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Pleckstrin homology-like domain family A member 2 (Beckwith-Wiedemann syndrome chromosomal region 1 candidate gene C protein) (Imprinted in placenta and liver protein) (Tumor-suppressing STF cDNA 3 protein) (Tumor-suppressing subchromosomal transferable fragment candidate gene 3 protein) (p17-Beckwith-Wiedemann region 1 C) (p17-BWR1C)

 PHLA2_HUMAN             Reviewed;         152 AA.
Q53GA4; O00496;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 2.
28-MAR-2018, entry version 107.
RecName: Full=Pleckstrin homology-like domain family A member 2;
AltName: Full=Beckwith-Wiedemann syndrome chromosomal region 1 candidate gene C protein;
AltName: Full=Imprinted in placenta and liver protein;
AltName: Full=Tumor-suppressing STF cDNA 3 protein;
AltName: Full=Tumor-suppressing subchromosomal transferable fragment candidate gene 3 protein;
AltName: Full=p17-Beckwith-Wiedemann region 1 C;
Short=p17-BWR1C;
Name=PHLDA2; Synonyms=BWR1C, HLDA2, IPL, TSSC3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9403053; DOI=10.1006/geno.1997.4981;
Hu R.-J., Lee M.P., Connors T.D., Johnson L.A., Burn T.C., Su K.,
Landes G.M., Feinberg A.P.;
"A 2.5-Mb transcript map of a tumor-suppressing subchromosomal
transferable fragment from 11p15.5, and isolation and sequence
analysis of three novel genes.";
Genomics 46:9-17(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=9328465; DOI=10.1093/hmg/6.12.2021;
Qian N., Frank D., O'Keefe D., Dao D., Zhao L., Yuan L., Wang Q.,
Keating M., Walsh C., Tycko B.;
"The IPL gene on chromosome 11p15.5 is imprinted in humans and mice
and is similar to TDAG51, implicated in Fas expression and
apoptosis.";
Hum. Mol. Genet. 6:2021-2029(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9520460; DOI=10.1073/pnas.95.7.3873;
Schwienbacher C., Sabbioni S., Campi M., Veronese A., Bernardi G.,
Menegatti A., Hatada I., Mukai T., Ohashi H., Barbanti-Brodano G.,
Croce C.M., Negrini M.;
"Transcriptional map of 170-kb region at chromosome 11p15.5:
identification and mutational analysis of the BWR1A gene reveals the
presence of mutations in tumor samples.";
Proc. Natl. Acad. Sci. U.S.A. 95:3873-3878(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical vein;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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).
[7]
TISSUE SPECIFICITY.
PubMed=10594239; DOI=10.1007/s003359901182;
Frank D., Mendelsohn C.L., Ciccone E., Svensson K., Ohlsson R.,
Tycko B.;
"A novel pleckstrin homology-related gene family defined by Ipl/Tssc3,
TDAG51, and Tih1: tissue-specific expression, chromosomal location,
and parental imprinting.";
Mamm. Genome 10:1150-1159(1999).
[8]
TISSUE SPECIFICITY.
PubMed=10749982; DOI=10.1093/hmg/9.5.757;
Mueller S., van den Boom D., Zirkel D., Koester H., Berthold F.,
Schwab M., Westphal M., Zumkeller W.;
"Retention of imprinting of the human apoptosis-related gene TSSC3 in
human brain tumors.";
Hum. Mol. Genet. 9:757-763(2000).
[9]
TISSUE SPECIFICITY.
PubMed=13129680; DOI=10.1016/S0143-4004(03)00130-9;
Saxena A., Frank D., Panichkul P., Van den Veyver I.B., Tycko B.,
Thaker H.;
"The product of the imprinted gene IPL marks human villous
cytotrophoblast and is lost in complete hydatidiform mole.";
Placenta 24:835-842(2003).
[10]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15457853;
Thaker H.M., Berlin A., Tycko B., Goldstein D.P., Berkowitz R.S.,
Castrillon D.H., Genest D.R.;
"Immunohistochemistry for the imprinted gene product IPL/PHLDA2 for
facilitating the differential diagnosis of complete hydatidiform
mole.";
J. Reprod. Med. 49:630-636(2004).
[11]
INDUCTION, AND IMPRINTING.
PubMed=15314611; DOI=10.1038/modpathol.3800175;
Fisher R.A., Nucci M.R., Thaker H.M., Weremowicz S., Genest D.R.,
Castrillon D.H.;
"Complete hydatidiform mole retaining a chromosome 11 of maternal
origin: molecular genetic analysis of a case.";
Mod. Pathol. 17:1155-1160(2004).
[12]
IMPRINTING.
PubMed=17303335; DOI=10.1016/j.bbagen.2007.01.004;
Tang K.-F., Wang Y., Wang P., Chen M., Chen Y., Hu H.-D., Hu P.,
Wang B., Yang W., Ren H.;
"Upregulation of PHLDA2 in Dicer knockdown HEK293 cells.";
Biochim. Biophys. Acta 1770:820-825(2007).
[13]
INDUCTION.
PubMed=16584773; DOI=10.1016/j.placenta.2006.01.025;
Kim H.-S., Roh C.-R., Chen B., Tycko B., Nelson D.M., Sadovsky Y.;
"Hypoxia regulates the expression of PHLDA2 in primary term human
trophoblasts.";
Placenta 28:77-84(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-141 AND SER-144,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-144 AND THR-151,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
LACK OF INDUCTION BY TP53.
PubMed=19203586; DOI=10.1016/j.cell.2008.12.002;
Kawase T., Ohki R., Shibata T., Tsutsumi S., Kamimura N., Inazawa J.,
Ohta T., Ichikawa H., Aburatani H., Tashiro F., Taya Y.;
"PH domain-only protein PHLDA3 is a p53-regulated repressor of Akt.";
Cell 136:535-550(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-42, 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).
