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Q02094

- RHAG_HUMAN

UniProt

Q02094 - RHAG_HUMAN

Protein

Ammonium transporter Rh type A

Gene

RHAG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      Previous versions | rss
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    Functioni

    Associated with rhesus blood group antigen expression. May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane.2 Publications

    GO - Molecular functioni

    1. ammonium transmembrane transporter activity Source: UniProtKB
    2. ankyrin binding Source: UniProtKB

    GO - Biological processi

    1. ammonium transmembrane transport Source: GOC
    2. ammonium transport Source: UniProtKB
    3. bicarbonate transport Source: Reactome
    4. carbon dioxide transport Source: UniProtKB
    5. cellular ion homeostasis Source: UniProtKB
    6. small molecule metabolic process Source: Reactome
    7. transmembrane transport Source: Reactome

    Keywords - Biological processi

    Ammonia transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
    REACT_20508. Rhesus glycoproteins mediate ammonium transport.

    Protein family/group databases

    TCDBi1.A.11.4.3. the ammonia transporter channel (amt) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ammonium transporter Rh type A
    Alternative name(s):
    Erythrocyte membrane glycoprotein Rh50
    Erythrocyte plasma membrane 50 kDa glycoprotein
    Short name:
    Rh50A
    Rhesus blood group family type A glycoprotein
    Short name:
    Rh family type A glycoprotein
    Short name:
    Rh type A glycoprotein
    Rhesus blood group-associated ammonia channel
    Rhesus blood group-associated glycoprotein
    CD_antigen: CD241
    Gene namesi
    Name:RHAG
    Synonyms:RH50
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:10006. RHAG.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: ProtInc
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Regulator type Rh-null hemolytic anemia (RHN) [MIM:268150]: Form of chronic hemolytic anemia in which the red blood cells have a stomatocytosis and spherocytosis morphology, an increased osmotic fragility, an altered ion transport system, and abnormal membrane phospholipid organization.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti79 – 791S → N in RHN. 1 Publication
    VAR_006921
    Natural varianti270 – 2701V → I in RHN. 2 Publications
    Corresponds to variant rs16879498 [ dbSNP | Ensembl ].
    VAR_015855
    Natural varianti279 – 2791G → E in RHN. 2 Publications
    Corresponds to variant rs28933991 [ dbSNP | Ensembl ].
    VAR_015856
    Natural varianti280 – 2801G → R in RHN. 1 Publication
    VAR_015857
    Natural varianti380 – 3801G → V in RHN. 1 Publication
    VAR_015858

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi268150. phenotype.
    Orphaneti3203. Overhydrated hereditary stomatocytosis.
    71275. Rh deficiency syndrome.
    PharmGKBiPA34381.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 409409Ammonium transporter Rh type APRO_0000168199Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi37 – 371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ02094.
    PRIDEiQ02094.

    PTM databases

    PhosphoSiteiQ02094.

    Expressioni

    Tissue specificityi

    Erythrocytes.1 Publication

    Gene expression databases

    ArrayExpressiQ02094.
    BgeeiQ02094.
    CleanExiHS_RHAG.
    GenevestigatoriQ02094.

    Organism-specific databases

    HPAiHPA055331.

    Interactioni

    Subunit structurei

    Heterotetramer.

    Protein-protein interaction databases

    BioGridi111937. 1 interaction.
    STRINGi9606.ENSP00000360217.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02094.
    SMRiQ02094. Positions 1-407.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 22CytoplasmicSequence Analysis
    Topological domaini24 – 5128ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini73 – 797CytoplasmicSequence Analysis
    Topological domaini101 – 11313ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini135 – 1428CytoplasmicSequence Analysis
    Topological domaini164 – 1674ExtracellularSequence Analysis
    Topological domaini189 – 20820CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini230 – 23910ExtracellularSequence Analysis
    Topological domaini261 – 2688CytoplasmicSequence Analysis
    Topological domaini292 – 2954ExtracellularSequence Analysis
    Topological domaini319 – 33214CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini354 – 3629ExtracellularSequence Analysis
    Topological domaini384 – 40926CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei3 – 2321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei52 – 7221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei80 – 10021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei114 – 13421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei143 – 16321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei168 – 18821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei209 – 22921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei240 – 26021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei269 – 29123HelicalSequence AnalysisAdd
    BLAST
    Transmembranei296 – 31823HelicalSequence AnalysisAdd
    BLAST
    Transmembranei333 – 35321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei363 – 38321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG276393.
    HOGENOMiHOG000007656.
    HOVERGENiHBG004374.
    InParanoidiQ02094.
    KOiK06580.
    OMAiNEESAYY.
    OrthoDBiEOG73NG3C.
    PhylomeDBiQ02094.
    TreeFamiTF314450.

