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Q9JIL4

- NHRF3_MOUSE

UniProt

Q9JIL4 - NHRF3_MOUSE

Protein

Na(+)/H(+) exchange regulatory cofactor NHE-RF3

Gene

Pdzk1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with SLC9A3R1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity By similarity. Required for normal cell-surface expression of SCARB1. Plays a role in maintaining normal plasma cholesterol levels via its effects on SCARB1. Plays a role in the normal localization and function of the chloride-anion exchanger SLC26A6 to the plasma membrane in the brush border of the proximal tubule of the kidney. May be involved in the regulation of proximal tubular Na+-dependent inorganic phosphate cotransport therefore playing an important role in tubule function.By similarity7 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. carnitine transport Source: Ensembl
    2. establishment of protein localization to plasma membrane Source: UniProtKB
    3. positive regulation of ion transmembrane transport Source: Ensembl
    4. positive regulation of protein targeting to membrane Source: UniProtKB
    5. regulation of anion transport Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Na(+)/H(+) exchange regulatory cofactor NHE-RF3
    Short name:
    NHERF-3
    Alternative name(s):
    CFTR-associated protein of 70 kDa
    Na(+)/H(+) exchanger regulatory factor 3
    Na/Pi cotransporter C-terminal-associated protein 1
    Short name:
    NaPi-Cap1
    PDZ domain-containing protein 1
    Sodium-hydrogen exchanger regulatory factor 3
    Gene namesi
    Name:Pdzk1
    Synonyms:Cap70, Nherf3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1928901. Pdzk1.

    Subcellular locationi

    Cytoplasm. Membrane; Peripheral membrane protein. Cell membrane
    Note: Localized in the brush border membrane of renal proximal tubule cells. Associated with peripheral membranes. Localizes to the apical compartment of proximal cells and to sinusoidal liver membranes.

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. brush border membrane Source: UniProtKB
    3. cytoplasm Source: UniProtKB-SubCell
    4. membrane raft Source: Ensembl
    5. microvillus membrane Source: Ensembl
    6. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141K → A: Impairs interaction of the first PDZ domain with SCARB1. 1 Publication
    Mutagenesisi20 – 201Y → A: Disrupts interaction of the first PDZ domain with SCARB1. Abolishes interaction with SCARB1; when associated with A-253. 2 Publications
    Mutagenesisi253 – 2531Y → A: Disrupts interaction of the third PDZ domain with SCARB1. Abolishes interaction with SCARB1; when associated with A-20. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 519519Na(+)/H(+) exchange regulatory cofactor NHE-RF3PRO_0000058288Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei488 – 4881Phosphothreonine1 Publication
    Modified residuei489 – 4891Phosphoserine1 Publication
    Modified residuei492 – 4921Phosphoserine1 Publication
    Modified residuei514 – 5141Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9JIL4.
    PaxDbiQ9JIL4.
    PRIDEiQ9JIL4.

    PTM databases

    PhosphoSiteiQ9JIL4.

    Expressioni

    Tissue specificityi

    Expressed in kidney, liver, small intestine. brain, lung, and testis (at protein level).2 Publications

    Gene expression databases

    ArrayExpressiQ9JIL4.
    BgeeiQ9JIL4.
    CleanExiMM_PDZK1.
    GenevestigatoriQ9JIL4.

    Interactioni

    Subunit structurei

    Interacts with PDZK1IP1 and ABCC2. Binds to the C-terminal region of SLC26A3. Interacts (via C-terminal PDZ domain) with SLC26A6 (via C-terminal domain). Interacts (via C-terminal PDZ domain) with SLC9A3 (via C-terminal domain) By similarity. Component of a complex, composed of PDZK1, SYNGAP1, KLHL17 and NMDA receptors. Interacts (via PDZ1 domain) directly with KLHL17; the interaction is important for integrity of actin cytoskeleton structures in neurons By similarity. Forms a heterodimeric complex with SLC9A3R1. Interacts with AKAP2, BCR, CFTR, SLCO1A1, SLC22A12, SLC22A4, SLC22A5, SLC26A6, SLC9A3R2 and SLC17A1. Interacts (via the first PDZ domain) with PTGIR (via non-isoprenylated C-terminus). Interacts (via PDZ domains 1 and 3) with SCARB1 (C-terminal domain).By similarity7 Publications

    Protein-protein interaction databases

    BioGridi208488. 2 interactions.
    IntActiQ9JIL4. 6 interactions.
    MINTiMINT-148595.

