P35348 (ADA1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 135.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Alpha-1A adrenergic receptor Alternative name(s): Alpha-1A adrenoreceptor Short name=Alpha-1A adrenoceptor Alpha-1C adrenergic receptor Alpha-adrenergic receptor 1c | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 466 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G11 proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes. Ref.16 Ref.17 |
| Subunit structure | Homo- and heterooligomer. Heterooligomerizes with ADRA1B homooligomers in cardiac myocytes. Ref.17 |
| Subcellular location | Nucleus membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note: Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes. Ref.16 Ref.17 |
| Tissue specificity | Expressed in heart, brain, liver and prostate, but not in kidney, lung, adrenal, aorta and pituitary. Within the prostate, expressed in the apex, base, periurethral and lateral lobe. Isoform 4 is the most abundant isoform expressed in the prostate with high levels also detected in liver and heart. Ref.5 Ref.7 Ref.15 |
| Post-translational modification | C-terminal Ser or Thr residues may be phosphorylated By similarity. |
| Sequence similarities | Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA1A sub-subfamily. |
| Sequence caution | Isoform 2: The sequence BAA06901.1 differs from that shown. Reason: Frameshift at position 465. Isoform 2: The sequence ACA05900.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
Alternative products
| This entry describes 9 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: P35348-1) Also known as: Alpha 1c-1; Alpha(1A-1); 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. | ||||||
| Isoform 2 (identifier: P35348-2) Also known as: Alpha 1c-2; Alpha(1A-2); The sequence of this isoform differs from the canonical sequence as follows: 424-466: VRSKSFLQVC...ISLSENGEEV → TKSRSVTRLE...CHQADATRPS | ||||||
| Isoform 3 (identifier: P35348-3) Also known as: Alpha 1c-3; Alpha(1A-3); The sequence of this isoform differs from the canonical sequence as follows: 424-429: VRSKSF → GHTPMT 430-466: Missing. | ||||||
| Isoform 4 (identifier: P35348-4) Also known as: Alpha(1A-4); The sequence of this isoform differs from the canonical sequence as follows: 424-466: VRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV → RGMDCRYFTKNCREHIKHVNFMMPPWRKGSEC | ||||||
| Isoform 5 (identifier: P35348-5) The sequence of this isoform differs from the canonical sequence as follows: 296-297: SF → KS 298-466: Missing. | ||||||
| Isoform 6 (identifier: P35348-6) The sequence of this isoform differs from the canonical sequence as follows: 295-342: GSFFPDFKPS...FKKAFQNVLR → DEETEAQEGK...VSRKDTCGVW 343-466: Missing. | ||||||
| Isoform 7 (identifier: P35348-7) Also known as: 2b/3b; The sequence of this isoform differs from the canonical sequence as follows: 296-324: SFFPDFKPSETVFKIVFWLGYLNSCINPI → TYILKYDVLFWRKGLSVCTRLRERKEIKN 325-466: Missing. | ||||||
| Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. | ||||||
| Isoform 8 (identifier: P35348-8) Also known as: 2c; The sequence of this isoform differs from the canonical sequence as follows: 295-466: GSFFPDFKPS...ISLSENGEEV → DEVSLCHQAG...GQDDLDLLTS | ||||||
| Isoform 9 (identifier: P35348-9) Also known as: 3c; The sequence of this isoform differs from the canonical sequence as follows: 296-466: SFFPDFKPSE...ISLSENGEEV → THTHDMKPAS...TVTDTGKTVT |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 466 | 466 | Alpha-1A adrenergic receptor | PRO_0000069063 | |||||||
Regions | |||||||||||
| Topological domain | 1 – 27 | 27 | Extracellular By similarity | ||||||||
| Transmembrane | 28 – 51 | 24 | Helical; Name=1; By similarity | ||||||||
| Topological domain | 52 – 64 | 13 | Cytoplasmic By similarity | ||||||||
| Transmembrane | 65 – 88 | 24 | Helical; Name=2; By similarity | ||||||||
| Topological domain | 89 – 99 | 11 | Extracellular By similarity | ||||||||
