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Protein

Radixin

Gene

RDX

Organism
Homo sapiens (Human)
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 – 2781PhosphatidylinositolBy similarity

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • ATPase binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase A binding Source: UniProtKB

GO - Biological processi

  • actin filament capping Source: UniProtKB-KW
  • apical protein localization Source: Ensembl
  • cellular response to thyroid hormone stimulus Source: UniProtKB
  • establishment of endothelial barrier Source: UniProtKB
  • establishment of protein localization Source: UniProtKB
  • establishment of protein localization to plasma membrane Source: UniProtKB
  • microvillus assembly Source: Ensembl
  • negative regulation of adherens junction organization Source: UniProtKB
  • negative regulation of cell size Source: UniProtKB
  • negative regulation of GTPase activity Source: UniProtKB
  • negative regulation of homotypic cell-cell adhesion Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cellular protein catabolic process Source: UniProtKB
  • positive regulation of early endosome to late endosome transport Source: UniProtKB
  • positive regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of protein localization to early endosome Source: UniProtKB
  • protein kinase A signaling Source: UniProtKB
  • regulation of actin filament bundle assembly Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of cell size Source: UniProtKB
  • regulation of GTPase activity Source: UniProtKB
  • regulation of organelle assembly Source: UniProtKB
  • regulation of Rap protein signal transduction Source: UniProtKB
  • regulation of ruffle assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-HSA-437239. Recycling pathway of L1.

Names & Taxonomyi

Protein namesi
Recommended name:
Radixin
Gene namesi
Name:RDX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:9944. RDX.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Deafness, autosomal recessive, 24 (DFNB24)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
See also OMIM:611022
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti578 – 5781D → N in DFNB24. 1 Publication
VAR_036859

Keywords - Diseasei

Deafness, Disease mutation, Non-syndromic deafness

Organism-specific databases

MalaCardsiRDX.
MIMi611022. phenotype.
Orphaneti90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
PharmGKBiPA34311.

Polymorphism and mutation databases

BioMutaiRDX.
DMDMi464541.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 583582RadixinPRO_0000219421Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei79 – 791N6-acetyllysineBy similarity
Modified residuei83 – 831N6-succinyllysineBy similarity
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 ROCK2By similarity

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiP35241.
MaxQBiP35241.
PaxDbiP35241.
PeptideAtlasiP35241.
PRIDEiP35241.

PTM databases

iPTMnetiP35241.
PhosphoSiteiP35241.
SwissPalmiP35241.

Expressioni

Gene expression databases

BgeeiP35241.
CleanExiHS_RDX.
ExpressionAtlasiP35241. baseline and differential.
GenevisibleiP35241. HS.

Organism-specific databases

HPAiCAB037312.
HPA000263.
HPA000763.

Interactioni

Subunit structurei

Binds SLC9A3R1 (PubMed:9430655). Interacts with NHERF1, NHERF2, LAYN, MME/NEP and ICAM2 (By similarity). Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ITGB2P051072EBI-2514878,EBI-300173

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • ATPase binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase A binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111894. 69 interactions.
IntActiP35241. 11 interactions.
MINTiMINT-1536950.
STRINGi9606.ENSP00000342830.

Structurei

3D structure databases

ProteinModelPortaliP35241.
SMRiP35241. Positions 1-583.
ModBaseiSearch...
MobiDBiSearch...

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 bindingBy similarity

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 (By similarity).By similarity

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
GeneTreeiENSGT00830000128251.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP35241.
KOiK05762.
OMAiLSREDSM.
OrthoDBiEOG7BGHK6.
PhylomeDBiP35241.
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]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P35241-1) [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

        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
LKQIEEQTIK AQKELEEQTR KALELDQERK RAKEEAERLE KERRAAEEAK
410 420 430 440 450
SAIAKQAADQ MKNQEQLAAE LAEFTAKIAL LEEAKKKKEE EATEWQHKAF
460 470 480 490 500
AAQEDLEKTK EELKTVMSAP PPPPPPPVIP PTENEHDEHD ENNAEASAEL
510 520 530 540 550
SNEGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD ETKKTQNDVL
560 570 580
HAENVKAGRD KYKTLRQIRQ GNTKQRIDEF EAM
Length:583
Mass (Da):68,564
Last modified:February 1, 1994 - v1
Checksum:i889687E1D675FFE7
GO
Isoform 2 (identifier: P35241-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-347: Missing.
     583-583: M → MWGPKLYALFQMRSCQSSIKQM

