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Q14CM0

- FRPD4_HUMAN

UniProt

Q14CM0 - FRPD4_HUMAN

Protein

FERM and PDZ domain-containing protein 4

Gene

FRMPD4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (22 Aug 2006)
      Previous versions | rss
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    Functioni

    Positive regulator of dendritic spine morphogenesis and density. Required for the maintenance of excitatory synaptic transmission. Binds phosphatidylinositol 4,5-bisphosphate.1 Publication

    GO - Molecular functioni

    1. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. positive regulation of synapse structural plasticity Source: UniProtKB

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FERM and PDZ domain-containing protein 4
    Alternative name(s):
    PDZ domain-containing protein 10
    PSD-95-interacting regulator of spine morphogenesis
    Short name:
    Preso
    Gene namesi
    Name:FRMPD4
    Synonyms:KIAA0316, PDZD10, PDZK10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:29007. FRMPD4.

    Subcellular locationi

    Cell projectiondendritic spine 1 Publication

    GO - Cellular componenti

    1. cytoskeleton Source: InterPro
    2. dendritic spine Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi102 – 1021R → A: Abolishes the interaction with ARHGEF7. Mutant overexpression in cultured neurons does not induce a significant increase in spine density contrary to wild type. 1 Publication
    Mutagenesisi1319 – 13224Missing: Abolishes the interaction with DLG1, DLG2, DLG3 and DLG4/PSD95. Reduces protein localization to dendritic spines.
    Mutagenesisi1320 – 13201T → D: Abolishes the interaction with DLG4/PSD95. Reduces protein localization to dendritic spines. 1 Publication

    Organism-specific databases

    PharmGKBiPA134977575.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13221322FERM and PDZ domain-containing protein 4PRO_0000307132Add
    BLAST

    Proteomic databases

    MaxQBiQ14CM0.
    PaxDbiQ14CM0.
    PRIDEiQ14CM0.

    PTM databases

    PhosphoSiteiQ14CM0.

    Expressioni

    Gene expression databases

    BgeeiQ14CM0.
    CleanExiHS_FRMPD4.
    GenevestigatoriQ14CM0.

    Organism-specific databases

    HPAiHPA035580.

    Interactioni

    Subunit structurei

    Interacts (via C-terminus) with DLG1, DLG2, DLG3 and DLG4/PSD95. Interacts (via N-terminus) with ARHGEF7; the interaction is mediated by the PDZ domain.1 Publication

    Protein-protein interaction databases

    BioGridi115105. 2 interactions.
    IntActiQ14CM0. 4 interactions.
    MINTiMINT-2795491.
    STRINGi9606.ENSP00000370057.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14CM0.
    SMRiQ14CM0. Positions 33-66, 87-151, 206-442.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 6634WWPROSITE-ProRule annotationAdd
    BLAST
    Domaini78 – 15578PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini204 – 519316FERMPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The FERM domain mediates the interaction with phosphatidylinositol 4,5-bisphosphate.1 Publication

    Sequence similaritiesi

    Contains 1 FERM domain.PROSITE-ProRule annotation
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
    Contains 1 WW domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG237011.
    HOGENOMiHOG000090222.
    HOVERGENiHBG106593.
    OMAiQETGTEN.
    OrthoDBiEOG7W419W.
    PhylomeDBiQ14CM0.
    TreeFamiTF316497.

    Family and domain databases

    Gene3Di1.20.80.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProiIPR019749. Band_41_domain.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR000299. FERM_domain.
    IPR001478. PDZ.
    IPR029071. Ubiquitin-rel_dom.
    IPR001202. WW_dom.
    [Graphical view]
    PfamiPF00373. FERM_M. 1 hit.
    PF00595. PDZ. 1 hit.
    [Graphical view]
    SMARTiSM00295. B41. 1 hit.
    SM00228. PDZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 1 hit.
    SSF50156. SSF50156. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS50057. FERM_3. 1 hit.
    PS50106. PDZ. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q14CM0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDVFSFVKIA KLSSHRTKSS GWPPPSGTWG LSQVPPYGWE MTANRDGRDY     50
    FINHMTQAIP FDDPRLESCQ IIPPAPRKVE MRRDPVLGFG FVAGSEKPVV 100
    VRSVTPGGPS EGKLIPGDQI VMINDEPVSA APRERVIDLV RSCKESILLT 150
    VIQPYPSPKS AFISAAKKAR LKSNPVKVRF SEEVIINGQV SETVKDNSLL 200
    FMPNVLKVYL ENGQTKSFRF DCSTSIKDVI LTLQEKLSIK GIEHFSLMLE 250
    QRTEGAGTKL LLLHEQETLT QVTQRPSSHK MRCLFRISFV PKDPIDLLRR 300
    DPVAFEYLYV QSCNDVVQER FGPELKYDIA LRLAALQMYI ATVTTKQTQK 350
    ISLKYIEKEW GLETFLPSAV LQSMKEKNIK KALSHLVKAN QNLVPPGKKL 400
    SALQAKVHYL KFLSDLRLYG GRVFKATLVQ AEKRSEVTLL VGPRYGISHV 450
    INTKTNLVAL LADFSHVNRI EMFSEEESLV RVELHVLDVK PITLLMESSD 500
    AMNLACLTAG YYRLLVDSRR SIFNMANKKN TATQETGPEN KGKHNLLGPD 550
    WNCIPQMTTF IGEGEQEAQI TYIDSKQKTV EITDSTMCPK EHRHLYIDNA 600
    YSSDGLNQQL SQPGEAPCEA DYRSLAQRSL LTLSGPETLK KAQESPRGAK 650
    VSFIFGDFAL DDGISPPTLG YETLLDEGPE MLEKQRNLYI GSANDMKGLD 700
    LTPEAEGIQF VENSVYANIG DVKSFQAAEG IEEPLLHDIC YAENTDDAED 750
    EDEVSCEEDL VVGEMNQPAI LNLSGSSDDI IDLTSLPPPE GDDNEDDFLL 800
    RSLNMAIAAP PPGFRDSSDE EDSQSQAASF PEDKEKGSSL QNDEIPVSLI 850
    DAVPTSAEGK CEKGLDNAVV STLGALEALS VSEEQQTSDN SGVAILRAYS 900
    PESSSDSGNE TNSSEMTESS ELATAQKQSE NLSRMFLATH EGYHPLAEEQ 950
    TEFPASKTPA GGLPPKSSHA LAARPATDLP PKVVPSKQLL HSDHMEMEPE 1000
    TMETKSVTDY FSKLHMGSVA YSCTSKRKSK LADGEGKAPP NGNTTGKKQQ 1050
    GTKTAEMEEE ASGKFGTVSS RDSQHLSTFN LERTAFRKDS QRWYVATEGG 1100
    MAEKSGLEAA TGKTFPRASG LGAREAEGKE EGAPDGETSD GSGLGQGDRF 1150
    LTDVTCASSA KDLDNPEDAD SSTCDHPSKL PEADESVARL CDYHLAKRMS 1200
    SLQSEGHFSL QSSQGSSVDA GCGTGSSGSA CATPVESPLC PSLGKHLIPD 1250
    ASGKGVNYIP SEERAPGLPN HGATFKELHP QTEGMCPRMT VPALHTAINT 1300
    EPLFGTLRDG CHRLPKIKET TV 1322
    Length:1,322
    Mass (Da):144,379
    Last modified:August 22, 2006 - v1
    Checksum:i79B73E41B89E2D08
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti130 – 1301A → T in BAA20774. (PubMed:9205841)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB002314 mRNA. Translation: BAA20774.3.
    AK289694 mRNA. Translation: BAF82383.1.
    BC113700 mRNA. Translation: AAI13701.1.
    BC113702 mRNA. Translation: AAI13703.1.
    CCDSiCCDS35201.1.
    RefSeqiNP_055543.2. NM_014728.3.
    UniGeneiHs.657507.

