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Phospholipase A-2-activating protein (PLA2P) (PLAP)

 PLAP_HUMAN              Reviewed;         795 AA.
Q9Y263; Q53EU5; Q5VY33; Q9NUL8; Q9NVE9; Q9UF53; Q9Y5L1;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
13-JUN-2006, sequence version 2.
12-SEP-2018, entry version 169.
RecName: Full=Phospholipase A-2-activating protein;
Short=PLA2P;
Short=PLAP;
Name=PLAA; Synonyms=PLAP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-795.
PubMed=10644453; DOI=10.1006/geno.1999.5999;
Beatty B., Qi S., Pienkowska M., Scherer S.W., Testa J.R., Cheng J.Q.,
Herbrick J.-A., Scheidl T., Zhang Z., Kola I., Seth A.;
"Chromosomal localization of phospholipase A2 activating protein, an
ets2 target gene, to 9p21.";
Genomics 62:529-532(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-795.
TISSUE=Kidney;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 49-795.
TISSUE=Fetal brain;
PubMed=10571045; DOI=10.1016/S0378-1119(99)00354-6;
Ruiz A., Nadal M., Puig S., Estivill X.;
"Cloning of the human phospholipase A2 activating protein (hPLAP) gene
on the chromosome 9p21 melanoma deleted region.";
Gene 239:155-161(1999).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 58-795.
PubMed=9931468; DOI=10.1016/S0167-4781(98)00249-8;
Chopra A.K., Ribardo D.A., Wood T.G., Prusak D.J., Xu X.-J.,
Peterson J.W.;
"Molecular characterization of cDNA for phospholipase A2-activating
protein.";
Biochim. Biophys. Acta 1444:125-130(1999).
[9]
FUNCTION, AND INDUCTION.
PubMed=18291623; DOI=10.1016/j.cellsig.2008.01.004;
Zhang F., Sha J., Wood T.G., Galindo C.L., Garner H.R., Burkart M.F.,
Suarez G., Sierra J.C., Agar S.L., Peterson J.W., Chopra A.K.;
"Alteration in the activation state of new inflammation-associated
targets by phospholipase A2-activating protein (PLAA).";
Cell. Signal. 20:844-861(2008).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-529, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
FUNCTION, INTERACTION WITH UBXN6; VCP AND YOD1, AND SUBCELLULAR
LOCATION.
PubMed=27753622; DOI=10.15252/embj.201695148;
Papadopoulos C., Kirchner P., Bug M., Grum D., Koerver L., Schulze N.,
Poehler R., Dressler A., Fengler S., Arhzaouy K., Lux V., Ehrmann M.,
Weihl C.C., Meyer H.;
"VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of
ruptured lysosomes by autophagy.";
EMBO J. 36:135-150(2017).
[14]
STRUCTURE BY NMR OF 386-465, AND INTERACTION WITH UBIQUITIN.
PubMed=19423704; DOI=10.1074/jbc.M109.009126;
Fu Q.-S., Zhou C.-J., Gao H.-C., Jiang Y.-J., Zhou Z.-R., Hong J.,
Yao W.-M., Song A.-X., Lin D.-H., Hu H.-Y.;
"Structural basis for ubiquitin recognition by a novel domain from
human phospholipase A2-activating protein.";
J. Biol. Chem. 284:19043-19052(2009).
[15]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 511-795 IN COMPLEX WITH VCP,
AND DOMAIN ARM REPEATS.
PubMed=19887378; DOI=10.1074/jbc.M109.044685;
Qiu L., Pashkova N., Walker J.R., Winistorfer S., Allali-Hassani A.,
Akutsu M., Piper R., Dhe-Paganon S.;
"Structure and function of the PLAA/Ufd3-p97/Cdc48 complex.";
J. Biol. Chem. 285:365-372(2010).
[16]
VARIANT NDMSBA VAL-23, CHARACTERIZATION OF VARIANT NDMSBA VAL-23, AND
INVOLVEMENT IN NDMSBA.