| Transmembrane | 100 – 122 | 23 | Helical; Name=3; By similarity | ||||||||
| Topological domain | 123 – 143 | 21 | Cytoplasmic By similarity | ||||||||
| Transmembrane | 144 – 167 | 24 | Helical; Name=4; By similarity | ||||||||
| Topological domain | 168 – 181 | 14 | Extracellular By similarity | ||||||||
| Transmembrane | 182 – 205 | 24 | Helical; Name=5; By similarity | ||||||||
| Topological domain | 206 – 273 | 68 | Cytoplasmic By similarity | ||||||||
| Transmembrane | 274 – 297 | 24 | Helical; Name=6; By similarity | ||||||||
| Topological domain | 298 – 305 | 8 | Extracellular By similarity | ||||||||
| Transmembrane | 306 – 329 | 24 | Helical; Name=7; By similarity | ||||||||
| Topological domain | 330 – 466 | 137 | Cytoplasmic By similarity | ||||||||
| Region | 334 – 349 | 16 | Nuclear localization signal | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 215 | 1 | Phosphoserine; by PKA Potential | ||||||||
| Lipidation | 345 | 1 | S-palmitoyl cysteine Potential | ||||||||
| Glycosylation | 7 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 13 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 22 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 99 ↔ 176 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 295 – 466 | 172 | GSFFP…NGEEV → DEVSLCHQAGVQWHDLGSLQ PPPPGFKRFSCLSLPSSWDY RDVPPGRRHQAQLIFVFLVE TGFHHVGQDDLDLLTS in isoform 8. | VSP_011046 | |||||||
| Alternative sequence | 295 – 342 | 48 | GSFFP…QNVLR → DEETEAQEGKNDSPSFKQPV HHAAVLGLEVMEKENLEGVS RKDTCGVW in isoform 6. | VSP_011053 | |||||||
| Alternative sequence | 296 – 466 | 171 | SFFPD…NGEEV → THTHDMKPASRPRLLSLLPK EGEHETHHWSCDPLSLESTP GAQEPCLTLGFTSLSSIHLT KAQIQHVTVTDTGKTVT in isoform 9. | VSP_011049 | |||||||
| Alternative sequence | 296 – 324 | 29 | SFFPD…CINPI → TYILKYDVLFWRKGLSVCTR LRERKEIKN in isoform 7. | VSP_011047 | |||||||
| Alternative sequence | 296 – 297 | 2 | SF → KS in isoform 5. | VSP_011051 | |||||||
| Alternative sequence | 298 – 466 | 169 | Missing in isoform 5. | VSP_011052 | |||||||
| Alternative sequence | 325 – 466 | 142 | Missing in isoform 7. | VSP_011048 | |||||||
| Alternative sequence | 343 – 466 | 124 | Missing in isoform 6. | VSP_011054 | |||||||
| Alternative sequence | 424 – 466 | 43 | VRSKS…NGEEV → TKSRSVTRLECSGMILAHCN LRLPGSRDSPASASQAAGTT GMCHQADATRPS in isoform 2. | VSP_011055 | |||||||
| Alternative sequence | 424 – 466 | 43 | VRSKS…NGEEV → RGMDCRYFTKNCREHIKHVN FMMPPWRKGSEC in isoform 4. | VSP_011050 | |||||||
| Alternative sequence | 424 – 429 | 6 | VRSKSF → GHTPMT in isoform 3. | VSP_011044 | |||||||
| Alternative sequence | 430 – 466 | 37 | Missing in isoform 3. | VSP_011045 | |||||||
| Natural variant | 40 | 1 | G → W in a breast cancer sample; somatic mutation. Ref.20 | VAR_035756 | |||||||
| Natural variant | 200 | 1 | I → S. Corresponds to variant rs2229125 [ dbSNP | Ensembl ]. | VAR_049370 | |||||||
| Natural variant | 347 | 1 | C → R Frequent polymorphism. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.14 Ref.15 Ref.18 Ref.19 Corresponds to variant rs1048101 [ dbSNP | Ensembl ]. | VAR_019509 | |||||||
| Natural variant | 414 | 1 | K → R. Corresponds to variant rs3730247 [ dbSNP | Ensembl ]. | VAR_049371 | |||||||
| Natural variant | 465 | 1 | E → D. Corresponds to variant rs2229126 [ dbSNP | Ensembl ]. | VAR_049372 | |||||||
Experimental info | |||||||||||
| Mutagenesis | 334 | 1 | K → A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-335; A-342; A-348 and A-349. Ref.17 | ||||||||
| Mutagenesis | 335 | 1 | K → A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-342; A-348 and A-349. Ref.17 | ||||||||
| Mutagenesis | 342 | 1 | R → A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-348 and A-349. Ref.17 | ||||||||
| Mutagenesis | 348 | 1 | R → A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-342 and A-349. Ref.17 | ||||||||
| Mutagenesis | 349 | 1 | K → A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-342 and A-348. Ref.17 | ||||||||
