Q9UPN3 (MACF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 130.
History...
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Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 Alternative name(s): 620 kDa actin-binding protein Short name=ABP620 Actin cross-linking family protein 7 Macrophin-1 Trabeculin-alpha | ||||
| 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 | 7388 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 By similarity. Ref.9 Ref.15 |
| Subunit structure | Isoform 2 interacts with MAPRE1, CLASP1, CLASP2, AXIN1 and LRP6 By similarity. Isoform 2 is found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B By similarity. Isoform 2 interacts with GOLGA4. Ref.9 |
| Subcellular location | Isoform 2: Cytoplasm › cytoskeleton. Cytoplasm. Golgi apparatus. Cell membrane. Cell projection › ruffle membrane. Note: The phosphorylated form is found in the cytoplasm while the non-phosphorylated form associates with the microtubules By similarity. Localizes to the tips of microtubules. APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization. Ref.9 Ref.10 Ref.15 Isoform 1: Cytoplasm. Golgi apparatus. Note: Localizes to the tips of microtubules. Ref.9 Ref.10 Ref.15 |
| Tissue specificity | Isoform 2 is ubiquitously expressed. Isoform 1 is expressed in cell lines NCI-H460, A-549 and HaCaT. Isoform 4 is expressed in heart, lung, pituitary and placenta, not found in brain, kidney, liver, pancreas or skeletal muscle. Ref.3 Ref.10 |
| Domain | The C-terminal tail is required for phosphorylation by GSK3B and for microtubule-binding By similarity. |
| 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 By similarity. |
| 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 24 LRR (leucine-rich) repeats. Contains 11 plectin repeats. Contains 1 SH3 domain. Contains 17 spectrin repeats. |
| Sequence caution | The sequence BAA83821.1 differs from that shown. Reason: Frameshift at positions 575 and 594. The sequence CAH70156.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAH73668.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI16417.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI21814.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| DISC1 | Q9NRI5 | 5 | EBI-522925,EBI-529989 |
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9UPN3-1) 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: Q9UPN3-2) Also known as: Macf1a; The sequence of this isoform differs from the canonical sequence as follows: 1543-3609: Missing. 5497-5497: K → KALEEDIENH...VLHRQHADHL | ||||||
| Isoform 3 (identifier: Q9UPN3-3) The sequence of this isoform differs from the canonical sequence as follows: 1-72: MSSSDEETLS...DPAERAVVRV → MFPVLWAGIP...CTSASRVAVI 1543-3609: Missing. 4410-4430: Missing. 5497-5497: K → KALEEDIENH...VLHRQHADHL | ||||||
| Isoform 5 (identifier: Q9UPN3-4) The sequence of this isoform differs from the canonical sequence as follows: 1543-3609: Missing. 4410-4430: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 4 (identifier: Q9UPN3-5) The sequence of this isoform differs from the canonical sequence as follows: 1-1565: Missing. 5497-5497: K → KALEEDIENH...VLHRQHADHL 7150-7150: R → RFFLGNQ |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 7388 | 7388 | Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 | PRO_0000073449 | |||||
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 | 240 – 264 | 25 | LRR 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 – 1621 | 45 | Plectin 1 | ||||||
| Repeat | 1654 – 1696 | 43 | Plectin 2 | ||||||
| Repeat | 1769 – 1809 | 41 | Plectin 3 | ||||||
| Repeat | 1811 – 1848 | 38 | Plectin 4 | ||||||
| Repeat | 1855 – 1886 | 32 | Plectin 5 | ||||||
| Repeat | 2290 – 2332 | 43 | Plectin 6 | ||||||
| Repeat | 2367 – 2410 | 44 | Plectin 7 | ||||||
| Repeat | 2411 – 2437 | 27 | Plectin 8 | ||||||
| Repeat | 2501 – 2543 | 43 | Plectin 9 | ||||||
| Repeat | 2581 – 2612 | 32 | Plectin 10 | ||||||
| Repeat | 2686 – 2730 | 45 | Plectin 11 | ||||||
| Repeat | 3239 – 3262 | 24 | LRR 9 | ||||||