PubMed=28413018; DOI=10.1016/j.ajhg.2017.03.008;
Hall E.A., Nahorski M.S., Murray L.M., Shaheen R., Perkins E.,
Dissanayake K.N., Kristaryanto Y., Jones R.A., Vogt J., Rivagorda M.,
Handley M.T., Mali G.R., Quidwai T., Soares D.C., Keighren M.A.,
McKie L., Mort R.L., Gammoh N., Garcia-Munoz A., Davey T.,
Vermeren M., Walsh D., Budd P., Aligianis I.A., Faqeih E.,
Quigley A.J., Jackson I.J., Kulathu Y., Jackson M., Ribchester R.R.,
von Kriegsheim A., Alkuraya F.S., Woods C.G., Maher E.R., Mill P.;
"PLAA mutations cause a lethal infantile epileptic encephalopathy by
disrupting ubiquitin-mediated endolysosomal degradation of synaptic
proteins.";
Am. J. Hum. Genet. 100:706-724(2017).
[17]
VARIANT NDMSBA PHE-752, CHARACTERIZATION OF VARIANT NDMSBA PHE-752,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=28007986; DOI=10.1093/brain/aww295;
Falik Zaccai T.C., Savitzki D., Zivony-Elboum Y., Vilboux T.,
Fitts E.C., Shoval Y., Kalfon L., Samra N., Keren Z., Gross B.,
Chasnyk N., Straussberg R., Mullikin J.C., Teer J.K., Geiger D.,
Kornitzer D., Bitterman-Deutsch O., Samson A.O., Wakamiya M.,
Peterson J.W., Kirtley M.L., Pinchuk I.V., Baze W.B., Gahl W.A.,
Kleta R., Anikster Y., Chopra A.K.;
"Phospholipase A2-activating protein is associated with a novel form
of leukoencephalopathy.";
Brain 140:370-386(2017).
-!- FUNCTION: Plays a role in protein ubiquitination, sorting and
degradation through its association with VCP (PubMed:27753622).
Involved in ubiquitin-mediated membrane proteins trafficking to
late endosomes in an ESCRT-dependent manner, and hence plays a
role in synaptic vesicle recycling (By similarity). May play a
role in macroautophagy, regulating for instance the clearance of
damaged lysosomes (PubMed:27753622). Plays a role in cerebellar
Purkinje cell development (By similarity). Positively regulates
cytosolic and calcium-independent phospholipase A2 activities in a
tumor necrosis factor alpha (TNF-alpha)- or lipopolysaccharide
(LPS)-dependent manner, and hence prostaglandin E2 biosynthesis
(PubMed:18291623, PubMed:28007986). {ECO:0000250|UniProtKB:P27612,
ECO:0000269|PubMed:18291623, ECO:0000269|PubMed:27753622,
ECO:0000269|PubMed:28007986}.
-!- SUBUNIT: Interacts with ubiquitin (PubMed:19423704). Interacts
with UBXN6, VCP and YOD1; may form a complex involved in
macroautophagy (PubMed:27753622, PubMed:19887378).
{ECO:0000269|PubMed:19423704, ECO:0000269|PubMed:19887378,
ECO:0000269|PubMed:27753622}.
-!- INTERACTION:
Q76353:- (xeno); NbExp=3; IntAct=EBI-1994037, EBI-6248077;
V9HW80:HEL-S-70; NbExp=3; IntAct=EBI-1994037, EBI-10175326;
O00629:KPNA4; NbExp=3; IntAct=EBI-1994037, EBI-396343;
Q04323:UBXN1; NbExp=5; IntAct=EBI-1994037, EBI-1058647;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28007986}.
Cytoplasm {ECO:0000269|PubMed:27753622,
ECO:0000269|PubMed:28007986}. Cell junction, synapse
{ECO:0000250|UniProtKB:P27612}. Note=Recruited to damaged
lysosomes decorated with K48-linked ubiquitin chains.
{ECO:0000269|PubMed:27753622}.
-!- INDUCTION: Up-regulated by tumor necrosis factor alpha (TNF-alpha)
(at protein level) (PubMed:18291623).
{ECO:0000269|PubMed:18291623}.
-!- DOMAIN: The PUL domain is composed of 6 armadillo-like repeats and
mediates the interaction with VCP C-terminus.
{ECO:0000269|PubMed:19887378}.
-!- DOMAIN: The PFU domain mediates interaction with ubiquitin.
{ECO:0000269|PubMed:19887378}.
