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Pleckstrin homology domain-containing family M member 1 (PH domain-containing family M member 1) (162 kDa adapter protein) (AP162)

 PKHM1_HUMAN             Reviewed;        1056 AA.
Q9Y4G2; Q6P2R5; Q8TEL9; Q9NPP5; Q9NYA0;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 3.
22-NOV-2017, entry version 133.
RecName: Full=Pleckstrin homology domain-containing family M member 1;
Short=PH domain-containing family M member 1;
AltName: Full=162 kDa adapter protein;
Short=AP162;
Name=PLEKHM1; Synonyms=KIAA0356;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=9205841; DOI=10.1093/dnares/4.2.141;
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 82-1056, TISSUE SPECIFICITY, FUNCTION,
AND INTERACTION WITH SIALYL-LEX POSITIVE MUCIN.
TISSUE=Colon carcinoma;
PubMed=12820725; DOI=10.1023/A:1022256610674;
Hartel-Schenk S., Gratchev A., Hanski M.-L., Ogorek D.,
Trendelenburg G., Hummel M., Hoepfner M., Scheruebl H., Zeitz M.,
Hanski C.;
"Novel adapter protein AP162 connects a sialyl-Le(x)-positive mucin
with an apoptotic signal transduction pathway.";
Glycoconj. J. 18:915-923(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 425-1056.
TISSUE=Spleen;
Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
"The nucleotide sequence of a long cDNA clone isolated from human
spleen.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-832.
The European IMAGE consortium;
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[6]
INVOLVEMENT IN OPTB6.
PubMed=17404618; DOI=10.1172/JCI30328;
van Wesenbeeck L., Odgren P.R., Coxon F.P., Frattini A., Moens P.,
Perdu B., MacKay C.A., Van Hul E., Timmermanns J.-P., Vanhoenacker F.,
Jacobs R., Peruzzi B., Teti A., Helfrich M.H., Rogers M.J., Villa A.,
Van Hul W.;
"Involvement of PLEKHM1 in osteoclastic vesicular transport and
osteopetrosis in incisors absent rats and humans.";
J. Clin. Invest. 117:919-930(2007).
[7]
FUNCTION, INTERACTION WITH RAB7, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF CYS-1021; CYS-1024; HIS-1029 AND CYS-1032.
PubMed=20943950; DOI=10.1091/mbc.E10-06-0495;
Tabata K., Matsunaga K., Sakane A., Sasaki T., Noda T., Yoshimori T.;
"Rubicon and PLEKHM1 negatively regulate the endocytic/autophagic
pathway via a novel Rab7-binding domain.";
Mol. Biol. Cell 21:4162-4172(2010).
[8]
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, 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).
[10]
FUNCTION, INTERACTION WITH RAB7A; VPS41 AND S.TYPHIMURIUM SIFA,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 720-LYS--LEU-722; GLU-729 AND
ARG-769.
PubMed=25500191; DOI=10.1016/j.chom.2014.11.011;
McEwan D.G., Richter B., Claudi B., Wigge C., Wild P., Farhan H.,
McGourty K., Coxon F.P., Franz-Wachtel M., Perdu B., Akutsu M.,
Habermann A., Kirchof A., Helfrich M.H., Odgren P.R., Van Hul W.,
Frangakis A.S., Rajalingam K., Macek B., Holden D.W., Bumann D.,
Dikic I.;
"PLEKHM1 regulates Salmonella-containing vacuole biogenesis and
infection.";
Cell Host Microbe 17:58-71(2015).
[11]
FUNCTION, INTERACTION WITH VPS41; VPS11; VPS39; GABARAP; GABARAPL;
GABARAPL2; MAP1LC3A; MAP1LC3B AND MAP1LC3C, SUBUNIT, SUBCELLULAR
LOCATION, AND DOMAIN.
PubMed=25498145; DOI=10.1016/j.molcel.2014.11.006;
McEwan D.G., Popovic D., Gubas A., Terawaki S., Suzuki H., Stadel D.,
Coxon F.P., Miranda de Stegmann D., Bhogaraju S., Maddi K.,
Kirchof A., Gatti E., Helfrich M.H., Wakatsuki S., Behrends C.,
Pierre P., Dikic I.;
"PLEKHM1 regulates autophagosome-lysosome fusion through HOPS complex
and LC3/GABARAP proteins.";
Mol. Cell 57:39-54(2015).