    Family and domain databases

    Gene3Di1.10.3430.10. 1 hit.
    InterProiIPR029020. Ammonium/urea_transptr.
    IPR024041. NH4_transpt_AmtB-like_dom.
    IPR002229. RhesusRHD.
    [Graphical view]
    PfamiPF00909. Ammonium_transp. 1 hit.
    [Graphical view]
    PRINTSiPR00342. RHESUSRHD.
    SUPFAMiSSF111352. SSF111352. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q02094-1) [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

    MRFTFPLMAI VLEIAMIVLF GLFVEYETDQ TVLEQLNITK PTDMGIFFEL    50
    YPLFQDVHVM IFVGFGFLMT FLKKYGFSSV GINLLVAALG LQWGTIVQGI 100
    LQSQGQKFNI GIKNMINADF SAATVLISFG AVLGKTSPTQ MLIMTILEIV 150
    FFAHNEYLVS EIFKASDIGA SMTIHAFGAY FGLAVAGILY RSGLRKGHEN 200
    EESAYYSDLF AMIGTLFLWM FWPSFNSAIA EPGDKQCRAI VNTYFSLAAC 250
    VLTAFAFSSL VEHRGKLNMV HIQNATLAGG VAVGTCADMA IHPFGSMIIG 300
    SIAGMVSVLG YKFLTPLFTT KLRIHDTCGV HNLHGLPGVV GGLAGIVAVA 350
    MGASNTSMAM QAAALGSSIG TAVVGGLMTG LILKLPLWGQ PSDQNCYDDS 400
    VYWKVPKTR 409
    Length:409
    Mass (Da):44,198
    Last modified:December 16, 2008 - v2
    Checksum:iF6F024399CC0C88D
    GO
    Isoform 2 (identifier: Q02094-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         316-351: PLFTTKLRIHDTCGVHNLHGLPGVVGGLAGIVAVAM → VYGHAGSCTGFLYRNSSCWRSDDRFNSKVASLGTAI
         352-409: Missing.

    Show »
    Length:351
    Mass (Da):38,420
    Checksum:i1BEF505C51B6F060
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21R → C AA sequence (PubMed:3146980)Curated
    Sequence conflicti37 – 371N → P AA sequence (PubMed:3146980)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti79 – 791S → N in RHN. 1 Publication
    VAR_006921
    Natural varianti242 – 2421N → D.1 Publication
    Corresponds to variant rs1058063 [ dbSNP | Ensembl ].
    VAR_047999
    Natural varianti270 – 2701V → I in RHN. 2 Publications
    Corresponds to variant rs16879498 [ dbSNP | Ensembl ].
    VAR_015855
    Natural varianti279 – 2791G → E in RHN. 2 Publications
    Corresponds to variant rs28933991 [ dbSNP | Ensembl ].
    VAR_015856
    Natural varianti280 – 2801G → R in RHN. 1 Publication
    VAR_015857
    Natural varianti380 – 3801G → V in RHN. 1 Publication
    VAR_015858

