Reviewed,
UniProtKB/Swiss-Prot P35611 (ADDA_HUMAN)
Last modified
November 3, 2009.
Version 100.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alpha-adducin Alternative name(s): Erythrocyte adducin subunit alpha | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete 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 | 737 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin. |
| Subunit structure | Heterodimer of an alpha and a beta subunit or an alpha and a gamma subunit. Binds ROCK1. |
| Subcellular location | Cytoplasm › cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. |
| Tissue specificity | Expressed in all tissues. Found in much higher levels in reticulocytes than the beta subunit. |
| Domain | Each subunit is comprised of three regions: a NH2-terminal protease-resistant globular head region, a short connecting subdomain, and a protease-sensitive tail region. |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Belongs to the aldolase class II family. Adducin subfamily. |
| Sequence caution | The sequence CAA98970.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform 1 (identifier: P35611-1) 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: P35611-2) The sequence of this isoform differs from the canonical sequence as follows: 621-631: DLVPEPTTGDD → GDGCAREYLLP 632-737: Missing. | ||||||
| Isoform 3 (identifier: P35611-3) The sequence of this isoform differs from the canonical sequence as follows: 471-471: K → KVWTNITHDHVKPLLQSLSSGVCVPSCITNCL |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 737 | 737 | Alpha-adducin | PRO_0000218530 | |||||
Regions | |||||||||
| Region | 717 – 734 | 18 | Interaction with calmodulin Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 12 | 1 | Phosphoserine Ref.11 Ref.12 | ||||||
| Modified residue | 59 | 1 | Phosphoserine; by PKA Ref.5 | ||||||
| Modified residue | 331 | 1 | Phosphothreonine Ref.12 | ||||||
| Modified residue | 334 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 353 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 355 | 1 | Phosphoserine Ref.10 Ref.8 | ||||||
| Modified residue | 358 | 1 | Phosphoserine Ref.11 Ref.12 Ref.10 Ref.8 Ref.7 | ||||||
| Modified residue | 408 | 1 | Phosphoserine; by PKA Ref.5 | ||||||
| Modified residue | 431 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 436 | 1 | Phosphoserine; by PKA Ref.12 Ref.5 | ||||||
| Modified residue | 445 | 1 | Phosphothreonine; by ROCK1 Ref.6 | ||||||
| Modified residue | 465 | 1 | Phosphoserine Ref.12 Ref.10 Ref.7 | ||||||
| Modified residue | 480 | 1 | Phosphothreonine; by ROCK1 Ref.6 | ||||||
| Modified residue | 481 | 1 | Phosphoserine; by PKA Ref.5 | ||||||
| Modified residue | 483 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 586 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 614 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 707 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 710 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 716 | 1 | Phosphoserine; by PKC Ref.5 Ref.9 | ||||||
| Modified residue | 726 | 1 | Phosphoserine; by PKA and PKC Ref.5 | ||||||
Natural variations | |||||||||
| Alternative sequence | 471 | 1 | K → KVWTNITHDHVKPLLQSLSS GVCVPSCITNCL in isoform 3. | VSP_000174 | |||||
| Alternative sequence | 621 – 631 | 11 | DLVPEPTTGDD → GDGCAREYLLP in isoform 2. | VSP_000175 | |||||
| Alternative sequence | 632 – 737 | 106 | Missing in isoform 2. | VSP_000176 | |||||
| Natural variant | 6 | 1 | R → C: dbSNP rs2295497. | VAR_022108 | |||||
| Natural variant | 270 | 1 | Y → N: dbSNP rs4971. | VAR_014863 | |||||
| Natural variant | 376 | 1 | E → D: dbSNP rs4972. | VAR_014864 | |||||
| Natural variant | 460 | 1 | G → W: dbSNP rs4961. Ref.13 Ref.14 | VAR_014184 | |||||
| Natural variant | 510 | 1 | N → I: dbSNP rs4962. | VAR_014865 | |||||
| Natural variant | 586 | 1 | S → C: dbSNP rs4963. Ref.14 Ref.1 | VAR_014185 | |||||
Experimental info | |||||||||
| Mutagenesis | 445 | 1 | T → D: Abolishes phosphorylation by ROCK1; when associated with D-480. Ref.6 | ||||||
| Mutagenesis | 480 | 1 | T → D: Abolishes phosphorylation by ROCK1; when associated with D-445. Ref.6 | ||||||
| Sequence conflict | 606 | 1 | A → E in AAB05645. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Primary structure and domain organization of human alpha and beta adducin." Joshi R.L., Gilligan D.M., Otto E., McLaughlin T., Bennett V.D. J. Cell Biol. 115:665-675(1991) [PubMed: 1840603] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 24-36; 41-47; 516-569 AND 722-729, VARIANT CYS-586. Tissue: Reticulocyte. |
| [2] | "Genomic organization of the human alpha-adducin gene and its alternately spliced isoforms." Lin B., Nasir J., McDonald H., Graham R., Rommens J.M., Goldberg Y.P., Hayden M.R. Genomics 25:93-99(1995) [PubMed: 7774961] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING. |