Show »
Length:257
Mass (Da):29,668
Checksum:iF763D99B9343B54A
GO
Isoform 3 (identifier: P35241-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     33-64: Missing.
     168-539: Missing.
     583-583: M → MWGPKLYALFQMRSCQSSIKQM

Show »
Length:200
Mass (Da):23,413
Checksum:i59D476B3466D4CD6
GO
Isoform 4 (identifier: P35241-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-156: MPKPINVRVT...LANDRLLPQR → MLSWNLPFSPIQLANNFLTS

Show »
Length:447
Mass (Da):52,679
Checksum:i6DD0EEED1757180C
GO
Isoform 5 (identifier: P35241-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     583-583: M → MWGPKLYALFQMRSCQSSIKQM

Show »
Length:604
Mass (Da):71,049
Checksum:i62FD7960876C937F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti435 – 4351K → R in BAH14432 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti328 – 3281K → E.1 Publication
Corresponds to variant rs17854427 [ dbSNP | Ensembl ].
VAR_036857
Natural varianti490 – 4901D → N.
Corresponds to variant rs34471100 [ dbSNP | Ensembl ].
VAR_036858
Natural varianti578 – 5781D → N in DFNB24. 1 Publication
VAR_036859

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 347347Missing in isoform 2. 1 PublicationVSP_045315Add
BLAST
Alternative sequencei1 – 156156MPKPI…LLPQR → MLSWNLPFSPIQLANNFLTS in isoform 4. 1 PublicationVSP_047276Add
BLAST
Alternative sequencei33 – 6432Missing in isoform 3. 1 PublicationVSP_045316Add
BLAST
Alternative sequencei168 – 539372Missing in isoform 3. 1 PublicationVSP_045317Add
BLAST
Alternative sequencei583 – 5831M → MWGPKLYALFQMRSCQSSIK QM in isoform 2, isoform 3 and isoform 5. 1 PublicationVSP_045318

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02320 mRNA. Translation: AAA36541.1.
AK316061 mRNA. Translation: BAH14432.1.
DQ916738 mRNA. Translation: ABI34710.1.
DQ916739 mRNA. Translation: ABI34711.1.
DQ916741 mRNA. Translation: ABI34713.1.
DQ916742 mRNA. Translation: ABI34714.1.
DQ916740 mRNA. Translation: ABI34712.1.
AP000901 Genomic DNA. No translation available.
AP002788 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67129.1.
BC047109 mRNA. Translation: AAH47109.1.
CCDSiCCDS58171.1. [P35241-2]
CCDS58172.1. [P35241-4]
CCDS58173.1. [P35241-3]
CCDS58174.1. [P35241-5]
CCDS8343.1. [P35241-1]
PIRiA46127.
RefSeqiNP_001247421.1. NM_001260492.1. [P35241-5]
NP_001247422.1. NM_001260493.1. [P35241-5]
NP_001247423.1. NM_001260494.1. [P35241-4]
NP_001247424.1. NM_001260495.1. [P35241-2]
NP_001247425.1. NM_001260496.1. [P35241-3]
NP_002897.1. NM_002906.3. [P35241-1]
UniGeneiHs.263671.
Hs.584560.
Hs.741211.

