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Q9Y263 (PLAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipase A-2-activating protein

Short name=PLA2P
Short name=PLAP
Gene names
Name:PLAA
Synonyms:PLAP
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length795 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the maintenance of ubiquitin levels By similarity.

Subunit structure

Interacts with ubiquitin. Interacts with VCP. Ref.12

Domain

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

The PFU domain mediates interaction with ubiquitin.

Sequence similarities

Belongs to the WD repeat PLAP family.

Contains 6 ARM repeats.

Contains 1 PFU domain.

Contains 1 PUL domain.

Contains 7 WD repeats.

Sequence caution

The sequence AAD03030.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAD42075.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAD42075.1 differs from that shown. Reason: Frameshift at position 698.

The sequence BAA92105.1 differs from that shown. Reason: Erroneous termination at position 545. Translated as Gln.

The sequence BAD97264.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAB42881.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAH72641.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 795795Phospholipase A-2-activating protein
PRO_0000051130

Regions

Repeat17 – 5640WD 1
Repeat63 – 10745WD 2
Repeat110 – 14839WD 3
Repeat149 – 18840WD 4
Repeat190 – 22738WD 5
Repeat229 – 26840WD 6
Repeat270 – 30738WD 7
Domain366 – 465100PFU
Domain533 – 794262PUL
Repeat546 – 58843ARM 1
Repeat589 – 62032ARM 2
Repeat621 – 66949ARM 3
Repeat670 – 71546ARM 4
Repeat716 – 75540ARM 5
Repeat756 – 79540ARM 6

Amino acid modifications

Modified residue501Phosphoserine Ref.9
Modified residue5291N6-acetyllysine Ref.10

Experimental info

Sequence conflict141L → F in AAD42075. Ref.5
Sequence conflict571E → D in AAD42075. Ref.5
Sequence conflict861A → F in AAD42075. Ref.5
Sequence conflict971F → L in AAD42075. Ref.5
Sequence conflict1721D → G in BAA91803. Ref.1
Sequence conflict3631E → K in BAD97264. Ref.6
Sequence conflict4221T → A in AAD42075. Ref.5
Sequence conflict5201N → S in BAA92105. Ref.1
Sequence conflict5311M → L in AAD42075. Ref.5
Sequence conflict5411V → L in AAD42075. Ref.5
Sequence conflict7461L → P in AAD42075. Ref.5

Secondary structure

...................................... 795
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y263 [UniParc].

Last modified June 13, 2006. Version 2.
Checksum: D6E7330AC9891637

FASTA79587,157
        10         20         30         40         50         60 
MTSGATRYRL SCSLRGHELD VRGLVCCAYP PGAFVSVSRD RTTRLWAPDS PNRSFTEMHC 

        70         80         90        100        110        120 
MSGHSNFVSC VCIIPSSDIY PHGLIATGGN DHNICIFSLD SPMPLYILKG HKNTVCSLSS 

       130        140        150        160        170        180 
GKFGTLLSGS WDTTAKVWLN DKCMMTLQGH TAAVWAVKIL PEQGLMLTGS ADKTVKLWKA 

       190        200        210        220        230        240 
GRCERTFSGH EDCVRGLAIL SETEFLSCAN DASIRRWQIT GECLEVYYGH TNYIYSISVF 

       250        260        270        280        290        300 
PNCRDFVTTA EDRSLRIWKH GECAQTIRLP AQSIWCCCVL DNGDIVVGAS DGIIRVFTES 

       310        320        330        340        350        360 
EDRTASAEEI KAFEKELSHA TIDSKTGDLG DINAEQLPGR EHLNEPGTRE GQTRLIRDGE 

       370        380        390        400        410        420 
KVEAYQWSVS EGRWIKIGDV VGSSGANQQT SGKVLYEGKE FDYVFSIDVN EGGPSYKLPY 

       430        440        450        460        470        480 
NTSDDPWLTA YNFLQKNDLN PMFLDQVAKF IIDNTKGQML GLGNPSFSDP FTGGGRYVPG 

