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Q9UBD6

- RHCG_HUMAN

UniProt

Q9UBD6 - RHCG_HUMAN

Protein

Ammonium transporter Rh type C

Gene

RHCG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Functions as an electroneutral and bidirectional ammonium transporter. May regulate transepithelial ammonia secretion.4 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. amine transport Source: UniProtKB
    2. ammonium transmembrane transport Source: GOC
    3. ammonium transport Source: UniProtKB
    4. cellular ion homeostasis Source: UniProtKB
    5. epithelial cell differentiation Source: UniProtKB
    6. homeostatic process Source: UniProtKB
    7. regulation of pH Source: Ensembl
    8. transepithelial ammonium transport Source: UniProtKB
    9. transmembrane transport Source: Reactome

    Keywords - Biological processi

    Ammonia transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_20508. Rhesus glycoproteins mediate ammonium transport.

    Protein family/group databases

    TCDBi1.A.11.4.1. the ammonia transporter channel (amt) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ammonium transporter Rh type C
    Alternative name(s):
    Rh glycoprotein kidney
    Rhesus blood group family type C glycoprotein
    Short name:
    Rh family type C glycoprotein
    Short name:
    Rh type C glycoprotein
    Tumor-related protein DRC2
    Gene namesi
    Name:RHCG
    Synonyms:C15orf6, CDRC2, PDRC2, RHGK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:18140. RHCG.

    Subcellular locationi

    Apical cell membrane 2 Publications; Multi-pass membrane protein 2 Publications
    Note: Also detected at the basolateral membrane and in subapical vesicles.By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. basolateral plasma membrane Source: UniProtKB
    3. cytoplasmic vesicle Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. integral component of plasma membrane Source: UniProtKB
    6. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi74 – 741F → L: Reduction of ammonia transport. 1 Publication
    Mutagenesisi137 – 1371V → I: Reduction of ammonia transport. 1 Publication
    Mutagenesisi177 – 1771D → N: Loss of function. 1 Publication
    Mutagenesisi235 – 2351F → V: Reduction of ammonia transport. 1 Publication

    Organism-specific databases

    PharmGKBiPA134876043.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 479479Ammonium transporter Rh type CPRO_0000283577Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi48 – 481N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    N-glycosylated.2 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9UBD6.
    PRIDEiQ9UBD6.

    PTM databases

    PhosphoSiteiQ9UBD6.

    Expressioni

    Tissue specificityi

    Expressed in brain, testis, placenta, pancreas, esophagus and prostate. Expressed in squamous epithelial tissues (at protein level). According to PubMed:11062476, specifically expressed in kidney.3 Publications

    Developmental stagei

    Specifically expressed in fetal kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ9UBD6.
    BgeeiQ9UBD6.
    CleanExiHS_RHCG.
    GenevestigatoriQ9UBD6.

    Organism-specific databases

    HPAiHPA041874.
    HPA043317.

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-59334N.
    STRINGi9606.ENSP00000268122.

    Structurei

    Secondary structure

    1
    479
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 2920
    Helixi55 – 7117
    Helixi73 – 775
    Helixi78 – 803
    Helixi85 – 10925
    Turni114 – 1163
    Beta strandi117 – 1193
    Helixi122 – 14221
    Helixi148 – 17023
    Turni181 – 1844
    Helixi185 – 19814
    Helixi204 – 2074
    Turni208 – 2103
    Helixi215 – 23521
    Turni236 – 2394
    Helixi243 – 27028
    Helixi279 – 2846
    Helixi285 – 2873
    Helixi288 – 2925
    Turni293 – 2997
    Helixi303 – 33230
    Helixi340 – 3434
    Helixi345 – 36016
    Helixi385 – 41632
    Helixi432 – 4343
    Turni440 – 4423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HD6X-ray2.10A2-479[»]
    ProteinModelPortaliQ9UBD6.
    SMRiQ9UBD6. Positions 2-443.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UBD6.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 99CytoplasmicSequence Analysis
    Topological domaini31 – 6030ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini82 – 854CytoplasmicSequence Analysis
    Topological domaini107 – 12317ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini145 – 1484CytoplasmicSequence Analysis
    Topological domaini170 – 1778ExtracellularSequence Analysis
    Topological domaini201 – 21818CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini240 – 25011ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini272 – 28110CytoplasmicSequence Analysis
    Topological domaini303 – 3031ExtracellularSequence Analysis
    Topological domaini325 – 34521CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini367 – 39428ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini416 – 47964CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei10 – 3021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei61 – 8121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei86 – 10621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei124 – 14421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei149 – 16921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei178 – 20023HelicalSequence AnalysisAdd
    BLAST
    Transmembranei219 – 23921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei251 – 27121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei282 – 30221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei304 – 32421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei346 – 36621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei395 – 41521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG276393.
    HOGENOMiHOG000007656.
    HOVERGENiHBG004374.
    InParanoidiQ9UBD6.
    KOiK06580.
    OMAiENCFEDE.
    PhylomeDBiQ9UBD6.
    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.

    Sequencei

    Sequence statusi: Complete.

    Q9UBD6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAWNTNLRWR LPLTCLLLQV IMVILFGVFV RYDFEADAHW WSERTHKNLS    50
    DMENEFYYRY PSFQDVHVMV FVGFGFLMTF LQRYGFSAVG FNFLLAAFGI 100
    QWALLMQGWF HFLQDRYIVV GVENLINADF CVASVCVAFG AVLGKVSPIQ 150
    LLIMTFFQVT LFAVNEFILL NLLKVKDAGG SMTIHTFGAY FGLTVTRILY 200
    RRNLEQSKER QNSVYQSDLF AMIGTLFLWM YWPSFNSAIS YHGDSQHRAA 250
    INTYCSLAAC VLTSVAISSA LHKKGKLDMV HIQNATLAGG VAVGTAAEMM 300
    LMPYGALIIG FVCGIISTLG FVYLTPFLES RLHIQDTCGI NNLHGIPGII 350
    GGIVGAVTAA SASLEVYGKE GLVHSFDFQG FNGDWTARTQ GKFQIYGLLV 400
    TLAMALMGGI IVGLILRLPF WGQPSDENCF EDAVYWEMPE GNSTVYIPED 450
    PTFKPSGPSV PSVPMVSPLP MASSVPLVP 479
    Length:479
    Mass (Da):53,179
    Last modified:May 1, 2000 - v1
    Checksum:iE5D8024D720D4589
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti242 – 2421H → R in AAP81044. 1 PublicationCurated
    Sequence conflicti442 – 4421N → D in AAP81044. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti202 – 2021R → C.
    Corresponds to variant rs17807723 [ dbSNP | Ensembl ].
    VAR_031496

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF193809 mRNA. Translation: AAF19372.1.
    AF219986
    , AF219981, AF219982, AF219983, AF219984, AF219985 Genomic DNA. Translation: AAG02171.1.
    AF081497 mRNA. Translation: AAD55748.1.
    AF284446 Genomic DNA. Translation: AAG02414.1.
    AY257182 mRNA. Translation: AAP81044.1.
    AK290899 mRNA. Translation: BAF83588.1.
    AK313238 mRNA. Translation: BAG36049.1.
    AC013391 Genomic DNA. No translation available.
    CH471101 Genomic DNA. Translation: EAX02051.1.
    BC030965 mRNA. Translation: AAH30965.1.
    CCDSiCCDS10351.1.
    RefSeqiNP_057405.1. NM_016321.2.
    UniGeneiHs.459284.

    Genome annotation databases

    EnsembliENST00000268122; ENSP00000268122; ENSG00000140519.
    GeneIDi51458.
    KEGGihsa:51458.
    UCSCiuc002bnz.2. human.

    Polymorphism databases

    DMDMi74734928.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF193809 mRNA. Translation: AAF19372.1 .
    AF219986
    , AF219981 , AF219982 , AF219983 , AF219984 , AF219985 Genomic DNA. Translation: AAG02171.1 .
    AF081497 mRNA. Translation: AAD55748.1 .
    AF284446 Genomic DNA. Translation: AAG02414.1 .
    AY257182 mRNA. Translation: AAP81044.1 .
    AK290899 mRNA. Translation: BAF83588.1 .
    AK313238 mRNA. Translation: BAG36049.1 .
    AC013391 Genomic DNA. No translation available.
    CH471101 Genomic DNA. Translation: EAX02051.1 .
    BC030965 mRNA. Translation: AAH30965.1 .
    CCDSi CCDS10351.1.
    RefSeqi NP_057405.1. NM_016321.2.
    UniGenei Hs.459284.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HD6 X-ray 2.10 A 2-479 [» ]
    ProteinModelPortali Q9UBD6.
    SMRi Q9UBD6. Positions 2-443.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59334N.
    STRINGi 9606.ENSP00000268122.

