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Q9H310

- RHBG_HUMAN

UniProt

Q9H310 - RHBG_HUMAN

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Protein

Ammonium transporter Rh type B

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

Functioni

Functions as a specific ammonium transporter.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. transepithelial ammonium transport Source: UniProtKB
  4. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Ammonia transport, Transport

Enzyme and pathway databases

ReactomeiREACT_20508. Rhesus glycoproteins mediate ammonium transport.

Protein family/group databases

TCDBi1.A.11.4.2. the ammonia transporter channel (amt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Ammonium transporter Rh type B
Alternative name(s):
Rhesus blood group family type B glycoprotein
Short name:
Rh family type B glycoprotein
Short name:
Rh type B glycoprotein
Gene namesi
Name:RHBG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:14572. RHBG.

Subcellular locationi

Basolateral cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei14 – 3421Helical; Reviewed predictionAdd
BLAST
Topological domaini35 – 6127Extracellular Reviewed predictionAdd
BLAST
Transmembranei62 – 8221Helical; Reviewed predictionAdd
BLAST
Topological domaini83 – 864Cytoplasmic Reviewed prediction
Transmembranei87 – 10721Helical; Reviewed predictionAdd
BLAST
Topological domaini108 – 12417Extracellular Reviewed predictionAdd
BLAST
Transmembranei125 – 14521Helical; Reviewed predictionAdd
BLAST
Topological domaini146 – 1494Cytoplasmic Reviewed prediction
Transmembranei150 – 17021Helical; Reviewed predictionAdd
BLAST
Topological domaini171 – 1788Extracellular Reviewed prediction
Transmembranei179 – 20123Helical; Reviewed predictionAdd
BLAST
Topological domaini202 – 21918Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei220 – 24021Helical; Reviewed predictionAdd
BLAST
Topological domaini241 – 25111Extracellular Reviewed predictionAdd
BLAST
Transmembranei252 – 27221Helical; Reviewed predictionAdd
BLAST
Topological domaini273 – 28210Cytoplasmic Reviewed prediction
Transmembranei283 – 30321Helical; Reviewed predictionAdd
BLAST
Topological domaini304 – 3041Extracellular Reviewed prediction
Transmembranei305 – 32521Helical; Reviewed predictionAdd
BLAST
Topological domaini326 – 34621Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei347 – 36721Helical; Reviewed predictionAdd
BLAST
Topological domaini368 – 39326Extracellular Reviewed predictionAdd
BLAST
Transmembranei394 – 41421Helical; Reviewed predictionAdd
BLAST
Topological domaini415 – 44127Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. anchored component of plasma membrane Source: UniProtKB
  2. basolateral plasma membrane Source: UniProtKB
  3. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  4. integral component of plasma membrane Source: UniProtKB
  5. plasma membrane Source: UniProtKB
  6. spectrin-associated cytoskeleton Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi419 – 4191F → A: Loss of interaction with ANK3. Intracellular retention; when associated with A-420 and A-421. 1 Publication
Mutagenesisi420 – 4201L → A: Partial loss of interaction with ANK3. Intracellular retention; when associated with A-419 and A-421. 1 Publication
Mutagenesisi421 – 4211D → A: Partial loss of interaction with ANK3. Intracellular retention; when associated with A-419 and A-420. 1 Publication

Organism-specific databases

PharmGKBiPA34385.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Ammonium transporter Rh type BPRO_0000283597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi49 – 491N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

N-glycosylated By similarity.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9H310.
PRIDEiQ9H310.

Expressioni

Tissue specificityi

Specifically expressed in kidney. Also detected in liver and ovary.1 Publication

Developmental stagei

Fetally expressed by kidney and to a lower extent in liver.1 Publication

Gene expression databases

ArrayExpressiQ9H310.
BgeeiQ9H310.
GenevestigatoriQ9H310.

Organism-specific databases

HPAiHPA048489.

Interactioni

Subunit structurei

Interacts (via C-terminus) with ANK2 and ANK3; required for targeting to the basolateral membrane.1 Publication

Protein-protein interaction databases

BioGridi121390. 1 interaction.
IntActiQ9H310. 1 interaction.
STRINGi9606.ENSP00000255013.

Structurei

3D structure databases

ProteinModelPortaliQ9H310.
SMRiQ9H310. Positions 12-423.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni416 – 4249Interaction with ANK3

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG276393.
HOVERGENiHBG004374.
KOiK06580.
PhylomeDBiQ9H310.
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H310-1) [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

MAGSPSRAAG RRLQLPLLCL FLQGATAVLF AVFVRYNHKT DAALWHRSNH    50
SNADNEFYFR YPSFQDVHAM VFVGFGFLMV FLQRYGFSSV GFTFLLAAFA 100
LQWSTLVQGF LHSFHGGHIH VGVESMINAD FCAGAVLISF GAVLGKTGPT 150
QLLLMALLEV VLFGINEFVL LHLLGVRDAG GSMTIHTFGA YFGLVLSRVL 200
YRPQLEKSKH RQGSVYHSDL FAMIGTIFLW IFWPSFNAAL TALGAGQHRT 250
ALNTYYSLAA STLGTFALSA LVGEDGRLDM VHIQNAALAG GVVVGTSSEM 300
MLTPFGALAA GFLAGTVSTL GYKFFTPILE SKFKVQDTCG VHNLHGMPGV 350
LGALLGVLVA GLATHEAYGD GLESVFPLIA EGQRSATSQA MHQLFGLFVT 400
LMFASVGGGL GGLLLKLPFL DSPPRLPALR GPSSLAGAWR A 441
Length:441
Mass (Da):47,231
Last modified:October 14, 2008 - v2
Checksum:i21EE1FE592F2E1EE
GO
Isoform 2 (identifier: Q9H310-2) [UniParc]FASTAAdd to Basket

Also known as: RhBG-2A

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     31-63: AVFVRYNHKTDAALWHRSNHSNADNEFYFRYPS → MNFTFATQKSLTLLPRLECNGAISAHCNLHLPG

Note: No experimental confirmation available.

Show »
Length:411
Mass (Da):43,675
Checksum:iB9C06223F4445B97
GO
Isoform 3 (identifier: Q9H310-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: Missing.
     175-175: G → GVRVWGGMESGVGGGQGQPLSQERGGGGGVLPLTPPPQ

Note: No experimental confirmation available.

Show »
Length:409
Mass (Da):42,978
Checksum:iD0FE23FCAC1344ED
GO
Isoform 4 (identifier: Q9H310-4) [UniParc]FASTAAdd to Basket

Also known as: RhBG-1A

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: Missing.

Show »
Length:372
Mass (Da):39,396
Checksum:i47C840C8A19763F5
GO
Isoform 5 (identifier: Q9H310-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: Missing.
     372-441: Missing.

Show »
Length:302
Mass (Da):32,092
Checksum:iB758ABDDBA1E2E90
GO

Sequence cautioni

The sequence AAG01086.1 differs from that shown. Reason: Frameshift at position 425.
The sequence AAL05978.1 differs from that shown. Reason: Frameshift at position 425.
The sequence AAN34363.1 differs from that shown. Reason: Frameshift at position 425.
The sequence AAN34364.1 differs from that shown. Reason: Frameshift at position 425.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761G → D.2 Publications
Corresponds to variant rs2245623 [ dbSNP | Ensembl ].
VAR_031497
Natural varianti143 – 1431V → D.1 Publication
Corresponds to variant rs11586833 [ dbSNP | Ensembl ].
VAR_031498
Natural varianti315 – 3151G → R.1 Publication
Corresponds to variant rs3748569 [ dbSNP | Ensembl ].
VAR_031499
Natural varianti339 – 3391C → R.
Corresponds to variant rs3748567 [ dbSNP | Ensembl ].
VAR_053637

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6969Missing in isoform 3, isoform 4 and isoform 5. VSP_024340Add
BLAST
Alternative sequencei1 – 3030Missing in isoform 2. VSP_024341Add
BLAST
Alternative sequencei31 – 6333AVFVR…FRYPS → MNFTFATQKSLTLLPRLECN GAISAHCNLHLPG in isoform 2. VSP_024342Add
BLAST
Alternative sequencei175 – 1751G → GVRVWGGMESGVGGGQGQPL SQERGGGGGVLPLTPPPQ in isoform 3. VSP_024343
Alternative sequencei372 – 44170Missing in isoform 5. VSP_037136Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF193807 mRNA. Translation: AAG01086.1. Frameshift.
AF219980
, AF219977, AF219978, AF219979 Genomic DNA. Translation: AAL05978.1. Frameshift.
AY139092 mRNA. Translation: AAN34363.1. Frameshift.
AY139093 mRNA. Translation: AAN34364.1. Frameshift.
AK054780 mRNA. Translation: BAG51423.1.
AK290840 mRNA. Translation: BAF83529.1.
AL589685, AL139130 Genomic DNA. Translation: CAI14175.1.
AL589685, AL139130 Genomic DNA. Translation: CAI14176.1.
AL589685, AL139130 Genomic DNA. Translation: CAI14177.1.
AL139130, AL589685 Genomic DNA. Translation: CAI12178.1.
AL139130, AL589685 Genomic DNA. Translation: CAI12179.1.
AL139130, AL589685 Genomic DNA. Translation: CAI12180.1.
CH471121 Genomic DNA. Translation: EAW52961.1.
BC065218 mRNA. Translation: AAH65218.1.
RefSeqiNP_001243324.1. NM_001256395.1.
NP_001243325.1. NM_001256396.1.
NP_065140.3. NM_020407.4.
UniGeneiHs.131835.