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei316 – 35136PLFTT…VAVAM → VYGHAGSCTGFLYRNSSCWR SDDRFNSKVASLGTAI in isoform 2. 1 PublicationVSP_047629Add
    BLAST
    Alternative sequencei352 – 40958Missing in isoform 2. 1 PublicationVSP_047630Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64594 mRNA. Translation: CAA45883.1.
    AF031548 mRNA. Translation: AAC04247.1.
    AF031549 mRNA. Translation: AAC04248.1.
    AF237387
    , AF237382, AF237383, AF237384, AF237385, AF237386 Genomic DNA. Translation: AAF78209.1.
    AK313505 mRNA. Translation: BAG36285.1.
    AL121950, AL590244 Genomic DNA. Translation: CAC10519.2.
    AL590244, AL121950 Genomic DNA. Translation: CAI13085.1.
    CH471081 Genomic DNA. Translation: EAX04337.1.
    CH471081 Genomic DNA. Translation: EAX04338.1.
    CCDSiCCDS4927.1. [Q02094-1]
    PIRiS29124.
    RefSeqiNP_000315.2. NM_000324.2. [Q02094-1]
    UniGeneiHs.120950.

    Genome annotation databases

    EnsembliENST00000229810; ENSP00000229810; ENSG00000112077. [Q02094-2]
    ENST00000371175; ENSP00000360217; ENSG00000112077. [Q02094-1]
    GeneIDi6005.
    KEGGihsa:6005.
    UCSCiuc003ozk.4. human. [Q02094-1]
    uc010jzm.3. human.

    Polymorphism databases

    DMDMi218511807.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64594 mRNA. Translation: CAA45883.1 .
    AF031548 mRNA. Translation: AAC04247.1 .
    AF031549 mRNA. Translation: AAC04248.1 .
    AF237387
    , AF237382 , AF237383 , AF237384 , AF237385 , AF237386 Genomic DNA. Translation: AAF78209.1 .
    AK313505 mRNA. Translation: BAG36285.1 .
    AL121950 , AL590244 Genomic DNA. Translation: CAC10519.2 .
    AL590244 , AL121950 Genomic DNA. Translation: CAI13085.1 .
    CH471081 Genomic DNA. Translation: EAX04337.1 .
    CH471081 Genomic DNA. Translation: EAX04338.1 .
    CCDSi CCDS4927.1. [Q02094-1 ]
    PIRi S29124.
    RefSeqi NP_000315.2. NM_000324.2. [Q02094-1 ]
    UniGenei Hs.120950.

    3D structure databases

    ProteinModelPortali Q02094.
    SMRi Q02094. Positions 1-407.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111937. 1 interaction.
    STRINGi 9606.ENSP00000360217.

    Chemistry

    GuidetoPHARMACOLOGYi 1198.

    Protein family/group databases

    TCDBi 1.A.11.4.3. the ammonia transporter channel (amt) family.

    PTM databases

    PhosphoSitei Q02094.

    Polymorphism databases

    DMDMi 218511807.

    Proteomic databases

    PaxDbi Q02094.
    PRIDEi Q02094.

    Protocols and materials databases

    DNASUi 6005.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229810 ; ENSP00000229810 ; ENSG00000112077 . [Q02094-2 ]
    ENST00000371175 ; ENSP00000360217 ; ENSG00000112077 . [Q02094-1 ]
    GeneIDi 6005.
    KEGGi hsa:6005.
    UCSCi uc003ozk.4. human. [Q02094-1 ]
    uc010jzm.3. human.

    Organism-specific databases

    CTDi 6005.
    GeneCardsi GC06M049619.
    H-InvDB HIX0005947.
    HGNCi HGNC:10006. RHAG.
    HPAi HPA055331.
    MIMi 180297. gene.
    268150. phenotype.
    neXtProti NX_Q02094.
    Orphaneti 3203. Overhydrated hereditary stomatocytosis.
    71275. Rh deficiency syndrome.
    PharmGKBi PA34381.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG276393.
    HOGENOMi HOG000007656.
    HOVERGENi HBG004374.
    InParanoidi Q02094.
    KOi K06580.
    OMAi NEESAYY.
    OrthoDBi EOG73NG3C.
    PhylomeDBi Q02094.
    TreeFami TF314450.

    Enzyme and pathway databases

    Reactomei REACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
    REACT_20508. Rhesus glycoproteins mediate ammonium transport.

