Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Atrial natriuretic peptide receptor 1

Gene

NPR1

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

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

  • ATP binding Source: InterPro
  • G-protein coupled peptide receptor activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • guanylate cyclase activity Source: UniProtKB
  • hormone binding Source: UniProtKB
  • natriuretic peptide receptor activity Source: UniProtKB
  • peptide hormone binding Source: Ensembl
  • protein kinase activity Source: InterPro

GO - Biological processi

  • body fluid secretion Source: UniProtKB
  • cell surface receptor signaling pathway Source: UniProtKB
  • cGMP biosynthetic process Source: UniProtKB
  • dopamine metabolic process Source: Ensembl
  • G-protein coupled receptor signaling pathway Source: GOC
  • intracellular signal transduction Source: InterPro
  • negative regulation of angiogenesis Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of smooth muscle cell proliferation Source: Ensembl
  • positive regulation of cGMP biosynthetic process Source: Ensembl
  • positive regulation of renal sodium excretion Source: UniProtKB
  • positive regulation of urine volume Source: UniProtKB
  • receptor guanylyl cyclase signaling pathway Source: UniProtKB
  • regulation of blood pressure Source: UniProtKB
  • regulation of blood vessel size Source: UniProtKB-KW
  • regulation of vascular permeability Source: UniProtKB
  • regulation of vasodilation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Receptor, Vasoactive

Keywords - Biological processi

cGMP biosynthesis

Keywords - Ligandi

Chloride, GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.6.1.2. 2681.
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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:7943. NPR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 473441ExtracellularSequence AnalysisAdd
BLAST
Transmembranei474 – 49421HelicalSequence AnalysisAdd
BLAST
Topological domaini495 – 1061567CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31736.

Chemistry

DrugBankiDB01612. Amyl Nitrite.
DB01613. Erythrityl Tetranitrate.
DB00883. Isosorbide Dinitrate.
DB04899. Nesiritide.
DB00727. Nitroglycerin.
DB00325. Nitroprusside.

Polymorphism and mutation databases

BioMutaiNPR1.
DMDMi113912.

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

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.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000118959.
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.
IPR029787. Nucleotide_cyclase.
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

« Hide

        10         20         30         40         50
MPGPRRPAGS RLRLLLLLLL PPLLLLLRGS HAGNLTVAVV LPLANTSYPW
60 70 80 90 100
SWARVGPAVE LALAQVKARP DLLPGWTVRT VLGSSENALG VCSDTAAPLA
110 120 130 140 150
AVDLKWEHNP AVFLGPGCVY AAAPVGRFTA HWRVPLLTAG APALGFGVKD
160 170 180 190 200
EYALTTRAGP SYAKLGDFVA ALHRRLGWER QALMLYAYRP GDEEHCFFLV
210 220 230 240 250
EGLFMRVRDR LNITVDHLEF AEDDLSHYTR LLRTMPRKGR VIYICSSPDA
260 270 280 290 300
FRTLMLLALE AGLCGEDYVF FHLDIFGQSL QGGQGPAPRR PWERGDGQDV
310 320 330 340 350
SARQAFQAAK IITYKDPDNP EYLEFLKQLK HLAYEQFNFT MEDGLVNTIP
360 370 380 390 400
ASFHDGLLLY IQAVTETLAH GGTVTDGENI TQRMWNRSFQ GVTGYLKIDS
410 420 430 440 450
SGDRETDFSL WDMDPENGAF RVVLNYNGTS QELVAVSGRK LNWPLGYPPP
460 470 480 490 500
DIPKCGFDNE DPACNQDHLS TLEVLALVGS LSLLGILIVS FFIYRKMQLE
510 520 530 540 550
KELASELWRV RWEDVEPSSL ERHLRSAGSR LTLSGRGSNY GSLLTTEGQF
560 570 580 590 600
QVFAKTAYYK GNLVAVKRVN RKRIELTRKV LFELKHMRDV QNEHLTRFVG
610 620 630 640 650
ACTDPPNICI LTEYCPRGSL QDILENESIT LDWMFRYSLT NDIVKGMLFL
660 670 680 690 700
HNGAICSHGN LKSSNCVVDG RFVLKITDYG LESFRDLDPE QGHTVYAKKL
710 720 730 740 750
WTAPELLRMA SPPVRGSQAG DVYSFGIILQ EIALRSGVFH VEGLDLSPKE
760 770 780 790 800
IIERVTRGEQ PPFRPSLALQ SHLEELGLLM QRCWAEDPQE RPPFQQIRLT
810 820 830 840 850
LRKFNRENSS NILDNLLSRM EQYANNLEEL VEERTQAYLE EKRKAEALLY
860 870 880 890 900
QILPHSVAEQ LKRGETVQAE AFDSVTIYFS DIVGFTALSA ESTPMQVVTL
910 920 930 940 950
LNDLYTCFDA VIDNFDVYKV ETIGDAYMVV SGLPVRNGRL HACEVARMAL
960 970 980 990 1000
ALLDAVRSFR IRHRPQEQLR LRIGIHTGPV CAGVVGLKMP RYCLFGDTVN
1010 1020 1030 1040 1050
TASRMESNGE ALKIHLSSET KAVLEEFGGF ELELRGDVEM KGKGKVRTYW
1060
LLGERGSSTR G
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP16066.
SMRiP16066. Positions 34-457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP16066.
ChEMBLiCHEMBL2111337.
DrugBankiDB01612. Amyl Nitrite.
DB01613. Erythrityl Tetranitrate.
DB00883. Isosorbide Dinitrate.
DB04899. Nesiritide.
DB00727. Nitroglycerin.
DB00325. Nitroprusside.
GuidetoPHARMACOLOGYi1747.

PTM databases

PhosphoSiteiP16066.

Polymorphism and mutation databases

BioMutaiNPR1.
DMDMi113912.

Proteomic databases

MaxQBiP16066.
PaxDbiP16066.
PRIDEiP16066.

Protocols and materials databases

DNASUi4881.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4881.
GeneCardsiGC01P153651.
HGNCiHGNC:7943. NPR1.
HPAiHPA031087.
MIMi108960. gene.
neXtProtiNX_P16066.
PharmGKBiPA31736.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000293307.
HOVERGENiHBG051862.
InParanoidiP16066.
KOiK12323.
OMAiCFFLVEG.
OrthoDBiEOG7Z69BJ.
PhylomeDBiP16066.
TreeFamiTF106338.

Enzyme and pathway databases

BRENDAi4.6.1.2. 2681.
SignaLinkiP16066.

Miscellaneous databases

GeneWikiiNPR1.
GenomeRNAii4881.
NextBioi18788.
PROiP16066.
SOURCEiSearch...

Gene expression databases

BgeeiP16066.
CleanExiHS_NPR1.
GenevestigatoriP16066.

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.
IPR029787. Nucleotide_cyclase.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: May 27, 2015
This is version 170 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  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.