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Protein

Phospholipase A-2-activating protein

Gene

PLAA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the maintenance of ubiquitin levels.By similarity

GO - Molecular functioni

  • phospholipase A2 activator activity Source: ProtInc

GO - Biological processi

  • inflammatory response Source: Ensembl
  • phospholipid metabolic process Source: ProtInc
  • signal transduction Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ9Y263.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase A-2-activating protein
Short name:
PLA2P
Short name:
PLAP
Gene namesi
Name:PLAA
Synonyms:PLAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:9043. PLAA.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33370.

Chemistry

ChEMBLiCHEMBL6114.

Polymorphism and mutation databases

BioMutaiPLAA.
DMDMi108935868.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 795795Phospholipase A-2-activating proteinPRO_0000051130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501PhosphoserineBy similarity
Modified residuei529 – 5291N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9Y263.
MaxQBiQ9Y263.
PaxDbiQ9Y263.
PRIDEiQ9Y263.

PTM databases

iPTMnetiQ9Y263.
PhosphoSiteiQ9Y263.

Expressioni

Gene expression databases

BgeeiQ9Y263.
CleanExiHS_PLAA.
ExpressionAtlasiQ9Y263. baseline and differential.
GenevisibleiQ9Y263. HS.

Organism-specific databases

HPAiCAB005035.
HPA020994.
HPA020996.

Interactioni

Subunit structurei

Interacts with ubiquitin. Interacts with VCP.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q763533EBI-1994037,EBI-6248077From a different organism.
HEL-S-70V9HW803EBI-1994037,EBI-10175326
KPNA4O006293EBI-1994037,EBI-396343
UBXN1Q043235EBI-1994037,EBI-1058647

Protein-protein interaction databases

BioGridi114774. 37 interactions.
IntActiQ9Y263. 15 interactions.
MINTiMINT-3084225.
STRINGi9606.ENSP00000380460.

Chemistry

BindingDBiQ9Y263.

Structurei

Secondary structure

1
795
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi390 – 3923Combined sources
Beta strandi394 – 3963Combined sources
Beta strandi399 – 4079Combined sources
Beta strandi410 – 4123Combined sources
Beta strandi416 – 4205Combined sources
Helixi426 – 43712Combined sources
Helixi443 – 45513Combined sources
Turni457 – 4604Combined sources
Helixi548 – 55912Combined sources
Helixi564 – 5663Combined sources
Helixi571 – 58414Combined sources
Helixi593 – 60311Combined sources
Turni607 – 6093Combined sources
Helixi611 – 62010Combined sources
Helixi624 – 6318Combined sources
Turni633 – 6353Combined sources
Helixi636 – 64510Combined sources
Helixi653 – 66513Combined sources
Helixi666 – 6683Combined sources
Helixi670 – 6789Combined sources
Helixi680 – 6889Combined sources
Helixi689 – 6913Combined sources
Helixi696 – 71520Combined sources
Helixi719 – 73315Combined sources
Helixi739 – 75315Combined sources
Helixi757 – 7659Combined sources
Helixi768 – 7714Combined sources
Helixi772 – 7776Combined sources
Helixi782 – 79211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K89NMR-A386-465[»]
2K8ANMR-A386-465[»]
2K8BNMR-B386-465[»]
2K8CNMR-B386-465[»]
3EBBX-ray1.90A/B/C/D511-795[»]
ProteinModelPortaliQ9Y263.
SMRiQ9Y263. Positions 6-378, 386-465, 531-795.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y263.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati17 – 5640WD 1Add
BLAST
Repeati63 – 10745WD 2Add
BLAST
Repeati110 – 14839WD 3Add
BLAST
Repeati149 – 18840WD 4Add
BLAST
Repeati190 – 22738WD 5Add
BLAST
Repeati229 – 26840WD 6Add
BLAST
Repeati270 – 30738WD 7Add
BLAST
Domaini366 – 465100PFUPROSITE-ProRule annotationAdd
BLAST
Domaini533 – 794262PULPROSITE-ProRule annotationAdd
BLAST
Repeati546 – 58843ARM 1Add
BLAST
Repeati589 – 62032ARM 2Add
BLAST
Repeati621 – 66949ARM 3Add
BLAST
Repeati670 – 71546ARM 4Add
BLAST
Repeati716 – 75540ARM 5Add
BLAST
Repeati756 – 79540ARM 6Add
BLAST

Domaini

The PUL domain is composed of 6 armadillo-like repeats and mediates the interaction with VCP C-terminus.1 Publication
The PFU domain mediates interaction with ubiquitin.1 Publication