Genome annotation databases

EnsembliENST00000343115; ENSP00000342830; ENSG00000137710. [P35241-1]
ENST00000405097; ENSP00000384136; ENSG00000137710. [P35241-5]
ENST00000528498; ENSP00000432112; ENSG00000137710. [P35241-5]
ENST00000528900; ENSP00000433580; ENSG00000137710. [P35241-2]
ENST00000530301; ENSP00000436277; ENSG00000137710. [P35241-3]
ENST00000530749; ENSP00000437301; ENSG00000137710. [P35241-5]
ENST00000544551; ENSP00000445826; ENSG00000137710. [P35241-4]
GeneIDi5962.
KEGGihsa:5962.
UCSCiuc001pku.4. human. [P35241-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02320 mRNA. Translation: AAA36541.1.
AK316061 mRNA. Translation: BAH14432.1.
DQ916738 mRNA. Translation: ABI34710.1.
DQ916739 mRNA. Translation: ABI34711.1.
DQ916741 mRNA. Translation: ABI34713.1.
DQ916742 mRNA. Translation: ABI34714.1.
DQ916740 mRNA. Translation: ABI34712.1.
AP000901 Genomic DNA. No translation available.
AP002788 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67129.1.
BC047109 mRNA. Translation: AAH47109.1.
CCDSiCCDS58171.1. [P35241-2]
CCDS58172.1. [P35241-4]
CCDS58173.1. [P35241-3]
CCDS58174.1. [P35241-5]
CCDS8343.1. [P35241-1]
PIRiA46127.
RefSeqiNP_001247421.1. NM_001260492.1. [P35241-5]
NP_001247422.1. NM_001260493.1. [P35241-5]
NP_001247423.1. NM_001260494.1. [P35241-4]
NP_001247424.1. NM_001260495.1. [P35241-2]
NP_001247425.1. NM_001260496.1. [P35241-3]
NP_002897.1. NM_002906.3. [P35241-1]
UniGeneiHs.263671.
Hs.584560.
Hs.741211.

3D structure databases

ProteinModelPortaliP35241.
SMRiP35241. Positions 1-583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111894. 69 interactions.
IntActiP35241. 11 interactions.
MINTiMINT-1536950.
STRINGi9606.ENSP00000342830.

PTM databases

iPTMnetiP35241.
PhosphoSiteiP35241.
SwissPalmiP35241.

Polymorphism and mutation databases

BioMutaiRDX.
DMDMi464541.

Proteomic databases

EPDiP35241.
MaxQBiP35241.
PaxDbiP35241.
PeptideAtlasiP35241.
PRIDEiP35241.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343115; ENSP00000342830; ENSG00000137710. [P35241-1]
ENST00000405097; ENSP00000384136; ENSG00000137710. [P35241-5]
ENST00000528498; ENSP00000432112; ENSG00000137710. [P35241-5]
ENST00000528900; ENSP00000433580; ENSG00000137710. [P35241-2]
ENST00000530301; ENSP00000436277; ENSG00000137710. [P35241-3]
ENST00000530749; ENSP00000437301; ENSG00000137710. [P35241-5]
ENST00000544551; ENSP00000445826; ENSG00000137710. [P35241-4]
GeneIDi5962.
KEGGihsa:5962.
UCSCiuc001pku.4. human. [P35241-1]

Organism-specific databases

CTDi5962.
GeneCardsiRDX.
GeneReviewsiRDX.
HGNCiHGNC:9944. RDX.
HPAiCAB037312.
HPA000263.
HPA000763.
MalaCardsiRDX.
MIMi179410. gene.
611022. phenotype.
neXtProtiNX_P35241.
Orphaneti90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
PharmGKBiPA34311.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
GeneTreeiENSGT00830000128251.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP35241.
KOiK05762.
OMAiLSREDSM.
OrthoDBiEOG7BGHK6.
PhylomeDBiP35241.
TreeFamiTF313935.

Enzyme and pathway databases

ReactomeiR-HSA-437239. Recycling pathway of L1.

Miscellaneous databases

ChiTaRSiRDX. human.
GeneWikiiRadixin.
GenomeRNAii5962.
PROiP35241.
SOURCEiSearch...

Gene expression databases

BgeeiP35241.
CleanExiHS_RDX.
ExpressionAtlasiP35241. baseline and differential.
GenevisibleiP35241. HS.

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. "Molecular cloning, cDNA sequence, and chromosomal assignment of the human radixin gene and two dispersed pseudogenes."
    Wilgenbus K.K., Milatovich A., Francke U., Furthmayr H.
    Genomics 16:199-206(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "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] (ISOFORM 4).
    Tissue: Hippocampus.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5), VARIANT DFNB24 ASN-578.
    Tissue: Retina.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1), VARIANT GLU-328.
    Tissue: Brain.
  7. "NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins."
    Murthy A., Gonzalez-Agosti C., Cordero E., Pinney D., Candia C., Solomon F., Gusella J., Ramesh V.
    J. Biol. Chem. 273:1273-1276(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC9A3R1.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRADI_HUMAN
AccessioniPrimary (citable) accession number: P35241
Secondary accession number(s): A7YIJ8
, A7YIK0, A7YIK3, B7Z9U6, F5H1A7, Q86Y61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 8, 2016
This is version 155 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.