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P08567 (PLEK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pleckstrin
Alternative name(s):
Platelet 47 kDa protein
Short name=p47
Gene names
Name:PLEK
Synonyms:P47
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major protein kinase C substrate of platelets.

Sequence similarities

Contains 1 DEP domain.

Contains 2 PH domains.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   DomainRepeat
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from direct assay PubMed 10497244. Source: BHF-UCL

blood coagulation

Traceable author statement. Source: Reactome

cell projection organization

Inferred from direct assay PubMed 9060471. Source: BHF-UCL

cortical actin cytoskeleton organization

Inferred from direct assay PubMed 10497244. Source: BHF-UCL

hematopoietic progenitor cell differentiation

Inferred from expression pattern Ref.2. Source: BHF-UCL

integrin-mediated signaling pathway

Inferred from direct assay PubMed 10995449. Source: BHF-UCL

negative regulation of G-protein coupled receptor protein signaling pathway

Inferred from direct assay PubMed 7782310. Source: BHF-UCL

negative regulation of calcium-mediated signaling

Non-traceable author statement PubMed 8999861. Source: BHF-UCL

negative regulation of inositol phosphate biosynthetic process

Inferred from direct assay PubMed 7559487PubMed 7782310. Source: BHF-UCL

phosphatidylinositol metabolic process

Inferred from direct assay PubMed 7559487. Source: BHF-UCL

phospholipase C-inhibiting G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 7782310. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

platelet aggregation

Inferred from sequence or structural similarity. Source: BHF-UCL

platelet degranulation

Inferred from expression pattern PubMed 7559487. Source: BHF-UCL

positive regulation of actin filament bundle assembly

Inferred from direct assay PubMed 10497244. Source: BHF-UCL

positive regulation of actin filament depolymerization

Inferred from direct assay PubMed 10497244. Source: BHF-UCL

positive regulation of inositol-polyphosphate 5-phosphatase activity

Inferred from direct assay PubMed 8999861. Source: BHF-UCL

positive regulation of integrin activation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of platelet activation

Inferred from sequence or structural similarity. Source: BHF-UCL

protein kinase C signaling

Inferred from sequence or structural similarity. Source: BHF-UCL

protein secretion by platelet

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of cell diameter

Inferred from direct assay PubMed 10995449. Source: BHF-UCL

ruffle organization

Inferred from direct assay PubMed 10497244. Source: BHF-UCL

thrombin receptor signaling pathway

Inferred from direct assay PubMed 7782310. Source: BHF-UCL

vesicle docking involved in exocytosis

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 8694752PubMed 9060471. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

ruffle membrane

Inferred from direct assay PubMed 9060471. Source: BHF-UCL

   Molecular_functionphosphatidylinositol-3,4-bisphosphate binding

Inferred from direct assay PubMed 15698571. Source: BHF-UCL

protein homodimerization activity

Inferred from direct assay PubMed 8694752. Source: BHF-UCL

protein kinase C binding

Inferred from direct assay Ref.8. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350Pleckstrin
PRO_0000053859

Regions

Domain4 – 10198PH 1
Domain136 – 22186DEP
Domain244 – 347104PH 2

Amino acid modifications

Modified residue641N6-acetyllysine Ref.10
Modified residue1131Phosphoserine; by PKC Ref.8
Modified residue1171Phosphoserine; by PKC Ref.8 Ref.9

Natural variations

Natural variant51R → W.
Corresponds to variant rs17035364 [ dbSNP | Ensembl ].
VAR_027797
Natural variant921W → R.
VAR_005524
Natural variant971K → N. Ref.1 Ref.2
Corresponds to variant rs3816281 [ dbSNP | Ensembl ].
VAR_027798
Natural variant1081K → Q.
Corresponds to variant rs34515106 [ dbSNP | Ensembl ].
VAR_056666
Natural variant3401R → K. Ref.1 Ref.2 Ref.3 Ref.7
Corresponds to variant rs1063479 [ dbSNP | Ensembl ].
VAR_027799

Experimental info

Sequence conflict2841E → G in CAG46876. Ref.3

Secondary structure

.............................................................. 350
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08567 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 2E292CB18B533261

FASTA35040,125
        10         20         30         40         50         60 
MEPKRIREGY LVKKGSVFNT WKPMWVVLLE DGIEFYKKKS DNSPKGMIPL KGSTLTSPCQ 

        70         80         90        100        110        120 
DFGKRMFVFK ITTTKQQDHF FQAAFLEERD AWVRDIKKAI KCIEGGQKFA RKSTRRSIRL 

       130        140        150        160        170        180 
PETIDLGALY LSMKDTEKGI KELNLEKDKK IFNHCFTGNC VIDWLVSNQS VRNRQEGLMI 