Sequence similaritiesi

Belongs to the WD repeat PLAP family.Curated
Contains 6 ARM repeats.Curated
Contains 1 PFU domain.PROSITE-ProRule annotation
Contains 1 PUL domain.PROSITE-ProRule annotation
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0301. Eukaryota.
ENOG410XS67. LUCA.
GeneTreeiENSGT00550000074944.
HOGENOMiHOG000174247.
HOVERGENiHBG008204.
InParanoidiQ9Y263.
KOiK14018.
OMAiYPRGLIA.
OrthoDBiEOG7D2FCZ.
PhylomeDBiQ9Y263.
TreeFamiTF105944.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR016024. ARM-type_fold.
IPR015155. PLAA_fam_Ub-bd_PFU.
IPR013535. PUL_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF09070. PFU. 1 hit.
PF08324. PUL. 1 hit.
PF00400. WD40. 6 hits.
[Graphical view]
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF50978. SSF50978. 1 hit.
PROSITEiPS51394. PFU. 1 hit.
PS51396. PUL. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y263-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSGATRYRL SCSLRGHELD VRGLVCCAYP PGAFVSVSRD RTTRLWAPDS
60 70 80 90 100
PNRSFTEMHC MSGHSNFVSC VCIIPSSDIY PHGLIATGGN DHNICIFSLD
110 120 130 140 150
SPMPLYILKG HKNTVCSLSS GKFGTLLSGS WDTTAKVWLN DKCMMTLQGH
160 170 180 190 200
TAAVWAVKIL PEQGLMLTGS ADKTVKLWKA GRCERTFSGH EDCVRGLAIL
210 220 230 240 250
SETEFLSCAN DASIRRWQIT GECLEVYYGH TNYIYSISVF PNCRDFVTTA
260 270 280 290 300
EDRSLRIWKH GECAQTIRLP AQSIWCCCVL DNGDIVVGAS DGIIRVFTES
310 320 330 340 350
EDRTASAEEI KAFEKELSHA TIDSKTGDLG DINAEQLPGR EHLNEPGTRE
360 370 380 390 400
GQTRLIRDGE KVEAYQWSVS EGRWIKIGDV VGSSGANQQT SGKVLYEGKE
410 420 430 440 450
FDYVFSIDVN EGGPSYKLPY NTSDDPWLTA YNFLQKNDLN PMFLDQVAKF
460 470 480 490 500
IIDNTKGQML GLGNPSFSDP FTGGGRYVPG SSGSSNTLPT ADPFTGAGRY
510 520 530 540 550
VPGSASMGTT MAGVDPFTGN SAYRSAASKT MNIYFPKKEA VTFDQANPTQ
560 570 580 590 600
ILGKLKELNG TAPEEKKLTE DDLILLEKIL SLICNSSSEK PTVQQLQILW
610 620 630 640 650
KAINCPEDIV FPALDILRLS IKHPSVNENF CNEKEGAQFS SHLINLLNPK
660 670 680 690 700
GKPANQLLAL RTFCNCFVGQ AGQKLMMSQR ESLMSHAIEL KSGSNKNIHI
710 720 730 740 750
ALATLALNYS VCFHKDHNIE GKAQCLSLIS TILEVVQDLE ATFRLLVALG
760 770 780 790
TLISDDSNAV QLAKSLGVDS QIKKYSSVSE PAKVSECCRF ILNLL
Length:795
Mass (Da):87,157
Last modified:June 13, 2006 - v2
Checksum:iD6E7330AC9891637
GO

Sequence cautioni

The sequence AAD03030.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAD42075.1 differs from that shown. Reason: Frameshift at position 698. Curated
The sequence AAD42075.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA92105.1 differs from that shown. Reason: Erroneous termination at position 545. Translated as Gln.Curated
The sequence BAD97264.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB42881.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAH72641.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141L → F in AAD42075 (PubMed:10644453).Curated
Sequence conflicti57 – 571E → D in AAD42075 (PubMed:10644453).Curated
Sequence conflicti86 – 861A → F in AAD42075 (PubMed:10644453).Curated
Sequence conflicti97 – 971F → L in AAD42075 (PubMed:10644453).Curated
Sequence conflicti172 – 1721D → G in BAA91803 (PubMed:14702039).Curated
Sequence conflicti363 – 3631E → K in BAD97264 (Ref. 6) Curated
Sequence conflicti422 – 4221T → A in AAD42075 (PubMed:10644453).Curated
Sequence conflicti520 – 5201N → S in BAA92105 (PubMed:14702039).Curated
Sequence conflicti531 – 5311M → L in AAD42075 (PubMed:10644453).Curated
Sequence conflicti541 – 5411V → L in AAD42075 (PubMed:10644453).Curated
Sequence conflicti746 – 7461L → P in AAD42075 (PubMed:10644453).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001642 mRNA. Translation: BAA91803.1.
AK002143 mRNA. Translation: BAA92105.1. Sequence problems.
AL133608 mRNA. Translation: CAB63739.1.
AL356133 Genomic DNA. Translation: CAH72641.1. Sequence problems.
BC032551 mRNA. Translation: AAH32551.1.
AF145020 mRNA. Translation: AAD42075.1. Sequence problems.
AK223544 mRNA. Translation: BAD97264.1. Different initiation.
AJ238243 mRNA. Translation: CAB42881.1. Different initiation.
AF083395 mRNA. Translation: AAD03030.1. Different initiation.
CCDSiCCDS35000.1.
PIRiT43447.
RefSeqiNP_001026859.1. NM_001031689.2.
UniGeneiHs.27182.