-!- FUNCTION: Proposed to act as a multivalent adapter protein that
regulates Rab7-dependent and HOPS complex-dependent fusion events
in the endolysosomal system and couples autophagic and the
endocytic trafficking pathways. Required for late stages of
endolysosomal maturation, facilitating both endocytosis-mediated
degradation of growth factor receptors and autophagosome
clearance. Seems to be involved in the terminal maturation of
autophagosomes and to mediate autophagosome-lysosome fusion
(PubMed:25498145). Positively regulates lysosome peripheral
distribution and ruffled border formation in osteoclasts (By
similarity). May be involved in negative regulation of endocytic
transport from early endosome to late endosome/lysosome
implicating its association with Rab7 (PubMed:20943950). May have
a role in sialyl-lex-mediated transduction of apoptotic signals
(PubMed:12820725). Involved in bone resorption (By similarity). In
case of infection contributes to Salmonella typhimurium
pathogenesis by supporting the integrity of the Salmonella-
containing vacuole (SCV) probably in concert with the HOPS complex
and Rab7 (PubMed:25500191). {ECO:0000250|UniProtKB:Q5PQS0,
ECO:0000250|UniProtKB:Q7TSI1, ECO:0000269|PubMed:12820725,
ECO:0000269|PubMed:20943950, ECO:0000269|PubMed:25498145,
ECO:0000269|PubMed:25500191, ECO:0000305}.
-!- SUBUNIT: Interacts (via N- and C-terminus) with RAB7A (GTP-bound
form) (PubMed:20943950, PubMed:25500191). Interacts with VPS41,
VPS11 and VPS39; indicative for an association with the HOPS
complex; the interaction with VPS41 seems to require RAB7A
(PubMed:25500191, PubMed:25498145). Interacts with GABARAP,
GABARAPL, GABARAPL2, MAP1LC3A, MAP1LC3B and MAP1LC3C
(PubMed:25498145). Interacts with PAFAH1B (By similarity).
Interacts with Salmonella typhimurium sifA (PubMed:25500191).
Interacts (via N- and C-terminus) with NDEL1 (By similarity).
Interacts (via C-terminus) with MAP3K7 (By similarity). Interacts
(via N- and C-terminus) with FAM98A (By similarity). Interacts
(via C-terminus) with DEF8; this interaction is weak but increased
in a RAB7A-dependent manner (By similarity). In colon carcinoma
and breast carcinoma cells, it interacts with sialyl-lex-positive
protein (PubMed:12820725). {ECO:0000250|UniProtKB:Q7TSI1,
ECO:0000269|PubMed:12820725, ECO:0000269|PubMed:20943950,
ECO:0000269|PubMed:25498145, ECO:0000269|PubMed:25500191}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Endosome membrane
{ECO:0000269|PubMed:20943950}. Lysosome
{ECO:0000269|PubMed:25500191}. Lysosome membrane
{ECO:0000269|PubMed:25498145}. Note=Localizes to the external
membrane of autolysosomes (PubMed:25498145). In case of infection
colocalizes with Salmonella typhimurium sifA in proximity of
Salmonella-containing vacuole (SCV) (PubMed:25500191).
{ECO:0000269|PubMed:25498145, ECO:0000269|PubMed:25500191}.
-!- TISSUE SPECIFICITY: Expressed in placenta, liver, prostate,
thymus, spleen, ovary, colon, colon carcinoma and peripheral blood
lymphocytes (PBL). Weakly expressed in brain, lung, kidney, and
testis. No expression in heart, skeletal muscle, pancreas and
small intestine. Predominantly expressed in the breast carcinoma
cell line MCF-7. {ECO:0000269|PubMed:12820725,
ECO:0000269|PubMed:9205841}.
-!- DOMAIN: The LIR (LC3-interacting region) motif mediates the
interaction with ATG8 family proteins GABARAP, GABARAPL,
GABARAPL2, and LC3A/B/C. {ECO:0000269|PubMed:25498145}.
-!- DISEASE: Osteopetrosis, autosomal recessive 6 (OPTB6)
[MIM:611497]: A rare genetic disease characterized by abnormally
dense bone, due to defective resorption of immature bone.
