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Q9JIL4

- NHRF3_MOUSE

UniProt

Q9JIL4 - NHRF3_MOUSE

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Protein
Na(+)/H(+) exchange regulatory cofactor NHE-RF3
Gene
Pdzk1, Cap70, Nherf3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.7 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
Complete GO annotation...

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.2 Publications

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
Complete GO annotation...

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-RF3
PRO_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).7 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ9JIL4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 9082PDZ 1
Add
BLAST
Domaini128 – 21588PDZ 2
Add
BLAST
Domaini243 – 32381PDZ 3
Add
BLAST
Domaini378 – 45881PDZ 4
Add
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.
Contains 4 PDZ (DHR) domains.

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241L → R in AAL84634. 1 Publication
Sequence conflicti135 – 1351L → S in AAL84634. 1 Publication
Sequence conflicti162 – 1621D → N in BAB24493. 1 Publication
Sequence conflicti162 – 1621D → N in BAC26598. 1 Publication
Sequence conflicti162 – 1621D → N in BAC26605. 1 Publication
Sequence conflicti162 – 1621D → N in BAB28007. 1 Publication
Sequence conflicti162 – 1621D → N in BAB29600. 1 Publication
Sequence conflicti162 – 1621D → S in AAL84634. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 114 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

Similar proteinsi