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Pleckstrin homology domain-containing family F member 2 (PH domain-containing family F member 2) (Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains) (EAPF) (PH and FYVE domain-containing protein 2) (Phafin-2) (Phafin2) (Zinc finger FYVE domain-containing protein 18)

 PKHF2_HUMAN             Reviewed;         249 AA.
Q9H8W4;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
28-MAR-2018, entry version 145.
RecName: Full=Pleckstrin homology domain-containing family F member 2;
Short=PH domain-containing family F member 2;
AltName: Full=Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains;
Short=EAPF;
AltName: Full=PH and FYVE domain-containing protein 2;
AltName: Full=Phafin-2;
Short=Phafin2;
AltName: Full=Zinc finger FYVE domain-containing protein 18;
Name=PLEKHF2; Synonyms=ZFYVE18;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Shi H., Hong W.;
"Phafin 2, PH and FYVE domain-containing protein 2.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Melanoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=B-cell;
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).
[5]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
DOMAIN.
PubMed=18288467; DOI=10.1007/s00109-007-0298-7;
Li C., Liu Q., Li N., Chen W., Wang L., Wang Y., Yu Y., Cao X.;
"EAPF/Phafin-2, a novel endoplasmic reticulum-associated protein,
facilitates TNF-alpha-triggered cellular apoptosis through endoplasmic
reticulum-mitochondrial apoptotic pathway.";
J. Mol. Med. 86:471-484(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, 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).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19995552; DOI=10.1016/j.bbrc.2009.12.016;
Lin W.J., Yang C.Y., Lin Y.C., Tsai M.C., Yang C.W., Tung C.Y.,
Ho P.Y., Kao F.J., Lin C.H.;
"Phafin2 modulates the structure and function of endosomes by a Rab5-
dependent mechanism.";
Biochem. Biophys. Res. Commun. 391:1043-1048(2010).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-248, 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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-248, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[12]
FUNCTION, INTERACTION WITH EEA1, AND SUBCELLULAR LOCATION.
PubMed=22816767; DOI=10.1111/j.1600-0854.2012.01400.x;
Pedersen N.M., Raiborg C., Brech A., Skarpen E., Roxrud I.,
Platta H.W., Liestol K., Stenmark H.;
"The PtdIns3P-binding protein Phafin 2 mediates epidermal growth
factor receptor degradation by promoting endosome fusion.";
Traffic 13:1547-1563(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: May play a role in early endosome fusion upstream of
RAB5, hence regulating receptor trafficking and fluid-phase
transport. Enhances cellular sensitivity to TNF-induced apoptosis
(PubMed:18288467). {ECO:0000269|PubMed:18288467,
ECO:0000269|PubMed:19995552, ECO:0000269|PubMed:22816767}.
-!- SUBUNIT: May interact with EEA1.
-!- INTERACTION:
Q96HD9:ACY3; NbExp=3; IntAct=EBI-742388, EBI-3916242;
Q13155:AIMP2; NbExp=3; IntAct=EBI-742388, EBI-745226;
Q9NPI1:BRD7; NbExp=4; IntAct=EBI-742388, EBI-711221;
Q96G97-4:BSCL2; NbExp=3; IntAct=EBI-742388, EBI-10178113;
Q9C0F1:CEP44; NbExp=3; IntAct=EBI-742388, EBI-744115;