Osteopetrosis occurs in two forms: a severe autosomal recessive
form occurring in utero, infancy, or childhood, and a benign
autosomal dominant form occurring in adolescence or adulthood.
Recessive osteopetrosis commonly manifests in early infancy with
macrocephaly, feeding difficulties, evolving blindness and
deafness, bone marrow failure, severe anemia, and
hepatosplenomegaly. Deafness and blindness are generally thought
to represent effects of pressure on nerves.
{ECO:0000269|PubMed:17404618}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Sialyl-lex is a carcinoma associated antigen.
-!- SEQUENCE CAUTION:
Sequence=BAA20813.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAB91652.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB002354; BAA20813.2; ALT_INIT; mRNA.
EMBL; BC064361; AAH64361.1; -; mRNA.
EMBL; AJ002220; CAB91652.1; ALT_INIT; mRNA.
EMBL; AK074103; BAB84929.1; -; mRNA.
EMBL; AL389948; CAB97526.1; -; mRNA.
CCDS; CCDS32671.1; -.
RefSeq; NP_055613.1; NM_014798.2.
RefSeq; XP_006722264.1; XM_006722201.3.
RefSeq; XP_011523825.1; XM_011525523.2.
RefSeq; XP_011523826.1; XM_011525524.1.
RefSeq; XP_016880940.1; XM_017025451.1.
RefSeq; XP_016880942.1; XM_017025453.1.
UniGene; Hs.514242; -.
PDB; 5DPR; X-ray; 2.50 A; A/B/C/D=627-638.
PDB; 5DPS; X-ray; 2.00 A; A/B/C=627-638.
PDB; 5DPT; X-ray; 2.90 A; A/B=627-638.
PDB; 5DPW; X-ray; 2.19 A; B/D/F/H/J/L/N/P=629-642.
PDBsum; 5DPR; -.
PDBsum; 5DPS; -.
PDBsum; 5DPT; -.
PDBsum; 5DPW; -.
ProteinModelPortal; Q9Y4G2; -.
SMR; Q9Y4G2; -.
BioGrid; 115178; 7.
IntAct; Q9Y4G2; 8.
MINT; MINT-1400097; -.
STRING; 9606.ENSP00000389913; -.
iPTMnet; Q9Y4G2; -.
PhosphoSitePlus; Q9Y4G2; -.
BioMuta; PLEKHM1; -.
DMDM; 160419247; -.
EPD; Q9Y4G2; -.
MaxQB; Q9Y4G2; -.
PaxDb; Q9Y4G2; -.
PeptideAtlas; Q9Y4G2; -.
PRIDE; Q9Y4G2; -.
Ensembl; ENST00000430334; ENSP00000389913; ENSG00000225190.
Ensembl; ENST00000613787; ENSP00000479066; ENSG00000277111.
Ensembl; ENST00000617688; ENSP00000483820; ENSG00000276358.
GeneID; 9842; -.
KEGG; hsa:9842; -.
UCSC; uc002ija.4; human.
CTD; 9842; -.
DisGeNET; 9842; -.
EuPathDB; HostDB:ENSG00000225190.8; -.
GeneCards; PLEKHM1; -.
H-InvDB; HIX0014106; -.
H-InvDB; HIX0174141; -.
HGNC; HGNC:29017; PLEKHM1.
HPA; HPA025018; -.
HPA; HPA039473; -.
MalaCards; PLEKHM1; -.
MIM; 611466; gene.
MIM; 611497; phenotype.
neXtProt; NX_Q9Y4G2; -.
OpenTargets; ENSG00000225190; -.
Orphanet; 210110; Intermediate osteopetrosis.
PharmGKB; PA134906881; -.
eggNOG; ENOG410ITGM; Eukaryota.
eggNOG; ENOG4111EZ2; LUCA.
GeneTree; ENSGT00550000074570; -.
HOGENOM; HOG000247013; -.
HOVERGEN; HBG056799; -.
InParanoid; Q9Y4G2; -.
OMA; PAFFKII; -.
OrthoDB; EOG091G013Y; -.
PhylomeDB; Q9Y4G2; -.
TreeFam; TF317067; -.
