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Protein

Pleckstrin homology domain-containing family F member 2

Gene

PLEKHF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri152 – 21261FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Pleckstrin homology domain-containing family F member 2
Short name:
PH domain-containing family F member 2
Alternative name(s):
Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains
Short name:
EAPF
PH and FYVE domain-containing protein 2
Phafin-2
Short name:
Phafin2
Zinc finger FYVE domain-containing protein 18
Gene namesi
Name:PLEKHF2
Synonyms:ZFYVE18
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:20757. PLEKHF2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Endosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394715.

Polymorphism and mutation databases

BioMutaiPLEKHF2.
DMDMi74762744.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Pleckstrin homology domain-containing family F member 2PRO_0000251600Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161PhosphoserineCombined sources
Modified residuei44 – 441N6-acetyllysineCombined sources
Modified residuei239 – 2391PhosphoserineCombined sources
Modified residuei248 – 2481PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9H8W4.
MaxQBiQ9H8W4.
PaxDbiQ9H8W4.
PeptideAtlasiQ9H8W4.
PRIDEiQ9H8W4.

PTM databases

iPTMnetiQ9H8W4.
PhosphoSiteiQ9H8W4.

Expressioni

Tissue specificityi

Expressed in placenta, ovary and small intestine, as well as in heart and pancreas. Also expressed in peripheral blood mononuclear cells and dendritic cells.1 Publication

Inductioni

Up-regulated by TNF, bacterial lipopolysaccharides (LPS) and phorbol myristate acetate (PMA) (at protein level).1 Publication

Gene expression databases

BgeeiQ9H8W4.
CleanExiHS_PLEKHF2.
GenevisibleiQ9H8W4. HS.

Organism-specific databases

HPAiHPA024829.

Interactioni

Subunit structurei

May interact with EEA1.

Binary interactionsi

WithEntry#Exp.IntActNotes
ACY3Q96HD93EBI-742388,EBI-3916242
AIMP2Q131553EBI-742388,EBI-745226
BSCL2Q96G97-43EBI-742388,EBI-10178113
CEP44Q9C0F13EBI-742388,EBI-744115
CHIC2Q9UKJ53EBI-742388,EBI-741528
DTX2Q86UW93EBI-742388,EBI-740376
FBXO28Q9NVF73EBI-742388,EBI-740282
FHL3Q96C983EBI-742388,EBI-10229248
FRMD8Q9BZ673EBI-742388,EBI-5773072
GFERP557893EBI-742388,EBI-718281
GPBP1Q86WP23EBI-742388,EBI-2349758
HSPB7Q9UBY93EBI-742388,EBI-739361
L3MBTL3Q96JM73EBI-742388,EBI-2686809
MBIPQ9NS733EBI-742388,EBI-741953
MBIPQ9NS73-53EBI-742388,EBI-10182361
MEAF6Q9HAF15EBI-742388,EBI-399266
NPM2Q86SE83EBI-742388,EBI-6658150
PRKAR1AP106443EBI-742388,EBI-476431
RABAC1Q9UI143EBI-742388,EBI-712367
RSPO2Q6UXX93EBI-742388,EBI-8481036
S100A1P232973EBI-742388,EBI-743686
S100A13Q995843EBI-742388,EBI-721909
SEPT2Q150193EBI-742388,EBI-741220
SEPT6Q141413EBI-742388,EBI-745901
SETBP1Q9Y6X03EBI-742388,EBI-2548259
TNFAIP8O953794EBI-742388,EBI-1049336
TRAF6Q9Y4K33EBI-742388,EBI-359276
TRAPPC3O436173EBI-742388,EBI-743566
TXNL4BQ9NX013EBI-742388,EBI-10309345
ZNF250P15622-33EBI-742388,EBI-10177272
ZNF398Q8TD173EBI-742388,EBI-8643207

Protein-protein interaction databases

BioGridi122791. 67 interactions.
IntActiQ9H8W4. 60 interactions.
MINTiMINT-1468345.
STRINGi9606.ENSP00000322373.

