Q08495 (DEMA_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 124.
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: Dematin Alternative name(s): Erythrocyte membrane protein band 4.9 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 405 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Actin-bundling protein. May function in mitogen-activated protein kinase pathway. Ref.6 |
| Subunit structure | Exists in solution as a trimer of two short isoforms and one long isoform linked by disulfide bonds Probable. Interacts with RASGRF2. Ref.2 Ref.6 |
| Subcellular location | |
| Tissue specificity | Heart, brain, lung, skeletal muscle, and kidney. |
| Domain | Contains at least two actin-binding sites, one in the headpiece domain and one in the amino-terminal portion. Consists of a large core fragment, the amino-terminal portion, and a small headpiece, the C-terminal portion. The headpiece can bind but cannot bundle actin filaments. |
| Post-translational modification | Actin-bundling activity is abolished upon phosphorylation by cAMP-dependent protein kinase. The N-terminus is blocked. |
| Sequence similarities | Belongs to the villin/gelsolin family. Contains 1 HP (headpiece) domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat |
| Ligand | Actin-binding |
| Molecular function | Actin capping |
| PTM | Disulfide bond Phosphoprotein |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | actin filament bundle assembly Traceable author statement Ref.2. Source: UniProtKB actin filament cappingInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | actin cytoskeleton Traceable author statement Ref.1. Source: UniProtKB nucleusInferred from direct assay. Source: HPA |
| Molecular function | actin binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform Long (identifier: Q08495-1) 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 Short (identifier: Q08495-2) The sequence of this isoform differs from the canonical sequence as follows: 320-341: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||
Molecule processing | ||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 405 | 405 | Dematin | PRO_0000218755 | ||||||||||||||||||
Regions | ||||||||||||||||||||||
| Domain | 337 – 405 | 69 | HP | |||||||||||||||||||
| Region | 224 – 308 | 85 | Interaction with RASGRF2 | |||||||||||||||||||
| Compositional bias | 216 – 222 | 7 | Poly-Glu | |||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||
| Modified residue | 10 | 1 | Phosphothreonine Ref.7 | |||||||||||||||||||
| Modified residue | 14 | 1 | Phosphoserine Ref.7 | |||||||||||||||||||
| Modified residue | 16 | 1 | Phosphoserine Ref.7 | |||||||||||||||||||
| Modified residue | 22 | 1 | Phosphoserine Ref.7 | |||||||||||||||||||
| Modified residue | 26 | 1 | Phosphoserine Ref.7 | |||||||||||||||||||
| Modified residue | 28 | 1 | Phosphoserine Ref.7 | |||||||||||||||||||
| Modified residue | 87 | 1 | Phosphoserine By similarity | |||||||||||||||||||
| Modified residue | 91 | 1 | Phosphothreonine By similarity | |||||||||||||||||||
| Modified residue | 92 | 1 | Phosphoserine Ref.7 | |||||||||||||||||||
| Modified residue | 96 | 1 | Phosphoserine Ref.7 Ref.10 | |||||||||||||||||||
| Modified residue | 105 | 1 | Phosphoserine Ref.7 Ref.10 | |||||||||||||||||||
| Modified residue | 156 | 1 | Phosphoserine Ref.7 | |||||||||||||||||||
| Modified residue | 226 | 1 | Phosphoserine Ref.7 Ref.8 Ref.9 | |||||||||||||||||||
| Modified residue | 289 | 1 | Phosphoserine Ref.7 | |||||||||||||||||||
| Modified residue | 333 | 1 | Phosphoserine Ref.7 | |||||||||||||||||||
| Modified residue | 372 | 1 | Phosphoserine Ref.7 | |||||||||||||||||||
| Modified residue | 403 | 1 | Phosphoserine; by PKA Ref.12 | |||||||||||||||||||
Natural variations | ||||||||||||||||||||||
| Alternative sequence | 320 – 341 | 22 | Missing in isoform Short. | VSP_004189 | ||||||||||||||||||
Experimental info | ||||||||||||||||||||||
| Sequence conflict | 81 | 1 | S → Q in AAA58438. Ref.1 | |||||||||||||||||||
| Sequence conflict | 81 | 1 | S → Q in AAC50223. Ref.2 | |||||||||||||||||||
| Sequence conflict | 292 | 1 | A → R in AAA58438. Ref.1 | |||||||||||||||||||
| Sequence conflict | 292 | 1 | A → R in AAC50223. Ref.2 | |||||||||||||||||||
| Sequence conflict | 347 | 1 | M → V in AAA58438. Ref.1 | |||||||||||||||||||
| Sequence conflict | 380 | 1 | F → S in AAA58438. Ref.1 | |||||||||||||||||||
Secondary structure | ||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||
| Turn | 346 – 348 | 3 | ||||||||||||||||||||
| Helix | 364 – 366 | 3 | ||||||||||||||||||||
| Helix | 368 – 370 | 3 | ||||||||||||||||||||
| Helix | 373 – 379 | 7 | ||||||||||||||||||||
| Beta strand | 380 – 382 | 3 | ||||||||||||||||||||
| Helix | 384 – 389 | 6 | ||||||||||||||||||||
| Helix | 392 – 402 | 11 | ||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning of human erythroid dematin reveals another member of the villin family." Rana A.P., Ruff P., Maalouf G.J., Speicher D.W., Chishti A.H. Proc. Natl. Acad. Sci. U.S.A. 90:6651-6655(1993) [PubMed: 8341682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), PARTIAL PROTEIN SEQUENCE. Tissue: Reticulocyte. |
