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Protein

Pleckstrin homology domain-containing family A member 3

Gene

PLEKHA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in Golgi to cell surface membrane traffic. Induces membrane tubulation. Binds preferentially to phosphatidylinositol 4-phosphate (PtdIns4P).1 Publication

GO - Molecular functioni

  • 1-phosphatidylinositol binding Source: Ensembl
  • phospholipid binding Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Pleckstrin homology domain-containing family A member 3
Short name:
PH domain-containing family A member 3
Alternative name(s):
Phosphatidylinositol-four-phosphate adapter protein 1
Short name:
FAPP-1
Short name:
Phosphoinositol 4-phosphate adapter protein 1
Gene namesi
Name:PLEKHA3
Synonyms:FAPP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:14338. PLEKHA3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33403.

Polymorphism and mutation databases

BioMutaiPLEKHA3.
DMDMi48474646.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 300300Pleckstrin homology domain-containing family A member 3PRO_0000053878Add
BLAST

Proteomic databases

MaxQBiQ9HB20.
PaxDbiQ9HB20.
PRIDEiQ9HB20.

PTM databases

iPTMnetiQ9HB20.
PhosphoSiteiQ9HB20.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiQ9HB20.
CleanExiHS_PLEKHA3.
ExpressionAtlasiQ9HB20. baseline and differential.
GenevisibleiQ9HB20. HS.

Organism-specific databases

HPAiHPA034496.
HPA034497.

Interactioni

Subunit structurei

Interacts with GTP-bound ARF1.1 Publication

Protein-protein interaction databases

BioGridi122427. 4 interactions.
IntActiQ9HB20. 2 interactions.
STRINGi9606.ENSP00000234453.

Structurei

Secondary structure

1
300
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Turni11 – 133Combined sources
Beta strandi15 – 239Combined sources
Beta strandi26 – 327Combined sources
Helixi33 – 386Combined sources
Beta strandi43 – 453Combined sources
Helixi46 – 483Combined sources
Beta strandi50 – 523Combined sources
Beta strandi58 – 658Combined sources
Turni66 – 683Combined sources
Beta strandi69 – 746Combined sources
Helixi78 – 8912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KCJNMR-A1-100[»]
2MDXNMR-A1-100[»]
3RCPX-ray1.90A1-99[»]
ProteinModelPortaliQ9HB20.
SMRiQ9HB20. Positions 1-100.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HB20.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9393PHPROSITE-ProRule annotationAdd
BLAST

Domaini

The PH domain of FAPPS binds the small GTPase ARF1 and phosphatidylinositol-4-phosphate (PtdIns4P) with high selectivity, and is required for recruitment of FAPPs to the trans-Golgi network (TGN).By similarity

Sequence similaritiesi

Contains 1 PH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3221. Eukaryota.
ENOG410YFEA. LUCA.
GeneTreeiENSGT00650000093230.
HOGENOMiHOG000231911.
HOVERGENiHBG053613.
InParanoidiQ9HB20.
OMAiRPVHCSR.
OrthoDBiEOG7FJH25.
PhylomeDBiQ9HB20.
TreeFamiTF317467.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HB20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGVLYKWTN YLTGWQPRWF VLDNGILSYY DSQDDVCKGS KGSIKMAVCE
60 70 80 90 100
IKVHSADNTR MELIIPGEQH FYMKAVNAAE RQRWLVALGS SKACLTDTRT
110 120 130 140 150
KKEKEISETS ESLKTKMSEL RLYCDLLMQQ VHTIQEFVHH DENHSSPSAE
160 170 180 190 200
NMNEASSLLS ATCNTFITTL EECVKIANAK FKPEMFQLHH PDPLVSPVSP
210 220 230 240 250
SPVQMMKRSV SHPGSCSSER SSHSIKEPVS TLHRLSQRRR RTYSDTDSCS
260 270 280 290 300
DIPLEDPDRP VHCSKNTLNG DLASATIPEE SRLMAKKQSE SEDTLPSFSS
Length:300
Mass (Da):33,861
Last modified:March 29, 2004 - v2
Checksum:i0B6EF45C7D17E82C
GO

Sequence cautioni

The sequence BAA90927.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti284 – 2841M → T in AAG15199 (PubMed:11001876).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF286162 mRNA. Translation: AAG15199.1.
AK000074 mRNA. Translation: BAA90927.1. Different initiation.
AK314459 mRNA. Translation: BAG37067.1.
AC009948 Genomic DNA. Translation: AAX88884.1.
CH471058 Genomic DNA. Translation: EAX11026.1.
BC044567 mRNA. Translation: AAH44567.1.
CCDSiCCDS33336.1.
RefSeqiNP_061964.3. NM_019091.3.
UniGeneiHs.41086.

