Q9QXZ0 (MACF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 127.
History...
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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Microtubule-actin cross-linking factor 1 Alternative name(s): Actin cross-linking family 7 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 7354 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Isoform 2 is a F-actin-binding protein which may play a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane. Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics. May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4. Plays a key role in wound healing and epidermal cell migration. Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate MT dynamics and polarize hair follicle stem cells. Ref.6 Ref.10 Ref.14 |
| Subunit structure | Isoform 2 interacts with AXIN1, LRP6 and GOLGA4 By similarity. Isoform 2 is found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B By similarity. Isoform 2 interacts with MAPRE1, CLASP1 AND CLASP2. Ref.10 |
| Subcellular location | Isoform 2: Cytoplasm. Cytoplasm › cytoskeleton. Golgi apparatus By similarity Ref.10 Ref.14. Cell membrane By similarity. Cell projection › ruffle membrane By similarity. Note: APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization By similarity. Localizes to the tips of microtubules. The phosphorylated form is found in the cytoplasm while the non-phosphorylated form associates with the microtubules. Ref.10 Ref.14 Isoform 1: Cytoplasm By similarity. Golgi apparatus By similarity Ref.10 Ref.14. |
| Tissue specificity | Enriched in the hair follicle stem cells (at protein level). Isoform 1 and isoform 2 are ubiquitous expressed, with higher levels seen in lung, heart, thymus, spleen and brain. Ref.2 Ref.6 Ref.14 |
| Developmental stage | Isoform 2 is highly expressed in neuronal tissues and the foregut of embryonic day 8.5 (E8.5) embryos and the head fold and primitive streak of E7.5 embryos (at protein level). Isoform 1 is expressed throughout the development of the embryo. Ref.6 |
| Domain | The C-terminal tail is required for phosphorylation by GSK3B and for microtubule-binding. |
| Post-translational modification | Phosphorylated on serine residues in the C-terminal tail by GSK3B. Phosphorylation inhibits microtubule-binding and this plays a critical role in bulge stem cell migration and skin wound repair. Wnt-signaling can repress phosphorylation. Ref.14 |
| Disruption phenotype | Mice die at the gastrulation stage and display developmental retardation at E7.5 with defects in the formation of the primitive streak, node, and mesoderm. Ref.6 |
| Sequence similarities | Belongs to the plakin or cytolinker family. Contains 1 actin-binding domain. Contains 2 CH (calponin-homology) domains. Contains 2 EF-hand domains. Contains 1 GAR domain. Contains 23 LRR (leucine-rich) repeats. Contains 10 plectin repeats. Contains 1 SH3 domain. Contains 17 spectrin repeats. |
| Sequence caution | The sequence AAC52989.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAM18553.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAM20969.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
Alternative products