       190        200        210        220        230        240 
ASSLLNEGYL QPAGDMSKSA VDGTAENPFL DNPDAFYYFP DSGFFCEENS SDDDVILKEE 

       250        260        270        280        290        300 
FRGVIIKQGC LLKQGHRRKN WKVRKFILRE DPAYLHYYDP AGAEDPLGAI HLRGCVVTSV 

       310        320        330        340        350 
ESNSNGRKSE EENLFEIITA DEVHYFLQAA TPKERTEWIR AIQMASRTGK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of the major protein kinase C substrate of platelets."
Tyers M., Rachubinski R.A., McCaw M.L., Varrichio A.M., Shorr R.G.L., Haslam R.J., Harley C.B.
Nature 333:470-473(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-97 AND LYS-340.
[2]"Molecular analysis of pleckstrin: the major protein kinase C substrate of platelets."
Tyers M., Haslam R.J., Rachubinski R.A., Harley C.B.
J. Cell. Biochem. 40:133-145(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-97 AND LYS-340.
[3]"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], VARIANT LYS-340.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Spleen.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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], VARIANT LYS-340.
Tissue: Lymph.
[8]"Phosphorylation of human pleckstrin on Ser-113 and Ser-117 by protein kinase C."
Craig K.L., Harley C.B.
Biochem. J. 314:937-942(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-113 AND SER-117.
[9]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[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.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Solution structure of a pleckstrin-homology domain."
Yoon H.S., Hajduk P.J., Petros A.M., Olejniczak E.T., Meadows R.P., Fesik S.W.
Nature 369:672-675(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-105.
[13]"Structure and dynamics of the human pleckstrin DEP domain: distinct molecular features of a novel DEP domain subfamily."
Civera C., Simon B., Stier G., Sattler M., Macias M.J.
Proteins 58:354-366(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 121-223.
[14]"Solution structure of the DEP domain and of the C-terminal PH domain of human pleckstrin."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 116-350.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07743 mRNA. Translation: CAA30564.1.
CR542056 mRNA. Translation: CAG46853.1.
CR542079 mRNA. Translation: CAG46876.1.
AK313756 mRNA. Translation: BAG36495.1.
AC015969 Genomic DNA. Translation: AAX93121.1.
CH471053 Genomic DNA. Translation: EAW99876.1.
BC018549 mRNA. Translation: AAH18549.1.
PIRS00755.
RefSeqNP_002655.2. NM_002664.2.
UniGeneHs.468840.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PLSNMR-A1-105[»]
1W4MNMR-A121-223[»]
1X05NMR-A235-350[»]
1XX0NMR-A234-350[»]
1ZM0X-ray2.10A/B240-350[»]
2CSONMR-A116-229[»]
2I5CX-ray1.75A/B/C243-347[»]
2I5FX-ray1.35A243-347[»]
ProteinModelPortalP08567.
SMRP08567. Positions 1-105, 118-230, 234-350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111357. 1 interaction.
IntActP08567. 9 interactions.
MINTMINT-8216753.
STRING9606.ENSP00000234313.

PTM databases

PhosphoSiteP08567.

Polymorphism databases

DMDM317373523.

2D gel databases

OGPP08567.

Proteomic databases

PaxDbP08567.
PRIDEP08567.

Protocols and materials databases

DNASU5341.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000234313; ENSP00000234313; ENSG00000115956.
GeneID5341.
KEGGhsa:5341.
UCSCuc002sen.4. human.

Organism-specific databases

CTD5341.
GeneCardsGC02P068504.
H-InvDBHIX0002122.
HGNCHGNC:9070. PLEK.
HPAHPA031838.
MIM173570. gene.
neXtProtNX_P08567.
PharmGKBPA33400.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44162.
HOGENOMHOG000294078.
HOVERGENHBG001361.
InParanoidP08567.
OMAYYFADSG.
OrthoDBEOG74XS6R.
PhylomeDBP08567.
TreeFamTF332246.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

BgeeP08567.
CleanExHS_PLEK.
GenevestigatorP08567.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.30.29.30. 2 hits.
InterProIPR000591. DEP_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00610. DEP. 1 hit.
PF00169. PH. 2 hits.
[Graphical view]
SMARTSM00049. DEP. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
PROSITEPS50186. DEP. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08567.
GenomeRNAi5341.
NextBio20702.
PROP08567.
SOURCESearch...

Entry information

Entry namePLEK_HUMAN
AccessionPrimary (citable) accession number: P08567
Secondary accession number(s): B2R9E8 expand/collapse secondary AC list , Q53SU8, Q6FGM8, Q6FGQ1, Q8WV81
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 154 of the entry and version 3 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM