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Protein

Adenylate cyclase type 1

Gene

ADCY1

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

Functioni

Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates responses to increased cellular Ca2+/calmodulin levels (By similarity). May be involved in regulatory processes in the central nervous system. May play a role in memory and learning. Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina (By similarity).By similarity

Catalytic activityi

ATP = 3',5'-cyclic AMP + diphosphate.By similarity

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).By similarity

Enzyme regulationi

Activated by calcium/calmodulin. Activated by forskolin. Activated by the G protein alpha subunit GNAS. Inhibited by the G protein beta and gamma subunit complex. Inhibited by the ATP analogs adenosine, 2'-deoxyadenosine and 2'-deoxy-3'-AMP.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi308 – 3081Magnesium 1; catalyticPROSITE-ProRule annotation
Metal bindingi308 – 3081Magnesium 2; catalyticPROSITE-ProRule annotation
Metal bindingi309 – 3091Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation
Metal bindingi352 – 3521Magnesium 1; catalyticPROSITE-ProRule annotation
Metal bindingi352 – 3521Magnesium 2; catalyticPROSITE-ProRule annotation
Binding sitei396 – 3961ATPBy similarity
Binding sitei920 – 9201ATPBy similarity
Binding sitei1044 – 10441ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi308 – 3136ATPBy similarity
Nucleotide bindingi350 – 3523ATPBy similarity
Nucleotide bindingi997 – 9993ATPBy similarity
Nucleotide bindingi1004 – 10085ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Biological rhythms, cAMP biosynthesis

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.6.1.1. 2681.
ReactomeiR-HSA-163359. Glucagon signaling in metabolic regulation.
R-HSA-163615. PKA activation.
R-HSA-164378. PKA activation in glucagon signalling.
R-HSA-170660. Adenylate cyclase activating pathway.
R-HSA-170670. Adenylate cyclase inhibitory pathway.
R-HSA-418555. G alpha (s) signalling events.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-418597. G alpha (z) signalling events.
R-HSA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-HSA-442720. CREB phosphorylation through the activation of Adenylate Cyclase.
R-HSA-5610787. Hedgehog 'off' state.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 1 (EC:4.6.1.1By similarity)
Alternative name(s):
ATP pyrophosphate-lyase 1
Adenylate cyclase type I
Adenylyl cyclase 1
Ca(2+)/calmodulin-activated adenylyl cyclase
Gene namesi
Name:ADCY1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:232. ADCY1.

Subcellular locationi

  • Membrane By similarity; Multi-pass membrane protein By similarity
  • Cell membrane 1 Publication; Multi-pass membrane protein Curated
  • Cytoplasm By similarity
  • Membrane raft By similarity

  • Note: Expressed in the cytoplasm of supporting cells and hair cells of the cochlea vestibule, as well as to the cochlear hair cell nuclei and stereocilia.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6363CytoplasmicSequence analysisAdd
BLAST
Transmembranei64 – 8421HelicalSequence analysisAdd
BLAST
Transmembranei88 – 10821HelicalSequence analysisAdd
BLAST
Transmembranei125 – 14521HelicalSequence analysisAdd
BLAST
Transmembranei158 – 17821HelicalSequence analysisAdd
BLAST
Transmembranei183 – 20321HelicalSequence analysisAdd
BLAST
Transmembranei214 – 23421HelicalSequence analysisAdd
BLAST
Topological domaini235 – 610376CytoplasmicSequence analysisAdd
BLAST
Transmembranei611 – 63121HelicalSequence analysisAdd
BLAST
Transmembranei635 – 65521HelicalSequence analysisAdd
BLAST
Transmembranei674 – 69421HelicalSequence analysisAdd
BLAST
Transmembranei725 – 74521HelicalSequence analysisAdd
BLAST
Transmembranei753 – 77321HelicalSequence analysisAdd
BLAST
Transmembranei775 – 79420HelicalSequence analysisAdd
BLAST
Topological domaini795 – 1119325CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • membrane raft Source: UniProtKB-SubCell
  • nucleus Source: Ensembl
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

Deafness, autosomal recessive, 44 (DFNB44)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of non-syndromic deafness characterized by prelingual profound hearing loss affecting all frequencies.
See also OMIM:610154

Keywords - Diseasei

Deafness, Non-syndromic deafness

Organism-specific databases

MalaCardsiADCY1.
MIMi610154. phenotype.
Orphaneti90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
PharmGKBiPA24560.

Chemistry

ChEMBLiCHEMBL2899.
DrugBankiDB00131. Adenosine monophosphate.
DB00171. Adenosine triphosphate.

Polymorphism and mutation databases

BioMutaiADCY1.
DMDMi62512172.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11191119Adenylate cyclase type 1PRO_0000195682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei551 – 5511PhosphoserineBy similarity
Glycosylationi704 – 7041N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ08828.
PRIDEiQ08828.

PTM databases

iPTMnetiQ08828.
PhosphoSiteiQ08828.

Expressioni

Tissue specificityi

Detected in zona glomerulosa and zona fasciculata in the adrenal gland (at protein level) (PubMed:11549699). Brain, retina and adrenal medulla.2 Publications

Gene expression databases

BgeeiQ08828.
CleanExiHS_ADCY1.
ExpressionAtlasiQ08828. baseline and differential.
GenevisibleiQ08828. HS.

Organism-specific databases

HPAiCAB018364.

Interactioni

Subunit structurei

Interacts with CALM.By similarity

Protein-protein interaction databases

STRINGi9606.ENSP00000297323.

Chemistry

BindingDBiQ08828.

Structurei

3D structure databases

ProteinModelPortaliQ08828.
SMRiQ08828. Positions 290-477, 860-1054.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni493 – 52028Interaction with calmodulinBy similarityAdd
BLAST
Regioni1024 – 104724Interaction with calmodulinBy similarityAdd
BLAST

Domaini

The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain.By similarity

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 2 guanylate cyclase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000119042.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiQ08828.
OMAiCLPWAWS.
OrthoDBiEOG7B8S30.
PhylomeDBiQ08828.
TreeFamiTF313845.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08828-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGAPRGGGG GGGGAGEPGG AERAAGTSRR RGLRACDEEF ACPELEALFR
60 70 80 90 100
GYTLRLEQAA TLKALAVLSL LAGALALAEL LGAPGPAPGL AKGSHPVHCV
110 120 130 140 150
LFLALLVVTN VRSLQVPQLQ QVGQLALLFS LTFALLCCPF ALGGPARGSA
160 170 180 190 200
GAAGGPATAE QGVWQLLLVT FVSYALLPVR SLLAIGFGLV VAASHLLVTA
210 220 230 240 250
TLVPAKRPRL WRTLGANALL FVGVNMYGVF VRILTERSQR KAFLQARSCI
260 270 280 290 300
EDRLRLEDEN EKQERLLMSL LPRNVAMEMK EDFLKPPERI FHKIYIQRHD
310 320 330 340 350
NVSILFADIV GFTGLASQCT AQELVKLLNE LFGKFDELAT ENHCRRIKIL
360 370 380 390 400
GDCYYCVSGL TQPKTDHAHC CVEMGLDMID TITSVAEATE VDLNMRVGLH
410 420 430 440 450
TGRVLCGVLG LRKWQYDVWS NDVTLANVME AAGLPGKVHI TKTTLACLNG
460 470 480 490 500
DYEVEPGYGH ERNSFLKTHN IETFFIVPSH RRKIFPGLIL SDIKPAKRMK
510 520 530 540 550
FKTVCYLLVQ LMHCRKMFKA EIPFSNVMTC EDDDKRRALR TASEKLRNRS
560 570 580 590 600
SFSTNVVYTT PGTRVNRYIS RLLEARQTEL EMADLNFFTL KYKHVEREQK
610 620 630 640 650
YHQLQDEYFT SAVVLTLILA ALFGLVYLLI FPQSVVVLLL LVFCICFLVA
660 670 680 690 700
CVLYLHITRV QCFPGCLTIQ IRTVLCIFIV VLIYSVAQGC VVGCLPWAWS
710 720 730 740 750
SKPNSSLVVL SSGGQRTALP TLPCESTHHA LLCCLVGTLP LAIFFRVSSL
760 770 780 790 800
PKMILLSGLT TSYILVLELS GYTRTGGGAV SGRSYEPIVA ILLFSCALAL
810 820 830 840 850
HARQVDIRLR LDYLWAAQAE EEREDMEKVK LDNRRILFNL LPAHVAQHFL
860 870 880 890 900
MSNPRNMDLY YQSYSQVGVM FASIPNFNDF YIELDGNNMG VECLRLLNEI
910 920 930 940 950
IADFDELMEK DFYKDIEKIK TIGSTYMAAV GLAPTSGTKA KKSISSHLST
960 970 980 990 1000
LADFAIEMFD VLDEINYQSY NDFVLRVGIN VGPVVAGVIG ARRPQYDIWG
1010 1020 1030 1040 1050
NTVNVASRMD STGVQGRIQV TEEVHRLLRR CPYHFVCRGK VSVKGKGEML
1060 1070 1080 1090 1100
TYFLEGRTDG NGSQIRSLGL DRKMCPFGRA GLQGRRPPVC PMPGVSVRAG
1110
LPPHSPGQYL PSAAAGKEA
Length:1,119
Mass (Da):123,440
Last modified:April 12, 2005 - v2
Checksum:iE8DDC8FCB58743D7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti456 – 4561P → L.
Corresponds to variant rs12721473 [ dbSNP | Ensembl ].
VAR_029186
Natural varianti940 – 9401A → T.
Corresponds to variant rs45444695 [ dbSNP | Ensembl ].
VAR_029187
Natural varianti984 – 9841V → M.
Corresponds to variant rs2293106 [ dbSNP | Ensembl ].
VAR_048246

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC069008 Genomic DNA. Translation: AAS07467.1.
AC091439 Genomic DNA. No translation available.
CH236960 Genomic DNA. Translation: EAL23741.1.
L05500 mRNA. Translation: AAA02907.1.
CCDSiCCDS34631.1.
PIRiA47007.
RefSeqiNP_066939.1. NM_021116.2.
UniGeneiHs.192215.