| This entry describes 4 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9QXZ0-1) Also known as: Macf1b; 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: Q9QXZ0-2) Also known as: Macf1a; The sequence of this isoform differs from the canonical sequence as follows: 1543-3569: Missing. | ||||||
| Isoform 3 (identifier: Q9QXZ0-3) The sequence of this isoform differs from the canonical sequence as follows: 1-73: MSSSDEETLS...PAERAVVRVA → EKEFVQAYEDVLERYK 1543-3569: Missing. | ||||||
| Note: Incomplete sequence. | ||||||
| Isoform 4 (identifier: Q9QXZ0-4) The sequence of this isoform differs from the canonical sequence as follows: 1-181: MSSSDEETLS...LIWTIILHFQ → MGNSLGCVKE...SEEDGTLSLE 1543-3569: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 7354 | 7354 | Microtubule-actin cross-linking factor 1 | PRO_0000073451 | |||||
Regions | |||||||||
| Domain | 1 – 295 | 295 | Actin-binding | ||||||
| Domain | 78 – 181 | 104 | CH 1 | ||||||
| Repeat | 148 – 171 | 24 | LRR 1 | ||||||
| Domain | 194 – 295 | 102 | CH 2 | ||||||
| Repeat | 377 – 399 | 23 | LRR 3 | ||||||
| Repeat | 441 – 464 | 24 | LRR 4 | ||||||
| Domain | 871 – 923 | 53 | SH3 | ||||||
| Repeat | 1050 – 1073 | 24 | LRR 5 | ||||||
| Repeat | 1128 – 1154 | 27 | LRR 6 | ||||||
| Repeat | 1187 – 1210 | 24 | LRR 7 | ||||||
| Repeat | 1257 – 1282 | 26 | LRR 8 | ||||||
| Repeat | 1577 – 1619 | 43 | Plectin 1 | ||||||
| Repeat | 1654 – 1696 | 43 | Plectin 2 | ||||||
| Repeat | 1769 – 1809 | 41 | Plectin 3 | ||||||
| Repeat | 1811 – 1848 | 38 | Plectin 4 | ||||||
| Repeat | 1855 – 1885 | 31 | Plectin 5 | ||||||
| Repeat | 2276 – 2316 | 41 | Plectin 6 | ||||||
| Repeat | 2352 – 2393 | 42 | Plectin 7 | ||||||
| Repeat | 2394 – 2425 | 32 | Plectin 8 | ||||||
| Repeat | 2487 – 2528 | 42 | Plectin 9 | ||||||
| Repeat | 2671 – 2715 | 45 | Plectin 10 | ||||||
| Repeat | 3225 – 3244 | 20 | LRR 9 | ||||||
| Repeat | 3606 – 3630 | 25 | LRR 10 | ||||||
| Repeat | 3657 – 3681 | 25 | LRR 11 | ||||||
| Repeat | 3845 – 3920 | 76 | Spectrin 1 | ||||||
| Repeat | 3898 – 3920 | 23 | LRR 12 | ||||||
| Repeat | 3962 – 4070 | 109 | Spectrin 2 | ||||||
| Repeat | 4087 – 4112 | 26 | LRR 13 | ||||||
| Repeat | 4223 – 4249 | 27 | LRR 14 | ||||||
| Repeat | 4428 – 4536 | 109 | Spectrin 3 | ||||||
| Repeat | 4473 – 4496 | 24 | LRR 15 | ||||||
| Repeat | 4563 – 4583 | 21 | LRR 16 | ||||||
| Repeat | 4728 – 4751 | 24 | LRR 17 | ||||||
| Repeat | 4759 – 4863 | 105 | Spectrin 4 | ||||||
| Repeat | 5010 – 5035 | 26 | LRR 18 | ||||||
| Repeat | 5131 – 5153 | 23 | LRR 19 | ||||||
| Repeat | 5195 – 5300 | 106 | Spectrin 5 | ||||||
| Repeat | 5240 – 5263 | 24 | LRR 20 | ||||||
| Repeat | 5307 – 5409 | 103 | Spectrin 6 | ||||||
| Repeat | 5414 – 5506 | 93 | Spectrin 7 | ||||||
| Repeat | 5631 – 5735 | 105 | Spectrin 8 | ||||||
| Repeat | 5654 – 5678 | 25 | LRR 21 | ||||||
| Repeat | 5742 – 5844 | 103 | Spectrin 9 | ||||||
| Repeat | 5763 – 5787 | 25 | LRR 22 | ||||||
| Repeat | 5961 – 6066 | 106 | Spectrin 10 | ||||||
| Repeat | 6071 – 6175 | 105 | Spectrin 11 | ||||||
| Repeat | 6181 – 6284 | 104 | Spectrin 12 | ||||||
| Repeat | 6289 – 6395 | 107 | Spectrin 13 | ||||||
| Repeat | 6400 – 6503 | 104 | Spectrin 14 | ||||||
| Repeat | 6452 – 6475 | 24 | LRR 23 | ||||||