| [3] | "Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. Wilson R.K.Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "Cloning of the alpha-adducin gene from the Huntington's disease candidate region of chromosome 4 by exon amplification." Taylor S.A., Snell R.G., Buckler A., Ambrose C., Duyao M., Church D., Lin C.S., Altherr M., Bates G.P., Groot N. Nat. Genet. 2:223-227(1992) [PubMed: 1345173] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 531-737 (ISOFORM 1/3). |
| [5] | "Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C." Matsuoka Y., Hughes C.A., Bennett V. J. Biol. Chem. 271:25157-25166(1996) [PubMed: 8810272] [Abstract] Cited for: PHOSPHORYLATION AT SER-59; SER-408; SER-436; SER-481; SER-716 AND SER-726, PARTIAL PROTEIN SEQUENCE. |
| [6] | "Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility." Fukata Y., Oshiro N., Kinoshita N., Kawano Y., Matsuoka Y., Bennett V., Matsuura Y., Kaibuchi K. J. Cell Biol. 145:347-361(1999) [PubMed: 10209029] [Abstract] Cited for: PHOSPHORYLATION AT THR-445 AND THR-480, MUTAGENESIS OF THR-445 AND THR-480. |
| [7] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-465, MASS SPECTROMETRY. Tissue: Epithelium. |
| [8] | "Phosphoproteomic analysis of synaptosomes from human cerebral cortex." DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P., Pant H.C., Dosemeci A. J. Proteome Res. 4:306-315(2005) [PubMed: 15822905] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-358, MASS SPECTROMETRY. Tissue: Brain cortex. |
| [9] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-707; SER-710 AND SER-716, MASS SPECTROMETRY. Tissue: Epithelium. |
| [10] | "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353; SER-355; SER-358 AND SER-465, MASS SPECTROMETRY. |
| [11] | "Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-358, MASS SPECTROMETRY. Tissue: Platelet. |
| [12] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-331; SER-334; SER-358; SER-431; SER-436 AND SER-465, MASS SPECTROMETRY. |
| [13] | "Human alpha-adducin gene, blood pressure, and sodium metabolism." Kamitani A., Wong Z.Y., Fraser R., Davies D.L., Connor J.M., Foy C.J., Watt G.C., Harrap S.B. Hypertension 32:138-143(1998) [PubMed: 9674650] [Abstract] Cited for: VARIANT TRP-460. |
| [14] | "Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis." Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A. Nat. Genet. 22:239-247(1999) [PubMed: 10391210] [Abstract] Cited for: VARIANTS TRP-460 AND CYS-586. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| X58141 mRNA. Translation: CAA41149.1. L29296 L29298 Genomic DNA. Translation: AAB05645.1. Z74617 Genomic DNA. Translation: CAA98970.1. Sequence problems. Z68280 Genomic DNA. No translation available. S70314 mRNA. Translation: AAB30914.2. | |
| IPI | IPI00019901. IPI00220158. IPI00253279. |
| PIR | S18207. |
| RefSeq | NP_001110.2. NP_054908.2. NP_054909.2. |
| UniGene | Hs.183706 Hs.701490 |
3D structure databases | |
| DisProt | DP00240. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P35611. |
PTM databases | |
| PhosphoSite | P35611. |
Proteomic databases | |
| PRIDE | P35611. |
Genome annotation databases | |
| Ensembl | ENST00000264758; ENSP00000264758; ENSG00000087274; Homo sapiens. [Genome view] ENST00000355842; ENSP00000348100; ENSG00000087274; Homo sapiens. [Genome view] ENST00000398123; ENSP00000381191; ENSG00000087274; Homo sapiens. [Genome view] ENST00000398124; ENSP00000381192; ENSG00000087274; Homo sapiens. [Genome view] ENST00000398125; ENSP00000381193; ENSG00000087274; Homo sapiens. [Genome view] ENST00000398129; ENSP00000381197; ENSG00000087274; Homo sapiens. [Genome view] ENST00000446856; ENSP00000399828; ENSG00000087274; Homo sapiens. [Genome view] |
| GeneID | 118. |
| KEGG | hsa:118. |
| UCSC | uc003gfp.1. human. uc003gfq.1. human. uc003gfr.1. human. |
Organism-specific databases | |
| CTD | 118. |
| GeneCards | GC04P002882. |
| HGNC | HGNC:243. ADD1. |
| HPA | CAB009794. |
| MIM | 102680. gene. |
| PharmGKB | PA31. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | P35611. |
| OMA | NSGRGDE. |
Enzyme and pathway databases | |
| Reactome | REACT_578. Apoptosis. |
Gene expression databases | |
| ArrayExpress | P35611. |
| Bgee | P35611. |
| CleanEx | HS_ADD1. |
| Genevestigator | P35611. |
Family and domain databases | |
| InterPro | IPR001303. Aldolase_II/adducin_N. [Graphical view] |
| Gene3D | G3DSA:3.40.225.10. Aldolase_II/adducin_N. 1 hit. |
| Pfam | PF00596. Aldolase_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 459. |
| PMAP-CutDB | P35611. |
| SOURCE | Search... |
Entry information
| Entry name | ADDA_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P35611 Secondary accession number(s): Q13734 Q9UJB6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| 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
| Human chromosome 4 Human chromosome 4: 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