-!- DISEASE: Neurodevelopmental disorder with progressive
microcephaly, spasticity, and brain anomalies (NDMSBA)
[MIM:617527]: An autosomal recessive neurodevelopmental disorder
characterized by progressive microcephaly, spastic quadriparesis,
global developmental delay, profound mental retardation and
severely impaired or absent motor function. More variable features
include seizures and optic atrophy. {ECO:0000269|PubMed:28007986,
ECO:0000269|PubMed:28413018}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the WD repeat PLAP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD03030.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAD42075.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAD42075.1; Type=Frameshift; Positions=698; Evidence={ECO:0000305};
Sequence=BAA92105.1; Type=Erroneous termination; Positions=545; Note=Translated as Gln.; Evidence={ECO:0000305};
Sequence=BAD97264.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB42881.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AK001642; BAA91803.1; -; mRNA.
EMBL; AK002143; BAA92105.1; ALT_SEQ; mRNA.
EMBL; AL133608; CAB63739.1; -; mRNA.
EMBL; AL356133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC032551; AAH32551.1; -; mRNA.
EMBL; AF145020; AAD42075.1; ALT_SEQ; mRNA.
EMBL; AK223544; BAD97264.1; ALT_INIT; mRNA.
EMBL; AJ238243; CAB42881.1; ALT_INIT; mRNA.
EMBL; AF083395; AAD03030.1; ALT_INIT; mRNA.
CCDS; CCDS35000.1; -.
PIR; T43447; T43447.
RefSeq; NP_001026859.1; NM_001031689.2.
UniGene; Hs.27182; -.
PDB; 2K89; NMR; -; A=386-465.
PDB; 2K8A; NMR; -; A=386-465.
PDB; 2K8B; NMR; -; B=386-465.
PDB; 2K8C; NMR; -; B=386-465.
PDB; 3EBB; X-ray; 1.90 A; A/B/C/D=511-795.
PDBsum; 2K89; -.
PDBsum; 2K8A; -.
PDBsum; 2K8B; -.
PDBsum; 2K8C; -.
PDBsum; 3EBB; -.
ProteinModelPortal; Q9Y263; -.
SMR; Q9Y263; -.
BioGrid; 114774; 42.
IntAct; Q9Y263; 16.
MINT; Q9Y263; -.
STRING; 9606.ENSP00000380460; -.
BindingDB; Q9Y263; -.
ChEMBL; CHEMBL6114; -.
iPTMnet; Q9Y263; -.
PhosphoSitePlus; Q9Y263; -.
BioMuta; PLAA; -.
DMDM; 108935868; -.
EPD; Q9Y263; -.
MaxQB; Q9Y263; -.
PaxDb; Q9Y263; -.
PeptideAtlas; Q9Y263; -.
PRIDE; Q9Y263; -.
ProteomicsDB; 85667; -.
DNASU; 9373; -.
Ensembl; ENST00000397292; ENSP00000380460; ENSG00000137055.
GeneID; 9373; -.
KEGG; hsa:9373; -.
UCSC; uc003zqd.4; human.
CTD; 9373; -.
DisGeNET; 9373; -.
EuPathDB; HostDB:ENSG00000137055.14; -.
GeneCards; PLAA; -.
HGNC; HGNC:9043; PLAA.
HPA; CAB005035; -.
HPA; HPA020994; -.
HPA; HPA020996; -.
MalaCards; PLAA; -.
MIM; 603873; gene.
MIM; 617527; phenotype.
neXtProt; NX_Q9Y263; -.
OpenTargets; ENSG00000137055; -.
PharmGKB; PA33370; -.
eggNOG; KOG0301; Eukaryota.
eggNOG; ENOG410XS67; LUCA.
GeneTree; ENSGT00550000074944; -.
HOGENOM; HOG000174247; -.
HOVERGEN; HBG008204; -.
InParanoid; Q9Y263; -.
KO; K14018; -.
OMA; KEGQVQM; -.
OrthoDB; EOG091G06FX; -.
PhylomeDB; Q9Y263; -.
TreeFam; TF105944; -.
SignaLink; Q9Y263; -.
ChiTaRS; PLAA; human.
EvolutionaryTrace; Q9Y263; -.
GeneWiki; PLAA_(gene); -.