| Repeat | 3264 – 3283 | 20 | LRR 10 | ||||||
| Repeat | 3646 – 3669 | 24 | LRR 11 | ||||||
| Repeat | 3696 – 3720 | 25 | LRR 12 | ||||||
| Repeat | 3883 – 3957 | 75 | Spectrin 1 | ||||||
| Repeat | 3936 – 3958 | 23 | LRR 13 | ||||||
| Repeat | 4000 – 4108 | 109 | Spectrin 2 | ||||||
| Repeat | 4125 – 4150 | 26 | LRR 14 | ||||||
| Repeat | 4261 – 4287 | 27 | LRR 15 | ||||||
| Repeat | 4466 – 4574 | 109 | Spectrin 3 | ||||||
| Repeat | 4511 – 4534 | 24 | LRR 16 | ||||||
| Repeat | 4601 – 4624 | 24 | LRR 17 | ||||||
| Repeat | 4769 – 4792 | 24 | LRR 18 | ||||||
| Repeat | 4800 – 4904 | 105 | Spectrin 4 | ||||||
| Repeat | 4909 – 5012 | 104 | Spectrin 5 | ||||||
| Repeat | 5051 – 5076 | 26 | LRR 19 | ||||||
| Repeat | 5172 – 5194 | 23 | LRR 20 | ||||||
| Repeat | 5236 – 5341 | 106 | Spectrin 6 | ||||||
| Repeat | 5281 – 5304 | 24 | LRR 21 | ||||||
| Repeat | 5348 – 5450 | 103 | Spectrin 7 | ||||||
| Repeat | 5455 – 5557 | 103 | Spectrin 8 | ||||||
| Repeat | 5695 – 5719 | 25 | LRR 22 | ||||||
| Repeat | 5783 – 5885 | 103 | Spectrin 9 | ||||||
| Repeat | 5804 – 5828 | 25 | LRR 23 | ||||||
| Repeat | 6005 – 6110 | 106 | Spectrin 10 | ||||||
| Repeat | 6115 – 6219 | 105 | Spectrin 11 | ||||||
| Repeat | 6225 – 6328 | 104 | Spectrin 12 | ||||||
| Repeat | 6333 – 6439 | 107 | Spectrin 13 | ||||||
| Repeat | 6443 – 6547 | 105 | Spectrin 14 | ||||||
| Repeat | 6496 – 6519 | 24 | LRR 24 | ||||||
| Repeat | 6552 – 6658 | 107 | Spectrin 15 | ||||||
| Repeat | 6665 – 6766 | 102 | Spectrin 16 | ||||||
| Repeat | 6771 – 6874 | 104 | Spectrin 17 | ||||||
| Domain | 7041 – 7076 | 36 | EF-hand 1 | ||||||
| Domain | 7077 – 7112 | 36 | EF-hand 2 | ||||||
| Domain | 7117 – 7189 | 73 | GAR | ||||||
| Calcium binding | 7054 – 7065 | 12 | 1 Potential | ||||||
| Calcium binding | 7090 – 7101 | 12 | 2 Potential | ||||||
| Region | 7117 – 7388 | 272 | C-terminal tail By similarity | ||||||
| Region | 7313 – 7328 | 16 | 4 X 4 AA tandem repeats of [GS]-S-R-[AR] | ||||||
| Compositional bias | 698 – 703 | 6 | Poly-Glu | ||||||
| Compositional bias | 1122 – 1127 | 6 | Poly-Ser | ||||||
| Compositional bias | 1414 – 1417 | 4 | Poly-Glu | ||||||
| Compositional bias | 1986 – 1989 | 4 | Poly-Leu | ||||||
| Compositional bias | 7222 – 7351 | 130 | Ser-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 280 | 1 | Phosphoserine Ref.16 Ref.18 | ||||||
| Modified residue | 1376 | 1 | Phosphoserine Ref.12 Ref.13 Ref.16 Ref.18 | ||||||
| Modified residue | 3927 | 1 | Phosphoserine Ref.12 Ref.16 Ref.18 | ||||||
| Modified residue | 4495 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 4496 | 1 | Phosphoserine Ref.12 Ref.18 | ||||||
| Modified residue | 4521 | 1 | Phosphoserine Ref.11 Ref.13 Ref.16 Ref.18 | ||||||
| Modified residue | 4962 | 1 | Phosphoserine Ref.18 | ||||||
| Modified residue | 6032 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 6210 | 1 | N6-acetyllysine Ref.14 | ||||||
| Modified residue | 6967 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 7254 | 1 | Phosphothreonine Ref.12 | ||||||
| Modified residue | 7292 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 7330 | 1 | Phosphoserine Ref.12 Ref.13 | ||||||
| Modified residue | 7333 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 1565 | 1565 | Missing in isoform 4. | VSP_043626 | |||||
| Alternative sequence | 1 – 72 | 72 | MSSSD…AVVRV → MFPVLWAGIPGRDVGSLQPL PPGFKQFCTSASRVAVI in isoform 3. | VSP_041390 | |||||
| Alternative sequence | 1543 – 3609 | 2067 | Missing in isoform 2, isoform 3 and isoform 5. | VSP_041391 | |||||
| Alternative sequence | 4410 – 4430 | 21 | Missing in isoform 3 and isoform 5. | VSP_041392 | |||||
| Alternative sequence | 5497 | 1 | K → KALEEDIENHATDVHQAVKI GQSLSSLTSPAEQGVLSEKI DSLQARYSEIQDRCCRKAAL LDQALSNARLFGEDEVEVLN WLAEVEDKLSSVFVKDFKQD VLHRQHADHL in isoform 2, isoform 3 and isoform 4. | VSP_041393 | |||||
| Alternative sequence | 7150 | 1 | R → RFFLGNQ in isoform 4. | VSP_043627 | |||||
| Natural variant | 302 | 1 | E → V in a breast cancer sample; somatic mutation. Ref.19 | VAR_035451 | |||||