Genome annotation databases

EnsembliENST00000297323; ENSP00000297323; ENSG00000164742.
GeneIDi107.
UCSCiuc003tne.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC069008 Genomic DNA. Translation: AAS07467.1.
AC091439 Genomic DNA. No translation available.
CH236960 Genomic DNA. Translation: EAL23741.1.
L05500 mRNA. Translation: AAA02907.1.
CCDSiCCDS34631.1.
PIRiA47007.
RefSeqiNP_066939.1. NM_021116.2.
UniGeneiHs.192215.

3D structure databases

ProteinModelPortaliQ08828.
SMRiQ08828. Positions 290-477, 860-1054.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000297323.

Chemistry

BindingDBiQ08828.
ChEMBLiCHEMBL2899.
DrugBankiDB00131. Adenosine monophosphate.
DB00171. Adenosine triphosphate.

PTM databases

iPTMnetiQ08828.
PhosphoSiteiQ08828.

Polymorphism and mutation databases

BioMutaiADCY1.
DMDMi62512172.

Proteomic databases

PaxDbiQ08828.
PRIDEiQ08828.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000297323; ENSP00000297323; ENSG00000164742.
GeneIDi107.
UCSCiuc003tne.4. human.

Organism-specific databases

CTDi107.
GeneCardsiADCY1.
H-InvDBHIX0033533.
HGNCiHGNC:232. ADCY1.
HPAiCAB018364.
MalaCardsiADCY1.
MIMi103072. gene.
610154. phenotype.
neXtProtiNX_Q08828.
Orphaneti90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
PharmGKBiPA24560.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000119042.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiQ08828.
OMAiCLPWAWS.
OrthoDBiEOG7B8S30.
PhylomeDBiQ08828.
TreeFamiTF313845.

Enzyme and pathway databases

BRENDAi4.6.1.1. 2681.
ReactomeiR-HSA-163359. Glucagon signaling in metabolic regulation.
R-HSA-163615. PKA activation.
R-HSA-164378. PKA activation in glucagon signalling.
R-HSA-170660. Adenylate cyclase activating pathway.
R-HSA-170670. Adenylate cyclase inhibitory pathway.
R-HSA-418555. G alpha (s) signalling events.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-418597. G alpha (z) signalling events.
R-HSA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-HSA-442720. CREB phosphorylation through the activation of Adenylate Cyclase.
R-HSA-5610787. Hedgehog 'off' state.

Miscellaneous databases

ChiTaRSiADCY1. human.
GeneWikiiADCY1.
GenomeRNAii107.
NextBioi415.
PROiQ08828.
SOURCEiSearch...

Gene expression databases

BgeeiQ08828.
CleanExiHS_ADCY1.
ExpressionAtlasiQ08828. baseline and differential.
GenevisibleiQ08828. HS.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Cloning, chromosomal mapping, and expression of human fetal brain type I adenylyl cyclase."
    Villacres E.C., Xia Z., Bookbinder L.H., Edelhoff S., Disteche C.M., Storm D.R.
    Genomics 16:473-478(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 281-1119, TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  4. "Expression and regulation of adenylyl cyclase isoforms in the human adrenal gland."
    Cote M., Guillon G., Payet M.D., Gallo-Payet N.
    J. Clin. Endocrinol. Metab. 86:4495-4503(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "Adenylate cyclase 1 (ADCY1) mutations cause recessive hearing impairment in humans and defects in hair cell function and hearing in zebrafish."
    Santos-Cortez R.L., Lee K., Giese A.P., Ansar M., Amin-Ud-Din M., Rehn K., Wang X., Aziz A., Chiu I., Hussain Ali R., Smith J.D., Shendure J., Bamshad M., Nickerson D.A., Ahmed Z.M., Ahmad W., Riazuddin S., Leal S.M.
    Hum. Mol. Genet. 23:3289-3298(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN DFNB44.

Entry informationi

Entry nameiADCY1_HUMAN
AccessioniPrimary (citable) accession number: Q08828
Secondary accession number(s): A4D2L8, Q75MI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: April 12, 2005
Last modified: January 20, 2016
This is version 149 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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

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 one 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.