| Repeat | 6508 – 6614 | 107 | Spectrin 15 | ||||||
| Repeat | 6621 – 6722 | 102 | Spectrin 16 | ||||||
| Repeat | 6726 – 6830 | 105 | Spectrin 17 | ||||||
| Domain | 7001 – 7036 | 36 | EF-hand 1 | ||||||
| Domain | 7037 – 7072 | 36 | EF-hand 2 | ||||||
| Domain | 7077 – 7155 | 79 | GAR | ||||||
| Calcium binding | 7014 – 7025 | 12 | 1 Potential | ||||||
| Calcium binding | 7050 – 7061 | 12 | 2 Potential | ||||||
| Region | 7077 – 7354 | 278 | C-terminal tail | ||||||
| Region | 7279 – 7294 | 16 | 4 X 4 AA tandem repeats of [GS]-S-R-[AR] | ||||||
| Compositional bias | 700 – 703 | 4 | Poly-Glu | ||||||
| Compositional bias | 1414 – 1417 | 4 | Poly-Glu | ||||||
| Compositional bias | 1986 – 1989 | 4 | Poly-Leu | ||||||
| Compositional bias | 3521 – 3576 | 56 | Gln-rich | ||||||
| Compositional bias | 7188 – 7325 | 138 | Ser-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 280 | 1 | Phosphoserine Ref.7 Ref.8 Ref.9 | ||||||
| Modified residue | 1376 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 3889 | 1 | Phosphoserine Ref.7 Ref.9 Ref.12 | ||||||
| Modified residue | 4458 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 4483 | 1 | Phosphoserine Ref.9 Ref.13 | ||||||
| Modified residue | 4921 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 5988 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 6166 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 6923 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 7220 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 7258 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 7296 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 7299 | 1 | Phosphoserine Ref.11 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 181 | 181 | MSSSD…ILHFQ → MGNSLGCVKEPKESIAVPEK APISPKKRVRFKRKWRGKKI LTPEASHREEALEGTGVIEE TETLTKLTARLPKEPGVGGA EHPPSDIFLPGDSAPNSGVG DQGMIVQVKESFQAEIQTAH LLLENESSVVGGAWDSLEEG MTVIAHLLDNPAERNCEKSV SQLVEFPRTASCSSRAVLLP LQGETAVEQGGTLLRHRHRS STLPRTDYPSETVDQDQPSE GWSVGGRTKSVPSAPPTGSW IAKCSVASSIPKQSGDPIHT EPTHVGLVSCKGPIMPASQS DLSVSGITVSILPSSSGYGS DGLRLHGIRPEDTEPEKTST PFSEEDGTLSLE in isoform 4. | VSP_041394 | |||||
| Alternative sequence | 1 – 73 | 73 | MSSSD…VVRVA → EKEFVQAYEDVLERYK in isoform 3. | VSP_041395 | |||||
| Alternative sequence | 1543 – 3569 | 2027 | Missing in isoform 2, isoform 3 and isoform 4. | VSP_041396 | |||||
Experimental info | |||||||||
| Sequence conflict | 242 | 1 | D → N in AAD32244. Ref.1 | ||||||
| Sequence conflict | 242 | 1 | D → N in AAC52988. Ref.4 | ||||||
| Sequence conflict | 242 | 1 | D → N in AAC52989. Ref.4 | ||||||
| Sequence conflict | 242 | 1 | D → N in AAC52990. Ref.4 | ||||||
| Sequence conflict | 393 | 1 | P → L in AAD32244. Ref.1 | ||||||
| Sequence conflict | 393 | 1 | P → L in AAY78553. Ref.2 | ||||||
| Sequence conflict | 393 | 1 | P → L in AAC52988. Ref.4 | ||||||
| Sequence conflict | 393 | 1 | P → L in AAC52989. Ref.4 | ||||||
| Sequence conflict | 794 | 1 | D → N in AAY78553. Ref.2 | ||||||
| Sequence conflict | 815 | 1 | C → A in AAD32244. Ref.1 | ||||||
| Sequence conflict | 815 | 1 | C → A in AAC52988. Ref.4 | ||||||
| Sequence conflict | 815 | 1 | C → A in AAC52989. Ref.4 | ||||||
| Sequence conflict | 815 | 1 | C → A in AAC52990. Ref.4 | ||||||