Q9UKJ5:CHIC2; NbExp=3; IntAct=EBI-742388, EBI-741528;
Q86UW9:DTX2; NbExp=3; IntAct=EBI-742388, EBI-740376;
Q9NVF7:FBXO28; NbExp=3; IntAct=EBI-742388, EBI-740282;
Q96C98:FHL3; NbExp=3; IntAct=EBI-742388, EBI-10229248;
Q9BZ67:FRMD8; NbExp=5; IntAct=EBI-742388, EBI-5773072;
P55789:GFER; NbExp=3; IntAct=EBI-742388, EBI-718281;
Q86WP2:GPBP1; NbExp=3; IntAct=EBI-742388, EBI-2349758;
Q9UBY9:HSPB7; NbExp=3; IntAct=EBI-742388, EBI-739361;
Q96JM7:L3MBTL3; NbExp=3; IntAct=EBI-742388, EBI-2686809;
O95751:LDOC1; NbExp=4; IntAct=EBI-742388, EBI-740738;
Q02750:MAP2K1; NbExp=4; IntAct=EBI-742388, EBI-492564;
P61244:MAX; NbExp=3; IntAct=EBI-742388, EBI-751711;
Q9NS73:MBIP; NbExp=3; IntAct=EBI-742388, EBI-741953;
Q9NS73-5:MBIP; NbExp=3; IntAct=EBI-742388, EBI-10182361;
Q9HAF1:MEAF6; NbExp=5; IntAct=EBI-742388, EBI-399266;
Q86SE8:NPM2; NbExp=3; IntAct=EBI-742388, EBI-6658150;
P10644:PRKAR1A; NbExp=3; IntAct=EBI-742388, EBI-476431;
Q9UI14:RABAC1; NbExp=3; IntAct=EBI-742388, EBI-712367;
Q6UXX9:RSPO2; NbExp=3; IntAct=EBI-742388, EBI-8481036;
P23297:S100A1; NbExp=3; IntAct=EBI-742388, EBI-743686;
Q99584:S100A13; NbExp=3; IntAct=EBI-742388, EBI-721909;
Q15019:SEPT2; NbExp=3; IntAct=EBI-742388, EBI-741220;
Q14141:SEPT6; NbExp=3; IntAct=EBI-742388, EBI-745901;
Q9Y6X0:SETBP1; NbExp=3; IntAct=EBI-742388, EBI-2548259;
O95379:TNFAIP8; NbExp=4; IntAct=EBI-742388, EBI-1049336;
Q9Y4K3:TRAF6; NbExp=3; IntAct=EBI-742388, EBI-359276;
O43617:TRAPPC3; NbExp=3; IntAct=EBI-742388, EBI-743566;
Q9NX01:TXNL4B; NbExp=3; IntAct=EBI-742388, EBI-10309345;
Q9H832:UBE2Z; NbExp=3; IntAct=EBI-742388, EBI-720977;
P15622-3:ZNF250; NbExp=3; IntAct=EBI-742388, EBI-10177272;
Q8TD17:ZNF398; NbExp=3; IntAct=EBI-742388, EBI-8643207;
Q9P0T4:ZNF581; NbExp=4; IntAct=EBI-742388, EBI-745520;
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000269|PubMed:19995552, ECO:0000269|PubMed:22816767};
Peripheral membrane protein {ECO:0000305|PubMed:19995552,
ECO:0000305|PubMed:22816767}. Endoplasmic reticulum
{ECO:0000269|PubMed:18288467}. Note=Colocalizes with EEA1 and RAB5
at endosomal membrane fusion hot spots (PubMed:19995552). May
translocate to the endoplasmic reticulum in the early phase of
apoptosis (PubMed:18288467). {ECO:0000269|PubMed:18288467,
ECO:0000269|PubMed:19995552}.
-!- TISSUE SPECIFICITY: Expressed in placenta, ovary and small
intestine, as well as in heart and pancreas. Also expressed in
peripheral blood mononuclear cells and dendritic cells.
{ECO:0000269|PubMed:18288467}.
-!- INDUCTION: Up-regulated by TNF, bacterial lipopolysaccharides
(LPS) and phorbol myristate acetate (PMA) (at protein level).
{ECO:0000269|PubMed:18288467}.
-!- DOMAIN: The PH and FYVE domains may be important for TNF-induced
localization to the endoplasmic reticulum and for enhanced
cellular sensitivity to TNF-induced apoptosis (PubMed:18288467).
The FYVE domain is important for binding to the endosomal
membrane. {ECO:0000269|PubMed:18288467}.
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EMBL; AF434819; AAL30774.1; -; mRNA.
EMBL; AK023249; BAB14486.1; -; mRNA.
EMBL; AL834473; CAD39132.1; -; mRNA.
EMBL; BC011806; AAH11806.1; -; mRNA.
CCDS; CCDS6267.1; -.
RefSeq; NP_078889.1; NM_024613.3.
UniGene; Hs.29724; -.
ProteinModelPortal; Q9H8W4; -.
SMR; Q9H8W4; -.