    Chemistry

    GuidetoPHARMACOLOGYi 1200.

    Protein family/group databases

    TCDBi 1.A.11.4.1. the ammonia transporter channel (amt) family.

    PTM databases

    PhosphoSitei Q9UBD6.

    Polymorphism databases

    DMDMi 74734928.

    Proteomic databases

    PaxDbi Q9UBD6.
    PRIDEi Q9UBD6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268122 ; ENSP00000268122 ; ENSG00000140519 .
    GeneIDi 51458.
    KEGGi hsa:51458.
    UCSCi uc002bnz.2. human.

    Organism-specific databases

    CTDi 51458.
    GeneCardsi GC15M090014.
    HGNCi HGNC:18140. RHCG.
    HPAi HPA041874.
    HPA043317.
    MIMi 605381. gene.
    neXtProti NX_Q9UBD6.
    PharmGKBi PA134876043.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG276393.
    HOGENOMi HOG000007656.
    HOVERGENi HBG004374.
    InParanoidi Q9UBD6.
    KOi K06580.
    OMAi ENCFEDE.
    PhylomeDBi Q9UBD6.
    TreeFami TF314450.

    Enzyme and pathway databases

    Reactomei REACT_20508. Rhesus glycoproteins mediate ammonium transport.

    Miscellaneous databases

    ChiTaRSi RHCG. human.
    EvolutionaryTracei Q9UBD6.
    GeneWikii RHCG.
    GenomeRNAii 51458.
    NextBioi 55075.
    PROi Q9UBD6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBD6.
    Bgeei Q9UBD6.
    CleanExi HS_RHCG.
    Genevestigatori Q9UBD6.

    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. "Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh glycoprotein homologues predominantly expressed in kidney and testis."
      Liu Z., Chen Y., Mo R., Hui C.-C., Cheng J.-F., Mohandas N., Huang C.-H.
      J. Biol. Chem. 275:25641-25651(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, GLYCOSYLATION.
      Tissue: Kidney.
    2. "RhCG is downregulated in oesophageal squamous cell carcinomas, but expressed in multiple squamous epithelia."
      Chen B.-S., Xu Z.-X., Xu X., Cai Y., Han Y.-L., Wang J., Xia S.-H., Hu H., Wei F., Wu M., Wang M.-R.
      Eur. J. Cancer 38:1927-1936(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Placenta.
    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].
      Tissue: Esophagus and Tongue.
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Functional characterization of RhCG glycoprotein from human renal proximal cells."
      Nakhoul N.L., Hamm L.L., Abdulnour-Nakhoul S.M., De Jong H.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney epithelium.
    7. "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].
      Tissue: Kidney.
    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, TISSUE SPECIFICITY.
    9. "NH3 is involved in the NH4+ transport induced by the functional expression of the human Rh C glycoprotein."
      Bakouh N., Benjelloun F., Hulin P., Brouillard F., Edelman A., Cherif-Zahar B., Planelles G.
      J. Biol. Chem. 279:15975-15983(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "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.
    11. "Structural involvement in substrate recognition of an essential aspartate residue conserved in Mep/Amt and Rh-type ammonium transporters."
      Marini A.-M., Boeckstaens M., Benjelloun F., Cherif-Zahar B., Andre B.
      Curr. Genet. 49:364-374(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-177.
    12. "Ammonium transport properties of HEK293 cells expressing RhCG mutants: preliminary analysis of structure/function by site-directed mutagenesis."
      Zidi-Yahiaoui N., Ripoche P., Le Van Kim C., Gane P., D'Ambrosio A.-M., Cartron J.-P., Colin Y., Mouro-Chanteloup I.
      Transfus. Clin. Biol. 13:128-131(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PHE-74; VAL-137 AND PHE-235.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-479, SUBUNIT, GLYCOSYLATION AT ASN-48.

    Entry informationi

    Entry nameiRHCG_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBD6
    Secondary accession number(s): A8K4D4, Q6X3Y4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 111 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3