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Q15102 (PA1B3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PAFAH1B3
Synonyms:PAFAHG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length231 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Plays an important role during the development of brain.

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

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.

Sequence similarities

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LNX1Q8TBB12EBI-711522,EBI-739832

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 231230Platelet-activating factor acetylhydrolase IB subunit gamma
PRO_0000058155

Sites

Active site471 By similarity
Active site1921 By similarity
Active site1951 By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.7 Ref.9 Ref.10

Natural variations

Natural variant2141R → G.
Corresponds to variant rs1043818 [ dbSNP | Ensembl ].
VAR_051261

Sequences

Sequence LengthMass (Da)Tools
Q15102 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 58A4CB8E7076AE23

FASTA23125,734
        10         20         30         40         50         60 
MSGEENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ LMHQCEIWRE 

        70         80         90        100        110        120 
LFSPLHALNF GIGGDGTQHV LWRLENGELE HIRPKIVVVW VGTNNHGHTA EQVTGGIKAI 

       130        140        150        160        170        180 
VQLVNERQPQ ARVVVLGLLP RGQHPNPLRE KNRQVNELVR AALAGHPRAH FLDADPGFVH 

       190        200        210        220        230 
SDGTISHHDM YDYLHLSRLG YTPVCRALHS LLLRLLAQDQ GQGAPLLEPA P 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"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] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC4246.
RefSeqNP_001139411.1. NM_001145939.1.
NP_001139412.1. NM_001145940.1.
NP_002564.1. NM_002573.3.
UniGeneHs.466831.

3D structure databases

ProteinModelPortalQ15102.
SMRQ15102. Positions 5-207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111087. 41 interactions.
IntActQ15102. 32 interactions.
MINTMINT-1368260.
STRING9606.ENSP00000262890.

Chemistry

ChEMBLCHEMBL5108.

PTM databases

PhosphoSiteQ15102.

Polymorphism databases

DMDM3024344.

2D gel databases

REPRODUCTION-2DPAGEIPI00014808.

Proteomic databases

PaxDbQ15102.
PeptideAtlasQ15102.
PRIDEQ15102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262890; ENSP00000262890; ENSG00000079462.
ENST00000538771; ENSP00000444935; ENSG00000079462.
GeneID5050.
KEGGhsa:5050.
UCSCuc002otg.2. human.

Organism-specific databases

CTD5050.
GeneCardsGC19M042801.
HGNCHGNC:8576. PAFAH1B3.
HPAHPA035639.
MIM603074. gene.
neXtProtNX_Q15102.
PharmGKBPA32907.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69837.
HOGENOMHOG000232143.
HOVERGENHBG053477.
InParanoidQ15102.
KOK16795.
OMAFAPLHCL.
OrthoDBEOG7HB5BS.
PhylomeDBQ15102.
TreeFamTF323955.

Gene expression databases

ArrayExpressQ15102.
BgeeQ15102.
CleanExHS_PAFAH1B3.
GenevestigatorQ15102.

Family and domain databases

Gene3D3.40.50.1110. 1 hit.
InterProIPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPAFAH1B3.
GenomeRNAi5050.
NextBio19460.
PROQ15102.
SOURCESearch...

Entry information

Entry namePA1B3_HUMAN
AccessionPrimary (citable) accession number: Q15102
Secondary accession number(s): Q53X88
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 127 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM