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Protein

Radixin

Gene

Rdx

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.

Enzyme regulationi

A head-to-tail association, of the N-terminal and C-terminal halves results in a closed conformation (inactive form) which is incapable of actin or membrane-binding.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei278 – 2781Phosphatidylinositol

GO - Molecular functioni

  • actin binding Source: MGI
  • ATPase binding Source: MGI
  • poly(A) RNA binding Source: MGI
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Radixin
Alternative name(s):
ESP10
Gene namesi
Name:Rdx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:97887. Rdx.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: MGI
  • apical plasma membrane Source: MGI
  • cell periphery Source: MGI
  • cleavage furrow Source: UniProtKB-SubCell
  • cortical actin cytoskeleton Source: UniProtKB
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • extrinsic component of membrane Source: InterPro
  • filopodium Source: UniProtKB
  • focal adhesion Source: MGI
  • lamellipodium Source: UniProtKB
  • microvillus Source: UniProtKB
  • myelin sheath Source: UniProtKB
  • plasma membrane Source: MGI
  • ruffle Source: MGI
  • stereocilium Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 583582RadixinPRO_0000219422Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei79 – 791N6-acetyllysineBy similarity
Modified residuei83 – 831N6-succinyllysineCombined sources
Modified residuei116 – 1161PhosphotyrosineBy similarity
Modified residuei117 – 1171S-nitrosocysteineBy similarity
Modified residuei139 – 1391N6-acetyllysineBy similarity
Modified residuei146 – 1461PhosphotyrosineBy similarity
Modified residuei165 – 1651N6-acetyllysineBy similarity
Modified residuei532 – 5321PhosphoserineBy similarity
Modified residuei533 – 5331PhosphoserineBy similarity
Modified residuei564 – 5641Phosphothreonine; by ROCK21 Publication

Post-translational modificationi

Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiP26043.
MaxQBiP26043.
PaxDbiP26043.
PRIDEiP26043.

2D gel databases

REPRODUCTION-2DPAGEP26043.

PTM databases

iPTMnetiP26043.
PhosphoSiteiP26043.
SwissPalmiP26043.

Expressioni

Gene expression databases

BgeeiP26043.
CleanExiMM_RDX.
ExpressionAtlasiP26043. baseline and differential.
GenevisibleiP26043. MM.

Interactioni

Subunit structurei

Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (PubMed:12522145). Binds SLC9A3R1 (By similarity). Interacts with LAYN (PubMed:15913605). Interacts with NHERF1 and NHERF2 (PubMed:16615918). Interacts with MME/NEP (PubMed:17459884). Interacts with ICAM2 (PubMed:12554651).By similarity5 Publications

GO - Molecular functioni

  • actin binding Source: MGI
  • ATPase binding Source: MGI
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi202845. 7 interactions.
DIPiDIP-29091N.
IntActiP26043. 5 interactions.
MINTiMINT-1862372.
STRINGi10090.ENSMUSP00000000590.

Structurei

Secondary structure

1
583
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Beta strandi15 – 206Combined sources
Helixi26 – 3611Combined sources
Helixi42 – 443Combined sources
Beta strandi45 – 517Combined sources
Beta strandi56 – 583Combined sources
Beta strandi61 – 644Combined sources
Helixi65 – 673Combined sources
Beta strandi74 – 829Combined sources
Helixi89 – 913Combined sources
Helixi96 – 11116Combined sources
Helixi119 – 13416Combined sources
Turni139 – 1413Combined sources
Turni144 – 1496Combined sources
Helixi155 – 1606Combined sources
Helixi165 – 17814Combined sources
Turni179 – 1813Combined sources
Helixi184 – 19512Combined sources
Turni199 – 2024Combined sources
Beta strandi204 – 2107Combined sources
Beta strandi215 – 2217Combined sources
Beta strandi224 – 2296Combined sources
Beta strandi232 – 2354Combined sources
Beta strandi237 – 2415Combined sources
Helixi242 – 2443Combined sources
Beta strandi245 – 2517Combined sources
Beta strandi254 – 26411Combined sources
Beta strandi267 – 2704Combined sources
Helixi274 – 29320Combined sources
Helixi300 – 31011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GC6X-ray2.90A1-297[»]
1GC7X-ray2.80A1-297[»]
1J19X-ray2.40A1-310[»]
2D10X-ray2.50A/B/C/D1-310[»]
2D11X-ray2.81A/B/C/D1-310[»]
2D2QX-ray2.80A/B1-310[»]
2EMSX-ray2.90A1-310[»]
2EMTX-ray2.80A/B1-310[»]
2YVCX-ray3.20A/B/C1-310[»]
2ZPYX-ray2.10A1-310[»]
3X23X-ray2.40A1-310[»]
ProteinModelPortaliP26043.
SMRiP26043. Positions 1-583.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26043.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 295291FERMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni60 – 634Phosphatidylinositol binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi311 – 522212Glu-richAdd
BLAST
Compositional biasi470 – 4778Poly-Pro

