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Q15599

- NHRF2_HUMAN

UniProt

Q15599 - NHRF2_HUMAN

Protein

Na(+)/H(+) exchange regulatory cofactor NHE-RF2

Gene

SLC9A3R2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (16 Feb 2004)
      Previous versions | rss
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    Functioni

    Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May also act as scaffold protein in the nucleus.2 Publications

    GO - Molecular functioni

    1. beta-catenin binding Source: UniProtKB
    2. phosphatase binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein C-terminus binding Source: UniProtKB
    5. receptor binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
    2. protein complex assembly Source: ProtInc

    Protein family/group databases

    TCDBi8.A.24.1.2. the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Na(+)/H(+) exchange regulatory cofactor NHE-RF2
    Short name:
    NHERF-2
    Alternative name(s):
    NHE3 kinase A regulatory protein E3KARP
    SRY-interacting protein 1
    Short name:
    SIP-1
    Sodium-hydrogen exchanger regulatory factor 2
    Solute carrier family 9 isoform A3 regulatory factor 2
    Tyrosine kinase activator protein 1
    Short name:
    TKA-1
    Gene namesi
    Name:SLC9A3R2
    Synonyms:NHERF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:11076. SLC9A3R2.

    Subcellular locationi

    Endomembrane system 1 Publication; Peripheral membrane protein 1 Publication. Nucleus 1 Publication. Apical cell membrane By similarity
    Note: Localizes with EZR and PODXL at the apical cell membrane of glomerular epithelium cells and the sides of the food processes By similarity. Nuclear, in a punctate pattern.By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. cytoplasm Source: Ensembl
    3. endomembrane system Source: UniProtKB-SubCell
    4. extracellular vesicular exosome Source: UniProt
    5. nucleus Source: ProtInc
    6. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35932.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 337337Na(+)/H(+) exchange regulatory cofactor NHE-RF2PRO_0000096805Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei183 – 1831Phosphoserine1 Publication
    Modified residuei254 – 2541Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15599.
    PaxDbiQ15599.
    PRIDEiQ15599.

    PTM databases

    PhosphoSiteiQ15599.

    Expressioni

    Tissue specificityi

    Widely expressed.2 Publications

    Gene expression databases

    ArrayExpressiQ15599.
    BgeeiQ15599.
    CleanExiHS_SLC9A3R2.
    GenevestigatoriQ15599.

    Organism-specific databases

    HPAiHPA001672.

    Interactioni

    Subunit structurei

    Homodimer, and heterodimer with SLC9A3R1. Binds PDZK1. Found in a complex with EZR, PODXL and SLC9A3R2 By similarity. Interacts (via the PDZ domains) with PODXL (via the C-terminal PDZ-binding motif DTHL); interaction is detected in glomerular epithelium cells By similarity. Binds ADRB2, SLC9A3, P2RY1, P2YR2, SRY, RDX and LPAR2. Interacts with MCC and PODXL. Interacts with SGK1 and KCNJ1/ROMK1. Interacts (via the PDZ domains) with SLC26A6 isoform 4 and isoform 5.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CFTRP135697EBI-1149760,EBI-349854
    LPAR2Q9HBW02EBI-1149760,EBI-765995
    mGluR1aQ9R0W02EBI-1149760,EBI-8505383From a different organism.
    PTENP604845EBI-1149760,EBI-696162
    SLC26A3P408795EBI-1149760,EBI-8542350

    Protein-protein interaction databases

    BioGridi114754. 41 interactions.
    DIPiDIP-29093N.
    IntActiQ15599. 20 interactions.
    MINTiMINT-126664.
    STRINGi9606.ENSP00000408005.

    Structurei

    Secondary structure

    1
    337
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 156
    Beta strandi23 – 275
    Beta strandi34 – 396
    Helixi44 – 474
    Beta strandi55 – 595
    Helixi69 – 7810
    Beta strandi82 – 887
    Beta strandi150 – 1556
    Beta strandi163 – 1675
    Beta strandi169 – 17911
    Helixi184 – 1885
    Beta strandi195 – 1995
    Helixi209 – 2168
    Beta strandi219 – 22810
    Helixi327 – 33610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D11X-ray2.81E/F/G/H310-337[»]
    2HE4X-ray1.45A147-228[»]
    2OCSX-ray1.50A9-91[»]
    4P0CX-ray1.34A9-90[»]
    ProteinModelPortaliQ15599.
    SMRiQ15599. Positions 9-91, 143-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15599.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 9080PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini150 – 23081PDZ 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 PDZ (DHR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG319972.
    HOGENOMiHOG000089940.
    HOVERGENiHBG052616.
    InParanoidiQ15599.
    KOiK13358.
    OMAiRGEHGYG.
    PhylomeDBiQ15599.
    TreeFamiTF350449.

