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P16066

- ANPRA_HUMAN

UniProt

P16066 - ANPRA_HUMAN

Protein

Atrial natriuretic peptide receptor 1

Gene

NPR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand.1 Publication

    Catalytic activityi

    GTP = 3',5'-cyclic GMP + diphosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei85 – 851ChlorideBy similarity
    Binding sitei117 – 1171Chloride; via amide nitrogenBy similarity
    Binding sitei118 – 1181Chloride; via amide nitrogenBy similarity

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. G-protein coupled peptide receptor activity Source: UniProtKB
    3. GTP binding Source: UniProtKB-KW
    4. guanylate cyclase activity Source: UniProtKB
    5. hormone binding Source: UniProtKB
    6. natriuretic peptide receptor activity Source: UniProtKB
    7. peptide hormone binding Source: Ensembl
    8. protein kinase activity Source: InterPro

    GO - Biological processi

    1. body fluid secretion Source: UniProtKB
    2. cell surface receptor signaling pathway Source: UniProtKB
    3. cGMP biosynthetic process Source: UniProtKB
    4. dopamine metabolic process Source: Ensembl
    5. G-protein coupled receptor signaling pathway Source: GOC
    6. intracellular signal transduction Source: Ensembl
    7. negative regulation of angiogenesis Source: UniProtKB
    8. negative regulation of cell growth Source: UniProtKB
    9. negative regulation of smooth muscle cell proliferation Source: Ensembl
    10. positive regulation of cGMP biosynthetic process Source: Ensembl
    11. positive regulation of renal sodium excretion Source: UniProtKB
    12. positive regulation of urine volume Source: UniProtKB
    13. receptor guanylyl cyclase signaling pathway Source: UniProtKB
    14. regulation of blood pressure Source: UniProtKB
    15. regulation of blood vessel size Source: UniProtKB-KW
    16. regulation of vascular permeability Source: UniProtKB
    17. regulation of vasodilation Source: UniProtKB

    Keywords - Molecular functioni

    Lyase, Receptor, Vasoactive

    Keywords - Biological processi

    cGMP biosynthesis

    Keywords - Ligandi

    Chloride, GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiP16066.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Atrial natriuretic peptide receptor 1 (EC:4.6.1.2)
    Alternative name(s):
    Atrial natriuretic peptide receptor type A
    Short name:
    ANP-A
    Short name:
    ANPR-A
    Short name:
    NPR-A
    Guanylate cyclase A
    Short name:
    GC-A
    Gene namesi
    Name:NPR1
    Synonyms:ANPRA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:7943. NPR1.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: UniProtKB
    2. receptor complex Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31736.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Add
    BLAST
    Chaini33 – 10611029Atrial natriuretic peptide receptor 1PRO_0000012360Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi34 – 341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi92 ↔ 118By similarity
    Disulfide bondi196 ↔ 245By similarity
    Glycosylationi212 – 2121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi386 – 3861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi455 ↔ 464By similarity
    Modified residuei519 – 5191Phosphoserine1 Publication
    Modified residuei529 – 5291Phosphoserine1 Publication
    Modified residuei532 – 5321Phosphothreonine1 Publication
    Modified residuei534 – 5341Phosphoserine1 Publication
    Modified residuei538 – 5381Phosphoserine1 Publication
    Modified residuei542 – 5421PhosphoserineBy similarity
    Modified residuei545 – 5451PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylation of the protein kinase-like domain is required for full activation by ANP.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP16066.
    PaxDbiP16066.
    PRIDEiP16066.

    PTM databases

    PhosphoSiteiP16066.

    Expressioni

    Gene expression databases

    ArrayExpressiP16066.
    BgeeiP16066.
    CleanExiHS_NPR1.
    GenevestigatoriP16066.

    Organism-specific databases

    HPAiHPA031087.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi110941. 6 interactions.
    DIPiDIP-46246N.
    IntActiP16066. 3 interactions.
    MINTiMINT-1192002.
    STRINGi9606.ENSP00000357669.

    Structurei

    3D structure databases

    ProteinModelPortaliP16066.
    SMRiP16066. Positions 34-457, 521-851, 869-1051.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini33 – 473441ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini495 – 1061567CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei474 – 49421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini528 – 805278Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini876 – 1006131Guanylate cyclasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
    Contains 1 guanylate cyclase domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000293307.
    HOVERGENiHBG051862.
    InParanoidiP16066.
    KOiK12323.
    OMAiCFFLVEG.
    OrthoDBiEOG7Z69BJ.
    PhylomeDBiP16066.
    TreeFamiTF106338.

    Family and domain databases

    Gene3Di3.30.70.1230. 1 hit.
    InterProiIPR001054. A/G_cyclase.
    IPR018297. A/G_cyclase_CS.
    IPR001828. ANF_lig-bd_rcpt.
    IPR011009. Kinase-like_dom.
    IPR001170. Ntpep_rcpt.
    IPR028082. Peripla_BP_I.
    IPR000719. Prot_kinase_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF01094. ANF_receptor. 1 hit.
    PF00211. Guanylate_cyc. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR00255. NATPEPTIDER.
    SMARTiSM00044. CYCc. 1 hit.
    [Graphical view]
    SUPFAMiSSF53822. SSF53822. 1 hit.
    SSF55073. SSF55073. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00458. ANF_RECEPTORS. 1 hit.
    PS00452. GUANYLATE_CYCLASE_1. 1 hit.
    PS50125. GUANYLATE_CYCLASE_2. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P16066-1 [UniParc]FASTAAdd to Basket

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    MPGPRRPAGS RLRLLLLLLL PPLLLLLRGS HAGNLTVAVV LPLANTSYPW     50
    SWARVGPAVE LALAQVKARP DLLPGWTVRT VLGSSENALG VCSDTAAPLA 100
    AVDLKWEHNP AVFLGPGCVY AAAPVGRFTA HWRVPLLTAG APALGFGVKD 150
    EYALTTRAGP SYAKLGDFVA ALHRRLGWER QALMLYAYRP GDEEHCFFLV 200
    EGLFMRVRDR LNITVDHLEF AEDDLSHYTR LLRTMPRKGR VIYICSSPDA 250
    FRTLMLLALE AGLCGEDYVF FHLDIFGQSL QGGQGPAPRR PWERGDGQDV 300
    SARQAFQAAK IITYKDPDNP EYLEFLKQLK HLAYEQFNFT MEDGLVNTIP 350
    ASFHDGLLLY IQAVTETLAH GGTVTDGENI TQRMWNRSFQ GVTGYLKIDS 400
    SGDRETDFSL WDMDPENGAF RVVLNYNGTS QELVAVSGRK LNWPLGYPPP 450
    DIPKCGFDNE DPACNQDHLS TLEVLALVGS LSLLGILIVS FFIYRKMQLE 500
    KELASELWRV RWEDVEPSSL ERHLRSAGSR LTLSGRGSNY GSLLTTEGQF 550
    QVFAKTAYYK GNLVAVKRVN RKRIELTRKV LFELKHMRDV QNEHLTRFVG 600
    ACTDPPNICI LTEYCPRGSL QDILENESIT LDWMFRYSLT NDIVKGMLFL 650
    HNGAICSHGN LKSSNCVVDG RFVLKITDYG LESFRDLDPE QGHTVYAKKL 700
    WTAPELLRMA SPPVRGSQAG DVYSFGIILQ EIALRSGVFH VEGLDLSPKE 750
    IIERVTRGEQ PPFRPSLALQ SHLEELGLLM QRCWAEDPQE RPPFQQIRLT 800
    LRKFNRENSS NILDNLLSRM EQYANNLEEL VEERTQAYLE EKRKAEALLY 850
    QILPHSVAEQ LKRGETVQAE AFDSVTIYFS DIVGFTALSA ESTPMQVVTL 900
    LNDLYTCFDA VIDNFDVYKV ETIGDAYMVV SGLPVRNGRL HACEVARMAL 950
    ALLDAVRSFR IRHRPQEQLR LRIGIHTGPV CAGVVGLKMP RYCLFGDTVN 1000
    TASRMESNGE ALKIHLSSET KAVLEEFGGF ELELRGDVEM KGKGKVRTYW 1050
    LLGERGSSTR G 1061
    Length:1,061
    Mass (Da):118,919
    Last modified:April 1, 1990 - v1
    Checksum:iE6B5BD0FCA32F70D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti344 – 3441G → V in AAH63304. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti182 – 1821A → V.1 Publication
    Corresponds to variant rs56019647 [ dbSNP | Ensembl ].
    VAR_042214
    Natural varianti270 – 2701F → C in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication
    VAR_042215
    Natural varianti755 – 7551V → M.1 Publication
    VAR_042216
    Natural varianti939 – 9391R → Q.1 Publication
    Corresponds to variant rs35240348 [ dbSNP | Ensembl ].
    VAR_042217
    Natural varianti967 – 9671E → K.1 Publication
    Corresponds to variant rs35479618 [ dbSNP | Ensembl ].
    VAR_042218

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15357 mRNA. Translation: CAA33417.1.
    AB010491 Genomic DNA. Translation: BAA31199.1.
    AF190631 Genomic DNA. Translation: AAF01340.1.
    EU326310 Genomic DNA. Translation: ACA05918.1.
    AL713889 Genomic DNA. Translation: CAI13613.1.
    CH471121 Genomic DNA. Translation: EAW53284.1.
    BC063304 mRNA. Translation: AAH63304.1.
    S72628 mRNA. Translation: AAD14112.1.
    CCDSiCCDS1051.1.
    PIRiS04459. OYHUAR.
    RefSeqiNP_000897.3. NM_000906.3.
    UniGeneiHs.490330.

    Genome annotation databases

    EnsembliENST00000368680; ENSP00000357669; ENSG00000169418.
    GeneIDi4881.
    KEGGihsa:4881.
    UCSCiuc001fcs.4. human.

    Polymorphism databases

    DMDMi113912.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15357 mRNA. Translation: CAA33417.1 .
    AB010491 Genomic DNA. Translation: BAA31199.1 .
    AF190631 Genomic DNA. Translation: AAF01340.1 .
    EU326310 Genomic DNA. Translation: ACA05918.1 .
    AL713889 Genomic DNA. Translation: CAI13613.1 .
    CH471121 Genomic DNA. Translation: EAW53284.1 .
    BC063304 mRNA. Translation: AAH63304.1 .
    S72628 mRNA. Translation: AAD14112.1 .
    CCDSi CCDS1051.1.
    PIRi S04459. OYHUAR.
    RefSeqi NP_000897.3. NM_000906.3.
    UniGenei Hs.490330.

    3D structure databases

    ProteinModelPortali P16066.
    SMRi P16066. Positions 34-457, 521-851, 869-1051.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110941. 6 interactions.
    DIPi DIP-46246N.
    IntActi P16066. 3 interactions.
    MINTi MINT-1192002.
    STRINGi 9606.ENSP00000357669.

    Chemistry

    BindingDBi P16066.
    ChEMBLi CHEMBL1988.
    DrugBanki DB01613. Erythrityl Tetranitrate.
    DB00883. Isosorbide Dinitrate.
    DB01020. Isosorbide Mononitrate.
    DB04899. Nesiritide.
    DB00435. Nitric Oxide.
    DB00727. Nitroglycerin.
    DB00325. Nitroprusside.
    GuidetoPHARMACOLOGYi 1747.

    PTM databases

    PhosphoSitei P16066.

    Polymorphism databases

    DMDMi 113912.