| Sequence conflict | 928 | 1 | E → G in AAD32244. Ref.1 | ||||||
| Sequence conflict | 928 | 1 | E → G in AAY78553. Ref.2 | ||||||
| Sequence conflict | 3795 | 1 | V → A in AAD32244. Ref.1 | ||||||
| Sequence conflict | 3795 | 1 | V → A in AAY78553. Ref.2 | ||||||
| Sequence conflict | 3909 | 1 | Q → H in AAC52988. Ref.4 | ||||||
| Sequence conflict | 3909 | 1 | Q → H in AAC52989. Ref.4 | ||||||
| Sequence conflict | 3909 | 1 | Q → H in AAC52990. Ref.4 | ||||||
| Sequence conflict | 4735 | 1 | A → V in AAD32244. Ref.1 | ||||||
| Sequence conflict | 4735 | 1 | A → V in AAY78553. Ref.2 | ||||||
| Sequence conflict | 4750 | 1 | N → S in AAD32244. Ref.1 | ||||||
| Sequence conflict | 4750 | 1 | N → S in AAY78553. Ref.2 | ||||||
| Sequence conflict | 4891 | 1 | S → F in AAD32244. Ref.1 | ||||||
| Sequence conflict | 4891 | 1 | S → F in AAY78553. Ref.2 | ||||||
| Sequence conflict | 5587 | 1 | A → V in AAD32244. Ref.1 | ||||||
| Sequence conflict | 5587 | 1 | A → V in AAY78553. Ref.2 | ||||||
| Sequence conflict | 5603 | 1 | L → R in AAD32244. Ref.1 | ||||||
| Sequence conflict | 5603 | 1 | L → R in AAY78553. Ref.2 | ||||||
| Sequence conflict | 5971 | 1 | A → V in AAD32244. Ref.1 | ||||||
| Sequence conflict | 5971 | 1 | A → V in AAY78553. Ref.2 | ||||||
| Sequence conflict | 6309 | 1 | N → T in AAD32244. Ref.1 | ||||||
| Sequence conflict | 6309 | 1 | N → T in AAY78553. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons." Leung C.L., Sun D., Zheng M., Knowles D.R., Liem R.K.H. J. Cell Biol. 147:1275-1286(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: BALB/c. |
| [2] | "Microtubule actin crosslinking factor 1b: a novel plakin that localizes to the Golgi complex." Lin C.-M., Chen H.-J., Leung C.L., Parry D.A.D., Liem R.K.H. J. Cell Sci. 118:3727-3738(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Strain: BALB/c. |
| [3] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.  Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [4] | "Cloning and characterization of mouse ACF7, a novel member of the dystonin subfamily of actin binding proteins." Bernier G., Mathieu M., De Repentigny Y., Vidal S.M., Kothary R. Genomics 38:19-29(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-3909 (ISOFORMS 2 AND 4), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Strain: BALB/c. Tissue: Brain. |
| [5] | Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 881-888; 5824-5832 AND 6671-6678, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain. |
| [6] | "The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt signaling pathway." Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K. Genes Dev. 20:1933-1945(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY. |
| [7] | "Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-3889, MASS SPECTROMETRY. Tissue: Brain. |
| [8] | "Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, MASS SPECTROMETRY. Tissue: Liver. |
| [9] | "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-3889; SER-4483 AND SER-5988, MASS SPECTROMETRY. Tissue: Brain cortex. |
| [10] | "ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has ATPase activity." Wu X., Kodama A., Fuchs E. Cell 135:137-148(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAPRE1; CLASP1 AND CLASP2. |
