9606.ENSP00000262890.

    Chemistry

    ChEMBLi CHEMBL5108.

    PTM databases

    PhosphoSitei Q15102.

    Polymorphism databases

    DMDMi 3024344.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00014808.

    Proteomic databases

    MaxQBi Q15102.
    PaxDbi Q15102.
    PeptideAtlasi Q15102.
    PRIDEi Q15102.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262890 ; ENSP00000262890 ; ENSG00000079462 .
    ENST00000538771 ; ENSP00000444935 ; ENSG00000079462 .
    GeneIDi 5050.
    KEGGi hsa:5050.
    UCSCi uc002otg.2. human.

    Organism-specific databases

    CTDi 5050.
    GeneCardsi GC19M042801.
    HGNCi HGNC:8576. PAFAH1B3.
    HPAi HPA035639.
    MIMi 603074. gene.
    neXtProti NX_Q15102.
    PharmGKBi PA32907.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG69837.
    HOGENOMi HOG000232143.
    HOVERGENi HBG053477.
    InParanoidi Q15102.
    KOi K16795.
    OMAi FAPLHCL.
    OrthoDBi EOG7HB5BS.
    PhylomeDBi Q15102.
    TreeFami TF323955.

    Miscellaneous databases

    GeneWikii PAFAH1B3.
    GenomeRNAii 5050.
    NextBioi 19460.
    PROi Q15102.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15102.
    Bgeei Q15102.
    CleanExi HS_PAFAH1B3.
    Genevestigatori Q15102.

    Family and domain databases

    Gene3Di 3.40.50.1110. 1 hit.
    InterProi IPR013831. SGNH_hydro-type_esterase_dom.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of human cytosolic platelet-activating factor acetylhydrolase gamma-subunit and its mRNA expression in human tissues."
      Adachi H., Tsujimoto M., Hattori M., Arai H., Inoue K.
      Biochem. Biophys. Res. Commun. 214:180-187(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal liver.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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].
      Tissue: Lung and Uterus.
    6. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 84-127; 133-141 AND 199-231, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    7. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPA1B3_HUMAN
    AccessioniPrimary (citable) accession number: Q15102
    Secondary accession number(s): Q53X88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 132 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3