| Sequence conflict | 43 | 1 | G → C in AAA93114. Ref.4 | ||||||||
| Sequence conflict | 129 | 1 | S → T in AAA93114. Ref.4 | ||||||||
| Sequence conflict | 130 | 1 | Y → H in AAK77197. Ref.9 | ||||||||
| Sequence conflict | 185 | 1 | V → A in AAH95512. Ref.14 | ||||||||
| Sequence conflict | 338 | 1 | Q → C Ref.2 | ||||||||
| Sequence conflict | 359 | 1 | T → P in AAA93114. Ref.4 | ||||||||
| Sequence conflict | 384 | 1 | T → A in AAK77197. Ref.9 | ||||||||
| Sequence conflict | 387 | 1 | R → G in AAK77197. Ref.9 | ||||||||
| Sequence conflict | 390 | 1 | K → R in AAK77197. Ref.9 | ||||||||
| Sequence conflict | 431 | 1 | Q → E in BAA04960. Ref.1 | ||||||||
| Sequence conflict | 437 | 1 | G → E in AAK77197. Ref.9 | ||||||||
| Sequence conflict | 442 | 1 | S → C in AAA93114. Ref.4 | ||||||||
| Isoform 4: | |||||||||||
| Sequence conflict | 453 | 1 | S → L in AAC06138. Ref.7 | ||||||||
| Isoform 6: | |||||||||||
| Sequence conflict | 302 | 1 | E → Q in AAR84650. Ref.8 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning, functional expression and tissue distribution of human cDNA for the alpha 1C-adrenergic receptor." Hirasawa A., Horie K., Tanaka T., Takagaki K., Murai M., Yano J., Tsujimoto G. Biochem. Biophys. Res. Commun. 195:902-909(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT ARG-347. Tissue: Prostate. |
| [2] | "Cloning, expression and characterization of human alpha adrenergic receptors alpha 1a, alpha 1b and alpha 1c." Weinberg D.H., Trivedi P., Tan C.P., Mitra S., Perkins-Barrow A., Borkowski D., Strader C.D., Bayne M. Biochem. Biophys. Res. Commun. 201:1296-1304(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-347. Tissue: Heart. |
| [3] | "The alpha 1-adrenergic receptor that mediates smooth muscle contraction in human prostate has the pharmacological properties of the cloned human alpha 1c subtype." Forray C., Bard J.A., Wetzel J.M., Chiu G., Shapiro E., Tang R., Lepor H., Hartig P.R., Weinshank R.L., Branchek T.A., Gluchowski C. Mol. Pharmacol. 45:703-708(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). Tissue: Hippocampus and Lymphocyte. |
| [4] | "The alpha 1C-adrenoceptor in human prostate: cloning, functional expression, and localization to specific prostatic cell types." Tseng-Crank J., Kost T., Goetz A., Hazum S., Roberson K.M., Haizlip J., Godinot N., Robertson C.N., Saussy D. Br. J. Pharmacol. 115:1475-1485(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-347. |
| [5] | "Cloning, functional expression and tissue distribution of human alpha 1c-adrenoceptor splice variants." Hirasawa A., Shibata K., Horie K., Takei Y., Obika K., Tanaka T., Muramoto N., Takagaki K., Yano J., Tsujimoto G. FEBS Lett. 363:256-260(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), VARIANT ARG-347, TISSUE SPECIFICITY. Tissue: Prostate. |
| [6] | "Cloning and pharmacological characterization of human alpha-1 adrenergic receptors: sequence corrections and direct comparison with other species homologues." Schwinn D.A., Johnston G.I., Page S.O., Mosley M.J., Wilson K.H., Worman N.P., Campbell S., Fidock M.D., Furness L.M., Parry-Smith D.J., Peter B., Bailey D.S. J. Pharmacol. Exp. Ther. 272:134-142(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-347. |
| [7] | "Molecular cloning, genomic characterization and expression of novel human alpha1A-adrenoceptor isoforms." Chang D.J., Chang T.K., Yamanishi S.S., Salazar F.H.R., Kosaka A.H., Khare R., Bhakta S., Jasper J.R., Shieh I.-S., Lesnick J.D., Ford A.P.D.W., Daniels D.V., Clarke D.E., Bach C.T., Chan H.W. FEBS Lett. 422:279-283(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY. Tissue: Prostate. |
| [8] | "Truncated isoforms inhibit [3H]prazosin binding and cellular trafficking of native human alpha1A-adrenoceptors." Coge F., Guenin S.P., Renouard-Try A., Rique H., Ouvry C., Fabry N., Beauverger P., Nicolas J.P., Galizzi J.-P., Boutin J.A., Canet E. Biochem. J. 343:231-239(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6; 7; 8 AND 9). Tissue: Liver. |
