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O75787

- RENR_HUMAN

UniProt

O75787 - RENR_HUMAN

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Protein

Renin receptor

Gene

ATP6AP2

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

Functioni

Functions as a renin and prorenin cellular receptor. May mediate renin-dependent cellular responses by activating ERK1 and ERK2. By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, it may also play a role in the renin-angiotensin system (RAS).1 Publication

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: Reactome
  2. receptor activity Source: InterPro

GO - Biological processi

  1. angiotensin maturation Source: HGNC
  2. cell death Source: UniProtKB-KW
  3. cellular protein metabolic process Source: Reactome
  4. eye pigmentation Source: UniProt
  5. head morphogenesis Source: UniProt
  6. positive regulation of transforming growth factor beta1 production Source: HGNC
  7. positive regulation of Wnt signaling pathway Source: UniProt
  8. proteolysis Source: GOC
  9. regulation of MAPK cascade Source: HGNC
  10. rostrocaudal neural tube patterning Source: UniProt
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER66-34369.
ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.

Names & Taxonomyi

Protein namesi
Recommended name:
Renin receptor
Alternative name(s):
ATPase H(+)-transporting lysosomal accessory protein 2
ATPase H(+)-transporting lysosomal-interacting protein 2
ER-localized type I transmembrane adaptor
Embryonic liver differentiation factor 10
N14F
Renin/prorenin receptor
Vacuolar ATP synthase membrane sector-associated protein M8-9
Short name:
ATP6M8-9
Short name:
V-ATPase M8.9 subunit
Gene namesi
Name:ATP6AP2
Synonyms:ATP6IP2, CAPER, ELDF10
ORF Names:HT028, MSTP009, PSEC0072
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:18305. ATP6AP2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 302286ExtracellularSequence AnalysisAdd
BLAST
Transmembranei303 – 32321HelicalSequence AnalysisAdd
BLAST
Topological domaini324 – 35027CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell body Source: Ensembl
  2. external side of plasma membrane Source: HGNC
  3. extracellular vesicular exosome Source: UniProtKB
  4. integral component of membrane Source: UniProtKB-KW
  5. neuron projection Source: Ensembl
  6. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked, with epilepsy (MRXE) [MIM:300423]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXE patients manifest mild to moderate mental retardation associated with epilepsy, delays in motor milestones and speech acquisition in infancy.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Parkinsonism with spasticity, X-linked (XPDS) [MIM:300911]: A syndrome characterized by parkinsonian features, such as cogwheel rigidity, resting tremor and bradykinesia, and variably penetrant spasticity.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Epilepsy, Mental retardation, Neurodegeneration, Parkinsonism

Organism-specific databases

MIMi300423. phenotype.
300911. phenotype.
Orphaneti93952. X-linked intellectual disability, Hedera type.
363654. X-linked parkinsonism-spasticity syndrome.
PharmGKBiPA25148.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 350334Renin receptorPRO_0000022203Add
BLAST

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75787.
PaxDbiO75787.
PRIDEiO75787.

PTM databases

PhosphoSiteiO75787.

Expressioni

Tissue specificityi

Expressed in brain, heart, placenta, liver, kidney and pancreas. Barely detectable in lung and skeletal muscles. In the kidney cortex it is restricted to the mesangium of glomeruli. In the coronary and kidney artery it is expressed in the subendothelium, associated to smooth muscles where it colocalizes with REN. Expressed in vascular structures and by syncytiotrophoblast cells in the mature fetal placenta.2 Publications

Gene expression databases

BgeeiO75787.
ExpressionAtlasiO75787. baseline and differential.
GenevestigatoriO75787.

Organism-specific databases

HPAiHPA003156.

Interactioni

Subunit structurei

Interacts with renin and the vacuolar proton-ATPase.1 Publication

Protein-protein interaction databases

BioGridi115461. 23 interactions.
IntActiO75787. 3 interactions.

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni334 – 3374Combined sources
Helixi338 – 3403Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LBSX-ray2.15A/B333-350[»]
3LC8X-ray2.00A/B333-350[»]
ProteinModelPortaliO75787.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG296465.
GeneTreeiENSGT00390000008856.
HOVERGENiHBG056579.
OMAiFRDGNWP.
OrthoDBiEOG7R56VH.
PhylomeDBiO75787.
TreeFamiTF106137.

Family and domain databases

InterProiIPR012493. Renin_rcpt.
[Graphical view]
PANTHERiPTHR13351. PTHR13351. 1 hit.
PfamiPF07850. Renin_r. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75787-1) [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
MAVFVVLLAL VAGVLGNEFS ILKSPGSVVF RNGNWPIPGE RIPDVAALSM
60 70 80 90 100
GFSVKEDLSW PGLAVGNLFH RPRATVMVMV KGVNKLALPP GSVISYPLEN
110 120 130 140 150
AVPFSLDSVA NSIHSLFSEE TPVVLQLAPS EERVYMVGKA NSVFEDLSVT
160 170 180 190 200
LRQLRNRLFQ ENSVLSSLPL NSLSRNNEVD LLFLSELQVL HDISSLLSRH
210 220 230 240 250
KHLAKDHSPD LYSLELAGLD EIGKRYGEDS EQFRDASKIL VDALQKFADD
260 270 280 290 300
MYSLYGGNAV VELVTVKSFD TSLIRKTRTI LEAKQAKNPA SPYNLAYKYN
310 320 330 340 350
FEYSVVFNMV LWIMIALALA VIITSYNIWN MDPGYDSIIY RMTNQKIRMD
Length:350
Mass (Da):39,008
Last modified:May 10, 2005 - v2
Checksum:i84084A4ACE9C5DE8
GO
Isoform 2 (identifier: O75787-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     101-132: Missing.

Note: No experimental confirmation available

Show »
Length:318
Mass (Da):35,612
Checksum:iE924E3EE0F2098D7
GO

Sequence cautioni

The sequence AAH10395.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAQ13511.1 differs from that shown. Reason: Frameshift at position 155. Translation N-terminally extended.Curated
The sequence CAA76984.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381G → W in AAK83467. 1 PublicationCurated
Sequence conflicti153 – 1542QL → HV in AAK83467. 1 PublicationCurated
Sequence conflicti258 – 2581N → K in BAC11582. (PubMed:16303743)Curated
Sequence conflicti285 – 2851Q → R(PubMed:10931946)Curated
Sequence conflicti285 – 2851Q → R(PubMed:17974005)Curated
Sequence conflicti287 – 2871Missing in AAH10395. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti90 – 901P → A.
Corresponds to variant rs9014 [ dbSNP | Ensembl ].
VAR_051313
Natural varianti290 – 2901A → P.
Corresponds to variant rs35798522 [ dbSNP | Ensembl ].
VAR_051314

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei101 – 13232Missing in isoform 2. 1 PublicationVSP_056910Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF291814 mRNA. Translation: AAM47531.1.
AY038990 mRNA. Translation: AAK83467.1.
AF109363 mRNA. Translation: AAQ13511.1. Frameshift.
AF248966 mRNA. Translation: AAG44564.1.
AK315948 mRNA. Translation: BAH14319.1.
AK075382 mRNA. Translation: BAC11582.1.
AC092473 Genomic DNA. No translation available.
BC010395 mRNA. Translation: AAH10395.1. Different initiation.
BC084541 mRNA. Translation: AAH84541.1.
AY429341 mRNA. Translation: AAR06910.1.
AL049929 mRNA. Translation: CAB43210.1.
Y17975 mRNA. Translation: CAA76984.1. Different initiation.
CCDSiCCDS14252.1.
PIRiT08667.
RefSeqiNP_005756.2. NM_005765.2.
UniGeneiHs.495960.

Genome annotation databases

EnsembliENST00000378438; ENSP00000367697; ENSG00000182220. [O75787-1]
GeneIDi10159.
KEGGihsa:10159.
UCSCiuc004det.3. human. [O75787-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF291814 mRNA. Translation: AAM47531.1 .
AY038990 mRNA. Translation: AAK83467.1 .
AF109363 mRNA. Translation: AAQ13511.1 . Frameshift.
AF248966 mRNA. Translation: AAG44564.1 .
AK315948 mRNA. Translation: BAH14319.1 .
AK075382 mRNA. Translation: BAC11582.1 .
AC092473 Genomic DNA. No translation available.
BC010395 mRNA. Translation: AAH10395.1 . Different initiation.
BC084541 mRNA. Translation: AAH84541.1 .
AY429341 mRNA. Translation: AAR06910.1 .
AL049929 mRNA. Translation: CAB43210.1 .
Y17975 mRNA. Translation: CAA76984.1 . Different initiation.
CCDSi CCDS14252.1.
PIRi T08667.
RefSeqi NP_005756.2. NM_005765.2.
UniGenei Hs.495960.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LBS X-ray 2.15 A/B 333-350 [» ]
3LC8 X-ray 2.00 A/B 333-350 [» ]
ProteinModelPortali O75787.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115461. 23 interactions.
IntActi O75787. 3 interactions.