ChiTaRS; PLEKHM1; human.
GeneWiki; PLEKHM1; -.
GenomeRNAi; 9842; -.
PRO; PR:Q9Y4G2; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000225190; -.
CleanEx; HS_PLEKHM1; -.
ExpressionAtlas; Q9Y4G2; baseline and differential.
Genevisible; Q9Y4G2; HS.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
GO; GO:0045780; P:positive regulation of bone resorption; ISS:UniProtKB.
GO; GO:1900029; P:positive regulation of ruffle assembly; ISS:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
CDD; cd00029; C1; 1.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR004012; Run_dom.
InterPro; IPR037213; Run_dom_sf.
InterPro; IPR025258; Zf-RING_9.
Pfam; PF02759; RUN; 1.
Pfam; PF13901; zf-RING_9; 1.
SMART; SM00109; C1; 1.
SMART; SM01175; DUF4206; 1.
SMART; SM00233; PH; 2.
SMART; SM00593; RUN; 1.
SUPFAM; SSF140741; SSF140741; 1.
SUPFAM; SSF50729; SSF50729; 2.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50826; RUN; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Autophagy; Complete proteome; Cytoplasm; Endosome;
Lysosome; Membrane; Metal-binding; Osteopetrosis; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Repeat;
Transport; Zinc; Zinc-finger.
CHAIN 1 1056 Pleckstrin homology domain-containing
family M member 1.
/FTId=PRO_0000309335.
DOMAIN 41 183 RUN. {ECO:0000255|PROSITE-
ProRule:PRU00178}.
DOMAIN 534 625 PH 1. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 683 777 PH 2. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
ZN_FING 986 1040 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
REGION 654 1056 Interaction with RAB7A.
{ECO:0000269|PubMed:25500191}.
MOTIF 632 638 LIR. {ECO:0000305}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TSI1}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 435 435 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TSI1}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TSI1}.
VARIANT 377 377 R -> H (in dbSNP:rs1859059).
/FTId=VAR_036932.
MUTAGEN 720 722 Missing: Disrupts interaction with RAB7A.
{ECO:0000269|PubMed:25500191}.
MUTAGEN 729 729 E->A: Disrupts interaction with RAB7A.
{ECO:0000269|PubMed:25500191}.
MUTAGEN 769 769 R->A: Disrupts interaction with RAB7A.
{ECO:0000269|PubMed:25500191}.
MUTAGEN 1021 1021 C->G: Disrupts interaction with Rab7 and
no localization to endososmal membranes;
when associated with G-1024, L-1029 and
G-1032. {ECO:0000269|PubMed:20943950}.
MUTAGEN 1024 1024 C->G: Disrupts interaction with Rab7 and
no localization to endososmal membranes;
when associated with G-1021, L-1029 and
G-1032. {ECO:0000269|PubMed:20943950}.
MUTAGEN 1029 1029 H->L: Disrupts interaction with Rab7 and
no localization to endososmal membranes;
when associated with G-1021, G-1024 and
G-1032. {ECO:0000269|PubMed:20943950}.
MUTAGEN 1032 1032 C->G: Disrupts interaction with Rab7and
no localization to endososmal membranes;
when associated with G-1021, G-1024 and
L-1029. {ECO:0000269|PubMed:20943950}.
CONFLICT 429 436 VVSSPTSP -> GLRPVSAR (in Ref. 4;
BAB84929). {ECO:0000305}.
CONFLICT 817 817 A -> G (in Ref. 4; BAB84929).
{ECO:0000305}.
STRAND 635 637 {ECO:0000244|PDB:5DPW}.
