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Protein

Platelet-activating factor acetylhydrolase IB subunit beta

Gene

PAFAH1B2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

EuPathDBiHostDB:ENSG00000168092.13
HGNCiHGNC:8575 PAFAH1B2
MIMi602508 gene
neXtProtiNX_P68402

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

BioGridi11108654 interactors.
IntActiP68402 25 interactors.
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

Gene3Di3.40.50.11101 hit
InterProiView protein in InterPro
IPR013830 SGNH_hydro
IPR036514 SGNH_hydro_sf
PfamiView protein in Pfam
PF13472 Lipase_GDSL_2, 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: March 28, 2018
This is version 145 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