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P68402

- PA1B2_HUMAN

UniProt

P68402 - PA1B2_HUMAN

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Protein

Platelet-activating factor acetylhydrolase IB subunit beta

Gene

PAFAH1B2

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei48 – 481By similarity
Active sitei193 – 1931By similarity
Active sitei196 – 1961By similarity

GO - Molecular functioni

  1. 1-alkyl-2-acetylglycerophosphocholine esterase activity Source: UniProtKB-EC

GO - Biological processi

  1. brain development Source: Ensembl
  2. lipid catabolic process Source: UniProtKB-KW
  3. lipid metabolic process Source: ProtInc
  4. positive regulation of macroautophagy Source: BHF-UCL
  5. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

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
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:8575. PAFAH1B2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Ensembl
  3. extracellular vesicular exosome Source: UniProt
  4. nucleolus Source: HPA
  5. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32906.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 229228Platelet-activating factor acetylhydrolase IB subunit betaPRO_0000058151Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei2 – 21Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP68402.
PaxDbiP68402.
PeptideAtlasiP68402.
PRIDEiP68402.

2D gel databases

REPRODUCTION-2DPAGEIPI00026546.

PTM databases

PhosphoSiteiP68402.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiP68402.
CleanExiHS_PAFAH1B2.
ExpressionAtlasiP68402. baseline and differential.
GenevestigatoriP68402.

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.

Protein-protein interaction databases

BioGridi111086. 37 interactions.
IntActiP68402. 15 interactions.
MINTiMINT-5002700.
STRINGi9606.ENSP00000304006.

Structurei

Secondary structure

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103
Beta strandi19 – 213
Helixi23 – 3715
Beta strandi41 – 477
Helixi48 – 536
Helixi57 – 626
Helixi64 – 663
Beta strandi68 – 725
Helixi78 – 869
Turni87 – 904
Beta strandi96 – 1016
Helixi111 – 12818
Beta strandi133 – 1375
Beta strandi143 – 1453
Helixi148 – 16316
Beta strandi164 – 1674
Beta strandi170 – 1734
Turni188 – 1903
Beta strandi194 – 1974
Helixi199 – 21921

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VYHX-ray3.40A/B/E/F/I/J/M/N/Q/R1-229[»]
ProteinModelPortaliP68402.
SMRiP68402. Positions 6-217.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68402.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG69837.
GeneTreeiENSGT00390000016520.
HOGENOMiHOG000232143.
HOVERGENiHBG053477.
InParanoidiP68402.
KOiK16795.
OMAiNIRPKVV.
OrthoDBiEOG7HB5BS.
PhylomeDBiP68402.
TreeFamiTF323955.

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]

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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Isoform 4 (identifier: P68402-4)
Sequence conflicti151 – 1511V → M in ABI58227. (PubMed:18155631)Curated
Sequence conflicti151 – 1511V → M in ABI58228. (PubMed:18155631)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei133 – 22997Missing in isoform 3. 1 PublicationVSP_043217Add
BLAST
Alternative sequencei138 – 22992GLLPR…QTTIA → IIYWQDEQDYHERKVQMD in isoform 2. 1 PublicationVSP_042896Add
BLAST
Alternative sequencei139 – 22991LLPRG…QTTIA → KAAASKYSISEIVRLEQGSV NWSIGTYPDDTPATTRPAIL QLFTGKMSRITMKEKSRWTE EILH in isoform 4. 1 PublicationVSP_044680Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_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.
UCSCiuc001pqe.2. human. [P68402-1]
uc009yzk.2. human. [P68402-2]

Polymorphism databases

DMDMi55977294.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS53713.1. [P68402-3 ]
CCDS53714.1. [P68402-4 ]
CCDS53715.1. [P68402-2 ]
CCDS8380.1. [P68402-1 ]
PIRi JC5409.
RefSeqi NP_001171675.1. NM_001184746.1. [P68402-4 ]
NP_001171676.1. NM_001184747.1. [P68402-2 ]
NP_001171677.1. NM_001184748.1. [P68402-3 ]
NP_002563.1. NM_002572.3. [P68402-1 ]
UniGenei Hs.728488.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VYH X-ray 3.40 A/B/E/F/I/J/M/N/Q/R 1-229 [» ]
ProteinModelPortali P68402.
SMRi P68402. Positions 6-217.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111086. 37 interactions.
IntActi P68402. 15 interactions.
MINTi MINT-5002700.
STRINGi 9606.ENSP00000304006.

Chemistry

ChEMBLi CHEMBL4463.

PTM databases

PhosphoSitei P68402.

Polymorphism databases

DMDMi 55977294.

2D gel databases

REPRODUCTION-2DPAGE IPI00026546.

Proteomic databases

MaxQBi P68402.
PaxDbi P68402.
PeptideAtlasi P68402.
PRIDEi P68402.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000419197 ; ENSP00000388742 ; ENSG00000168092 . [P68402-3 ]
ENST00000527958 ; ENSP00000435289 ; ENSG00000168092 . [P68402-1 ]
ENST00000529887 ; ENSP00000434951 ; ENSG00000168092 . [P68402-2 ]
ENST00000530272 ; ENSP00000431365 ; ENSG00000168092 . [P68402-4 ]
GeneIDi 5049.
KEGGi hsa:5049.
UCSCi uc001pqe.2. human. [P68402-1 ]
uc009yzk.2. human. [P68402-2 ]

Organism-specific databases

CTDi 5049.
GeneCardsi GC11P117014.
H-InvDB HIX0022939.
HGNCi HGNC:8575. PAFAH1B2.
HPAi HPA051836.
MIMi 602508. gene.
neXtProti NX_P68402.
PharmGKBi PA32906.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG69837.
GeneTreei ENSGT00390000016520.
HOGENOMi HOG000232143.
HOVERGENi HBG053477.
InParanoidi P68402.
KOi K16795.
OMAi NIRPKVV.
OrthoDBi EOG7HB5BS.
PhylomeDBi P68402.
TreeFami TF323955.

Miscellaneous databases

ChiTaRSi PAFAH1B2. human.
EvolutionaryTracei P68402.
GeneWikii PAFAH1B2.
GenomeRNAii 5049.
NextBioi 19456.
PROi P68402.
SOURCEi Search...

Gene expression databases

Bgeei P68402.
CleanExi HS_PAFAH1B2.
ExpressionAtlasi P68402. baseline and differential.
Genevestigatori P68402.

Family and domain databases

Gene3Di 3.40.50.1110. 1 hit.
InterProi IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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. 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].

Entry informationi

Entry nameiPA1B2_HUMAN
AccessioniPrimary (citable) accession number: P68402
Secondary accession number(s): A8DPS5
, A8DPS6, A8DPS7, E9PEJ5, E9PLP3, O00687, Q29459, Q6IBR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: October 29, 2014
This is version 114 of the entry and version 1 of the sequence. [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

External Data

Dasty 3