PKHF2_HUMAN
ID PKHF2_HUMAN Reviewed; 249 AA.
AC Q9H8W4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Pleckstrin homology domain-containing family F member 2;
DE Short=PH domain-containing family F member 2;
DE AltName: Full=Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains;
DE Short=EAPF;
DE AltName: Full=PH and FYVE domain-containing protein 2;
DE AltName: Full=Phafin-2;
DE Short=Phafin2;
DE AltName: Full=Zinc finger FYVE domain-containing protein 18;
GN Name=PLEKHF2; Synonyms=ZFYVE18;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shi H., Hong W.;
RT "Phafin 2, PH and FYVE domain-containing protein 2.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND DOMAIN.
RX PubMed=18288467; DOI=10.1007/s00109-007-0298-7;
RA Li C., Liu Q., Li N., Chen W., Wang L., Wang Y., Yu Y., Cao X.;
RT "EAPF/Phafin-2, a novel endoplasmic reticulum-associated protein,
RT facilitates TNF-alpha-triggered cellular apoptosis through endoplasmic
RT reticulum-mitochondrial apoptotic pathway.";
RL J. Mol. Med. 86:471-484(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19995552; DOI=10.1016/j.bbrc.2009.12.016;
RA Lin W.J., Yang C.Y., Lin Y.C., Tsai M.C., Yang C.W., Tung C.Y., Ho P.Y.,
RA Kao F.J., Lin C.H.;
RT "Phafin2 modulates the structure and function of endosomes by a Rab5-
RT dependent mechanism.";
RL Biochem. Biophys. Res. Commun. 391:1043-1048(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-248, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-248, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP FUNCTION, INTERACTION WITH EEA1, AND SUBCELLULAR LOCATION.
RX PubMed=22816767; DOI=10.1111/j.1600-0854.2012.01400.x;
RA Pedersen N.M., Raiborg C., Brech A., Skarpen E., Roxrud I., Platta H.W.,
RA Liestol K., Stenmark H.;
RT "The PtdIns3P-binding protein Phafin 2 mediates epidermal growth factor
RT receptor degradation by promoting endosome fusion.";
RL Traffic 13:1547-1563(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May play a role in early endosome fusion upstream of RAB5,
CC hence regulating receptor trafficking and fluid-phase transport.
CC Enhances cellular sensitivity to TNF-induced apoptosis
CC (PubMed:18288467). {ECO:0000269|PubMed:18288467,
CC ECO:0000269|PubMed:19995552, ECO:0000269|PubMed:22816767}.
CC -!- SUBUNIT: May interact with EEA1.
CC -!- INTERACTION:
CC Q9H8W4; Q9H172: ABCG4; NbExp=3; IntAct=EBI-742388, EBI-8584118;
CC Q9H8W4; Q96HD9: ACY3; NbExp=4; IntAct=EBI-742388, EBI-3916242;
CC Q9H8W4; O75689: ADAP1; NbExp=3; IntAct=EBI-742388, EBI-714732;
CC Q9H8W4; Q13155: AIMP2; NbExp=3; IntAct=EBI-742388, EBI-745226;
CC Q9H8W4; A1A5B4: ANO9; NbExp=3; IntAct=EBI-742388, EBI-3843564;
CC Q9H8W4; Q4LE39-3: ARID4B; NbExp=3; IntAct=EBI-742388, EBI-11957452;
CC Q9H8W4; Q12797-6: ASPH; NbExp=3; IntAct=EBI-742388, EBI-12092171;
CC Q9H8W4; Q9NY43: BARHL2; NbExp=3; IntAct=EBI-742388, EBI-10316571;
CC Q9H8W4; O75934: BCAS2; NbExp=3; IntAct=EBI-742388, EBI-1050106;
CC Q9H8W4; Q9H6U6: BCAS3; NbExp=3; IntAct=EBI-742388, EBI-6083685;
CC Q9H8W4; Q9UL45: BLOC1S6; NbExp=4; IntAct=EBI-742388, EBI-465781;
CC Q9H8W4; Q96IK1-2: BOD1; NbExp=3; IntAct=EBI-742388, EBI-18924329;
CC Q9H8W4; Q9NPI1: BRD7; NbExp=3; IntAct=EBI-742388, EBI-711221;
CC Q9H8W4; Q96G97-4: BSCL2; NbExp=3; IntAct=EBI-742388, EBI-10178113;
CC Q9H8W4; Q8TAV5: C11orf45; NbExp=3; IntAct=EBI-742388, EBI-12810853;
CC Q9H8W4; P01024: C3; NbExp=3; IntAct=EBI-742388, EBI-905851;
CC Q9H8W4; Q9HC52: CBX8; NbExp=3; IntAct=EBI-742388, EBI-712912;
CC Q9H8W4; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-742388, EBI-10749669;
CC Q9H8W4; Q86WR0: CCDC25; NbExp=3; IntAct=EBI-742388, EBI-2690264;
CC Q9H8W4; Q86Y33-5: CDC20B; NbExp=3; IntAct=EBI-742388, EBI-11983537;
CC Q9H8W4; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-742388, EBI-744115;
CC Q9H8W4; Q8TCT0: CERK; NbExp=3; IntAct=EBI-742388, EBI-10274247;
CC Q9H8W4; Q9Y6H1: CHCHD2; NbExp=3; IntAct=EBI-742388, EBI-2321769;
CC Q9H8W4; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-742388, EBI-741528;
CC Q9H8W4; P10606: COX5B; NbExp=3; IntAct=EBI-742388, EBI-1053725;
CC Q9H8W4; P05813: CRYBA1; NbExp=3; IntAct=EBI-742388, EBI-7043337;
CC Q9H8W4; Q15038: DAZAP2; NbExp=3; IntAct=EBI-742388, EBI-724310;
CC Q9H8W4; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-742388, EBI-9679045;
CC Q9H8W4; Q86X45: DNAAF11; NbExp=3; IntAct=EBI-742388, EBI-9379658;
CC Q9H8W4; Q92608: DOCK2; NbExp=3; IntAct=EBI-742388, EBI-448771;
CC Q9H8W4; Q8IZD9: DOCK3; NbExp=3; IntAct=EBI-742388, EBI-1752361;
CC Q9H8W4; Q86UW9: DTX2; NbExp=3; IntAct=EBI-742388, EBI-740376;
CC Q9H8W4; Q13115: DUSP4; NbExp=3; IntAct=EBI-742388, EBI-6591081;
CC Q9H8W4; Q99613: EIF3C; NbExp=3; IntAct=EBI-742388, EBI-353741;
CC Q9H8W4; A0A0C4DGQ7: EML2; NbExp=3; IntAct=EBI-742388, EBI-12112376;
CC Q9H8W4; Q9UPT5-1: EXOC7; NbExp=3; IntAct=EBI-742388, EBI-6251402;
CC Q9H8W4; P16930: FAH; NbExp=3; IntAct=EBI-742388, EBI-4397076;
CC Q9H8W4; Q9NVF7: FBXO28; NbExp=6; IntAct=EBI-742388, EBI-740282;
CC Q9H8W4; Q969U6: FBXW5; NbExp=3; IntAct=EBI-742388, EBI-741068;
CC Q9H8W4; Q92913: FGF13; NbExp=3; IntAct=EBI-742388, EBI-1054883;
CC Q9H8W4; Q96C98: FHL3; NbExp=3; IntAct=EBI-742388, EBI-10229248;
CC Q9H8W4; P21333-2: FLNA; NbExp=5; IntAct=EBI-742388, EBI-9641086;
CC Q9H8W4; Q9BZ67: FRMD8; NbExp=8; IntAct=EBI-742388, EBI-5773072;
CC Q9H8W4; P55040: GEM; NbExp=3; IntAct=EBI-742388, EBI-744104;
CC Q9H8W4; P55789: GFER; NbExp=3; IntAct=EBI-742388, EBI-718281;
CC Q9H8W4; Q86WP2: GPBP1; NbExp=3; IntAct=EBI-742388, EBI-2349758;
CC Q9H8W4; Q6IC98: GRAMD4; NbExp=3; IntAct=EBI-742388, EBI-10962409;
CC Q9H8W4; Q9BX10: GTPBP2; NbExp=3; IntAct=EBI-742388, EBI-6115579;
CC Q9H8W4; Q9Y5Z4: HEBP2; NbExp=3; IntAct=EBI-742388, EBI-741593;
CC Q9H8W4; Q9UBY9: HSPB7; NbExp=6; IntAct=EBI-742388, EBI-739361;
CC Q9H8W4; Q9ULG1: INO80; NbExp=3; IntAct=EBI-742388, EBI-769345;
CC Q9H8W4; O43448: KCNAB3; NbExp=3; IntAct=EBI-742388, EBI-12050557;
CC Q9H8W4; Q587J8: KHDC3L; NbExp=3; IntAct=EBI-742388, EBI-22731520;
CC Q9H8W4; P60014: KRTAP10-10; NbExp=3; IntAct=EBI-742388, EBI-11955579;
CC Q9H8W4; Q6L8H1: KRTAP5-4; NbExp=3; IntAct=EBI-742388, EBI-11963072;
CC Q9H8W4; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-742388, EBI-2686809;
CC Q9H8W4; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-742388, EBI-11985629;
CC Q9H8W4; O95751: LDOC1; NbExp=5; IntAct=EBI-742388, EBI-740738;
CC Q9H8W4; Q86UL8-2: MAGI2; NbExp=3; IntAct=EBI-742388, EBI-12081182;
CC Q9H8W4; Q02750: MAP2K1; NbExp=3; IntAct=EBI-742388, EBI-492564;
CC Q9H8W4; P61244: MAX; NbExp=4; IntAct=EBI-742388, EBI-751711;
CC Q9H8W4; Q9NS73: MBIP; NbExp=3; IntAct=EBI-742388, EBI-741953;
CC Q9H8W4; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-742388, EBI-10182361;
CC Q9H8W4; P02686-2: MBP; NbExp=3; IntAct=EBI-742388, EBI-12159027;
CC Q9H8W4; Q9HAF1: MEAF6; NbExp=5; IntAct=EBI-742388, EBI-399266;
CC Q9H8W4; P55081: MFAP1; NbExp=3; IntAct=EBI-742388, EBI-1048159;
CC Q9H8W4; Q504T8: MIDN; NbExp=3; IntAct=EBI-742388, EBI-7153979;
CC Q9H8W4; Q9BU76: MMTAG2; NbExp=3; IntAct=EBI-742388, EBI-742459;
CC Q9H8W4; A2RU80: MPP4; NbExp=3; IntAct=EBI-742388, EBI-18924629;
CC Q9H8W4; Q9BV20: MRI1; NbExp=3; IntAct=EBI-742388, EBI-747381;
CC Q9H8W4; Q16718: NDUFA5; NbExp=3; IntAct=EBI-742388, EBI-746417;
CC Q9H8W4; Q12857-2: NFIA; NbExp=3; IntAct=EBI-742388, EBI-12119652;
CC Q9H8W4; Q86SE8: NPM2; NbExp=3; IntAct=EBI-742388, EBI-6658150;
CC Q9H8W4; Q86SE8-2: NPM2; NbExp=3; IntAct=EBI-742388, EBI-12193061;
CC Q9H8W4; O96028: NSD2; NbExp=3; IntAct=EBI-742388, EBI-2693298;
CC Q9H8W4; P50583: NUDT2; NbExp=3; IntAct=EBI-742388, EBI-10096247;
CC Q9H8W4; Q99572: P2RX7; NbExp=3; IntAct=EBI-742388, EBI-1753251;
CC Q9H8W4; Q9BY11: PACSIN1; NbExp=3; IntAct=EBI-742388, EBI-721769;
CC Q9H8W4; Q9NWT1: PAK1IP1; NbExp=3; IntAct=EBI-742388, EBI-7641942;
CC Q9H8W4; Q16654: PDK4; NbExp=3; IntAct=EBI-742388, EBI-2861674;
CC Q9H8W4; Q92569: PIK3R3; NbExp=3; IntAct=EBI-742388, EBI-79893;
CC Q9H8W4; Q96CD2: PPCDC; NbExp=3; IntAct=EBI-742388, EBI-724333;
CC Q9H8W4; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-742388, EBI-2557469;
CC Q9H8W4; P54619: PRKAG1; NbExp=3; IntAct=EBI-742388, EBI-1181439;
CC Q9H8W4; P10644: PRKAR1A; NbExp=3; IntAct=EBI-742388, EBI-476431;
CC Q9H8W4; P26045: PTPN3; NbExp=3; IntAct=EBI-742388, EBI-1047946;
CC Q9H8W4; Q96N64-2: PWWP2A; NbExp=3; IntAct=EBI-742388, EBI-18924849;
CC Q9H8W4; P51157: RAB28; NbExp=3; IntAct=EBI-742388, EBI-11898753;
CC Q9H8W4; Q5JT25-2: RAB41; NbExp=3; IntAct=EBI-742388, EBI-12315199;
CC Q9H8W4; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-742388, EBI-712367;
CC Q9H8W4; P10276: RARA; NbExp=3; IntAct=EBI-742388, EBI-413374;
CC Q9H8W4; Q0VAM2-3: RASGEF1B; NbExp=3; IntAct=EBI-742388, EBI-12013954;
CC Q9H8W4; O43665: RGS10; NbExp=3; IntAct=EBI-742388, EBI-1057034;
CC Q9H8W4; P57771-2: RGS8; NbExp=3; IntAct=EBI-742388, EBI-12058229;
CC Q9H8W4; Q8IXW5: RPAP2; NbExp=3; IntAct=EBI-742388, EBI-395878;
CC Q9H8W4; Q96AT9: RPE; NbExp=3; IntAct=EBI-742388, EBI-372480;
CC Q9H8W4; Q9NS64: RPRM; NbExp=3; IntAct=EBI-742388, EBI-1052363;
CC Q9H8W4; P63220: RPS21; NbExp=6; IntAct=EBI-742388, EBI-714051;
CC Q9H8W4; Q6UXX9: RSPO2; NbExp=3; IntAct=EBI-742388, EBI-8481036;
CC Q9H8W4; P23297: S100A1; NbExp=3; IntAct=EBI-742388, EBI-743686;
CC Q9H8W4; Q99584: S100A13; NbExp=3; IntAct=EBI-742388, EBI-721909;
CC Q9H8W4; Q96NU1: SAMD11; NbExp=3; IntAct=EBI-742388, EBI-14067109;
CC Q9H8W4; Q96KG9-4: SCYL1; NbExp=3; IntAct=EBI-742388, EBI-12023020;
CC Q9H8W4; Q9UDX3: SEC14L4; NbExp=3; IntAct=EBI-742388, EBI-10320311;
CC Q9H8W4; Q15019: SEPTIN2; NbExp=3; IntAct=EBI-742388, EBI-741220;
CC Q9H8W4; Q14141: SEPTIN6; NbExp=3; IntAct=EBI-742388, EBI-745901;
CC Q9H8W4; Q9Y6X0: SETBP1; NbExp=3; IntAct=EBI-742388, EBI-2548259;
CC Q9H8W4; Q9Y6X0-2: SETBP1; NbExp=6; IntAct=EBI-742388, EBI-12235818;
CC Q9H8W4; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-742388, EBI-12938570;
CC Q9H8W4; Q9BQB4: SOST; NbExp=3; IntAct=EBI-742388, EBI-5746563;
CC Q9H8W4; Q86W54-2: SPATA24; NbExp=3; IntAct=EBI-742388, EBI-12041693;
CC Q9H8W4; Q9Y4P9-2: SPEF1; NbExp=3; IntAct=EBI-742388, EBI-12303571;
CC Q9H8W4; Q9BUD6: SPON2; NbExp=3; IntAct=EBI-742388, EBI-10298801;
CC Q9H8W4; Q96FJ0: STAMBPL1; NbExp=3; IntAct=EBI-742388, EBI-745021;
CC Q9H8W4; Q13188: STK3; NbExp=3; IntAct=EBI-742388, EBI-992580;
CC Q9H8W4; Q17RD7: SYT16; NbExp=3; IntAct=EBI-742388, EBI-10238936;
CC Q9H8W4; Q5QJ74: TBCEL; NbExp=3; IntAct=EBI-742388, EBI-10244795;
CC Q9H8W4; O15273: TCAP; NbExp=3; IntAct=EBI-742388, EBI-954089;
CC Q9H8W4; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-742388, EBI-11955057;
CC Q9H8W4; Q9P2Z0: THAP10; NbExp=3; IntAct=EBI-742388, EBI-745404;
CC Q9H8W4; Q9NWX6: THG1L; NbExp=3; IntAct=EBI-742388, EBI-746510;
CC Q9H8W4; O95379: TNFAIP8; NbExp=4; IntAct=EBI-742388, EBI-1049336;
CC Q9H8W4; Q8WVP5: TNFAIP8L1; NbExp=3; IntAct=EBI-742388, EBI-752102;
CC Q9H8W4; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-742388, EBI-11952721;
CC Q9H8W4; Q9Y4K3: TRAF6; NbExp=3; IntAct=EBI-742388, EBI-359276;
CC Q9H8W4; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-742388, EBI-11996766;
CC Q9H8W4; O43617: TRAPPC3; NbExp=3; IntAct=EBI-742388, EBI-743566;
CC Q9H8W4; O43715: TRIAP1; NbExp=3; IntAct=EBI-742388, EBI-2820212;
CC Q9H8W4; Q8IYM9: TRIM22; NbExp=3; IntAct=EBI-742388, EBI-954123;
CC Q9H8W4; Q8N5M4: TTC9C; NbExp=3; IntAct=EBI-742388, EBI-2851213;
CC Q9H8W4; Q9NX01: TXNL4B; NbExp=3; IntAct=EBI-742388, EBI-10309345;
CC Q9H8W4; Q9H832: UBE2Z; NbExp=9; IntAct=EBI-742388, EBI-720977;
CC Q9H8W4; Q16851: UGP2; NbExp=3; IntAct=EBI-742388, EBI-743729;
CC Q9H8W4; P46094: XCR1; NbExp=3; IntAct=EBI-742388, EBI-12960721;
CC Q9H8W4; Q9H0D6: XRN2; NbExp=3; IntAct=EBI-742388, EBI-372110;
CC Q9H8W4; O95070: YIF1A; NbExp=3; IntAct=EBI-742388, EBI-2799703;
CC Q9H8W4; P25490: YY1; NbExp=3; IntAct=EBI-742388, EBI-765538;
CC Q9H8W4; Q15916: ZBTB6; NbExp=6; IntAct=EBI-742388, EBI-7227791;
CC Q9H8W4; Q6UX98: ZDHHC24; NbExp=3; IntAct=EBI-742388, EBI-10254561;
CC Q9H8W4; Q68DK2-5: ZFYVE26; NbExp=3; IntAct=EBI-742388, EBI-8656416;
CC Q9H8W4; P49910: ZNF165; NbExp=3; IntAct=EBI-742388, EBI-741694;
CC Q9H8W4; P15622-3: ZNF250; NbExp=3; IntAct=EBI-742388, EBI-10177272;
CC Q9H8W4; Q8TD17: ZNF398; NbExp=3; IntAct=EBI-742388, EBI-8643207;
CC Q9H8W4; Q8NDP4: ZNF439; NbExp=3; IntAct=EBI-742388, EBI-747580;
CC Q9H8W4; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-742388, EBI-745520;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:19995552, ECO:0000269|PubMed:22816767}; Peripheral
CC membrane protein {ECO:0000305|PubMed:19995552,
CC ECO:0000305|PubMed:22816767}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:18288467}. Note=Colocalizes with EEA1 and RAB5 at
CC endosomal membrane fusion hot spots (PubMed:19995552). May translocate
CC to the endoplasmic reticulum in the early phase of apoptosis
CC (PubMed:18288467). {ECO:0000269|PubMed:18288467,
CC ECO:0000269|PubMed:19995552}.
CC -!- TISSUE SPECIFICITY: Expressed in placenta, ovary and small intestine,
CC as well as in heart and pancreas. Also expressed in peripheral blood
CC mononuclear cells and dendritic cells. {ECO:0000269|PubMed:18288467}.
CC -!- INDUCTION: Up-regulated by TNF, bacterial lipopolysaccharides (LPS) and
CC phorbol myristate acetate (PMA) (at protein level).