PTM databases

PhosphoSitei O75787.

Proteomic databases

MaxQBi O75787.
PaxDbi O75787.
PRIDEi O75787.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378438 ; ENSP00000367697 ; ENSG00000182220 . [O75787-1 ]
GeneIDi 10159.
KEGGi hsa:10159.
UCSCi uc004det.3. human. [O75787-1 ]

Organism-specific databases

CTDi 10159.
GeneCardsi GC0XP040440.
HGNCi HGNC:18305. ATP6AP2.
HPAi HPA003156.
MIMi 300423. phenotype.
300556. gene.
300911. phenotype.
neXtProti NX_O75787.
Orphaneti 93952. X-linked intellectual disability, Hedera type.
363654. X-linked parkinsonism-spasticity syndrome.
PharmGKBi PA25148.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG296465.
GeneTreei ENSGT00390000008856.
HOVERGENi HBG056579.
OMAi FRDGNWP.
OrthoDBi EOG7R56VH.
PhylomeDBi O75787.
TreeFami TF106137.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER66-34369.
Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.

Miscellaneous databases

ChiTaRSi ATP6AP2. human.
GeneWikii ATP6AP2.
GenomeRNAii 10159.
NextBioi 38460.
PROi O75787.
SOURCEi Search...

Gene expression databases

Bgeei O75787.
ExpressionAtlasi O75787. baseline and differential.
Genevestigatori O75787.

Family and domain databases

InterProi IPR012493. Renin_rcpt.
[Graphical view ]
PANTHERi PTHR13351. PTHR13351. 1 hit.
Pfami PF07850. Renin_r. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Pivotal role of the renin/prorenin receptor in angiotensin II production and cellular responses to renin."
    Nguyen G., Delarue F., Burckle C., Bouzhir L., Giller T., Sraer J.-D.
    J. Clin. Invest. 109:1417-1427(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH REN, PHOSPHORYLATION, TISSUE SPECIFICITY, FUNCTION.
    Tissue: Mesangial cell.
  2. "Cell cycle-dependent subcellular localization of the protein tyrosine phosphatase PTPCAAX1 and its implication in cell cycle regulation."
    Wang J., Kirby C., Herbst R.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Cervix carcinoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Aorta.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hypothalamus.
  5. "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 2).
    Tissue: Brain cortex.
  6. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Teratocarcinoma.
  7. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 1).
    Tissue: Brain and Prostate.
  9. "The cloning of a novel gene related with erythroid differentiation."
    Zhang S., Yan H., Yang F.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-350 (ISOFORM 1).
    Tissue: Liver.
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-350 (ISOFORM 1).
    Tissue: Brain.
  11. "Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules."
    Ludwig J., Kerscher S., Brandt U., Pfeiffer K., Getlawi F., Apps D.K., Schaegger H.
    J. Biol. Chem. 273:10939-10947(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 188-350 (ISOFORM 1).
  12. "A unique exonic splice enhancer mutation in a family with X-linked mental retardation and epilepsy points to a novel role of the renin receptor."
    Ramser J., Abidi F.E., Burckle C.A., Lenski C., Toriello H., Wen G., Lubs H.A., Engert S., Stevenson R.E., Meindl A., Schwartz C.E., Nguyen G.
    Hum. Mol. Genet. 14:1019-1027(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MRXE, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: INVOLVEMENT IN XPDS.

Entry informationi

Entry nameiRENR_HUMAN
AccessioniPrimary (citable) accession number: O75787
Secondary accession number(s): B7Z9I3
, Q5QTQ7, Q6T7F5, Q8NBP3, Q8NG15, Q96FV6, Q96LB5, Q9H2P8, Q9UG89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 10, 2005
Last modified: November 26, 2014
This is version 132 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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

External Data

Dasty 3