Structurei

3D structure databases

ProteinModelPortaliQ9H8W4.
SMRiQ9H8W4. Positions 2-137, 149-212.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 13197PHPROSITE-ProRule annotationAdd
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri152 – 21261FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1729. Eukaryota.
ENOG410XPJK. LUCA.
GeneTreeiENSGT00750000117280.
HOGENOMiHOG000231519.
HOVERGENiHBG059973.
InParanoidiQ9H8W4.
OMAiINKCVSD.
OrthoDBiEOG7PK90K.
PhylomeDBiQ9H8W4.
TreeFamiTF315235.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H8W4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDRLANSEA NTRRISIVEN CFGAAGQPLT IPGRVLIGEG VLTKLCRKKP
60 70 80 90 100
KARQFFLFND ILVYGNIVIQ KKKYNKQHII PLENVTIDSI KDEGDLRNGW
110 120 130 140 150
LIKTPTKSFA VYAATATEKS EWMNHINKCV TDLLSKSGKT PSNEHAAVWV
160 170 180 190 200
PDSEATVCMR CQKAKFTPVN RRHHCRKCGF VVCGPCSEKR FLLPSQSSKP
210 220 230 240
VRICDFCYDL LSAGDMATCQ PARSDSYSQS LKSPLNDMSD DDDDDDSSD
Length:249
Mass (Da):27,798
Last modified:March 1, 2001 - v1
Checksum:iF5E3F84595A98886
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF434819 mRNA. Translation: AAL30774.1.
AK023249 mRNA. Translation: BAB14486.1.
AL834473 mRNA. Translation: CAD39132.1.
BC011806 mRNA. Translation: AAH11806.1.
CCDSiCCDS6267.1.
RefSeqiNP_078889.1. NM_024613.3.
UniGeneiHs.29724.

Genome annotation databases

EnsembliENST00000315367; ENSP00000322373; ENSG00000175895.
ENST00000519516; ENSP00000427792; ENSG00000175895.
GeneIDi79666.
KEGGihsa:79666.
UCSCiuc003yhn.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF434819 mRNA. Translation: AAL30774.1.
AK023249 mRNA. Translation: BAB14486.1.
AL834473 mRNA. Translation: CAD39132.1.
BC011806 mRNA. Translation: AAH11806.1.
CCDSiCCDS6267.1.
RefSeqiNP_078889.1. NM_024613.3.
UniGeneiHs.29724.

3D structure databases

ProteinModelPortaliQ9H8W4.
SMRiQ9H8W4. Positions 2-137, 149-212.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122791. 67 interactions.
IntActiQ9H8W4. 60 interactions.
MINTiMINT-1468345.
STRINGi9606.ENSP00000322373.

PTM databases

iPTMnetiQ9H8W4.
PhosphoSiteiQ9H8W4.

Polymorphism and mutation databases

BioMutaiPLEKHF2.
DMDMi74762744.

Proteomic databases

EPDiQ9H8W4.
MaxQBiQ9H8W4.
PaxDbiQ9H8W4.
PeptideAtlasiQ9H8W4.
PRIDEiQ9H8W4.

Protocols and materials databases

DNASUi79666.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315367; ENSP00000322373; ENSG00000175895.
ENST00000519516; ENSP00000427792; ENSG00000175895.
GeneIDi79666.
KEGGihsa:79666.
UCSCiuc003yhn.3. human.

Organism-specific databases

CTDi79666.
GeneCardsiPLEKHF2.
HGNCiHGNC:20757. PLEKHF2.
HPAiHPA024829.
MIMi615208. gene.
neXtProtiNX_Q9H8W4.
PharmGKBiPA128394715.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1729. Eukaryota.
ENOG410XPJK. LUCA.
GeneTreeiENSGT00750000117280.
HOGENOMiHOG000231519.
HOVERGENiHBG059973.
InParanoidiQ9H8W4.
OMAiINKCVSD.
OrthoDBiEOG7PK90K.
PhylomeDBiQ9H8W4.
TreeFamiTF315235.

Miscellaneous databases

GeneWikiiPLEKHF2.
GenomeRNAii79666.
PROiQ9H8W4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H8W4.
CleanExiHS_PLEKHF2.
GenevisibleiQ9H8W4. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Phafin 2, PH and FYVE domain-containing protein 2."
    Shi H., Hong W.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Melanoma.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: B-cell.
  5. "EAPF/Phafin-2, a novel endoplasmic reticulum-associated protein, facilitates TNF-alpha-triggered cellular apoptosis through endoplasmic reticulum-mitochondrial apoptotic pathway."
    Li C., Liu Q., Li N., Chen W., Wang L., Wang Y., Yu Y., Cao X.
    J. Mol. Med. 86:471-484(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, DOMAIN.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Phafin2 modulates the structure and function of endosomes by a Rab5-dependent mechanism."
    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.
    Biochem. Biophys. Res. Commun. 391:1043-1048(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "The PtdIns3P-binding protein Phafin 2 mediates epidermal growth factor receptor degradation by promoting endosome fusion."
    Pedersen N.M., Raiborg C., Brech A., Skarpen E., Roxrud I., Platta H.W., Liestol K., Stenmark H.
    Traffic 13:1547-1563(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EEA1, SUBCELLULAR LOCATION.
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPKHF2_HUMAN
AccessioniPrimary (citable) accession number: Q9H8W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.