Full text data of PLEK2
PLEK2
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Pleckstrin-2
Pleckstrin-2
UniProt
Q9NYT0
ID PLEK2_HUMAN Reviewed; 353 AA.
AC Q9NYT0; Q96JT0;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Pleckstrin-2;
GN Name=PLEK2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Inazu T.;
RT "Homo sapiens pleckstrin 2: cloning and characterization.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [4]
RP STRUCTURE BY NMR OF 238-353.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C-terminal PH domain of human pleckstrin
RT 2.";
RL Submitted (OCT-2005) to the PDB data bank.
CC -!- FUNCTION: May help orchestrate cytoskeletal arrangement.
CC Contribute to lamellipodia formation.
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium membrane;
CC Peripheral membrane protein. Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Contains 1 DEP domain.
CC -!- SIMILARITY: Contains 2 PH domains.
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; AF228603; AAF34791.1; -; mRNA.
DR EMBL; BC001226; AAH01226.1; -; mRNA.
DR EMBL; BC008056; AAH08056.2; -; mRNA.
DR RefSeq; NP_057529.1; NM_016445.1.
DR UniGene; Hs.170473; -.
DR PDB; 1X1G; NMR; -; A=238-353.
DR PDBsum; 1X1G; -.
DR ProteinModelPortal; Q9NYT0; -.
DR SMR; Q9NYT0; 4-95, 129-235, 241-353.
DR PhosphoSite; Q9NYT0; -.
DR DMDM; 20532216; -.
DR PaxDb; Q9NYT0; -.
DR PRIDE; Q9NYT0; -.
DR DNASU; 26499; -.
DR Ensembl; ENST00000216446; ENSP00000216446; ENSG00000100558.
DR GeneID; 26499; -.
DR KEGG; hsa:26499; -.
DR UCSC; uc001xjh.1; human.
DR CTD; 26499; -.
DR GeneCards; GC14M067853; -.
DR HGNC; HGNC:19238; PLEK2.
DR HPA; HPA001208; -.
DR MIM; 608007; gene.
DR neXtProt; NX_Q9NYT0; -.
DR PharmGKB; PA134963543; -.
DR eggNOG; NOG44162; -.
DR HOGENOM; HOG000294078; -.
DR HOVERGEN; HBG001361; -.
DR InParanoid; Q9NYT0; -.
DR OMA; TEYFLEA; -.
DR OrthoDB; EOG74XS6R; -.
DR PhylomeDB; Q9NYT0; -.
DR EvolutionaryTrace; Q9NYT0; -.
DR GeneWiki; PLEK2; -.
DR GenomeRNAi; 26499; -.
DR NextBio; 48764; -.
DR PRO; PR:Q9NYT0; -.
DR ArrayExpress; Q9NYT0; -.
DR Bgee; Q9NYT0; -.
DR CleanEx; HS_PLEK2; -.
DR Genevestigator; Q9NYT0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00169; PH; 2.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00233; PH; 2.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cell projection;
KW Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 353 Pleckstrin-2.
FT /FTId=PRO_0000053862.
FT DOMAIN 4 104 PH 1.
FT DOMAIN 139 225 DEP.
FT DOMAIN 247 353 PH 2.
FT MOD_RES 1 1 N-acetylmethionine.
FT VARIANT 80 80 T -> M (in dbSNP:rs34300264).
FT /FTId=VAR_050504.
FT STRAND 246 257
FT STRAND 259 275
FT STRAND 277 281
FT STRAND 283 285
FT STRAND 294 296
FT STRAND 306 309
FT STRAND 322 324
FT STRAND 332 334
FT HELIX 339 352
SQ SEQUENCE 353 AA; 39971 MW; CE355BF917F2385E CRC64;
MEDGVLKEGF LVKRGHIVHN WKARWFILRQ NTLVYYKLEG GRRVTPPKGR ILLDGCTITC
PCLEYENRPL LIKLKTQTST EYFLEACSRE ERDAWAFEIT GAIHAGQPGK VQQLHSLRNS
FKLPPHISLH RIVDKMHDSN TGIRSSPNME QGSTYKKTFL GSSLVDWLIS NSFTASRLEA
VTLASMLMEE NFLRPVGVRS MGAIRSGDLA EQFLDDSTAL YTFAESYKKK ISPKEEISLS
TVELSGTVVK QGYLAKQGHK RKNWKVRRFV LRKDPAFLHY YDPSKEENRP VGGFSLRGSL
VSALEDNGVP TGVKGNVQGN LFKVITKDDT HYYIQASSKA ERAEWIEAIK KLT
//
ID PLEK2_HUMAN Reviewed; 353 AA.