| [2] | "Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily." Azim A.C., Knoll J.H.M., Beggs A.H., Chishti A.H. J. Biol. Chem. 270:17407-17413(1995) [PubMed: 7615546] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PHOSPHORYLATION BY CAPK, SUBUNIT, ALTERNATIVE SPLICING. Tissue: Reticulocyte. |
| [3] | "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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT). Tissue: Amygdala and Kidney. |
| [4] | "Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). |
| [5] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT). Tissue: Brain and Liver. |
| [6] | "Dematin interacts with the Ras-guanine nucleotide exchange factor Ras-GRF2 and modulates mitogen-activated protein kinase pathways." Lutchman M., Kim A.C., Cheng L., Whitehead I.P., Oh S.S., Hanspal M., Boukharov A.A., Hanada T., Chishti A.H. Eur. J. Biochem. 269:638-649(2002) [PubMed: 11856323] [Abstract] Cited for: FUNCTION, INTERACTION WITH RASGRF2, SUBCELLULAR LOCATION. |
| [7] | "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 THR-10; SER-14; SER-16; SER-22; SER-26; SER-28; SER-92; SER-96; SER-105; SER-156; SER-226; SER-289; SER-333 AND SER-372, MASS SPECTROMETRY. Tissue: Platelet. |
| [8] | "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, MASS SPECTROMETRY. Tissue: T-cell. |
| [9] | "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, MASS SPECTROMETRY. Tissue: Liver. |
| [10] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-105, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [11] | "The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site." Frank B.S., Vardar D., Chishti A.H., McKnight C.J. J. Biol. Chem. 279:7909-7916(2004) [PubMed: 14660664] [Abstract] Cited for: STRUCTURE BY NMR OF 342-405. |
| [12] | "A phosphorylation-induced conformation change in dematin headpiece." Jiang Z.G., McKnight C.J. Structure 14:379-387(2006) [PubMed: 16472756] [Abstract] Cited for: STRUCTURE BY NMR OF 342-405, PHOSPHORYLATION AT SER-403. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | L19713 mRNA. Translation: AAA58438.1. U28389 mRNA. Translation: AAC50223.1. AK055842 mRNA. Translation: BAG51582.1. AK289650 mRNA. Translation: BAF82339.1. BT007396 mRNA. Translation: AAP36060.1. BC006318 mRNA. Translation: AAH06318.1. BC017445 mRNA. Translation: AAH17445.1. BC052805 mRNA. Translation: AAH52805.1. | ||||||||||||||||||
| IPI | IPI00292290. IPI01015007. | ||||||||||||||||||
| PIR | A48222. I39062. | ||||||||||||||||||
| RefSeq | NP_001107607.1. NM_001114135.2. NP_001107608.1. NM_001114136.1. NP_001107609.1. NM_001114137.1. NP_001107610.1. NM_001114138.1. NP_001107611.1. NM_001114139.1. NP_001969.2. NM_001978.2. | ||||||||||||||||||
| UniGene | Hs.106124. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q08495. | ||||||||||||||||||
| SMR | Q08495. Positions 341-405. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | Q08495. 4 interactions. | ||||||||||||||||||
| MINT | MINT-1390442. | ||||||||||||||||||
| STRING | Q08495. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | Q08495. | ||||||||||||||||||
Polymorphism databases | |||||||||||||||||||
| DMDM | 22654240. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | Q08495. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000265800; ENSP00000265800; ENSG00000158856. ENST00000358242; ENSP00000350977; ENSG00000158856. ENST00000432128; ENSP00000416111; ENSG00000158856. | ||||||||||||||||||
| GeneID | 2039. | ||||||||||||||||||
| KEGG | hsa:2039. | ||||||||||||||||||
| UCSC | uc010ltr.1. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 2039. | ||||||||||||||||||
| GeneCards | GC08P021906. | ||||||||||||||||||
| H-InvDB | HIX0007358. | ||||||||||||||||||
| HGNC | HGNC:3382. EPB49. | ||||||||||||||||||
| HPA | HPA024290. | ||||||||||||||||||
| MIM | 125305. gene. | ||||||||||||||||||
| neXtProt | NX_Q08495. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | prNOG15761. | ||||||||||||||||||
| GeneTree | ENSGT00570000079028. | ||||||||||||||||||
| HOVERGEN | HBG031499. | ||||||||||||||||||
| OMA | PSYGRTT. | ||||||||||||||||||
| OrthoDB | EOG4XD3RG. | ||||||||||||||||||
| PhylomeDB | Q08495. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | Q08495. | ||||||||||||||||||
| Bgee | Q08495. | ||||||||||||||||||
| CleanEx | HS_EPB49. | ||||||||||||||||||
| Genevestigator | Q08495. | ||||||||||||||||||
| GermOnline | ENSG00000158856. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR003128. Villin_headpiece. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:1.10.950.10. VHP. 1 hit. | ||||||||||||||||||
| Pfam | PF02209. VHP. 1 hit. [Graphical view] | ||||||||||||||||||
| SMART | SM00153. VHP. 1 hit. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF47050. VHP. 1 hit. | ||||||||||||||||||
| PROSITE | PS51089. HP. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| NextBio | 8281. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | DEMA_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q08495 Secondary accession number(s): A8K0T5 Q9BRE3 | ||||||||
| 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
| Human chromosome 8 Human chromosome 8: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with