GenomeRNAi; 9373; -.
PRO; PR:Q9Y263; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000137055; Expressed in 211 organ(s), highest expression level in testis.
CleanEx; HS_PLAA; -.
ExpressionAtlas; Q9Y263; baseline and differential.
Genevisible; Q9Y263; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0016005; F:phospholipase A2 activator activity; TAS:ProtInc.
GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0016236; P:macroautophagy; IMP:UniProtKB.
GO; GO:1900045; P:negative regulation of protein K63-linked ubiquitination; ISS:UniProtKB.
GO; GO:0006644; P:phospholipid metabolic process; TAS:ProtInc.
GO; GO:1903861; P:positive regulation of dendrite extension; ISS:UniProtKB.
GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
GO; GO:0032430; P:positive regulation of phospholipase A2 activity; IMP:UniProtKB.
GO; GO:1903423; P:positive regulation of synaptic vesicle recycling; ISS:UniProtKB.
GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0010992; P:ubiquitin recycling; IBA:GO_Central.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISS:UniProtKB.
Gene3D; 1.10.150.410; -; 1.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR015155; PFU.
InterPro; IPR038122; PFU_sf.
InterPro; IPR033510; PLAA/Doa1/Lub1.
InterPro; IPR013535; PUL_dom.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR19849; PTHR19849; 2.
Pfam; PF09070; PFU; 1.
Pfam; PF08324; PUL; 1.
Pfam; PF00400; WD40; 6.
SMART; SM00320; WD40; 7.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS51394; PFU; 1.
PROSITE; PS51396; PUL; 1.
PROSITE; PS50082; WD_REPEATS_2; 3.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell junction; Complete proteome;
Cytoplasm; Developmental protein; Disease mutation;
Mental retardation; Neurogenesis; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Synapse; WD repeat.
CHAIN 1 795 Phospholipase A-2-activating protein.
/FTId=PRO_0000051130.
REPEAT 17 56 WD 1.
REPEAT 63 107 WD 2.
REPEAT 110 148 WD 3.
REPEAT 149 188 WD 4.
REPEAT 190 227 WD 5.
REPEAT 229 268 WD 6.
REPEAT 270 307 WD 7.
DOMAIN 366 465 PFU. {ECO:0000255|PROSITE-
ProRule:PRU00727}.
DOMAIN 533 794 PUL. {ECO:0000255|PROSITE-
ProRule:PRU00729}.
REPEAT 546 588 ARM 1.
REPEAT 589 620 ARM 2.
REPEAT 621 669 ARM 3.
REPEAT 670 715 ARM 4.
REPEAT 716 755 ARM 5.
REPEAT 756 795 ARM 6.
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 529 529 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 23 23 G -> V (in NDMSBA; dbSNP:rs747956857).
{ECO:0000269|PubMed:28413018}.
/FTId=VAR_079276.
VARIANT 752 752 L -> F (in NDMSBA; no effect on protein
stability; no effect on subcellular
localization; decreased function in
positive regulation of cytosolic
phospholipase A2 activity; in patient
cells homozygous for the mutation;
dbSNP:rs1114167457).
{ECO:0000269|PubMed:28007986}.
/FTId=VAR_079277.
CONFLICT 14 14 L -> F (in Ref. 5; AAD42075).
{ECO:0000305}.
CONFLICT 57 57 E -> D (in Ref. 5; AAD42075).
{ECO:0000305}.
CONFLICT 86 86 A -> F (in Ref. 5; AAD42075).
{ECO:0000305}.
CONFLICT 97 97 F -> L (in Ref. 5; AAD42075).
{ECO:0000305}.
CONFLICT 172 172 D -> G (in Ref. 1; BAA91803).
{ECO:0000305}.
CONFLICT 363 363 E -> K (in Ref. 6; BAD97264).
{ECO:0000305}.
CONFLICT 422 422 T -> A (in Ref. 5; AAD42075).
{ECO:0000305}.
CONFLICT 520 520 N -> S (in Ref. 1; BAA92105).
{ECO:0000305}.
CONFLICT 531 531 M -> L (in Ref. 5; AAD42075).
{ECO:0000305}.
CONFLICT 541 541 V -> L (in Ref. 5; AAD42075).
{ECO:0000305}.