SEQUENCE 1056 AA; 117443 MW; 24004093CFA89079 CRC64;
MLSVVENGLD PQAAIPVIKK KLVGSVKALQ KQYVSLDTVV TSEDGDANTM CSALEAVFIH
GLHAKHIRAE AGGKRKKSAH QKPLPQPVFW PLLKAVTHKH IISELEHLTF VNTDVGRCRA
WLRLALNDGL MECYLKLLLQ EQARLHEYYQ PTALLRDAEE GEFLLSFLQG LTSLSFELSY
KSAILNEWTL TPLALSGLCP LSELDPLSTS GAELQRKESL DSISHSSGSE DIEVHHSGHK
IRRNQKLTAS SLSLDTASSS QLSCSLNSDS CLLQENGSKS PDHCEEPMSC DSDLGTANAE
DSDRSLQEVL LEFSKAQVNS VPTNGLSQET EIPTPQASLS LHGLNTSTYL HCEAPAEPLP
AQAASGTQDG VHVQEPRPQA PSPLDLQQPV ESTSGQQPSS TVSETAREVG QGNGLQKAQA
HDGAGLKLVV SSPTSPKNKS WISEDDFYRP SREQPLESAS DHPIASYRGT PGSRPGLHRH
FSQEPRKNCS LGALDQACVP SPGRRQAQAA PSQGHKSFRV VHRRQMGLSN PFRGLMKLGT
VERRGAMGIW KELFCELSPL EFRLYLSNEE HTCVENCSLL RCESVGPAHS DGRFELVFSG
KKLALRASSQ DEAEDWLDRV REALQKVRPQ QEDEWVNVQY PDQPEEPPEA PQGCLSPSDL
LSEPAALQGT QFDWSSAQVP EPDAIKESLL YLYMDRTWMP YIFSLSLEAL KCFRIRNNEK
MLSDSHGVET IRDILPDTSL GGPSFFKIIT AKAVLKLQAG NAEEAALWRD LVRKVLASYL
ETAEEAVTLG GSLDENCQEV LKFATRENGF LLQYLVAIPM EKGLDSQGCF CAGCSRQIGF
SFVRPKLCAF SGLYYCDICH QDDASVIPAR IIHNWDLTKR PICRQALKFL TQIRAQPLIN
LQMVNASLYE HVERMHLIGR RREQLKLLGD YLGLCRSGAL KELSKRLNHR NYLLESPHRF
SVADLQQIAD GVYEGFLKAL IEFASQHVYH CDLCTQRGFI CQICQHHDII FPFEFDTTVR
CAECKTVFHQ SCQAVVKKGC PRCARRRKYQ EQNIFA


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EIAAB31264 Pepp1,PEPP-1,PH domain-containing family A member 4,Phosphoinositol 3-phosphate-binding protein 1,Pleckstrin homology domain-containing family A member 4,Plekha4,Rat,Rattus norvegicus
EIAAB31266 Mouse,Mus musculus,Pepp1,PEPP-1,PH domain-containing family A member 4,Phosphoinositol 3-phosphate-binding protein 1,Pleckstrin homology domain-containing family A member 4,Plekha4
EIAAB31293 Homo sapiens,Human,PH domain-containing family G member 4,Pleckstrin homology domain-containing family G member 4,PLEKHG4,PRTPHN1,Puratrophin-1,Purkinje cell atrophy-associated protein 1
EIAAB31265 Homo sapiens,Human,PEPP1,PEPP-1,PH domain-containing family A member 4,Phosphoinositol 3-phosphate-binding protein 1,Pleckstrin homology domain-containing family A member 4,PLEKHA4
EIAAB31269 Homo sapiens,Human,KIAA0969,PEPP3,PEPP-3,PH domain-containing family A member 6,Phosphoinositol 3-phosphate-binding protein 3,Pleckstrin homology domain-containing family A member 6,PLEKHA6
EIAAB31267 Homo sapiens,Human,KIAA1686,PEPP2,PEPP-2,PH domain-containing family A member 5,Phosphoinositol 3-phosphate-binding protein 2,Pleckstrin homology domain-containing family A member 5,PLEKHA5
EIAAB31295 Neuronal RhoA GEF protein,PH domain-containing family G member 5,Pleckstrin homology domain-containing family G member 5,Plekhg5,Rat,Rattus norvegicus,Tech,Transcript highly enriched in cortex and hip
EIAAB31286 Homo sapiens,Human,PH and FYVE domain-containing protein 2,PH domain-containing family F member 2,Phafin-2,Pleckstrin homology domain-containing family F member 2,PLEKHF2,ZFYVE18,Zinc finger FYVE doma
EIAAB31317 Homo sapiens,Human,KIAA0842,PH domain-containing family M member 2,Pleckstrin homology domain-containing family M member 2,PLEKHM2,Salmonella-induced filaments A and kinesin-interacting protein,SifA a


 

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