-!- FUNCTION: Plays a role in regulating placenta growth. May act via
its PH domain that competes with other PH domain-containing
proteins, thereby preventing their binding to membrane lipids (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in placenta and adult prostate
gland. In placenta, it is present in all cells of the villous
cytotrophoblast. The protein is absent in cells from hydatidiform
moles. Hydatidiform mole is a gestation characterized by abnormal
development of both fetus and trophoblast. The majority of
hydatidiform moles are associated with an excess of paternal to
maternal genomes and are likely to result from the abnormal
expression of imprinted genes (at protein level). Expressed at low
levels in adult liver and lung, and fetal liver. Expressed in
adult brain and neuroblastoma, medullablastoma and glioblastoma
cell lines. {ECO:0000269|PubMed:10594239,
ECO:0000269|PubMed:10749982, ECO:0000269|PubMed:13129680,
ECO:0000269|PubMed:15457853, ECO:0000269|PubMed:9328465}.
-!- INDUCTION: Maternal PHLDA2 allele is activated, while paternal
Phlda2 is repressed due to genomic imprinting. Down-regulated by
hypoxia. Although highly similar to PHLDA3 protein, it is not
regulated by p53/TP53. {ECO:0000269|PubMed:15314611,
ECO:0000269|PubMed:16584773}.
-!- DOMAIN: The PH domain binds phosphoinositides with a broad
specificity. It may compete with the PH domain of some other
proteins, thereby interfering with their binding to
phosphatidylinositol 4,5-bisphosphate (PIP2) and
phosphatidylinositol 3,4,5-trisphosphate (PIP3) (By similarity).
{ECO:0000250}.
-!- MISCELLANEOUS: The PHLDA2 locus is imprinted. Loss of imprinting
results in overexpression. Imprinting is dependent on RNAi
machinery.
-!- SIMILARITY: Belongs to the PHLDA2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF019953; AAC51912.1; -; mRNA.
EMBL; AF001294; AAB86680.1; -; mRNA.
EMBL; AF035444; AAC17458.1; -; mRNA.
EMBL; CR407664; CAG28592.1; -; mRNA.
EMBL; AK223027; BAD96747.1; -; mRNA.
EMBL; BC005034; AAH05034.1; -; mRNA.
CCDS; CCDS7741.1; -.
RefSeq; NP_003302.1; NM_003311.3.
UniGene; Hs.154036; -.
ProteinModelPortal; Q53GA4; -.
SMR; Q53GA4; -.
BioGrid; 113113; 3.
IntAct; Q53GA4; 5.
STRING; 9606.ENSP00000319231; -.
iPTMnet; Q53GA4; -.
PhosphoSitePlus; Q53GA4; -.
BioMuta; PHLDA2; -.
DMDM; 84029394; -.
EPD; Q53GA4; -.
MaxQB; Q53GA4; -.
PaxDb; Q53GA4; -.
PeptideAtlas; Q53GA4; -.
PRIDE; Q53GA4; -.
DNASU; 7262; -.
Ensembl; ENST00000314222; ENSP00000319231; ENSG00000181649.
Ensembl; ENST00000618418; ENSP00000483602; ENSG00000274538.
GeneID; 7262; -.
KEGG; hsa:7262; -.
UCSC; uc001lxa.2; human.
CTD; 7262; -.
DisGeNET; 7262; -.
EuPathDB; HostDB:ENSG00000181649.5; -.
GeneCards; PHLDA2; -.
HGNC; HGNC:12385; PHLDA2.
HPA; HPA003994; -.
MIM; 602131; gene.
neXtProt; NX_Q53GA4; -.
OpenTargets; ENSG00000181649; -.
PharmGKB; PA37053; -.
eggNOG; ENOG410IZC3; Eukaryota.
eggNOG; ENOG4111IXF; LUCA.
GeneTree; ENSGT00440000039564; -.
HOGENOM; HOG000115528; -.
HOVERGEN; HBG052730; -.
InParanoid; Q53GA4; -.
OMA; KKVDCVE; -.
OrthoDB; EOG091G0RST; -.
PhylomeDB; Q53GA4; -.
TreeFam; TF332320; -.
GeneWiki; PHLDA2; -.
GenomeRNAi; 7262; -.
PRO; PR:Q53GA4; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000181649; -.
CleanEx; HS_PHLDA2; -.
Genevisible; Q53GA4; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0001890; P:placenta development; IEA:Ensembl.
GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0070873; P:regulation of glycogen metabolic process; IEA:Ensembl.
GO; GO:1903547; P:regulation of growth hormone activity; IEA:Ensembl.
GO; GO:0060721; P:regulation of spongiotrophoblast cell proliferation; IEA:Ensembl.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
SMART; SM00233; PH; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Membrane; Phosphoprotein;
Reference proteome.
CHAIN 1 152 Pleckstrin homology-like domain family A
member 2.
/FTId=PRO_0000053900.
DOMAIN 7 99 PH.
COMPBIAS 126 133 Poly-Ala.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 42 42 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 141 141 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976}.
MOD_RES 151 151 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
CONFLICT 24 24 W -> R (in Ref. 5; BAD96747).
{ECO:0000305}.
SEQUENCE 152 AA; 17092 MW; 3A1168CBB859FC3B CRC64;
MKSPDEVLRE GELEKRSDSL FQLWKKKRGV LTSDRLSLFP ASPRARPKEL RFHSILKVDC
VERTGKYVYF TIVTTDHKEI DFRCAGESCW NAAIALALID FQNRRALQDF RSRQERTAPA
APAEDAVAAA AAAPSEPSEP SRPSPQPKPR TP


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