| [9] | "RT-PCR cloning and sequence analysis of adrenergic receptor subtype-alpha-1a cDNA from human prostrate cell-line DU-145." Banerjee A.G.N., Aarti A. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [10] | "Genome-wide discovery and analysis of human seven transmembrane helix receptor genes." Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [11] | "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Kopatz S.A., Aronstam R.S., Sharma S.V. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). |
| [12] | "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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Cerebellum. |
| [13] | NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [14] | "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), VARIANT ARG-347. |
| [15] | "Identification of alpha 1-adrenoceptor subtypes present in the human prostate." Faure C., Pimoule C., Vallancien G., Langer S.Z., Graham D. Life Sci. 54:1595-1605(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-400 (ISOFORMS 1/2/3/4), TISSUE SPECIFICITY, VARIANT ARG-347. Tissue: Prostate. |
| [16] | "Nuclear alpha1-adrenergic receptors signal activated ERK localization to caveolae in adult cardiac myocytes." Wright C.D., Chen Q., Baye N.L., Huang Y., Healy C.L., Kasinathan S., O'Connell T.D. Circ. Res. 103:992-1000(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION. |
| [17] | "Nuclear localization drives alpha1-adrenergic receptor oligomerization and signaling in cardiac myocytes." Wright C.D., Wu S.C., Dahl E.F., Sazama A.J., O'Connell T.D. Cell. Signal. 24:794-802(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, SUBUNIT, FUNCTION, MUTAGENESIS OF LYS-334; LYS-335; ARG-342; ARG-348 AND LYS-349. |
| [18] | "Alpha 1a-adrenoceptor polymorphism: pharmacological characterization and association with benign prostatic hypertrophy." Shibata K., Hirasawa A., Moriyama N., Kawabe K., Ogawa S., Tsujimoto G. Br. J. Pharmacol. 118:1403-1408(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ARG-347. |
| [19] | "Alpha 1A-adrenergic receptor polymorphism and vascular response." Sofowora G.G., Dishy V., Landau R., Xie H.G., Prasad H.C., Byrne D.W., Smiley R.M., Kim R.B., Wood A.J., Stein C.M. Clin. Pharmacol. Ther. 75:539-545(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ARG-347. |
| [20] | "The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E.Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-40. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D25235 mRNA. Translation: BAA04960.1. U03866 Genomic DNA. Translation: AAB60353.1. U02569 mRNA. Translation: AAA93114.1. D32201 mRNA. Translation: BAA06900.1. D32202 mRNA. Translation: BAA06901.1. Frameshift. L31774 mRNA. Translation: AAB59486.1. AF013261 mRNA. Translation: AAC06138.1. AY491775 mRNA. Translation: AAR84644.1. AY491776 mRNA. Translation: AAR84645.1. AY491777 mRNA. Translation: AAR84646.1. AY491778 mRNA. Translation: AAR84647.1. AY491779 mRNA. Translation: AAR84648.1. AY491780 mRNA. Translation: AAR84649.1. AY491781 mRNA. Translation: AAR84650.1. AF395806 mRNA. Translation: AAK77197.1. AB065703 Genomic DNA. Translation: BAC05926.1. AY389505 Genomic DNA. Translation: AAQ91331.1. AK289548 mRNA. Translation: BAF82237.1. EU326301 Genomic DNA. Translation: ACA05899.1. EU326301 Genomic DNA. Translation: ACA05900.1. Sequence problems. EU326301 Genomic DNA. Translation: ACA05902.1. EU326301 Genomic DNA. Translation: ACA05903.1. EU326301 Genomic DNA. Translation: ACA05904.1. EU326301 Genomic DNA. Translation: ACA05905.1. EU326301 Genomic DNA. Translation: ACA05906.1. EU326301 Genomic DNA. Translation: ACA05907.1. BC095512 mRNA. Translation: AAH95512.1. |
| IPI | IPI00430195. IPI00430197. IPI00430199. IPI00430201. IPI00430202. IPI00430203. IPI00430204. IPI00430205. IPI00954300. |