AC Q9NYT0; Q96JT0;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Pleckstrin-2;
GN Name=PLEK2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Inazu T.;
RT "Homo sapiens pleckstrin 2: cloning and characterization.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [4]
RP STRUCTURE BY NMR OF 238-353.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C-terminal PH domain of human pleckstrin
RT 2.";
RL Submitted (OCT-2005) to the PDB data bank.
CC -!- FUNCTION: May help orchestrate cytoskeletal arrangement.
CC Contribute to lamellipodia formation.
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium membrane;
CC Peripheral membrane protein. Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Contains 1 DEP domain.
CC -!- SIMILARITY: Contains 2 PH domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF228603; AAF34791.1; -; mRNA.
DR EMBL; BC001226; AAH01226.1; -; mRNA.
DR EMBL; BC008056; AAH08056.2; -; mRNA.
DR RefSeq; NP_057529.1; NM_016445.1.
DR UniGene; Hs.170473; -.
DR PDB; 1X1G; NMR; -; A=238-353.
DR PDBsum; 1X1G; -.
DR ProteinModelPortal; Q9NYT0; -.
DR SMR; Q9NYT0; 4-95, 129-235, 241-353.
DR PhosphoSite; Q9NYT0; -.
DR DMDM; 20532216; -.
DR PaxDb; Q9NYT0; -.
DR PRIDE; Q9NYT0; -.
DR DNASU; 26499; -.
DR Ensembl; ENST00000216446; ENSP00000216446; ENSG00000100558.
DR GeneID; 26499; -.
DR KEGG; hsa:26499; -.
DR UCSC; uc001xjh.1; human.
DR CTD; 26499; -.
DR GeneCards; GC14M067853; -.
DR HGNC; HGNC:19238; PLEK2.
DR HPA; HPA001208; -.
DR MIM; 608007; gene.
DR neXtProt; NX_Q9NYT0; -.
DR PharmGKB; PA134963543; -.
DR eggNOG; NOG44162; -.
DR HOGENOM; HOG000294078; -.
DR HOVERGEN; HBG001361; -.
DR InParanoid; Q9NYT0; -.
DR OMA; TEYFLEA; -.
DR OrthoDB; EOG74XS6R; -.
DR PhylomeDB; Q9NYT0; -.
DR EvolutionaryTrace; Q9NYT0; -.
DR GeneWiki; PLEK2; -.
DR GenomeRNAi; 26499; -.
DR NextBio; 48764; -.
DR PRO; PR:Q9NYT0; -.
DR ArrayExpress; Q9NYT0; -.
DR Bgee; Q9NYT0; -.
DR CleanEx; HS_PLEK2; -.
DR Genevestigator; Q9NYT0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00169; PH; 2.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00233; PH; 2.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cell projection;
KW Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 353 Pleckstrin-2.
FT /FTId=PRO_0000053862.
FT DOMAIN 4 104 PH 1.
FT DOMAIN 139 225 DEP.
FT DOMAIN 247 353 PH 2.
FT MOD_RES 1 1 N-acetylmethionine.
FT VARIANT 80 80 T -> M (in dbSNP:rs34300264).
FT /FTId=VAR_050504.