    Family and domain databases

    Gene3Di2.30.42.10. 2 hits.
    InterProiIPR015098. EBP50_C-term.
    IPR017300. NaH_exchngr_reg_CF_NHE-RF.
    IPR001478. PDZ.
    [Graphical view]
    PfamiPF09007. EBP50_C-term. 1 hit.
    PF00595. PDZ. 2 hits.
    [Graphical view]
    PIRSFiPIRSF037866. EBP50. 1 hit.
    ProDomiPD283022. EBP50_C-term. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00228. PDZ. 2 hits.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 2 hits.
    PROSITEiPS50106. PDZ. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15599-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAPEPLRPR LCRLVRGEQG YGFHLHGEKG RRGQFIRRVE PGSPAEAAAL    50
    RAGDRLVEVN GVNVEGETHH QVVQRIKAVE GQTRLLVVDQ ETDEELRRRQ 100
    LTCTEEMAQR GLPPAHDPWE PKPDWAHTGS HSSEAGKKDV SGPLRELRPR 150
    LCHLRKGPQG YGFNLHSDKS RPGQYIRSVD PGSPAARSGL RAQDRLIEVN 200
    GQNVEGLRHA EVVASIKARE DEARLLVVDP ETDEHFKRLR VTPTEEHVEG 250
    PLPSPVTNGT SPAQLNGGSA CSSRSDLPGS DKDTEDGSAW KQDPFQESGL 300
    HLSPTAAEAK EKARAMRVNK RAPQMDWNRK REIFSNF 337
    Length:337
    Mass (Da):37,414
    Last modified:February 16, 2004 - v2
    Checksum:i4F5D341590D22ED7
    GO
    Isoform 2 (identifier: Q15599-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         286-296: Missing.

    Show »
    Length:326
    Mass (Da):36,153
    Checksum:i59EB725D61D896DC
    GO
    Isoform 3 (identifier: Q15599-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-27: MAAPEPLRPRLCRLVRGEQGYGFHLHG → MARSGSATPPARAPGAPPRSPPQRLVQ
         28-138: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:226
    Mass (Da):24,718
    Checksum:i51D77F534CB2328A
    GO

    Sequence cautioni

    The sequence CAA90511.1 differs from that shown. Reason: Frameshift at position 309.
    The sequence AAH14513.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511Missing in CAA90511. (PubMed:9314537)Curated
    Sequence conflicti180 – 1801D → Y in BM920873. (PubMed:15489334)Curated
    Sequence conflicti334 – 3363FSN → LQH in BM920873. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2727MAAPE…FHLHG → MARSGSATPPARAPGAPPRS PPQRLVQ in isoform 3. 1 PublicationVSP_046849Add
    BLAST
    Alternative sequencei28 – 138111Missing in isoform 3. 1 PublicationVSP_046850Add
    BLAST
    Alternative sequencei286 – 29611Missing in isoform 2. 1 PublicationVSP_009378Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82108 mRNA. Translation: AAB53042.1.
    Z50150 mRNA. Translation: CAA90511.1. Frameshift.
    AF004900 mRNA. Translation: AAC63061.1.
    AF035771 mRNA. Translation: AAC52090.1.
    AB014460 Genomic DNA. Translation: BAA32696.1.
    AB016243 Genomic DNA. Translation: BAA33216.1.
    AC005600 Genomic DNA. Translation: AAC34208.1.
    AC093513 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85563.1.
    CH471112 Genomic DNA. Translation: EAW85564.1.
    CH471112 Genomic DNA. Translation: EAW85565.1.
    CH471112 Genomic DNA. Translation: EAW85566.1.
    BC014513 mRNA. Translation: AAH14513.2. Different initiation.
    BC106001 mRNA. Translation: AAI06002.1.
    BM920873 mRNA. No translation available.
    CCDSiCCDS45382.1. [Q15599-1]
    CCDS45383.1. [Q15599-2]
    CCDS58407.1. [Q15599-3]
    PIRiG01158.
    RefSeqiNP_001123484.1. NM_001130012.2. [Q15599-1]
    NP_001239002.1. NM_001252073.1. [Q15599-3]
    NP_004776.3. NM_004785.5. [Q15599-2]
    UniGeneiHs.440896.