    Structurei

    Secondary structure

    1
    519
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 136
    Beta strandi23 – 253
    Beta strandi34 – 363
    Helixi43 – 464
    Beta strandi54 – 585
    Beta strandi64 – 663
    Helixi68 – 7710
    Turni78 – 803
    Beta strandi81 – 877
    Helixi89 – 979
    Helixi102 – 1043
    Beta strandi242 – 2476
    Beta strandi252 – 2543
    Beta strandi256 – 2594
    Beta strandi265 – 2695
    Helixi276 – 2805
    Beta strandi286 – 2916
    Helixi301 – 3099
    Turni310 – 3134
    Beta strandi314 – 3218

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D90NMR-A242-330[»]
    2EDZNMR-A1-107[»]
    3NGHX-ray1.80A/B7-106[»]
    3R68X-ray1.30A238-323[»]
    3R69X-ray1.50A/B241-322[»]
    4F8KX-ray1.70A/B7-106[»]
    ProteinModelPortaliQ9JIL4.
    SMRiQ9JIL4. Positions 1-107, 125-492.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9JIL4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 9082PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini128 – 21588PDZ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini243 – 32381PDZ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini378 – 45881PDZ 4PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The PDZ 2 and 3 domains seem to be involved in the interaction with SLC26A3.By similarity
    Interaction with the C-terminus of CFTR could be mediated through independent binding of PDZ 1, 3 and 4 domains.
    The PDZ 1 and 3 domains seem to be involved in the interaction with SLCO1A1.By similarity
    The PDZ 1 domain interacts with BCR.By similarity
    The PDZ 2 and 4 domains do not interact with the C-terminal region of SCARB1.

    Sequence similaritiesi

    Belongs to the NHER family.Curated
    Contains 4 PDZ (DHR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG315208.
    GeneTreeiENSGT00530000062999.
    HOGENOMiHOG000113782.
    HOVERGENiHBG082115.
    InParanoidiQ9JIL4.
    PhylomeDBiQ9JIL4.
    TreeFamiTF350449.

    Family and domain databases

    Gene3Di2.30.42.10. 4 hits.
    InterProiIPR001478. PDZ.
    [Graphical view]
    PfamiPF00595. PDZ. 4 hits.
    [Graphical view]
    SMARTiSM00228. PDZ. 4 hits.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 4 hits.
    PROSITEiPS50106. PDZ. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9JIL4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASTFNPREC KLSKQEGQNY GFFLRIEKDT DGHLIRVIEE GSPAEKAGLL    50
    DGDRVLRING VFVDKEEHAQ VVELVRKSGN SVTLLVLDGD SYEKAVKNQV 100
    DLKELDQSQR EAALNDKKPG PGMNGAVEPC AQPRLCYLVK EGNSFGFSLK 150
    TIQGKKGVYL TDIMPQGVAM KAGVLADDHL IEVNGENVEN ASHEEVVEKV 200
    TKSGSRIMFL LVDKETARCH SEQKTQFKRE TASLKLLPHQ PRVVVIKKGS 250
    NGYGFYLRAG PEQKGQIIKD IEPGSPAEAA GLKNNDLVVA VNGKSVEALD 300
    HDGVVEMIRK GGDQTTLLVL DKEAESIYSL ARFSPLLYCQ SQELPNGSVK 350
    EGPAPIPAPL EATGSEPTED AEGHKPKLCR LLKEDDSYGF HLNAIRGQPG 400
    SFVKEVQQGG PADKAGLENE DVIIEVNGEN VQEEPYDRVV ERIKSSGKHV 450
    TLLVCGKMAY SYFQAKKIPI VSSMAEPLVA GPDEKGETSA ESEHDAHPAK 500
    DRTLSTASHS SSNSEDTEM 519
    Length:519
    Mass (Da):56,499
    Last modified:October 1, 2000 - v1
    Checksum:i681B57F4E237BC28
    GO