Domaini

The N-terminal domain interacts with the C-terminal domain of LAYN. An interdomain interaction between its N-terminal and C-terminal domains inhibits its ability to bind LAYN. In the presence of acidic phospholipids, the interdomain interaction is inhibited and this enhances binding to LAYN.

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
GeneTreeiENSGT00830000128251.
HOVERGENiHBG002185.
InParanoidiP26043.
KOiK05762.
OMAiLSREDSM.
OrthoDBiEOG7BGHK6.
TreeFamiTF313935.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR011174. ERM.
IPR011259. ERM_C_dom.
IPR000798. Ez/rad/moesin-like.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR008954. Moesin_tail.
IPR011993. PH_dom-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFiPIRSF002305. ERM. 1 hit.
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26043-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTVGLR EVWFFGLQYV
60 70 80 90 100
DSKGYSTWLK LNKKVTQQDV KKENPLQFKF RAKFFPEDVS EELIQEITQR
110 120 130 140 150
LFFLQVKEAI LNDEIYCPPE TAVLLASYAV QAKYGDYNKE IHKPGYLAND
160 170 180 190 200
RLLPQRVLEQ HKLTKEQWEE RIQNWHEEHR GMLREDSMME YLKIAQDLEM
210 220 230 240 250
YGVNYFEIKN KKGTELWLGV DALGLNIYEH DDKLTPKIGF PWSEIRNISF
260 270 280 290 300
NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
310 320 330 340 350
EVQQMKAQAR EEKHQKQLER AQLENEKKKR EIAEKEKERI EREKEELMER
360 370 380 390 400
LRQIEEQTVK AQKELEEQTR KALELEQERQ RAKEEAERLD RERRAAEEAK
410 420 430 440 450
SAIAKQAADQ MKNQEQLAAE LAEFTAKIAL LEEAKKKKEE EATEWQHKAF
460 470 480 490 500
AAQEDLEKTK EELKTVMSAP PPPPPPPVIP PTENEHDEQD ENSAEASAEL
510 520 530 540 550
SSEGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD ETKKTQNDVL
560 570 580
HAENVKAGRD KYKTLRQIRQ GNTKQRIDEF EAM
Length:583
Mass (Da):68,543
Last modified:July 27, 2011 - v3
Checksum:i25752653017F0879
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti312 – 3132EK → VL in CAA43087 (PubMed:1955455).Curated
Sequence conflicti514 – 5141R → W in CAA43087 (PubMed:1955455).Curated
Sequence conflicti575 – 5762QR → HA AA sequence (PubMed:1955455).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60672 mRNA. Translation: CAA43087.1.
AK162204 mRNA. Translation: BAE36790.1.
CCDSiCCDS40634.1.
PIRiA41129.
RefSeqiNP_001098086.1. NM_001104616.1.
NP_033067.2. NM_009041.3.
UniGeneiMm.245746.
Mm.472057.

Genome annotation databases

EnsembliENSMUST00000000590; ENSMUSP00000000590; ENSMUSG00000032050.
ENSMUST00000163153; ENSMUSP00000128249; ENSMUSG00000032050.
GeneIDi19684.
KEGGimmu:19684.
UCSCiuc009plq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60672 mRNA. Translation: CAA43087.1.
AK162204 mRNA. Translation: BAE36790.1.
CCDSiCCDS40634.1.
PIRiA41129.
RefSeqiNP_001098086.1. NM_001104616.1.
NP_033067.2. NM_009041.3.
UniGeneiMm.245746.
Mm.472057.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GC6X-ray2.90A1-297[»]
1GC7X-ray2.80A1-297[»]
1J19X-ray2.40A1-310[»]
2D10X-ray2.50A/B/C/D1-310[»]
2D11X-ray2.81A/B/C/D1-310[»]
2D2QX-ray2.80A/B1-310[»]
2EMSX-ray2.90A1-310[»]
2EMTX-ray2.80A/B1-310[»]
2YVCX-ray3.20A/B/C1-310[»]
2ZPYX-ray2.10A1-310[»]
3X23X-ray2.40A1-310[»]
ProteinModelPortaliP26043.
SMRiP26043. Positions 1-583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202845. 7 interactions.
DIPiDIP-29091N.
IntActiP26043. 5 interactions.
MINTiMINT-1862372.
STRINGi10090.ENSMUSP00000000590.