| Natural variant | 4357 | 1 | M → V. Ref.2 Corresponds to variant rs2296172 [ dbSNP | Ensembl ]. | VAR_048625 | |||||
| Natural variant | 6201 | 1 | K → R. Corresponds to variant rs682351 [ dbSNP | Ensembl ]. | VAR_048626 | |||||
| Natural variant | 6308 | 1 | A → T. Corresponds to variant rs587404 [ dbSNP | Ensembl ]. | VAR_048627 | |||||
| Natural variant | 6462 | 1 | E → Q in a breast cancer sample; somatic mutation. Ref.19 | VAR_035452 | |||||
| Natural variant | 6628 | 1 | S → T. Ref.2 Ref.3 Corresponds to variant rs668556 [ dbSNP | Ensembl ]. | VAR_048628 | |||||
| Natural variant | 6752 | 1 | T → I. Corresponds to variant rs2296174 [ dbSNP | Ensembl ]. | VAR_048629 | |||||
| Natural variant | 6855 | 1 | I → V. Corresponds to variant rs12068423 [ dbSNP | Ensembl ]. | VAR_048630 | |||||
| Natural variant | 7093 | 1 | G → E in a breast cancer sample; somatic mutation. Ref.19 | VAR_065256 | |||||
Experimental info | |||||||||
| Sequence conflict | 1295 – 1296 | 2 | TA → LP in AAL39000. Ref.4 | ||||||
| Sequence conflict | 1487 | 1 | T → A in BAA83821. Ref.1 | ||||||
| Sequence conflict | 1487 | 1 | T → A in AAL39000. Ref.4 | ||||||
| Sequence conflict | 3277 | 1 | P → S in AAL38997. Ref.3 | ||||||
| Sequence conflict | 4030 | 1 | V → A in BAA83821. Ref.1 | ||||||
| Sequence conflict | 4119 | 1 | E → D in BAA83821. Ref.1 | ||||||
| Sequence conflict | 4150 | 1 | E → K in AAF06360. Ref.2 | ||||||
| Sequence conflict | 4388 | 1 | C → Y in BAA83821. Ref.1 | ||||||
| Sequence conflict | 4411 – 4417 | 7 | SILPSVG → EYRLFKI in BAA86565. Ref.5 | ||||||
| Sequence conflict | 4590 | 1 | R → Q in BAA83821. Ref.1 | ||||||
| Sequence conflict | 6791 | 1 | Missing in AAF06360. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning of macrophin, a human homologue of Drosophila kakapo with a close structural similarity to plectin and dystrophin." Okuda T., Matsuda S., Nakatsugawa S., Ichigotani Y., Iwahashi N., Takahashi M., Ishigaki T., Hamaguchi M. Biochem. Biophys. Res. Commun. 264:568-574(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). |
| [2] | "Molecular cloning and characterization of human trabeculin-alpha, a giant protein defining a new family of actin-binding proteins." Sun Y., Zhang J., Kraeft S.-K., Auclair D., Chang M.-S., Liu Y., Sutherland R., Salgia R., Griffin J.D., Ferland L.H., Chen L.B. J. Biol. Chem. 274:33522-33530(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANTS VAL-4357 AND THR-6628. |
| [3] | "MACF1 gene structure: a hybrid of plectin and dystrophin." Gong T.-W.L., Besirli C.G., Lomax M.I. Mamm. Genome 12:852-861(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-6770 (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, VARIANT THR-6628. |
| [4] | "The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.  Bentley D.R.Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O. DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 868-4417 (ISOFORM 2). Tissue: Brain. |
| [6] | "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain." Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O. DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 868-7388 (ISOFORM 5). Tissue: Brain. |
| [7] | "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION. |
| [8] | Ohara O. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| [9] | "Interaction between p230 and MACF1 is associated with transport of a glycosyl phosphatidyl inositol-anchored protein from the Golgi to the cell periphery." Kakinuma T., Ichikawa H., Tsukada Y., Nakamura T., Toh B.H. Exp. Cell Res. 298:388-398(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GOLGA4. |
| [10] | "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: IDENTIFICATION OF ISOFORM 1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. |