    Genome annotation databases

    EnsembliENST00000424542; ENSP00000408005; ENSG00000065054. [Q15599-1]
    ENST00000432365; ENSP00000402857; ENSG00000065054. [Q15599-2]
    ENST00000566198; ENSP00000456895; ENSG00000065054. [Q15599-3]
    GeneIDi9351.
    KEGGihsa:9351.
    UCSCiuc002coi.3. human. [Q15599-1]
    uc002coj.3. human.

    Polymorphism databases

    DMDMi42559433.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82108 mRNA. Translation: AAB53042.1 .
    Z50150 mRNA. Translation: CAA90511.1 . Frameshift.
    AF004900 mRNA. Translation: AAC63061.1 .
    AF035771 mRNA. Translation: AAC52090.1 .
    AB014460 Genomic DNA. Translation: BAA32696.1 .
    AB016243 Genomic DNA. Translation: BAA33216.1 .
    AC005600 Genomic DNA. Translation: AAC34208.1 .
    AC093513 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85563.1 .
    CH471112 Genomic DNA. Translation: EAW85564.1 .
    CH471112 Genomic DNA. Translation: EAW85565.1 .
    CH471112 Genomic DNA. Translation: EAW85566.1 .
    BC014513 mRNA. Translation: AAH14513.2 . Different initiation.
    BC106001 mRNA. Translation: AAI06002.1 .
    BM920873 mRNA. No translation available.
    CCDSi CCDS45382.1. [Q15599-1 ]
    CCDS45383.1. [Q15599-2 ]
    CCDS58407.1. [Q15599-3 ]
    PIRi G01158.
    RefSeqi NP_001123484.1. NM_001130012.2. [Q15599-1 ]
    NP_001239002.1. NM_001252073.1. [Q15599-3 ]
    NP_004776.3. NM_004785.5. [Q15599-2 ]
    UniGenei Hs.440896.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D11 X-ray 2.81 E/F/G/H 310-337 [» ]
    2HE4 X-ray 1.45 A 147-228 [» ]
    2OCS X-ray 1.50 A 9-91 [» ]
    4P0C X-ray 1.34 A 9-90 [» ]
    ProteinModelPortali Q15599.
    SMRi Q15599. Positions 9-91, 143-337.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114754. 41 interactions.
    DIPi DIP-29093N.
    IntActi Q15599. 20 interactions.
    MINTi MINT-126664.
    STRINGi 9606.ENSP00000408005.

    Protein family/group databases

    TCDBi 8.A.24.1.2. the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family.

    PTM databases

    PhosphoSitei Q15599.

    Polymorphism databases

    DMDMi 42559433.

    Proteomic databases

    MaxQBi Q15599.
    PaxDbi Q15599.
    PRIDEi Q15599.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000424542 ; ENSP00000408005 ; ENSG00000065054 . [Q15599-1 ]
    ENST00000432365 ; ENSP00000402857 ; ENSG00000065054 . [Q15599-2 ]
    ENST00000566198 ; ENSP00000456895 ; ENSG00000065054 . [Q15599-3 ]
    GeneIDi 9351.
    KEGGi hsa:9351.
    UCSCi uc002coi.3. human. [Q15599-1 ]
    uc002coj.3. human.

    Organism-specific databases

    CTDi 9351.
    GeneCardsi GC16P002075.
    HGNCi HGNC:11076. SLC9A3R2.
    HPAi HPA001672.
    MIMi 606553. gene.
    neXtProti NX_Q15599.
    PharmGKBi PA35932.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG319972.
    HOGENOMi HOG000089940.
    HOVERGENi HBG052616.
    InParanoidi Q15599.
    KOi K13358.
    OMAi RGEHGYG.
    PhylomeDBi Q15599.
    TreeFami TF350449.

    Miscellaneous databases

    EvolutionaryTracei Q15599.
    GenomeRNAii 9351.
    NextBioi 35017.
    PROi Q15599.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15599.
    Bgeei Q15599.
    CleanExi HS_SLC9A3R2.
    Genevestigatori Q15599.