    Genome annotation databases

    EnsembliENST00000380682; ENSP00000370057; ENSG00000169933.
    GeneIDi9758.
    KEGGihsa:9758.
    UCSCiuc004cuz.2. human.

    Polymorphism databases

    DMDMi121948742.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB002314 mRNA. Translation: BAA20774.3 .
    AK289694 mRNA. Translation: BAF82383.1 .
    BC113700 mRNA. Translation: AAI13701.1 .
    BC113702 mRNA. Translation: AAI13703.1 .
    CCDSi CCDS35201.1.
    RefSeqi NP_055543.2. NM_014728.3.
    UniGenei Hs.657507.

    3D structure databases

    ProteinModelPortali Q14CM0.
    SMRi Q14CM0. Positions 33-66, 87-151, 206-442.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115105. 2 interactions.
    IntActi Q14CM0. 4 interactions.
    MINTi MINT-2795491.
    STRINGi 9606.ENSP00000370057.

    PTM databases

    PhosphoSitei Q14CM0.

    Polymorphism databases

    DMDMi 121948742.

    Proteomic databases

    MaxQBi Q14CM0.
    PaxDbi Q14CM0.
    PRIDEi Q14CM0.

    Protocols and materials databases

    DNASUi 9758.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380682 ; ENSP00000370057 ; ENSG00000169933 .
    GeneIDi 9758.
    KEGGi hsa:9758.
    UCSCi uc004cuz.2. human.

    Organism-specific databases

    CTDi 9758.
    GeneCardsi GC0XP012066.
    H-InvDB HIX0016653.
    HGNCi HGNC:29007. FRMPD4.
    HPAi HPA035580.
    MIMi 300838. gene.
    neXtProti NX_Q14CM0.
    PharmGKBi PA134977575.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG237011.
    HOGENOMi HOG000090222.
    HOVERGENi HBG106593.
    OMAi QETGTEN.
    OrthoDBi EOG7W419W.
    PhylomeDBi Q14CM0.
    TreeFami TF316497.

    Miscellaneous databases

    ChiTaRSi FRMPD4. human.
    GenomeRNAii 9758.
    NextBioi 36727.
    PROi Q14CM0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q14CM0.
    CleanExi HS_FRMPD4.
    Genevestigatori Q14CM0.

    Family and domain databases

    Gene3Di 1.20.80.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProi IPR019749. Band_41_domain.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR000299. FERM_domain.
    IPR001478. PDZ.
    IPR029071. Ubiquitin-rel_dom.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF00373. FERM_M. 1 hit.
    PF00595. PDZ. 1 hit.
    [Graphical view ]
    SMARTi SM00295. B41. 1 hit.
    SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    SSF50156. SSF50156. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50057. FERM_3. 1 hit.
    PS50106. PDZ. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    2. Ohara O., Nagase T., Kikuno R., Nomura N.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "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: Amygdala.
    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: Brain.
    5. "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that regulates dendritic spine morphogenesis."
      Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y., Kang G.B., Eom S.H., Kim H., Kim E.
      J. Neurosci. 28:14546-14556(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DLG1; DLG2; DLG3; DLG4; ARHGEF7 AND PHOSPHATIDYLINOSITOL-4,5-BIPHOSPHATE, DOMAIN FERM, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-102; 1319-GLU--VAL-1322 AND THR-1320.
    6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.

    Entry informationi

    Entry nameiFRPD4_HUMAN
    AccessioniPrimary (citable) accession number: Q14CM0
    Secondary accession number(s): A8K0X9, O15032
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 2007
    Last sequence update: August 22, 2006
    Last modified: October 1, 2014
    This is version 73 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 X
      Human chromosome X: 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

    External Data

    Dasty 3