Genome annotation databases

EnsembliENST00000234453; ENSP00000234453; ENSG00000116095.
GeneIDi65977.
KEGGihsa:65977.
UCSCiuc002umn.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF286162 mRNA. Translation: AAG15199.1.
AK000074 mRNA. Translation: BAA90927.1. Different initiation.
AK314459 mRNA. Translation: BAG37067.1.
AC009948 Genomic DNA. Translation: AAX88884.1.
CH471058 Genomic DNA. Translation: EAX11026.1.
BC044567 mRNA. Translation: AAH44567.1.
CCDSiCCDS33336.1.
RefSeqiNP_061964.3. NM_019091.3.
UniGeneiHs.41086.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KCJNMR-A1-100[»]
2MDXNMR-A1-100[»]
3RCPX-ray1.90A1-99[»]
ProteinModelPortaliQ9HB20.
SMRiQ9HB20. Positions 1-100.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122427. 4 interactions.
IntActiQ9HB20. 2 interactions.
STRINGi9606.ENSP00000234453.

PTM databases

iPTMnetiQ9HB20.
PhosphoSiteiQ9HB20.

Polymorphism and mutation databases

BioMutaiPLEKHA3.
DMDMi48474646.

Proteomic databases

MaxQBiQ9HB20.
PaxDbiQ9HB20.
PRIDEiQ9HB20.

Protocols and materials databases

DNASUi65977.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000234453; ENSP00000234453; ENSG00000116095.
GeneIDi65977.
KEGGihsa:65977.
UCSCiuc002umn.4. human.

Organism-specific databases

CTDi65977.
GeneCardsiPLEKHA3.
HGNCiHGNC:14338. PLEKHA3.
HPAiHPA034496.
HPA034497.
MIMi607774. gene.
neXtProtiNX_Q9HB20.
PharmGKBiPA33403.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3221. Eukaryota.
ENOG410YFEA. LUCA.
GeneTreeiENSGT00650000093230.
HOGENOMiHOG000231911.
HOVERGENiHBG053613.
InParanoidiQ9HB20.
OMAiRPVHCSR.
OrthoDBiEOG7FJH25.
PhylomeDBiQ9HB20.
TreeFamiTF317467.

Miscellaneous databases

EvolutionaryTraceiQ9HB20.
GenomeRNAii65977.
NextBioi67418.
PROiQ9HB20.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HB20.
CleanExiHS_PLEKHA3.
ExpressionAtlasiQ9HB20. baseline and differential.
GenevisibleiQ9HB20. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities."
    Dowler S.J., Currie R.A., Campbell D.G., Deak M., Kular G., Downes C.P., Alessi D.R.
    Biochem. J. 351:19-31(2000) [PubMed] [Europe PMC] [Abstract]
    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].
    Tissue: Brain and Colon.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Brain.
  6. "FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P."
    Godi A., Di Campli A., Konstantakopoulos A., Di Tullio G., Alessi D.R., Kular G.S., Daniele T., Marra P., Lucocq J.M., De Matteis M.A.
    Nat. Cell Biol. 6:393-404(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains."
    Lenoir M., Coskun U., Grzybek M., Cao X., Buschhorn S.B., James J., Simons K., Overduin M.
    EMBO Rep. 11:279-284(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-100.
  9. "Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain."
    He J., Scott J.L., Heroux A., Roy S., Lenoir M., Overduin M., Stahelin R.V., Kutateladze T.G.
    J. Biol. Chem. 286:18650-18657(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-99 OF MUTANT SER-94, INTERACTION WITH ARF1.

Entry informationi

Entry nameiPKHA3_HUMAN
AccessioniPrimary (citable) accession number: Q9HB20
Secondary accession number(s): Q4ZG69, Q86TQ1, Q9NXT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: April 13, 2016
This is version 117 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.