    Proteomic databases

    MaxQBi P16066.
    PaxDbi P16066.
    PRIDEi P16066.

    Protocols and materials databases

    DNASUi 4881.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368680 ; ENSP00000357669 ; ENSG00000169418 .
    GeneIDi 4881.
    KEGGi hsa:4881.
    UCSCi uc001fcs.4. human.

    Organism-specific databases

    CTDi 4881.
    GeneCardsi GC01P153651.
    HGNCi HGNC:7943. NPR1.
    HPAi HPA031087.
    MIMi 108960. gene.
    neXtProti NX_P16066.
    PharmGKBi PA31736.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000293307.
    HOVERGENi HBG051862.
    InParanoidi P16066.
    KOi K12323.
    OMAi CFFLVEG.
    OrthoDBi EOG7Z69BJ.
    PhylomeDBi P16066.
    TreeFami TF106338.

    Enzyme and pathway databases

    SignaLinki P16066.

    Miscellaneous databases

    GeneWikii NPR1.
    GenomeRNAii 4881.
    NextBioi 18788.
    PROi P16066.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16066.
    Bgeei P16066.
    CleanExi HS_NPR1.
    Genevestigatori P16066.

    Family and domain databases

    Gene3Di 3.30.70.1230. 1 hit.
    InterProi IPR001054. A/G_cyclase.
    IPR018297. A/G_cyclase_CS.
    IPR001828. ANF_lig-bd_rcpt.
    IPR011009. Kinase-like_dom.
    IPR001170. Ntpep_rcpt.
    IPR028082. Peripla_BP_I.
    IPR000719. Prot_kinase_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF01094. ANF_receptor. 1 hit.
    PF00211. Guanylate_cyc. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR00255. NATPEPTIDER.
    SMARTi SM00044. CYCc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53822. SSF53822. 1 hit.
    SSF55073. SSF55073. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00458. ANF_RECEPTORS. 1 hit.
    PS00452. GUANYLATE_CYCLASE_1. 1 hit.
    PS50125. GUANYLATE_CYCLASE_2. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human atrial natriuretic peptide receptor defines a new paradigm for second messenger signal transduction."
      Lowe D.G., Chang M.S., Hellmiss R., Chen E., Singh S., Garbers D.L., Goeddel D.V.
      EMBO J. 8:1377-1384(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Blood.
    3. "Identification of functional polymorphisms in noncoding regions of the human natriuretic peptide receptor A gene."
      Maeda N., Knowles J.W.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Placenta.
    8. "Expression of mRNA for atrial natriuretic peptide receptor guanylate cyclase (ANPRA) in human retina."
      Pardhasaradhi K., Kutty R.K., Gentleman S., Krishna G.
      Cell. Mol. Neurobiol. 14:1-7(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 634-1048.
      Tissue: Retina.
    9. "Extracellular domain-IgG fusion proteins for three human natriuretic peptide receptors. Hormone pharmacology and application to solid phase screening of synthetic peptide antisera."
      Bennett B.D., Bennett G.L., Vitangcol R.V., Jewett J.R., Burnier J., Henzel W., Lowe D.G.
      J. Biol. Chem. 266:23060-23067(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIGAND-BINDING.
    10. "Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP)."
      Koller K.J., Lowe D.G., Bennett G.L., Minamino N., Kangawa K., Matsuo H., Goeddel D.V.
      Science 252:120-123(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Mass spectrometric identification of phosphorylation sites in guanylyl cyclase A and B."
      Yoder A.R., Stone M.D., Griffin T.J., Potter L.R.
      Biochemistry 49:10137-10145(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-519; SER-529; THR-532; SER-534 AND SER-538.
    12. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-182; CYS-270; MET-755; GLN-939 AND LYS-967.

    Entry informationi

    Entry nameiANPRA_HUMAN
    AccessioniPrimary (citable) accession number: P16066
    Secondary accession number(s): B0ZBF0, Q5SR08, Q6P4Q3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 163 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

    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