| PIR | JN0765. S65656. S65657. |
| RefSeq | NP_000671.2. NM_000680.2. NP_150645.2. NM_033302.2. NP_150646.3. NM_033303.3. NP_150647.2. NM_033304.2. |
| UniGene | Hs.709175. |
3D structure databases | |
| ProteinModelPortal | P35348. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-33401N. |
| IntAct | P35348. 3 interactions. |
Protein family/group databases | |
| GPCRDB | Search... |
PTM databases | |
| PhosphoSite | P35348. |
Polymorphism databases | |
| DMDM | 1168246. |
Proteomic databases | |
| PaxDb | P35348. |
| PRIDE | P35348. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000276393; ENSP00000276393; ENSG00000120907. ENST00000354550; ENSP00000346557; ENSG00000120907. ENST00000358857; ENSP00000351725; ENSG00000120907. ENST00000380572; ENSP00000369946; ENSG00000120907. ENST00000380573; ENSP00000369947; ENSG00000120907. ENST00000380581; ENSP00000369955; ENSG00000120907. ENST00000380582; ENSP00000369956; ENSG00000120907. ENST00000380586; ENSP00000369960; ENSG00000120907. ENST00000380587; ENSP00000369961; ENSG00000120907. ENST00000519096; ENSP00000431073; ENSG00000120907. ENST00000521711; ENSP00000430414; ENSG00000120907. |
| GeneID | 148. |
| KEGG | hsa:148. |
| UCSC | uc003xfe.1. human. uc003xfg.1. human. uc003xfh.1. human. uc010lul.1. human. uc010lum.1. human. uc022atd.1. human. |
Organism-specific databases | |
| CTD | 148. |
| GeneCards | GC08M026605. |
| HGNC | HGNC:277. ADRA1A. |
| HPA | HPA029678. |
| MIM | 104221. gene. |
| neXtProt | NX_P35348. |
| PharmGKB | PA34. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | NOG253615. |
| HOVERGEN | HBG106962. |
| KO | K04135. |
| OMA | NCTHPPA. |
Enzyme and pathway databases | |
| Reactome | REACT_111102. Signal Transduction. |
| SignaLink | P35348. |
Gene expression databases | |
| ArrayExpress | P35348. |
| Bgee | P35348. |
| CleanEx | HS_ADRA1A. |
| Genevestigator | P35348. |
| GermOnline | ENSG00000120907. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR001004. Adrene_rcpt_A1Cs. IPR002233. Adrnrgc_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view] |
| Pfam | PF00001. 7tm_1. 1 hit. [Graphical view] |
| PRINTS | PR01103. ADRENERGICR. PR00557. ADRENRGCA1AR. PR00237. GPCRRHODOPSN. |
| PROSITE | PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| BindingDB | P35348. |
| ChEMBL | CHEMBL229. |
| DrugBank | DB00346. Alfuzosin. DB01118. Amiodarone. DB00182. Amphetamine. DB00865. Benzphetamine. DB00217. Bethanidine. DB01136. Carvedilol. DB00298. Dapiprazole. DB04840. Debrisoquin. DB01576. Dextroamphetamine. DB00590. Doxazosin. DB00751. Epinastine. DB00668. Epinephrine. DB00696. Ergotamine. DB00875. Flupenthixol. DB00226. Guanadrel Sulfate. DB01170. Guanethidine. DB00598. Labetalol. DB01255. Lisdexamfetamine. DB00934. Maprotiline. DB01365. Mephentermine. DB00610. Metaraminol. DB01577. Methamphetamine. DB01403. Methotrimeprazine. DB00723. Methoxamine. DB00211. Midodrine. DB01149. Nefazodone. DB00699. Nicergoline. DB00665. Nilutamide. DB00368. Norepinephrine. DB00506. Norgestrel. DB00935. Oxymetazoline. DB00850. Perphenazine. DB01579. Phendimetrazine. DB00925. Phenoxybenzamine. DB00388. Phenylephrine. DB00397. Phenylpropanolamine. DB00457. Prazosin. DB00420. Promazine. DB01069. Promethazine. DB01608. Propericiazine. DB00777. Propiomazine. DB00852. Pseudoephedrine. DB00734. Risperidone. DB06144. Sertindole. DB00706. Tamsulosin. DB01162. Terazosin. DB00679. Thioridazine. DB00797. Tolazoline. DB00656. Trazodone. DB00831. Trifluoperazine. DB00246. Ziprasidone. |
| GenomeRNAi | 148. |
| NextBio | 585. |
| SOURCE | Search... |
Entry information
| Entry name | ADA1A_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P35348 Secondary accession number(s): A8K0I3 Q9UD67 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| 7-transmembrane G-linked receptors List of 7-transmembrane G-linked receptor entries |
| Human chromosome 8 Human chromosome 8: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