BioGrid; 122791; 67.
IntAct; Q9H8W4; 108.
MINT; Q9H8W4; -.
STRING; 9606.ENSP00000322373; -.
iPTMnet; Q9H8W4; -.
PhosphoSitePlus; Q9H8W4; -.
BioMuta; PLEKHF2; -.
DMDM; 74762744; -.
EPD; Q9H8W4; -.
MaxQB; Q9H8W4; -.
PaxDb; Q9H8W4; -.
PeptideAtlas; Q9H8W4; -.
PRIDE; Q9H8W4; -.
DNASU; 79666; -.
Ensembl; ENST00000315367; ENSP00000322373; ENSG00000175895.
Ensembl; ENST00000519516; ENSP00000427792; ENSG00000175895.
GeneID; 79666; -.
KEGG; hsa:79666; -.
UCSC; uc003yhn.3; human.
CTD; 79666; -.
EuPathDB; HostDB:ENSG00000175895.3; -.
GeneCards; PLEKHF2; -.
HGNC; HGNC:20757; PLEKHF2.
HPA; HPA024829; -.
MIM; 615208; gene.
neXtProt; NX_Q9H8W4; -.
OpenTargets; ENSG00000175895; -.
PharmGKB; PA128394715; -.
eggNOG; KOG1729; Eukaryota.
eggNOG; ENOG410XPJK; LUCA.
GeneTree; ENSGT00890000139405; -.
HOGENOM; HOG000231519; -.
HOVERGEN; HBG059973; -.
InParanoid; Q9H8W4; -.
OMA; GEHAAVW; -.
OrthoDB; EOG091G0OVV; -.
PhylomeDB; Q9H8W4; -.
TreeFam; TF315235; -.
GeneWiki; PLEKHF2; -.
GenomeRNAi; 79666; -.
PRO; PR:Q9H8W4; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000175895; -.
CleanEx; HS_PLEKHF2; -.
Genevisible; Q9H8W4; HS.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0030133; C:transport vesicle; IDA:LIFEdb.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
CDD; cd01218; PH_Phafin2-like; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR037871; PH_Phafin.
InterPro; IPR000306; Znf_FYVE.
InterPro; IPR017455; Znf_FYVE-rel.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF01363; FYVE; 1.
Pfam; PF00169; PH; 1.
SMART; SM00064; FYVE; 1.
SMART; SM00233; PH; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50178; ZF_FYVE; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Endoplasmic reticulum; Endosome;
Membrane; Metal-binding; Phosphoprotein; Protein transport;
Reference proteome; Transport; Zinc; Zinc-finger.
CHAIN 1 249 Pleckstrin homology domain-containing
family F member 2.
/FTId=PRO_0000251600.
DOMAIN 35 131 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
ZN_FING 152 212 FYVE-type. {ECO:0000255|PROSITE-
ProRule:PRU00091}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 44 44 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 239 239 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
SEQUENCE 249 AA; 27798 MW; F5E3F84595A98886 CRC64;
MVDRLANSEA NTRRISIVEN CFGAAGQPLT IPGRVLIGEG VLTKLCRKKP KARQFFLFND
ILVYGNIVIQ KKKYNKQHII PLENVTIDSI KDEGDLRNGW LIKTPTKSFA VYAATATEKS
EWMNHINKCV TDLLSKSGKT PSNEHAAVWV PDSEATVCMR CQKAKFTPVN RRHHCRKCGF
VVCGPCSEKR FLLPSQSSKP VRICDFCYDL LSAGDMATCQ PARSDSYSQS LKSPLNDMSD
DDDDDDSSD


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18-003-42077 FYVE. RhoGEF and PH domain-containing protein 1 - Faciogenital dysplasia 1 protein; Zinc finger FYVE domain-containing protein 3; Rho_Rac guanine nucleotide exchange factor FGD1; Rho_Rac GEF Polyclona 0.05 mg Aff Pur
EIAAB31260 Mouse,Mus musculus,PH domain-containing adaptor PHAD47,PH domain-containing family A member 2,Pleckstrin homology domain-containing family A member 2,Plekha2,Tandem PH domain-containing protein 2,Tapp


 

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