Genome annotation databases

EnsembliENST00000397292; ENSP00000380460; ENSG00000137055.
GeneIDi9373.
KEGGihsa:9373.
UCSCiuc003zqd.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001642 mRNA. Translation: BAA91803.1.
AK002143 mRNA. Translation: BAA92105.1. Sequence problems.
AL133608 mRNA. Translation: CAB63739.1.
AL356133 Genomic DNA. Translation: CAH72641.1. Sequence problems.
BC032551 mRNA. Translation: AAH32551.1.
AF145020 mRNA. Translation: AAD42075.1. Sequence problems.
AK223544 mRNA. Translation: BAD97264.1. Different initiation.
AJ238243 mRNA. Translation: CAB42881.1. Different initiation.
AF083395 mRNA. Translation: AAD03030.1. Different initiation.
CCDSiCCDS35000.1.
PIRiT43447.
RefSeqiNP_001026859.1. NM_001031689.2.
UniGeneiHs.27182.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K89NMR-A386-465[»]
2K8ANMR-A386-465[»]
2K8BNMR-B386-465[»]
2K8CNMR-B386-465[»]
3EBBX-ray1.90A/B/C/D511-795[»]
ProteinModelPortaliQ9Y263.
SMRiQ9Y263. Positions 6-378, 386-465, 531-795.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114774. 37 interactions.
IntActiQ9Y263. 15 interactions.
MINTiMINT-3084225.
STRINGi9606.ENSP00000380460.

Chemistry

BindingDBiQ9Y263.
ChEMBLiCHEMBL6114.

PTM databases

iPTMnetiQ9Y263.
PhosphoSiteiQ9Y263.

Polymorphism and mutation databases

BioMutaiPLAA.
DMDMi108935868.

Proteomic databases

EPDiQ9Y263.
MaxQBiQ9Y263.
PaxDbiQ9Y263.
PRIDEiQ9Y263.

Protocols and materials databases

DNASUi9373.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000397292; ENSP00000380460; ENSG00000137055.
GeneIDi9373.
KEGGihsa:9373.
UCSCiuc003zqd.4. human.

Organism-specific databases

CTDi9373.
GeneCardsiPLAA.
HGNCiHGNC:9043. PLAA.
HPAiCAB005035.
HPA020994.
HPA020996.
MIMi603873. gene.
neXtProtiNX_Q9Y263.
PharmGKBiPA33370.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0301. Eukaryota.
ENOG410XS67. LUCA.
GeneTreeiENSGT00550000074944.
HOGENOMiHOG000174247.
HOVERGENiHBG008204.
InParanoidiQ9Y263.
KOiK14018.
OMAiYPRGLIA.
OrthoDBiEOG7D2FCZ.
PhylomeDBiQ9Y263.
TreeFamiTF105944.

Enzyme and pathway databases

SignaLinkiQ9Y263.

Miscellaneous databases

ChiTaRSiPLAA. human.
EvolutionaryTraceiQ9Y263.
GeneWikiiPLAA_(gene).
GenomeRNAii9373.
NextBioi35110.
PROiQ9Y263.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y263.
CleanExiHS_PLAA.
ExpressionAtlasiQ9Y263. baseline and differential.
GenevisibleiQ9Y263. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR016024. ARM-type_fold.
IPR015155. PLAA_fam_Ub-bd_PFU.
IPR013535. PUL_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF09070. PFU. 1 hit.
PF08324. PUL. 1 hit.
PF00400. WD40. 6 hits.
[Graphical view]
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF50978. SSF50978. 1 hit.
PROSITEiPS51394. PFU. 1 hit.
PS51396. PUL. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. "DNA sequence and analysis of human chromosome 9."
    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.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Uterus.
  5. "Chromosomal localization of phospholipase A2 activating protein, an ets2 target gene, to 9p21."
    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.
    Genomics 62:529-532(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-795.
  6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-795.
    Tissue: Kidney.
  7. "Cloning of the human phospholipase A2 activating protein (hPLAP) gene on the chromosome 9p21 melanoma deleted region."
    Ruiz A., Nadal M., Puig S., Estivill X.
    Gene 239:155-161(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-795.
    Tissue: Fetal brain.
  8. "Molecular characterization of cDNA for phospholipase A2-activating protein."
    Chopra A.K., Ribardo D.A., Wood T.G., Prusak D.J., Xu X.-J., Peterson J.W.
    Biochim. Biophys. Acta 1444:125-130(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-795.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structural basis for ubiquitin recognition by a novel domain from human phospholipase A2-activating protein."
    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.
    J. Biol. Chem. 284:19043-19052(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 386-465, INTERACTION WITH UBIQUITIN.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 511-795 IN COMPLEX WITH VCP, DOMAIN ARM REPEATS.

Entry informationi

Entry nameiPLAP_HUMAN
AccessioniPrimary (citable) accession number: Q9Y263
Secondary accession number(s): Q53EU5
, Q5VY33, Q9NUL8, Q9NVE9, Q9UF53, Q9Y5L1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 13, 2006
Last modified: May 11, 2016
This is version 146 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.