Genome annotation databases

EnsembliENST00000255013; ENSP00000255013; ENSG00000132677. [Q9H310-4]
ENST00000368249; ENSP00000357232; ENSG00000132677. [Q9H310-1]
ENST00000400992; ENSP00000383777; ENSG00000132677. [Q9H310-3]
GeneIDi57127.
KEGGihsa:57127.
UCSCiuc009wrz.4. human. [Q9H310-3]
uc010pho.3. human. [Q9H310-1]
uc031pqo.1. human. [Q9H310-2]

Polymorphism databases

DMDMi209572666.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF193807 mRNA. Translation: AAG01086.1 . Frameshift.
AF219980
, AF219977 , AF219978 , AF219979 Genomic DNA. Translation: AAL05978.1 . Frameshift.
AY139092 mRNA. Translation: AAN34363.1 . Frameshift.
AY139093 mRNA. Translation: AAN34364.1 . Frameshift.
AK054780 mRNA. Translation: BAG51423.1 .
AK290840 mRNA. Translation: BAF83529.1 .
AL589685 , AL139130 Genomic DNA. Translation: CAI14175.1 .
AL589685 , AL139130 Genomic DNA. Translation: CAI14176.1 .
AL589685 , AL139130 Genomic DNA. Translation: CAI14177.1 .
AL139130 , AL589685 Genomic DNA. Translation: CAI12178.1 .
AL139130 , AL589685 Genomic DNA. Translation: CAI12179.1 .
AL139130 , AL589685 Genomic DNA. Translation: CAI12180.1 .
CH471121 Genomic DNA. Translation: EAW52961.1 .
BC065218 mRNA. Translation: AAH65218.1 .
RefSeqi NP_001243324.1. NM_001256395.1.
NP_001243325.1. NM_001256396.1.
NP_065140.3. NM_020407.4.
UniGenei Hs.131835.

3D structure databases

ProteinModelPortali Q9H310.
SMRi Q9H310. Positions 12-423.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121390. 1 interaction.
IntActi Q9H310. 1 interaction.
STRINGi 9606.ENSP00000255013.

Protein family/group databases

TCDBi 1.A.11.4.2. the ammonia transporter channel (amt) family.

Polymorphism databases

DMDMi 209572666.

Proteomic databases

PaxDbi Q9H310.
PRIDEi Q9H310.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000255013 ; ENSP00000255013 ; ENSG00000132677 . [Q9H310-4 ]
ENST00000368249 ; ENSP00000357232 ; ENSG00000132677 . [Q9H310-1 ]
ENST00000400992 ; ENSP00000383777 ; ENSG00000132677 . [Q9H310-3 ]
GeneIDi 57127.
KEGGi hsa:57127.
UCSCi uc009wrz.4. human. [Q9H310-3 ]
uc010pho.3. human. [Q9H310-1 ]
uc031pqo.1. human. [Q9H310-2 ]

Organism-specific databases

CTDi 57127.
GeneCardsi GC01P156339.
HGNCi HGNC:14572. RHBG.
HPAi HPA048489.
MIMi 607079. gene.
neXtProti NX_Q9H310.
PharmGKBi PA34385.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG276393.
HOVERGENi HBG004374.
KOi K06580.
PhylomeDBi Q9H310.
TreeFami TF314450.

Enzyme and pathway databases

Reactomei REACT_20508. Rhesus glycoproteins mediate ammonium transport.

Miscellaneous databases

GeneWikii RHBG.
GenomeRNAii 57127.
NextBioi 63029.
PROi Q9H310.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H310.
Bgeei Q9H310.
Genevestigatori Q9H310.

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

« Hide 'large scale' publications
  1. "Rh type B glycoprotein is a new member of the Rh superfamily and a putative ammonia transporter in mammals."
    Liu Z., Peng J., Mo R., Hui C.-C., Huang C.-H.
    J. Biol. Chem. 276:1424-1433(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION.
    Tissue: Liver.
  2. "Characterization of alternatively spliced Rh type B glycoprotein (RhBG) isoforms in human tissues resulting from exonic inclusion of Alu repeat like sequences."
    Liu Z., Chen Y., Huang C.-H.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4).
    Tissue: Liver.
  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 5), VARIANT ASP-76.
    Tissue: Cerebellum and Liver.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-76.
  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 3), VARIANTS ASP-143 AND ARG-315.
    Tissue: Ovary.
  7. "Electroneutral ammonium transport by basolateral rhesus B glycoprotein."
    Ludewig U.
    J. Physiol. (Lond.) 559:751-759(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Human Rhesus B and Rhesus C glycoproteins: properties of facilitated ammonium transport in recombinant kidney cells."
    Zidi-Yahiaoui N., Mouro-Chanteloup I., D'Ambrosio A.-M., Lopez C., Gane P., Le van Kim C., Cartron J.-P., Colin Y., Ripoche P.
    Biochem. J. 391:33-40(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "The ammonium transporter RhBG: requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells."
    Lopez C., Metral S., Eladari D., Drevensek S., Gane P., Chambrey R., Bennett V., Cartron J.-P., Le Van Kim C., Colin Y.
    J. Biol. Chem. 280:8221-8228(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-419; LEU-420 AND ASP-421, INTERACTION WITH ANK2 AND ANK3.

Entry informationi

Entry nameiRHBG_HUMAN
AccessioniPrimary (citable) accession number: Q9H310
Secondary accession number(s): A8K475
, Q5SZW4, Q5SZW6, Q5SZW7, Q6P193, Q6YJI2, Q6YJI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 14, 2008
Last modified: September 3, 2014
This is version 97 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

External Data

Dasty 3

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