CC {ECO:0000269|PubMed:18288467}.
CC -!- DOMAIN: The PH and FYVE domains may be important for TNF-induced
CC localization to the endoplasmic reticulum and for enhanced cellular
CC sensitivity to TNF-induced apoptosis (PubMed:18288467). The FYVE domain
CC is important for binding to the endosomal membrane.
CC {ECO:0000269|PubMed:18288467}.
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DR EMBL; AF434819; AAL30774.1; -; mRNA.
DR EMBL; AK023249; BAB14486.1; -; mRNA.
DR EMBL; AL834473; CAD39132.1; -; mRNA.
DR EMBL; BC011806; AAH11806.1; -; mRNA.
DR CCDS; CCDS6267.1; -.
DR RefSeq; NP_078889.1; NM_024613.3.
DR AlphaFoldDB; Q9H8W4; -.
DR SMR; Q9H8W4; -.
DR BioGRID; 122791; 175.
DR IntAct; Q9H8W4; 168.
DR MINT; Q9H8W4; -.
DR STRING; 9606.ENSP00000322373; -.
DR iPTMnet; Q9H8W4; -.
DR PhosphoSitePlus; Q9H8W4; -.
DR BioMuta; PLEKHF2; -.
DR DMDM; 74762744; -.
DR EPD; Q9H8W4; -.
DR jPOST; Q9H8W4; -.
DR MassIVE; Q9H8W4; -.
DR MaxQB; Q9H8W4; -.
DR PaxDb; Q9H8W4; -.
DR PeptideAtlas; Q9H8W4; -.
DR PRIDE; Q9H8W4; -.
DR ProteomicsDB; 81249; -.
DR Antibodypedia; 25937; 121 antibodies from 22 providers.
DR DNASU; 79666; -.
DR Ensembl; ENST00000315367.4; ENSP00000322373.3; ENSG00000175895.4.
DR Ensembl; ENST00000519516.1; ENSP00000427792.1; ENSG00000175895.4.
DR GeneID; 79666; -.
DR KEGG; hsa:79666; -.
DR MANE-Select; ENST00000315367.4; ENSP00000322373.3; NM_024613.4; NP_078889.1.
DR UCSC; uc003yhn.3; human.
DR CTD; 79666; -.
DR GeneCards; PLEKHF2; -.
DR HGNC; HGNC:20757; PLEKHF2.
DR HPA; ENSG00000175895; Tissue enhanced (bone).
DR MIM; 615208; gene.
DR neXtProt; NX_Q9H8W4; -.
DR OpenTargets; ENSG00000175895; -.
DR PharmGKB; PA128394715; -.
DR VEuPathDB; HostDB:ENSG00000175895; -.
DR eggNOG; KOG1729; Eukaryota.
DR GeneTree; ENSGT00940000156408; -.
DR HOGENOM; CLU_064864_1_0_1; -.
DR InParanoid; Q9H8W4; -.
DR OMA; VCMRCKK; -.
DR OrthoDB; 1237900at2759; -.
DR PhylomeDB; Q9H8W4; -.
DR TreeFam; TF315235; -.
DR PathwayCommons; Q9H8W4; -.
DR SignaLink; Q9H8W4; -.
DR SIGNOR; Q9H8W4; -.
DR BioGRID-ORCS; 79666; 20 hits in 1080 CRISPR screens.
DR ChiTaRS; PLEKHF2; human.
DR GeneWiki; PLEKHF2; -.
DR GenomeRNAi; 79666; -.
DR Pharos; Q9H8W4; Tbio.
DR PRO; PR:Q9H8W4; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9H8W4; protein.
DR Bgee; ENSG00000175895; Expressed in secondary oocyte and 184 other tissues.
DR Genevisible; Q9H8W4; HS.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0030133; C:transport vesicle; IDA:LIFEdb.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd01218; PH_Phafin2-like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037871; PH_Phafin.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Endosome; Membrane; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..249
FT /note="Pleckstrin homology domain-containing family F
FT member 2"
FT /id="PRO_0000251600"
FT DOMAIN 35..131
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 152..212
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 221..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
SQ 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