    Miscellaneous databases

    GeneWikii RHAG.
    GenomeRNAii 6005.
    NextBioi 23423.
    PROi Q02094.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02094.
    Bgeei Q02094.
    CleanExi HS_RHAG.
    Genevestigatori Q02094.

    Family and domain databases

    Gene3Di 1.10.3430.10. 1 hit.
    InterProi IPR029020. Ammonium/urea_transptr.
    IPR024041. NH4_transpt_AmtB-like_dom.
    IPR002229. RhesusRHD.
    [Graphical view ]
    Pfami PF00909. Ammonium_transp. 1 hit.
    [Graphical view ]
    PRINTSi PR00342. RHESUSRHD.
    SUPFAMi SSF111352. SSF111352. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of cDNA clones for a 50 kDa glycoprotein of the human erythrocyte membrane associated with Rh (rhesus) blood-group antigen expression."
      Ridgwell K., Spurr N.K., Laguda B., Macgeoch C., Avent N.D., Tanner M.J.A.
      Biochem. J. 287:223-228(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-242.
      Tissue: Bone marrow and Liver.
    2. "The human Rh50 glycoprotein gene. Structural organization and associated splicing defect resulting in Rh(null) disease."
      Huang C.-H.
      J. Biol. Chem. 273:2207-2213(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
    3. "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 1), VARIANT ILE-270.
      Tissue: Heart.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Identification of 5' flanking sequence of RH50 gene and the core region for erythroid-specific expression."
      Iwamoto S., Omi T., Yamasaki M., Okuda H., Kawano M., Kajii E.
      Biochem. Biophys. Res. Commun. 243:233-240(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-52, TISSUE SPECIFICITY.
    7. "Protein-sequence studies on Rh-related polypeptides suggest the presence of at least two groups of proteins which associate in the human red-cell membrane."
      Avent N.D., Ridgwell K., Mawby W.J., Tanner M.J.A., Anstee D.J., Kumpel B.
      Biochem. J. 256:1043-1046(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-39.
    8. "The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast."
      Marini A.-M., Matassi G., Raynal V., Andre B., Cartron J.-P., Cherif-Zahar B.
      Nat. Genet. 26:341-344(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter."
      Westhoff C.M., Ferreri-Jacobia M., Mak D.-O.D., Foskett J.K.
      J. Biol. Chem. 277:12499-12502(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Mechanism of genetic complementation of ammonium transport in yeast by human erythrocyte Rh-associated glycoprotein."
      Westhoff C.M., Siegel D.L., Burd C.G., Foskett J.K.
      J. Biol. Chem. 279:17443-17448(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    11. "Candidate gene acting as a suppressor of the RH locus in most cases of Rh-deficiency."
      Cherif-Zahar B., Raynal V., Gane P., Mattei M.-G., Bailly P., Gibbs B., Colin Y., Cartron J.-P.
      Nat. Genet. 12:168-173(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RHN ASN-79.
    12. "A novel single missense mutation identified along the RH50 gene in a composite heterozygous Rhnull blood donor of the regulator type."
      Hyland C.A., Cherif-Zahar B., Cowley N., Raynal V., Parkes J., Saul A., Cartron J.-P.
      Blood 91:1458-1463(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RHN GLU-279.
    13. "Rh50 glycoprotein gene and rhnull disease: a silent splice donor is trans to a Gly279-->Glu missense mutation in the conserved transmembrane segment."
      Huang C.-H., Liu Z., Cheng G., Chen Y.
      Blood 92:1776-1784(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RHN GLU-279.
    14. "Molecular basis for Rh(null) syndrome: identification of three new missense mutations in the Rh50 glycoprotein gene."
      Huang C.-H., Cheng G., Liu Z., Chen Y., Reid M.E., Halverson G., Okubo Y.
      Am. J. Hematol. 62:25-32(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RHN ILE-270; ARG-280 AND VAL-380.

    Entry informationi

    Entry nameiRHAG_HUMAN
    AccessioniPrimary (citable) accession number: Q02094
    Secondary accession number(s): B2R8T8
    , O43514, O43515, Q7L8L3, Q9H454
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 126 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3