PTM databases

iPTMnetiP26043.
PhosphoSiteiP26043.
SwissPalmiP26043.

2D gel databases

REPRODUCTION-2DPAGEP26043.

Proteomic databases

EPDiP26043.
MaxQBiP26043.
PaxDbiP26043.
PRIDEiP26043.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000590; ENSMUSP00000000590; ENSMUSG00000032050.
ENSMUST00000163153; ENSMUSP00000128249; ENSMUSG00000032050.
GeneIDi19684.
KEGGimmu:19684.
UCSCiuc009plq.2. mouse.

Organism-specific databases

CTDi5962.
MGIiMGI:97887. Rdx.

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
GeneTreeiENSGT00830000128251.
HOVERGENiHBG002185.
InParanoidiP26043.
KOiK05762.
OMAiLSREDSM.
OrthoDBiEOG7BGHK6.
TreeFamiTF313935.

Miscellaneous databases

ChiTaRSiRdx. mouse.
EvolutionaryTraceiP26043.
PROiP26043.
SOURCEiSearch...

Gene expression databases

BgeeiP26043.
CleanExiMM_RDX.
ExpressionAtlasiP26043. baseline and differential.
GenevisibleiP26043. MM.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR011174. ERM.
IPR011259. ERM_C_dom.
IPR000798. Ez/rad/moesin-like.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR008954. Moesin_tail.
IPR011993. PH_dom-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFiPIRSF002305. ERM. 1 hit.
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-53 AND 263-277.
    Tissue: Liver.
  2. "The ezrin-like family of tyrosine kinase substrates: receptor-specific pattern of tyrosine phosphorylation and relationship to malignant transformation."
    Fazioli F., Wong W.T., Ullrich S.J., Sakaguchi K., Appella E., Di Fiore P.P.
    Oncogene 8:1335-1345(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION.
    Strain: BALB/cJ.
    Tissue: Keratinocyte.
  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.
  4. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 84-100, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  5. "Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association."
    Matsui T., Maeda M., Doi Y., Yonemura S., Amano M., Kaibuchi K., Tsukita S., Tsukita S.
    J. Cell Biol. 140:647-657(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-564, ENZYME REGULATION.
  6. "Identification of targets for calcium signaling through the copine family of proteins. Characterization of a coiled-coil copine-binding motif."
    Tomsig J.L., Snyder S.L., Creutz C.E.
    J. Biol. Chem. 278:10048-10054(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CPNE1 AND CPNE4.
  7. "Layilin, a cell surface hyaluronan receptor, interacts with merlin and radixin."
    Bono P., Cordero E., Johnson K., Borowsky M., Ramesh V., Jacks T., Hynes R.O.
    Exp. Cell Res. 308:177-187(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LAYN.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain."
    Hamada K., Shimizu T., Matsui T., Tsukita S., Hakoshima T.
    EMBO J. 19:4449-4462(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-297 IN COMPLEX WITH INOSITOL-1,4,5-TRISPHOSPHATE.
  11. "Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex."
    Hamada K., Shimizu T., Yonemura S., Tsukita S., Tsukita S., Hakoshima T.
    EMBO J. 22:502-514(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-310 IN COMPLEX WITH ICAM2.
  12. "Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304."
    Kitano K., Yusa F., Hakoshima T.
    Acta Crystallogr. F 62:340-345(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-310.
  13. "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 (2.5 ANGSTROMS) OF 1-310 IN COMPLEXES WITH NHERF1 AND NHERF2.
  14. "Structural basis for type II membrane protein binding by ERM proteins revealed by the radixin-neutral endopeptidase 24.11 (NEP) complex."
    Terawaki S., Kitano K., Hakoshima T.
    J. Biol. Chem. 282:19854-19862(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-310 IN COMPLEX WITH MME/NEP.

Entry informationi

Entry nameiRADI_MOUSE
AccessioniPrimary (citable) accession number: P26043
Secondary accession number(s): Q3TS85, Q9QW27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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.