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Protein

Platelet-activating factor acetylhydrolase IB subunit beta

Gene

PAFAH1B2

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.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei48By similarity1
Active sitei193By similarity1
Active sitei196By similarity1

GO - Molecular functioni

GO - Biological processi

  • brain development Source: GO_Central
  • lipid catabolic process Source: UniProtKB-KW
  • lipid metabolic process Source: ProtInc
  • neutrophil degranulation Source: Reactome
  • positive regulation of macroautophagy Source: BHF-UCL
  • spermatogenesis Source: Ensembl

Keywordsi

Molecular functionHydrolase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.47. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
SIGNORiP68402.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PAFAH1B2
Synonyms:PAFAHB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:8575. PAFAH1B2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: HPA
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • fibrillar center Source: HPA
  • ficolin-1-rich granule lumen Source: Reactome
  • nucleolus Source: HPA
  • plasma membrane Source: HPA
  • secretory granule lumen Source: Reactome

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi5049.
OpenTargetsiENSG00000168092.
PharmGKBiPA32906.

Chemistry databases

ChEMBLiCHEMBL4463.

Polymorphism and mutation databases

BioMutaiPAFAH1B2.
DMDMi55977294.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000581512 – 229Platelet-activating factor acetylhydrolase IB subunit betaAdd BLAST228

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei64PhosphoserineCombined sources1
Modified residuei220PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP68402.
PaxDbiP68402.
PeptideAtlasiP68402.
PRIDEiP68402.

2D gel databases

REPRODUCTION-2DPAGEiIPI00026546.

PTM databases

iPTMnetiP68402.
PhosphoSitePlusiP68402.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000168092.
CleanExiHS_PAFAH1B2.
ExpressionAtlasiP68402. baseline and differential.
GenevisibleiP68402. HS.

Organism-specific databases

HPAiHPA051836.

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
PAFAH1B3Q151025EBI-713724,EBI-711522

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111086. 53 interactors.
IntActiP68402. 18 interactors.
MINTiMINT-5002700.
STRINGi9606.ENSP00000435289.

Structurei

Secondary structure

1229
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 10Combined sources3
Beta strandi19 – 21Combined sources3
Helixi23 – 37Combined sources15
Beta strandi41 – 47Combined sources7
Helixi48 – 53Combined sources6
Helixi57 – 62Combined sources6
Helixi64 – 66Combined sources3
Beta strandi68 – 72Combined sources5
Helixi78 – 86Combined sources9
Turni87 – 90Combined sources4
Beta strandi96 – 101Combined sources6
Helixi111 – 128Combined sources18
Beta strandi133 – 137Combined sources5
Beta strandi143 – 145Combined sources3
Helixi148 – 163Combined sources16
Beta strandi164 – 167Combined sources4
Beta strandi170 – 173Combined sources4
Turni188 – 190Combined sources3
Beta strandi194 – 197Combined sources4
Helixi199 – 219Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VYHX-ray3.40A/B/E/F/I/J/M/N/Q/R1-229[»]
ProteinModelPortaliP68402.
SMRiP68402.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68402.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IMK6. Eukaryota.
ENOG410XPWQ. LUCA.
GeneTreeiENSGT00390000016520.
HOGENOMiHOG000232143.
HOVERGENiHBG053477.
InParanoidiP68402.
KOiK16795.
OMAiRGQQPNK.
OrthoDBiEOG091G0OII.
PhylomeDBiP68402.
TreeFamiTF323955.

Family and domain databases

InterProiView protein in InterPro
IPR013830. SGNH_hydro.
PfamiView protein in Pfam
PF13472. Lipase_GDSL_2. 1 hit.
SUPFAMiSSF52266. SSF52266. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P68402-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV
60 70 80 90 100
QLMQQYEIWR ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV
110 120 130 140 150
WVGTNNHENT AEEVAGGIEA IVQLINTRQP QAKIIVLGLL PRGEKPNPLR
160 170 180 190 200
QKNAKVNQLL KVSLPKLANV QLLDTDGGFV HSDGAISCHD MFDFLHLTGG
210 220
GYAKICKPLH ELIMQLLEET PEEKQTTIA
Length:229
Mass (Da):25,569
Last modified:November 23, 2004 - v1
Checksum:i14CF5D48621AA504
GO
Isoform 2 (identifier: P68402-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     138-229: GLLPRGEKPN...TPEEKQTTIA → IIYWQDEQDYHERKVQMD

Show »
Length:155
Mass (Da):17,833
Checksum:iA4AF3D6025CD9E43
GO
Isoform 3 (identifier: P68402-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     133-229: Missing.

Show »
Length:132
Mass (Da):14,888
Checksum:i6663DB0A3B3202D7
GO
Isoform 4 (identifier: P68402-4) [UniParc]FASTAAdd to basket

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

Show »
Length:202
Mass (Da):22,734
Checksum:i07A9CD88A4B99B35
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform 4 (identifier: P68402-4)
Sequence conflicti151V → M in ABI58227 (PubMed:18155631).Curated1
Sequence conflicti151V → M in ABI58228 (PubMed:18155631).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_043217133 – 229Missing in isoform 3. 1 PublicationAdd BLAST97
Alternative sequenceiVSP_042896138 – 229GLLPR…QTTIA → IIYWQDEQDYHERKVQMD in isoform 2. 1 PublicationAdd BLAST92
Alternative sequenceiVSP_044680139 – 229LLPRG…QTTIA → KAAASKYSISEIVRLEQGSV NWSIGTYPDDTPATTRPAIL QLFTGKMSRITMKEKSRWTE EILH in isoform 4. 1 PublicationAdd BLAST91

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS53713.1. [P68402-3]
CCDS53714.1. [P68402-4]
CCDS53715.1. [P68402-2]
CCDS8380.1. [P68402-1]
PIRiJC5409.
RefSeqiNP_001171675.1. NM_001184746.1. [P68402-4]
NP_001171676.1. NM_001184747.1. [P68402-2]
NP_001171677.1. NM_001184748.1. [P68402-3]
NP_001296360.1. NM_001309431.1.
NP_002563.1. NM_002572.3. [P68402-1]
UniGeneiHs.728488.

Genome annotation databases

EnsembliENST00000419197; ENSP00000388742; ENSG00000168092. [P68402-3]
ENST00000527958; ENSP00000435289; ENSG00000168092. [P68402-1]
ENST00000529887; ENSP00000434951; ENSG00000168092. [P68402-2]
ENST00000530272; ENSP00000431365; ENSG00000168092. [P68402-4]
GeneIDi5049.
KEGGihsa:5049.
UCSCiuc009yzk.3. human. [P68402-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiPA1B2_HUMAN
AccessioniPrimary (citable) accession number: P68402
Secondary accession number(s): A8DPS5
, A8DPS6, A8DPS7, E9PEJ5, E9PLP3, O00687, Q29459, Q6IBR6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: August 30, 2017
This is version 141 of the entry and version 1 of the sequence. See 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families