       490        500        510        520        530        540 
SSGSSNTLPT ADPFTGAGRY VPGSASMGTT MAGVDPFTGN SAYRSAASKT MNIYFPKKEA 

       550        560        570        580        590        600 
VTFDQANPTQ ILGKLKELNG TAPEEKKLTE DDLILLEKIL SLICNSSSEK PTVQQLQILW 

       610        620        630        640        650        660 
KAINCPEDIV FPALDILRLS IKHPSVNENF CNEKEGAQFS SHLINLLNPK GKPANQLLAL 

       670        680        690        700        710        720 
RTFCNCFVGQ AGQKLMMSQR ESLMSHAIEL KSGSNKNIHI ALATLALNYS VCFHKDHNIE 

       730        740        750        760        770        780 
GKAQCLSLIS TILEVVQDLE ATFRLLVALG TLISDDSNAV QLAKSLGVDS QIKKYSSVSE 

       790 
PAKVSECCRF ILNLL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
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. expand/collapse author list , 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: 15164053] [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: 15489334] [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: 10644453] [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: 10571045] [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: 9931468] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-795.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-529, MASS SPECTROMETRY.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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: 19423704] [Abstract]
Cited for: STRUCTURE BY NMR OF 386-465, INTERACTION WITH UBIQUITIN.
[13]"Structure and function of the PLAA/Ufd3-p97/Cdc48 complex."
Qiu L., Pashkova N., Walker J.R., Winistorfer S., Allali-Hassani A., Akutsu M., Piper R., Dhe-Paganon S.
J. Biol. Chem. 285:365-372(2010) [PubMed: 19887378] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 511-795 IN COMPLEX WITH VCP, ARM REPEATS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00218465.
PIRT43447.
RefSeqNP_001026859.1. NM_001031689.2.
UniGeneHs.27182.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K89NMR-A386-465[»]
2K8ANMR-A386-465[»]
2K8BNMR-B386-465[»]
2K8CNMR-B386-465[»]
3EBBX-ray1.90A/B/C/D511-795[»]
ProteinModelPortalQ9Y263.
SMRQ9Y263. Positions 5-306, 386-795.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Y263. 10 interactions.
STRINGQ9Y263.

PTM databases

PhosphoSiteQ9Y263.

Polymorphism databases

DMDM108935868.

Proteomic databases

PRIDEQ9Y263.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000397292; ENSP00000380460; ENSG00000137055.
GeneID9373.
KEGGhsa:9373.
UCSCuc003zqd.1. human.

Organism-specific databases

CTD9373.
GeneCardsGC09M026903.
H-InvDBHIX0007960.
HGNCHGNC:9043. PLAA.
HPACAB005035.
HPA020994.
HPA020996.
MIM603873. gene.
neXtProtNX_Q9Y263.
PharmGKBPA33370.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08100.
GeneTreeENSGT00550000074944.
HOVERGENHBG008204.
InParanoidQ9Y263.
OMARSLRIWK.
OrthoDBEOG4DJJVW.
PhylomeDBQ9Y263.

Gene expression databases

ArrayExpressQ9Y263.
BgeeQ9Y263.
CleanExHS_PLAA.
GenevestigatorQ9Y263.
GermOnlineENSG00000137055. Homo sapiens.

Family and domain databases

InterProIPR015155. PLAA_fam_Ub-bd_PFU.
IPR013535. PUL.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR011046. WD40_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
Gene3DG3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KOK14018.
PfamPF09070. PFU. 1 hit.
PF08324. PUL. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. WD40_like. 1 hit.
PROSITEPS50176. ARM_REPEAT. False negative.
PS51394. PFU. 1 hit.
PS51396. PUL. 1 hit.
PS00678. WD_REPEATS_1. False negative.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio35110.
SOURCESearch...

Entry information

Entry namePLAP_HUMAN
AccessionPrimary (citable) accession number: Q9Y263
Secondary accession number(s): Q53EU5 expand/collapse secondary AC list , Q5VY33, Q9NUL8, Q9NVE9, Q9UF53, Q9Y5L1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 13, 2006
Last modified: January 25, 2012
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families