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Protein

Ammonium transporter Rh type C

Gene

RHCG

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

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
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.11.4.1. 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 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:18140. RHCG.

Subcellular locationi

  1. Apical cell membrane 2 Publications; Multi-pass membrane protein 2 Publications

  2. Note: Also detected at the basolateral membrane and in subapical vesicles.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Transmembranei10 – 3021HelicalSequence AnalysisAdd
BLAST
Topological domaini31 – 6030ExtracellularSequence AnalysisAdd
BLAST
Transmembranei61 – 8121HelicalSequence AnalysisAdd
BLAST
Topological domaini82 – 854CytoplasmicSequence Analysis
Transmembranei86 – 10621HelicalSequence AnalysisAdd
BLAST
Topological domaini107 – 12317ExtracellularSequence AnalysisAdd
BLAST
Transmembranei124 – 14421HelicalSequence AnalysisAdd
BLAST
Topological domaini145 – 1484CytoplasmicSequence Analysis
Transmembranei149 – 16921HelicalSequence AnalysisAdd
BLAST
Topological domaini170 – 1778ExtracellularSequence Analysis
Transmembranei178 – 20023HelicalSequence AnalysisAdd
BLAST
Topological domaini201 – 21818CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei219 – 23921HelicalSequence AnalysisAdd
BLAST
Topological domaini240 – 25011ExtracellularSequence AnalysisAdd
BLAST
Transmembranei251 – 27121HelicalSequence AnalysisAdd
BLAST
Topological domaini272 – 28110CytoplasmicSequence Analysis
Transmembranei282 – 30221HelicalSequence AnalysisAdd
BLAST
Topological domaini303 – 3031ExtracellularSequence Analysis
Transmembranei304 – 32421HelicalSequence AnalysisAdd
BLAST
Topological domaini325 – 34521CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei346 – 36621HelicalSequence AnalysisAdd
BLAST
Topological domaini367 – 39428ExtracellularSequence AnalysisAdd
BLAST
Transmembranei395 – 41521HelicalSequence AnalysisAdd
BLAST
Topological domaini416 – 47964CytoplasmicSequence AnalysisAdd
BLAST

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: UniProtKB
  5. integral component of plasma membrane Source: UniProtKB
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiRHCG.
DMDMi74734928.

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...)1 Publication

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

BgeeiQ9UBD6.
CleanExiHS_RHCG.
ExpressionAtlasiQ9UBD6. baseline and differential.
GenevestigatoriQ9UBD6.

Organism-specific databases

HPAiHPA041874.
HPA043317.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi119552. 1 interaction.
DIPiDIP-59334N.
STRINGi9606.ENSP00000268122.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9UBD6.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG276393.
GeneTreeiENSGT00390000005787.
HOGENOMiHOG000007656.
HOVERGENiHBG004374.
InParanoidiQ9UBD6.
KOiK06580.
OMAiSQHRAAI.
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

        10         20         30         40         50
MAWNTNLRWR LPLTCLLLQV IMVILFGVFV RYDFEADAHW WSERTHKNLS
60 70 80 90 100
DMENEFYYRY PSFQDVHVMV FVGFGFLMTF LQRYGFSAVG FNFLLAAFGI
110 120 130 140 150
QWALLMQGWF HFLQDRYIVV GVENLINADF CVASVCVAFG AVLGKVSPIQ
160 170 180 190 200
LLIMTFFQVT LFAVNEFILL NLLKVKDAGG SMTIHTFGAY FGLTVTRILY
210 220 230 240 250
RRNLEQSKER QNSVYQSDLF AMIGTLFLWM YWPSFNSAIS YHGDSQHRAA
260 270 280 290 300
INTYCSLAAC VLTSVAISSA LHKKGKLDMV HIQNATLAGG VAVGTAAEMM
310 320 330 340 350
LMPYGALIIG FVCGIISTLG FVYLTPFLES RLHIQDTCGI NNLHGIPGII
360 370 380 390 400
GGIVGAVTAA SASLEVYGKE GLVHSFDFQG FNGDWTARTQ GKFQIYGLLV
410 420 430 440 450
TLAMALMGGI IVGLILRLPF WGQPSDENCF EDAVYWEMPE GNSTVYIPED
460 470
PTFKPSGPSV PSVPMVSPLP MASSVPLVP
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 (Ref. 6) Curated
Sequence conflicti442 – 4421N → D in AAP81044 (Ref. 6) Curated

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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiRHCG.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi119552. 1 interaction.
DIPiDIP-59334N.
STRINGi9606.ENSP00000268122.

Protein family/group databases

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

PTM databases

PhosphoSiteiQ9UBD6.

Polymorphism and mutation databases

BioMutaiRHCG.
DMDMi74734928.

Proteomic databases

PaxDbiQ9UBD6.
PRIDEiQ9UBD6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51458.
GeneCardsiGC15M090014.
HGNCiHGNC:18140. RHCG.
HPAiHPA041874.
HPA043317.
MIMi605381. gene.
neXtProtiNX_Q9UBD6.
PharmGKBiPA134876043.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG276393.
GeneTreeiENSGT00390000005787.
HOGENOMiHOG000007656.
HOVERGENiHBG004374.
InParanoidiQ9UBD6.
KOiK06580.
OMAiSQHRAAI.
PhylomeDBiQ9UBD6.
TreeFamiTF314450.

Enzyme and pathway databases

ReactomeiREACT_20508. Rhesus glycoproteins mediate ammonium transport.

Miscellaneous databases

ChiTaRSiRHCG. human.
EvolutionaryTraceiQ9UBD6.
GeneWikiiRHCG.
GenomeRNAii51458.
NextBioi55075.
PROiQ9UBD6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UBD6.
CleanExiHS_RHCG.
ExpressionAtlasiQ9UBD6. baseline and differential.
GenevestigatoriQ9UBD6.

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. "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: April 29, 2015
This is version 114 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

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.