CONFLICT 746 746 L -> P (in Ref. 5; AAD42075).
{ECO:0000305}.
STRAND 390 392 {ECO:0000244|PDB:2K89}.
STRAND 394 396 {ECO:0000244|PDB:2K89}.
STRAND 399 407 {ECO:0000244|PDB:2K89}.
STRAND 410 412 {ECO:0000244|PDB:2K89}.
STRAND 416 420 {ECO:0000244|PDB:2K89}.
HELIX 426 437 {ECO:0000244|PDB:2K89}.
HELIX 443 455 {ECO:0000244|PDB:2K89}.
TURN 457 460 {ECO:0000244|PDB:2K89}.
HELIX 548 559 {ECO:0000244|PDB:3EBB}.
HELIX 564 566 {ECO:0000244|PDB:3EBB}.
HELIX 571 584 {ECO:0000244|PDB:3EBB}.
HELIX 593 603 {ECO:0000244|PDB:3EBB}.
TURN 607 609 {ECO:0000244|PDB:3EBB}.
HELIX 611 620 {ECO:0000244|PDB:3EBB}.
HELIX 624 631 {ECO:0000244|PDB:3EBB}.
TURN 633 635 {ECO:0000244|PDB:3EBB}.
HELIX 636 645 {ECO:0000244|PDB:3EBB}.
HELIX 653 665 {ECO:0000244|PDB:3EBB}.
HELIX 666 668 {ECO:0000244|PDB:3EBB}.
HELIX 670 678 {ECO:0000244|PDB:3EBB}.
HELIX 680 688 {ECO:0000244|PDB:3EBB}.
HELIX 689 691 {ECO:0000244|PDB:3EBB}.
HELIX 696 715 {ECO:0000244|PDB:3EBB}.
HELIX 719 733 {ECO:0000244|PDB:3EBB}.
HELIX 739 753 {ECO:0000244|PDB:3EBB}.
HELIX 757 765 {ECO:0000244|PDB:3EBB}.
HELIX 768 771 {ECO:0000244|PDB:3EBB}.
HELIX 772 777 {ECO:0000244|PDB:3EBB}.
HELIX 782 792 {ECO:0000244|PDB:3EBB}.
SEQUENCE 795 AA; 87157 MW; D6E7330AC9891637 CRC64;
MTSGATRYRL SCSLRGHELD VRGLVCCAYP PGAFVSVSRD RTTRLWAPDS PNRSFTEMHC
MSGHSNFVSC VCIIPSSDIY PHGLIATGGN DHNICIFSLD SPMPLYILKG HKNTVCSLSS
GKFGTLLSGS WDTTAKVWLN DKCMMTLQGH TAAVWAVKIL PEQGLMLTGS ADKTVKLWKA
GRCERTFSGH EDCVRGLAIL SETEFLSCAN DASIRRWQIT GECLEVYYGH TNYIYSISVF
PNCRDFVTTA EDRSLRIWKH GECAQTIRLP AQSIWCCCVL DNGDIVVGAS DGIIRVFTES
EDRTASAEEI KAFEKELSHA TIDSKTGDLG DINAEQLPGR EHLNEPGTRE GQTRLIRDGE
KVEAYQWSVS EGRWIKIGDV VGSSGANQQT SGKVLYEGKE FDYVFSIDVN EGGPSYKLPY
NTSDDPWLTA YNFLQKNDLN PMFLDQVAKF IIDNTKGQML GLGNPSFSDP FTGGGRYVPG
SSGSSNTLPT ADPFTGAGRY VPGSASMGTT MAGVDPFTGN SAYRSAASKT MNIYFPKKEA
VTFDQANPTQ ILGKLKELNG TAPEEKKLTE DDLILLEKIL SLICNSSSEK PTVQQLQILW
KAINCPEDIV FPALDILRLS IKHPSVNENF CNEKEGAQFS SHLINLLNPK GKPANQLLAL
RTFCNCFVGQ AGQKLMMSQR ESLMSHAIEL KSGSNKNIHI ALATLALNYS VCFHKDHNIE
GKAQCLSLIS TILEVVQDLE ATFRLLVALG TLISDDSNAV QLAKSLGVDS QIKKYSSVSE
PAKVSECCRF ILNLL


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