FT STRAND 246 257
FT STRAND 259 275
FT STRAND 277 281
FT STRAND 283 285
FT STRAND 294 296
FT STRAND 306 309
FT STRAND 322 324
FT STRAND 332 334
FT HELIX 339 352
SQ SEQUENCE 353 AA; 39971 MW; CE355BF917F2385E CRC64;
MEDGVLKEGF LVKRGHIVHN WKARWFILRQ NTLVYYKLEG GRRVTPPKGR ILLDGCTITC
PCLEYENRPL LIKLKTQTST EYFLEACSRE ERDAWAFEIT GAIHAGQPGK VQQLHSLRNS
FKLPPHISLH RIVDKMHDSN TGIRSSPNME QGSTYKKTFL GSSLVDWLIS NSFTASRLEA
VTLASMLMEE NFLRPVGVRS MGAIRSGDLA EQFLDDSTAL YTFAESYKKK ISPKEEISLS
TVELSGTVVK QGYLAKQGHK RKNWKVRRFV LRKDPAFLHY YDPSKEENRP VGGFSLRGSL
VSALEDNGVP TGVKGNVQGN LFKVITKDDT HYYIQASSKA ERAEWIEAIK KLT
//
MIM
608007
*RECORD*
*FIELD* NO
608007
*FIELD* TI
*608007 PLECKSTRIN 2; PLEK2
*FIELD* TX
CLONING
Using the sequence of human pleckstrin (PLEK; 173570) as query, Hu et
read moreal. (1999) identified mouse pleckstrin-2, which encodes a deduced
353-amino acid protein. By EST database searching with mouse Plek2, they
identified the human homolog, which encodes a deduced protein that is
identical to mouse Plek and 39% identical to human PLEK. Like PLEK,
human PLEK2 contains an N- and a C-terminal PH domain plus an
intervening DEP domain. Unlike PLEK, which contains 3 phosphorylation
sites, PLEK2 contains only 1 site comparable to ser117 in PLEK. Northern
blot analysis of human tissues detected ubiquitous expression of a
1.7-kb PLEK2 transcript, with highest expression in thymus, prostate,
testis, ovary, small bowel, and large bowel.
GENE FUNCTION
Using transfection experiments in COS-7 cells, Hu et al. (1999)
determined that, unlike PLEK, PLEK2 is not an efficient substrate of
PKC. PLEK2 is bound to the cell membrane, and its PH domains appear to
contribute to lamellipodia formation. Overexpression of PLEK2 causes
large lamellipodia and peripheral ruffle formation. Hu et al. (1999)
suggested that PLEK2 may help orchestrate cytoskeletal arrangement.
*FIELD* RF
1. Hu, M. H.; Bauman, E. M.; Roll, R. L.; Yeilding, N.; Abrams, C.
S.: Pleckstrin 2, a widely expressed paralog of pleckstrin involved
in actin rearrangement. J. Biol. Chem. 274: 21515-21518, 1999.
*FIELD* CD
Carol A. Bocchini: 8/4/2003
*FIELD* ED
tkritzer: 08/05/2003
carol: 8/4/2003
*RECORD*
*FIELD* NO
608007
*FIELD* TI
*608007 PLECKSTRIN 2; PLEK2
*FIELD* TX
CLONING
Using the sequence of human pleckstrin (PLEK; 173570) as query, Hu et
read moreal. (1999) identified mouse pleckstrin-2, which encodes a deduced
353-amino acid protein. By EST database searching with mouse Plek2, they
identified the human homolog, which encodes a deduced protein that is
identical to mouse Plek and 39% identical to human PLEK. Like PLEK,
human PLEK2 contains an N- and a C-terminal PH domain plus an
intervening DEP domain. Unlike PLEK, which contains 3 phosphorylation
sites, PLEK2 contains only 1 site comparable to ser117 in PLEK. Northern
blot analysis of human tissues detected ubiquitous expression of a
1.7-kb PLEK2 transcript, with highest expression in thymus, prostate,
testis, ovary, small bowel, and large bowel.
GENE FUNCTION
Using transfection experiments in COS-7 cells, Hu et al. (1999)
determined that, unlike PLEK, PLEK2 is not an efficient substrate of
PKC. PLEK2 is bound to the cell membrane, and its PH domains appear to
contribute to lamellipodia formation. Overexpression of PLEK2 causes
large lamellipodia and peripheral ruffle formation. Hu et al. (1999)
suggested that PLEK2 may help orchestrate cytoskeletal arrangement.
*FIELD* RF
1. Hu, M. H.; Bauman, E. M.; Roll, R. L.; Yeilding, N.; Abrams, C.
S.: Pleckstrin 2, a widely expressed paralog of pleckstrin involved
in actin rearrangement. J. Biol. Chem. 274: 21515-21518, 1999.
*FIELD* CD
Carol A. Bocchini: 8/4/2003
*FIELD* ED
tkritzer: 08/05/2003
carol: 8/4/2003