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Protein

Ammonium transporter Rh type A

Gene

RHAG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. erythrocyte development Source: Ensembl
  7. multicellular organismal iron ion homeostasis Source: Ensembl
  8. small molecule metabolic process Source: Reactome
  9. transmembrane transport Source: Reactome
Complete GO annotation...

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 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:10006. RHAG.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22CytoplasmicSequence Analysis
Transmembranei3 – 2321HelicalSequence AnalysisAdd
BLAST
Topological domaini24 – 5128ExtracellularSequence AnalysisAdd
BLAST
Transmembranei52 – 7221HelicalSequence AnalysisAdd
BLAST
Topological domaini73 – 797CytoplasmicSequence Analysis
Transmembranei80 – 10021HelicalSequence AnalysisAdd
BLAST
Topological domaini101 – 11313ExtracellularSequence AnalysisAdd
BLAST
Transmembranei114 – 13421HelicalSequence AnalysisAdd
BLAST
Topological domaini135 – 1428CytoplasmicSequence Analysis
Transmembranei143 – 16321HelicalSequence AnalysisAdd
BLAST
Topological domaini164 – 1674ExtracellularSequence Analysis
Transmembranei168 – 18821HelicalSequence AnalysisAdd
BLAST
Topological domaini189 – 20820CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei209 – 22921HelicalSequence AnalysisAdd
BLAST
Topological domaini230 – 23910ExtracellularSequence Analysis
Transmembranei240 – 26021HelicalSequence AnalysisAdd
BLAST
Topological domaini261 – 2688CytoplasmicSequence Analysis
Transmembranei269 – 29123HelicalSequence AnalysisAdd
BLAST
Topological domaini292 – 2954ExtracellularSequence Analysis
Transmembranei296 – 31823HelicalSequence AnalysisAdd
BLAST
Topological domaini319 – 33214CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei333 – 35321HelicalSequence AnalysisAdd
BLAST
Topological domaini354 – 3629ExtracellularSequence Analysis
Transmembranei363 – 38321HelicalSequence AnalysisAdd
BLAST
Topological domaini384 – 40926CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Regulator type Rh-null hemolytic anemia (RHN)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionForm 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.

See also OMIM:268150
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.

Polymorphism and mutation databases

BioMutaiRHAG.
DMDMi218511807.

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

BgeeiQ02094.
CleanExiHS_RHAG.
ExpressionAtlasiQ02094. baseline and differential.
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...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG276393.
GeneTreeiENSGT00390000005787.
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. AlignAdd to basket

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

        10         20         30         40         50
MRFTFPLMAI VLEIAMIVLF GLFVEYETDQ TVLEQLNITK PTDMGIFFEL
60 70 80 90 100
YPLFQDVHVM IFVGFGFLMT FLKKYGFSSV GINLLVAALG LQWGTIVQGI
110 120 130 140 150
LQSQGQKFNI GIKNMINADF SAATVLISFG AVLGKTSPTQ MLIMTILEIV
160 170 180 190 200
FFAHNEYLVS EIFKASDIGA SMTIHAFGAY FGLAVAGILY RSGLRKGHEN
210 220 230 240 250
EESAYYSDLF AMIGTLFLWM FWPSFNSAIA EPGDKQCRAI VNTYFSLAAC
260 270 280 290 300
VLTAFAFSSL VEHRGKLNMV HIQNATLAGG VAVGTCADMA IHPFGSMIIG
310 320 330 340 350
SIAGMVSVLG YKFLTPLFTT KLRIHDTCGV HNLHGLPGVV GGLAGIVAVA
360 370 380 390 400
MGASNTSMAM QAAALGSSIG TAVVGGLMTG LILKLPLWGQ PSDQNCYDDS

VYWKVPKTR
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:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000371175; ENSP00000360217; ENSG00000112077. [Q02094-1]
GeneIDi6005.
KEGGihsa:6005.
UCSCiuc003ozk.4. human. [Q02094-1]
uc010jzm.3. human.

Polymorphism and mutation databases

BioMutaiRHAG.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi111937. 1 interaction.
STRINGi9606.ENSP00000360217.

Chemistry

GuidetoPHARMACOLOGYi1198.

Protein family/group databases

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

PTM databases

PhosphoSiteiQ02094.

Polymorphism and mutation databases

BioMutaiRHAG.
DMDMi218511807.

Proteomic databases

PaxDbiQ02094.
PRIDEiQ02094.

Protocols and materials databases

DNASUi6005.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371175; ENSP00000360217; ENSG00000112077. [Q02094-1]
GeneIDi6005.
KEGGihsa:6005.
UCSCiuc003ozk.4. human. [Q02094-1]
uc010jzm.3. human.

Organism-specific databases

CTDi6005.
GeneCardsiGC06M049619.
H-InvDBHIX0005947.
HGNCiHGNC:10006. RHAG.
HPAiHPA055331.
MIMi180297. gene.
268150. phenotype.
neXtProtiNX_Q02094.
Orphaneti3203. Overhydrated hereditary stomatocytosis.
71275. Rh deficiency syndrome.
PharmGKBiPA34381.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG276393.
GeneTreeiENSGT00390000005787.
HOGENOMiHOG000007656.
HOVERGENiHBG004374.
InParanoidiQ02094.
KOiK06580.
OMAiNEESAYY.
OrthoDBiEOG73NG3C.
PhylomeDBiQ02094.
TreeFamiTF314450.

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.

Miscellaneous databases

ChiTaRSiRHAG. human.
GeneWikiiRHAG.
GenomeRNAii6005.
NextBioi23423.
PROiQ02094.
SOURCEiSearch...

Gene expression databases

BgeeiQ02094.
CleanExiHS_RHAG.
ExpressionAtlasiQ02094. baseline and differential.
GenevestigatoriQ02094.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 130 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

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 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.