| [11] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4521, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1376; SER-3927; SER-4495; SER-4496; SER-6967; THR-7254; SER-7292 AND SER-7330, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [13] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1376; SER-4521 AND SER-7330, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [14] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6210, MASS SPECTROMETRY. |
| [15] | "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells." Zaoui K., Benseddik K., Daou P., Salaun D., Badache A. Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION. |
| [16] | "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-1376; SER-3927 AND SER-4521, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [17] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [18] | "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-1376; SER-3927; SER-4496; SER-4521 AND SER-4962, MASS SPECTROMETRY. |
| [19] | "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: VARIANTS [LARGE SCALE ANALYSIS] VAL-302; GLN-6462 AND GLU-7093. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB029290 mRNA. Translation: BAA83821.1. Frameshift. AF141968 mRNA. Translation: AAF06360.1. AF317696 mRNA. Translation: AAL09459.1. AF325341 AF325340 Genomic DNA. Translation: AAL38997.1.AF325341 AF325340 Genomic DNA. Translation: AAL39000.1.AL442071 AL365277 Genomic DNA. Translation: CAH73668.1. Sequence problems.AL442071, AL137853, AL365277 Genomic DNA. Translation: CAH73671.1. AL137853 AL442071 Genomic DNA. Translation: CAI21814.1. Sequence problems.AL137853, AL365277, AL442071 Genomic DNA. Translation: CAI21816.1. AL365277 AL442071 Genomic DNA. Translation: CAI16417.1. Sequence problems.AL365277, AL137853, AL442071 Genomic DNA. Translation: CAI16422.1. AL355477 AL442071 Genomic DNA. Translation: CAH70156.1. Sequence problems.AL356055 Genomic DNA. No translation available. AB033077 mRNA. Translation: BAA86565.1. AB007934 mRNA. Translation: BAA32310.3. |
| IPI | IPI00256861. IPI00432363. IPI00478226. IPI00550385. IPI01018940. |
| PIR | T00079. |
| RefSeq | NP_036222.3. NM_012090.4. |
| UniGene | Hs.472475. Hs.692278. |
3D structure databases | |
| ProteinModelPortal | Q9UPN3. |
| SMR | Q9UPN3. Positions 69-298. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-50616N. |
| IntAct | Q9UPN3. 23 interactions. |
| MINT | MINT-1195815. |
| STRING | 9606.ENSP00000289893. |
PTM databases | |
| PhosphoSite | Q9UPN3. |
Polymorphism databases | |
| DMDM | 296434581. 56405387. |
Proteomic databases | |
| PaxDb | Q9UPN3. |
| PRIDE | Q9UPN3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000289893; ENSP00000289893; ENSG00000127603. ENST00000361689; ENSP00000354573; ENSG00000127603. ENST00000372915; ENSP00000362006; ENSG00000127603. ENST00000545844; ENSP00000439537; ENSG00000127603. |
| GeneID | 23499. |
| KEGG | hsa:23499. |
| UCSC | uc001cda.1. human. uc021ols.1. human. |
Organism-specific databases | |
| CTD | 23499. |
| GeneCards | GC01P039546. |
| HGNC | HGNC:13664. MACF1. |
| HPA | HPA013713. |
| MIM | 608271. gene. |
| neXtProt | NX_Q9UPN3. |
| PharmGKB | PA30518. |
| HUGE | Search... Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| HOGENOM | HOG000049054. |
| HOVERGEN | HBG031127. |
| OrthoDB | EOG4XKV61. |
Enzyme and pathway databases | |
| Pathway_Interaction_DB | wnt_canonical_pathway. Canonical Wnt signaling pathway. |
Gene expression databases | |
| ArrayExpress | Q9UPN3. |
| Bgee | Q9UPN3. |
| CleanEx | HS_MACF1. |
| Genevestigator | Q9UPN3. |
| GermOnline | ENSG00000127603. Homo sapiens. |
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. 11 hits. PF00435. Spectrin. 17 hits. [Graphical view] |
| SMART | SM00033. CH. 2 hits. SM00054. EFh. 2 hits. SM00243. GAS2. 1 hit. SM00250. PLEC. 20 hits. SM00150. SPEC. 33 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. human. |
| GenomeRNAi | 23499. |
| NextBio | 45871. |
| SOURCE | Search... |
Entry information
| Entry name | MACF1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9UPN3 Secondary accession number(s): B1ALC5 Q9ULG9 | ||||||||
| 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 1 Human chromosome 1: 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 |