    Sequence cautioni

    The sequence AAL84634.1 differs from that shown. Reason: Frameshift at positions 229 and 261.
    The sequence BAC26605.1 differs from that shown. Reason: Frameshift at position 519. The frameshift causes a read through of the stop codon.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241L → R in AAL84634. (PubMed:11051556)Curated
    Sequence conflicti135 – 1351L → S in AAL84634. (PubMed:11051556)Curated
    Sequence conflicti162 – 1621D → N in BAB24493. (PubMed:16141072)Curated
    Sequence conflicti162 – 1621D → N in BAC26598. (PubMed:16141072)Curated
    Sequence conflicti162 – 1621D → N in BAC26605. (PubMed:16141072)Curated
    Sequence conflicti162 – 1621D → N in BAB28007. (PubMed:16141072)Curated
    Sequence conflicti162 – 1621D → N in BAB29600. (PubMed:16141072)Curated
    Sequence conflicti162 – 1621D → S in AAL84634. (PubMed:11051556)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF474247 mRNA. Translation: AAL84634.1. Frameshift.
    AF220100 mRNA. Translation: AAF73863.1.
    AK006269 mRNA. Translation: BAB24493.1.
    AK029752 mRNA. Translation: BAC26598.1.
    AK029764 mRNA. Translation: BAC26605.1. Frameshift.
    AK012070 mRNA. Translation: BAB28007.1.
    AK014879 mRNA. Translation: BAB29600.1.
    BC013512 mRNA. Translation: AAH13512.1.
    CCDSiCCDS17649.1.
    RefSeqiNP_001139473.1. NM_001146001.1.
    NP_067492.2. NM_021517.2.
    XP_006501895.1. XM_006501832.1.
    XP_006501896.1. XM_006501833.1.
    XP_006501897.1. XM_006501834.1.
    UniGeneiMm.489677.

    Genome annotation databases

    EnsembliENSMUST00000058865; ENSMUSP00000058936; ENSMUSG00000038298.
    ENSMUST00000107069; ENSMUSP00000102684; ENSMUSG00000038298.
    ENSMUST00000107070; ENSMUSP00000102685; ENSMUSG00000038298.
    ENSMUST00000153256; ENSMUSP00000118846; ENSMUSG00000038298.
    GeneIDi59020.
    KEGGimmu:59020.
    UCSCiuc008qoi.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF474247 mRNA. Translation: AAL84634.1 . Frameshift.
    AF220100 mRNA. Translation: AAF73863.1 .
    AK006269 mRNA. Translation: BAB24493.1 .
    AK029752 mRNA. Translation: BAC26598.1 .
    AK029764 mRNA. Translation: BAC26605.1 . Frameshift.
    AK012070 mRNA. Translation: BAB28007.1 .
    AK014879 mRNA. Translation: BAB29600.1 .
    BC013512 mRNA. Translation: AAH13512.1 .
    CCDSi CCDS17649.1.
    RefSeqi NP_001139473.1. NM_001146001.1.
    NP_067492.2. NM_021517.2.
    XP_006501895.1. XM_006501832.1.
    XP_006501896.1. XM_006501833.1.
    XP_006501897.1. XM_006501834.1.
    UniGenei Mm.489677.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D90 NMR - A 242-330 [» ]
    2EDZ NMR - A 1-107 [» ]
    3NGH X-ray 1.80 A/B 7-106 [» ]
    3R68 X-ray 1.30 A 238-323 [» ]
    3R69 X-ray 1.50 A/B 241-322 [» ]
    4F8K X-ray 1.70 A/B 7-106 [» ]
    ProteinModelPortali Q9JIL4.
    SMRi Q9JIL4. Positions 1-107, 125-492.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 208488. 2 interactions.
    IntActi Q9JIL4. 6 interactions.
    MINTi MINT-148595.

    PTM databases

    PhosphoSitei Q9JIL4.

    Proteomic databases

    MaxQBi Q9JIL4.
    PaxDbi Q9JIL4.
    PRIDEi Q9JIL4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000058865 ; ENSMUSP00000058936 ; ENSMUSG00000038298 .
    ENSMUST00000107069 ; ENSMUSP00000102684 ; ENSMUSG00000038298 .
    ENSMUST00000107070 ; ENSMUSP00000102685 ; ENSMUSG00000038298 .
    ENSMUST00000153256 ; ENSMUSP00000118846 ; ENSMUSG00000038298 .
    GeneIDi 59020.
    KEGGi mmu:59020.
    UCSCi uc008qoi.2. mouse.

