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P68402 (PA1B2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. 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·Alt products·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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length229 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.

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.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P68402-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P68402-2)

The sequence of this isoform differs from the canonical sequence as follows:
     138-229: GLLPRGEKPN...TPEEKQTTIA → IIYWQDEQDYHERKVQMD
Isoform 3 (identifier: P68402-3)

The sequence of this isoform differs from the canonical sequence as follows:
     133-229: Missing.
Isoform 4 (identifier: P68402-4)

The sequence of this isoform differs from the canonical sequence as follows:
     139-229: LLPRGEKPNP...TPEEKQTTIA → KAAASKYSIS...KSRWTEEILH

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 229228Platelet-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 residue21N-acetylserine Ref.10 Ref.11 Ref.13
Modified residue21Phosphoserine Ref.11 Ref.13

Natural variations

Alternative sequence133 – 22997Missing in isoform 3.
VSP_043217
Alternative sequence138 – 22992GLLPR…QTTIA → IIYWQDEQDYHERKVQMD in isoform 2.
VSP_042896
Alternative sequence139 – 22991LLPRG…QTTIA → KAAASKYSISEIVRLEQGSV NWSIGTYPDDTPATTRPAIL QLFTGKMSRITMKEKSRWTE EILH in isoform 4.
VSP_044680

Experimental info

Isoform 4:
Sequence conflict1511V → M in ABI58227. Ref.2
Sequence conflict1511V → M in ABI58228. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [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

Isoform 2 [UniParc].

Checksum: A4AF3D6025CD9E43
Show »

FASTA15517,833
Isoform 3 [UniParc].

Checksum: 6663DB0A3B3202D7
Show »

FASTA13214,888
Isoform 4 [UniParc].

Checksum: 07A9CD88A4B99B35
Show »

FASTA20222,734

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Fetal liver.
[2]"Novel isoforms of intracellular platelet activating factor acetylhydrolase (PAFAH1b2) in human testis; encoded by alternatively spliced mRNAs."
Scott B.T., Olson N., Long G.L., Bovill E.G.
Prostaglandins Other Lipid Mediat. 85:69-80(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), ALTERNATIVE SPLICING.
Tissue: Testis.
[3]"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. expand/collapse author list , 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] (ISOFORM 1).
Tissue: Trachea.
[4]"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 (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton 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].
[8]"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] (ISOFORM 1).
Tissue: Lung.
[9]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 61-79, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[10]"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].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63390 mRNA. Translation: BAA19917.1.
DQ836738 mRNA. Translation: ABI58225.1.
DQ836739 mRNA. Translation: ABI58226.1.
DQ836740 mRNA. Translation: ABI58227.1.
DQ836741 mRNA. Translation: ABI58228.1.
DQ836742 mRNA. Translation: ABI58229.1.
DQ836743 mRNA. Translation: ABI58230.1.
AK292973 mRNA. Translation: BAF85662.1.
CR456736 mRNA. Translation: CAG33017.1.
EF445007 Genomic DNA. Translation: ACA06040.1.
AP005018 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67281.1.
BC000398 mRNA. Translation: AAH00398.1.
BC019301 mRNA. Translation: AAH19301.1.
PIRJC5409.
RefSeqNP_001171675.1. NM_001184746.1.
NP_001171676.1. NM_001184747.1.
NP_001171677.1. NM_001184748.1.
NP_002563.1. NM_002572.3.
UniGeneHs.728488.

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...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111086. 37 interactions.
IntActP68402. 15 interactions.
MINTMINT-5002700.
STRING9606.ENSP00000304006.

Chemistry

ChEMBLCHEMBL4463.

PTM databases

PhosphoSiteP68402.

Polymorphism databases

DMDM55977294.

2D gel databases

REPRODUCTION-2DPAGEIPI00026546.

Proteomic databases

PaxDbP68402.
PeptideAtlasP68402.
PRIDEP68402.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000419197; ENSP00000388742; ENSG00000168092. [P68402-3]
ENST00000527958; ENSP00000435289; ENSG00000168092. [P68402-1]
ENST00000529887; ENSP00000434951; ENSG00000168092. [P68402-2]
ENST00000530272; ENSP00000431365; ENSG00000168092. [P68402-4]
GeneID5049.
KEGGhsa:5049.
UCSCuc001pqe.2. human. [P68402-1]
uc009yzk.2. human. [P68402-2]

Organism-specific databases

CTD5049.
GeneCardsGC11P117014.
H-InvDBHIX0022939.
HGNCHGNC:8575. PAFAH1B2.
HPAHPA051836.
MIM602508. gene.
neXtProtNX_P68402.
PharmGKBPA32906.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69837.
HOGENOMHOG000232143.
HOVERGENHBG053477.
InParanoidP68402.
KOK16795.
OMANIRPKVV.
OrthoDBEOG7HB5BS.
PhylomeDBP68402.
TreeFamTF323955.

Gene expression databases

ArrayExpressP68402.
BgeeP68402.
CleanExHS_PAFAH1B2.
GenevestigatorP68402.

Family and domain databases

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

Other

ChiTaRSPAFAH1B2. human.
EvolutionaryTraceP68402.
GeneWikiPAFAH1B2.
GenomeRNAi5049.
NextBio19456.
PROP68402.
SOURCESearch...

Entry information

Entry namePA1B2_HUMAN
AccessionPrimary (citable) accession number: P68402
Secondary accession number(s): A8DPS5 expand/collapse secondary AC list , A8DPS6, A8DPS7, E9PEJ5, E9PLP3, O00687, Q29459, Q6IBR6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: April 16, 2014
This is version 109 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 11

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