    Family and domain databases

    Gene3Di 2.30.42.10. 2 hits.
    InterProi IPR015098. EBP50_C-term.
    IPR017300. NaH_exchngr_reg_CF_NHE-RF.
    IPR001478. PDZ.
    [Graphical view ]
    Pfami PF09007. EBP50_C-term. 1 hit.
    PF00595. PDZ. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF037866. EBP50. 1 hit.
    ProDomi PD283022. EBP50_C-term. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00228. PDZ. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 2 hits.
    PROSITEi PS50106. PDZ. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human testis determining factor SRY binds a nuclear factor containing PDZ protein interaction domains."
      Poulat F., de Santa Barbara P., Desclozeaux M., Soullier S., Moniot B., Bonneaud N., Boizet B., Berta P.
      J. Biol. Chem. 272:7167-7172(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Cervix carcinoma, Fetal brain and Testis.
    2. "Identification of EBP50: a PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family."
      Reczek D., Berryman M., Bretscher A.
      J. Cell Biol. 139:169-179(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    3. "cAMP-mediated inhibition of the epithelial brush border Na+/H+ exchanger, NHE3, requires an associated regulatory protein."
      Yun C.H.C., Oh S., Zizak M., Steplock D., Tsao S., Tse C.-M., Weinman E.J., Donowitz M.
      Proc. Natl. Acad. Sci. U.S.A. 94:3010-3015(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH SLC9A3, TISSUE SPECIFICITY.
      Tissue: Embryo.
    4. "Genomic structure and sequence of a human homologue (NTHL1/NTH1) of Escherichia coli endonuclease III with those of the adjacent parts of TSC2 and SLC9A3R2 genes."
      Imai K., Sarker A.H., Akiyama K., Ikeda S., Yao M., Tsutsui K., Shohmori T., Seki S.
      Gene 222:287-295(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "A C-terminal motif found in the beta2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins."
      Hall R.A., Ostedgaard L.S., Premont R.T., Blitzer J.T., Rahman N., Welsh M.J., Lefkowitz R.J.
      Proc. Natl. Acad. Sci. U.S.A. 95:8496-8501(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ADRB2; P2RY1 AND P2YR2.
      Tissue: Lung.
    6. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 1 AND 3).
      Tissue: Kidney and Testis.
    9. "cAMP-induced phosphorylation and inhibition of Na(+)/H(+) exchanger 3 (NHE3) are dependent on the presence but not the phosphorylation of NHE regulatory factor."
      Zizak M., Lamprecht G., Steplock D., Tariq N., Shenolikar S., Donowitz M., Yun C.H.C., Weinman E.J.
      J. Biol. Chem. 274:24753-24758(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SLC9A3.
    10. "Isoforms of SLC26A6 mediate anion transport and have functional PDZ interaction domains."
      Lohi H., Lamprecht G., Markovich D., Heil A., Kujala M., Seidler U., Kere J.
      Am. J. Physiol. 284:C769-C779(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC26A6.
    11. "Molecular requirements for the regulation of the renal outer medullary K(+) channel ROMK1 by the serum- and glucocorticoid-inducible kinase SGK1."
      Palmada M., Embark H.M., Yun C., Bohmer C., Lang F.
      Biochem. Biophys. Res. Commun. 311:629-634(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SGK1 AND KCNJ1/ROMK1.
    12. "NHERF2 specifically interacts with LPA2 receptor and defines the specificity and efficiency of receptor-mediated phospholipase C-beta3 activation."
      Oh Y.-S., Jo N.W., Choi J.W., Kim H.S., Seo S.-W., Kang K.-O., Hwang J.-I., Heo K., Kim S.-H., Kim Y.-H., Kim I.-H., Kim J.H., Banno Y., Ryu S.H., Suh P.-G.
      Mol. Cell. Biol. 24:5069-5079(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LPAR2.
    13. "Gp135/podocalyxin and NHERF-2 participate in the formation of a preapical domain during polarization of MDCK cells."
      Meder D., Shevchenko A., Simons K., Fuellekrug J.
      J. Cell Biol. 168:303-313(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PODXL.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "MCC, a new interacting protein for Scrib, is required for cell migration in epithelial cells."
      Arnaud C., Sebbagh M., Nola S., Audebert S., Bidaut G., Hermant A., Gayet O., Dusetti N.J., Ollendorff V., Santoni M.J., Borg J.P., Lecine P.
      FEBS Lett. 583:2326-2332(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MCC.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Structural basis for NHERF recognition by ERM proteins."
      Terawaki S., Maesaki R., Hakoshima T.
      Structure 14:777-789(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 310-337 IN COMPLEX WITH RDX.
    18. "The crystal structure of the first and second PDZ domain of human NHERF-2 (SLC9A3R2) interacting with a mode 1 PDZ binding motif."
      Structural genomics consortium (SGC)
      Submitted (JAN-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 9-232.

    Entry informationi

    Entry nameiNHRF2_HUMAN
    AccessioniPrimary (citable) accession number: Q15599
    Secondary accession number(s): D3DU84
    , D3DU85, H3BSV6, O00272, O00556, Q3KQY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: February 16, 2004
    Last modified: October 1, 2014
    This is version 143 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 16
      Human chromosome 16: 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

    External Data

    Dasty 3