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Protein

Platelet-activating factor acetylhydrolase IB subunit gamma

Gene

PAFAH1B3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. platelet-activating factor acetyltransferase activity Source: GO_Central

GO - Biological processi

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

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. cytoplasm Source: GO_Central
  2. cytosol Source: Ensembl
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB
Complete GO annotation...

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

BgeeiQ15102.
CleanExiHS_PAFAH1B3.
ExpressionAtlasiQ15102. baseline and differential.
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. 42 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.
GeneTreeiENSGT00390000016520.
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

        10         20         30         40         50
MSGEENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ
60 70 80 90 100
LMHQCEIWRE LFSPLHALNF GIGGDGTQHV LWRLENGELE HIRPKIVVVW
110 120 130 140 150
VGTNNHGHTA EQVTGGIKAI VQLVNERQPQ ARVVVLGLLP RGQHPNPLRE
160 170 180 190 200
KNRQVNELVR AALAGHPRAH FLDADPGFVH SDGTISHHDM YDYLHLSRLG
210 220 230
YTPVCRALHS LLLRLLAQDQ GQGAPLLEPA P
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi111087. 42 interactions.
IntActiQ15102. 32 interactions.
MINTiMINT-1368260.
STRINGi9606.ENSP00000262890.

Chemistry

ChEMBLiCHEMBL5108.

PTM databases

PhosphoSiteiQ15102.

Polymorphism databases

DMDMi3024344.

2D gel databases

REPRODUCTION-2DPAGEIPI00014808.

Proteomic databases

MaxQBiQ15102.
PaxDbiQ15102.
PeptideAtlasiQ15102.
PRIDEiQ15102.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5050.
GeneCardsiGC19M042801.
HGNCiHGNC:8576. PAFAH1B3.
HPAiHPA035639.
MIMi603074. gene.
neXtProtiNX_Q15102.
PharmGKBiPA32907.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG69837.
GeneTreeiENSGT00390000016520.
HOGENOMiHOG000232143.
HOVERGENiHBG053477.
InParanoidiQ15102.
KOiK16795.
OMAiFAPLHCL.
OrthoDBiEOG7HB5BS.
PhylomeDBiQ15102.
TreeFamiTF323955.

Miscellaneous databases

ChiTaRSiPAFAH1B3. human.
GeneWikiiPAFAH1B3.
GenomeRNAii5050.
NextBioi19460.
PROiQ15102.
SOURCEiSearch...

Gene expression databases

BgeeiQ15102.
CleanExiHS_PAFAH1B3.
ExpressionAtlasiQ15102. baseline and differential.
GenevestigatoriQ15102.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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: March 4, 2015
This is version 137 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.