P68402 (PA1B2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	229 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Lipid degradation Lipid metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from electronic annotation. Source: Compara lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid metabolic process Traceable author statement Ref.1. Source: ProtInc positive regulation of macroautophagy Inferred from mutant phenotype PubMed 22354037. Source: BHF-UCL spermatogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Traceable author statement PubMed 16130169. Source: UniProtKB cytosol Inferred from electronic annotation. Source: Compara nucleolus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	1-alkyl-2-acetylglycerophosphocholine esterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.10

Chain

2 – 229

228

Platelet-activating factor acetylhydrolase IB subunit beta

PRO_0000058151

Sites

Active site

48

1

By similarity

Active site

193

1

By similarity

Active site

196

1

By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.10 Ref.12

Modified residue

2

1

Phosphoserine Ref.10 Ref.12

Natural variations

Alternative sequence

133 – 229

97

Missing in isoform 3.

VSP_043217

Alternative sequence

138 – 229

92

GLLPR…QTTIA → IIYWQDEQDYHERKVQMD in isoform 2.

VSP_042896

Alternative sequence

139 – 229

91

LLPRG…QTTIA → KAAASKYSISEIVRLEQGSV NWSIGTYPDDTPATTRPAIL QLFTGKMSRITMKEKSRWTE EILH in isoform 4.

VSP_044680

Experimental info

Isoform 4:

Sequence conflict

151

1

V → M in ABI58227. Ref.2

Sequence conflict

151

1

V → M in ABI58228. Ref.2

Secondary structure

1

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229

Helix Strand Turn

Details...

Helix

8 – 10

3

Beta strand

19 – 21

3

Helix

23 – 37

15

Beta strand

41 – 47

7

Helix

48 – 53

6

Helix

57 – 62

6

Helix

64 – 66

3

Beta strand

68 – 72

5

Helix

78 – 86

9

Turn

87 – 90

4

Beta strand

96 – 101

6

Helix

111 – 128

18

Beta strand

133 – 137

5

Beta strand

143 – 145

3

Helix

148 – 163

16

Beta strand

164 – 167

4

Beta strand

170 – 173

4

Turn

188 – 190

3

Beta strand

194 – 197

4

Helix

199 – 219

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 14CF5D48621AA504	FASTA	229	25,569
	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
	Isoform 2 [UniParc]. Checksum: A4AF3D6025CD9E43	FASTA	155	17,833
	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 IVQLINTRQP QAKIIVLIIY WQDEQDYHER KVQMD
	Isoform 3 [UniParc]. Checksum: 6663DB0A3B3202D7	FASTA	132	14,888
	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 IVQLINTRQP QA
	Isoform 4 [UniParc]. Checksum: 07A9CD88A4B99B35	FASTA	202	22,734
	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 QAKIIVLGKA AASKYSISEI VRLEQGSVNW SIGTYPDDTP ATTRPAILQL 190 200 FTGKMSRITM KEKSRWTEEI LH

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[10]	"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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"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, MASS SPECTROMETRY.
+	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.

IPI

IPI00026546.
IPI00976543.
IPI00980480.

PIR

JC5409.

RefSeq

NP_001171675.1. NM_001184746.1.
NP_001171676.1. NM_001184747.1.
NP_001171677.1. NM_001184748.1.
NP_002563.1. NM_002572.3.

UniGene

Hs.597488.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VYH	X-ray	3.40	A/B/E/F/I/J/M/N/Q/R	1-229	[»]

ProteinModelPortal

P68402.

ModBase

Search...

Protein-protein interaction databases

IntAct

P68402. 15 interactions.

MINT

MINT-5002700.

STRING

9606.ENSP00000304006.

PTM databases

PhosphoSite

P68402.

Polymorphism databases

DMDM

55977294.

2D gel databases

REPRODUCTION-2DPAGE

IPI00026546.

Proteomic databases

PaxDb

P68402.

PeptideAtlas

P68402.

PRIDE

P68402.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000419197; ENSP00000388742; ENSG00000168092.
ENST00000527958; ENSP00000435289; ENSG00000168092.
ENST00000529887; ENSP00000434951; ENSG00000168092.
ENST00000530272; ENSP00000431365; ENSG00000168092.

GeneID

5049.

KEGG

hsa:5049.

UCSC

uc001pqe.2. human.

Organism-specific databases

CTD

5049.

GeneCards

GC11P117048.

H-InvDB

HIX0022939.

HGNC

HGNC:8575. PAFAH1B2.

HPA

HPA051836.

MIM

602508. gene.

neXtProt

NX_P68402.

PharmGKB

PA32906.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG69837.

HOGENOM

HOG000232143.

HOVERGEN

HBG053477.

InParanoid

P68402.

KO

K16795.

OMA

LQQYEIW.

PhylomeDB

P68402.

Enzyme and pathway databases

Pathway_Interaction_DB

lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.

Gene expression databases

ArrayExpress

P68402.

Bgee

P68402.

CleanEx

HS_PAFAH1B2.

Genevestigator

P68402.

GermOnline

ENSG00000168092. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.1110. 1 hit.

InterPro

IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]

PROSITE

PS01098. LIPASE_GDSL_SER. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL4463.

ChiTaRS

PAFAH1B2. human.

EvolutionaryTrace

P68402.

GenomeRNAi

5049.

NextBio

19456.

SOURCE

Search...

Entry information

Entry name

PA1B2_HUMAN

Accession

Primary (citable) accession number: P68402
Secondary accession number(s): A8DPS5 , 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:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.