    Organism-specific databases

    CTDi 5174.
    MGIi MGI:1928901. Pdzk1.

    Phylogenomic databases

    eggNOGi NOG315208.
    GeneTreei ENSGT00530000062999.
    HOGENOMi HOG000113782.
    HOVERGENi HBG082115.
    InParanoidi Q9JIL4.
    PhylomeDBi Q9JIL4.
    TreeFami TF350449.

    Miscellaneous databases

    EvolutionaryTracei Q9JIL4.
    NextBioi 314580.
    PROi Q9JIL4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JIL4.
    Bgeei Q9JIL4.
    CleanExi MM_PDZK1.
    Genevestigatori Q9JIL4.

    Family and domain databases

    Gene3Di 2.30.42.10. 4 hits.
    InterProi IPR001478. PDZ.
    [Graphical view ]
    Pfami PF00595. PDZ. 4 hits.
    [Graphical view ]
    SMARTi SM00228. PDZ. 4 hits.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 4 hits.
    PROSITEi PS50106. PDZ. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Accessory protein facilitated CFTR-CFTR interaction, a molecular mechanism to potentiate the chloride channel activity."
      Wang S., Yue H., Derin R.B., Guggino W.B., Li M.
      Cell 103:169-179(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 351-376 AND 467-485, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH CFTR.
    2. "Targeted disruption of the PDZK1 gene by homologous recombination."
      Kocher O., Pal R., Roberts M., Cirovic C., Gilchrist A.
      Mol. Cell. Biol. 23:1175-1180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Testis.
    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].
      Strain: FVB/N.
      Tissue: Kidney.
    5. "Interaction of the type IIa Na/Pi-cotransporter with PDZ proteins."
      Gisler S.M., Stagljar I., Traebert M., Bacic D., Biber J., Murer H.
      J. Biol. Chem. 276:9206-9213(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC17A1.
    6. Cited for: FUNCTION, INTERACTION WITH AKAP2; SLC22A12; SLC22A4; SLC26A6; SLC9A3R1; SLC9A3R2 AND PDZK1IP1.
    7. "PDZK1 directly regulates the function of organic cation/carnitine transporter OCTN2."
      Kato Y., Sai Y., Yoshida K., Watanabe C., Hirata T., Tsuji A.
      Mol. Pharmacol. 67:734-743(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SLC22A5.
    8. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-488; SER-489; SER-492 AND SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "Solution structure of the third PDZ domain of PDZ domain containing protein 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (DEC-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 242-331.
    11. "In vitro and in vivo analysis of the binding of the C terminus of the HDL receptor scavenger receptor class B, type I (SR-BI), to the PDZ1 domain of its adaptor protein PDZK1."
      Kocher O., Birrane G., Tsukamoto K., Fenske S., Yesilaltay A., Pal R., Daniels K., Ladias J.A., Krieger M.
      J. Biol. Chem. 285:34999-35010(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 7-106, INTERACTION WITH SCARB1, FUNCTION, MUTAGENESIS OF LYS-14 AND TYR-20.
    12. "Identification of the PDZ3 domain of the adaptor protein PDZK1 as a second, physiologically functional binding site for the C terminus of the high density lipoprotein receptor scavenger receptor class B type I."
      Kocher O., Birrane G., Yesilaltay A., Shechter S., Pal R., Daniels K., Krieger M.
      J. Biol. Chem. 286:25171-25186(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 238-323 IN COMPLEX WITH SCARB1, INTERACTION WITH SCARB1, MUTAGENESIS OF TYR-20 AND TYR-253, FUNCTION.
    13. "Molecular analysis of the prostacyclin receptor's interaction with the PDZ1 domain of its adaptor protein PDZK1."
      Birrane G., Mulvaney E.P., Pal R., Kinsella B.T., Kocher O.
      PLoS ONE 8:E53819-E53819(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 7-106 IN COMPLEX WITH PTGIR, INTERACTION WITH PTGIR.

    Entry informationi

    Entry nameiNHRF3_MOUSE
    AccessioniPrimary (citable) accession number: Q9JIL4
    Secondary accession number(s): Q8CDP5, Q8R4G2, Q9CQ72
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Disruption of the gene was not associated with abnormal growth and development or redistribution of interacting proteins. However, a modulation of expression of selective ion channels in the kidney, as well as increased serum cholesterol levels were observed.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3