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P68402 (PA1B2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Platelet-activating factor acetylhydrolase IB subunit beta

EC=3.1.1.47
Alternative name(s):
PAF acetylhydrolase 30 kDa subunit
Short name=PAF-AH 30 kDa subunit
PAF-AH subunit beta
Short name=PAFAH subunit beta
Gene names
Name:PAFAH1B2
Synonyms:PAFAHB
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit.

Catalytic activity

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

Subunit structure

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.

Subcellular location

Cytoplasm.

Tissue specificity

Ubiquitous. Ref.1

Sequence similarities

Belongs to the 'GDSL' lipolytic enzyme family. Platelet-activating factor acetylhydrolase IB beta/gamma subunits subfamily.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentCytoplasm
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Traceable author statement. Source: UniProtKB

   Molecular function1-alkyl-2-acetylglycerophosphocholine esterase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 229229Platelet-activating factor acetylhydrolase IB subunit beta
PRO_0000058151

Sites

Active site481 By similarity
Active site1931 By similarity
Active site1961 By similarity

Amino acid modifications

Modified residue21Phosphoserine Ref.4

Secondary structure

...................................... 229
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68402 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 14CF5D48621AA504

FASTA22925,569
        10         20         30         40         50         60 
MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV QLMQQYEIWR 

        70         80         90        100        110        120 
ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV WVGTNNHENT AEEVAGGIEA 

       130        140        150        160        170        180 
IVQLINTRQP QAKIIVLGLL PRGEKPNPLR QKNAKVNQLL KVSLPKLANV QLLDTDGGFV 

       190        200        210        220 
HSDGAISCHD MFDFLHLTGG GYAKICKPLH ELIMQLLEET PEEKQTTIA 

« Hide

References

« Hide 'large scale' references
[1]"Differential tissue distribution of the beta- and gamma-subunits of human cytosolic platelet-activating factor acetylhydrolase (isoform I)."
Adachi H., Tsujimoto M., Hattori M., Arai H., Inoue K.
Biochem. Biophys. Res. Commun. 233:10-13(1997) [PubMed: 9144386] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Fetal liver.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[3]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 61-79, MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[4]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63390 mRNA. Translation: BAA19917.1.
BC000398 mRNA. Translation: AAH00398.1.
BC019301 mRNA. Translation: AAH19301.1.
IPIIPI00026546.
PIRJC5409.
RefSeqNP_001171677.1. NM_001184748.1.
NP_002563.1. NM_002572.3.
UniGeneHs.597488.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VYHX-ray3.40A/B/E/F/I/J/M/N/Q/R1-229[»]
ProteinModelPortalP68402.
SMRP68402. Positions 6-217.
ModBaseSearch...

Protein-protein interaction databases

IntActP68402. 14 interactions.
MINTMINT-5002700.
STRINGP68402.

PTM databases

PhosphoSiteP68402.

Polymorphism databases

DMDM55977294.

2D gel databases

REPRODUCTION-2DPAGEIPI00026546.

Proteomic databases

PeptideAtlasP68402.
PRIDEP68402.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304808; ENSP00000304006; ENSG00000168092.
GeneID5049.
KEGGhsa:5049.
UCSCuc001pqe.1. human.

Organism-specific databases

CTD5049.
GeneCardsGC11P117048.
H-InvDBHIX0010160.
HIX0022939.
HGNCHGNC:8575. PAFAH1B2.
MIM602508. gene.
neXtProtNX_P68402.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG09501.
HOGENOMHBG715888.
HOVERGENHBG053477.
InParanoidP68402.
OMARFVQECK.
PhylomeDBP68402.

Enzyme and pathway databases

Pathway_Interaction_DBlis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.

Gene expression databases

ArrayExpressP68402.
BgeeP68402.
CleanExHS_PAFAH1B2.
GenevestigatorP68402.
GermOnlineENSG00000168092. Homo sapiens.

Family and domain databases

InterProIPR013830. Esterase_SGNH_hydro-type.
IPR013831. Esterase_SGNH_hydro-type_subgr.
IPR001087. Lipase_GDSL.
[Graphical view]
Gene3DG3DSA:3.40.50.1110. Esterase_SGNH_hydro-type_subgr. 1 hit.
KOK01062.
PfamPF00657. Lipase_GDSL. 1 hit.
[Graphical view]
SUPFAMSSF52266. Esterase_SGNH_hydro-type. 1 hit.
PROSITEPS01098. LIPASE_GDSL_SER. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio19456.
SOURCESearch...

Entry information

Entry namePA1B2_HUMAN
AccessionPrimary (citable) accession number: P68402
Secondary accession number(s): O00687, Q29459
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families