| [11] | "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7296 AND SER-7299, MASS SPECTROMETRY. Tissue: Liver. |
| [12] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3889, MASS SPECTROMETRY. Tissue: Melanoma. |
| [13] | "The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4483, MASS SPECTROMETRY. Tissue: Macrophage. |
| [14] | "Skin stem cells orchestrate directional migration by regulating microtubule-ACF7 connections through GSK3beta." Wu X., Shen Q.T., Oristian D.S., Lu C.P., Zheng Q., Wang H.W., Fuchs E. Cell 144:341-352(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF150755 mRNA. Translation: AAD32244.1. DQ067088 mRNA. Translation: AAY78553.1. AL606932, AL606918 Genomic DNA. Translation: CAM18553.1. Sequence problems. AL606918, AL606932 Genomic DNA. Translation: CAM20969.1. Sequence problems. U67203 mRNA. Translation: AAC52988.1. U67204 mRNA. Translation: AAC52989.1. Different initiation. U67205 mRNA. Translation: AAC52990.1. |
| IPI | IPI00229613. IPI00405977. IPI00884482. IPI01019257. |
| PIR | T30847. T30849. T42725. |
| UniGene | Mm.402299. Mm.485351. |
3D structure databases | |
| ProteinModelPortal | Q9QXZ0. |
| SMR | Q9QXZ0. Positions 69-298. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9QXZ0. 7 interactions. |
| MINT | MINT-1634787. |
| STRING | 10090.ENSMUSP00000081324. |
PTM databases | |
| PhosphoSite | Q9QXZ0. |
Proteomic databases | |
| PaxDb | Q9QXZ0. |
| PRIDE | Q9QXZ0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| KEGG | mmu:11426. |
Organism-specific databases | |
| CTD | 23499. |
| MGI | MGI:108559. Macf1. |
Phylogenomic databases | |
| eggNOG | COG5069. |
| GeneTree | ENSGT00700000104214. |
| HOGENOM | HOG000049054. |
| HOVERGEN | HBG031127. |
| InParanoid | Q4PLL5. |
Gene expression databases | |
| ArrayExpress | Q9QXZ0. |
| Bgee | Q9QXZ0. |
| CleanEx | MM_MACF1. |
| Genevestigator | Q9QXZ0. |
| GermOnline | ENSMUSG00000028649. Mus musculus. |
Family and domain databases | |
| Gene3D | 1.10.238.10. 1 hit. 1.10.418.10. 2 hits. 3.30.920.20. 1 hit. |
| InterPro | IPR001589. Actinin_actin-bd_CS. IPR001715. CH-domain. IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR003108. GAS2_dom. IPR001101. Plectin_repeat. IPR018159. Spectrin/alpha-actinin. IPR002017. Spectrin_repeat. [Graphical view] |
| Pfam | PF00307. CH. 2 hits. PF13499. EF_hand_5. 1 hit. PF02187. GAS2. 1 hit. PF00681. Plectin. 10 hits. PF00435. Spectrin. 18 hits. [Graphical view] |
| SMART | SM00033. CH. 2 hits. SM00054. EFh. 2 hits. SM00243. GAS2. 1 hit. SM00250. PLEC. 19 hits. SM00150. SPEC. 34 hits. [Graphical view] |
| SUPFAM | SSF47576. Calponin-homology. 1 hit. SSF143575. SSF143575. 1 hit. |
| PROSITE | PS00019. ACTININ_1. 1 hit. PS00020. ACTININ_2. 1 hit. PS50021. CH. 2 hits. PS00018. EF_HAND_1. 2 hits. PS50222. EF_HAND_2. 2 hits. PS51460. GAR. 1 hit. PS50002. SH3. False negative. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | MACF1. mouse. |
| NextBio | 278682. |
| SOURCE | Search... |
Entry information
| Entry name | MACF1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9QXZ0 Secondary accession number(s): B1ARU3 Q4PLL5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |