MICAL1

Protein-coding gene in the species Homo sapiens
MICAL1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1WYL, 2CO8

Identifiers
AliasesMICAL1, MICAL, MICAL-1, NICAL, microtubule associated monooxygenase, calponin and LIM domain containing 1
External IDsOMIM: 607129; MGI: 2385847; HomoloGene: 11246; GeneCards: MICAL1; OMA:MICAL1 - orthologs
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[1]
Chromosome 10 (mouse)
Genomic location for MICAL1
Genomic location for MICAL1
Band10|10 B1Start41,352,310 bp[1]
End41,363,028 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right coronary artery

  • left coronary artery

  • canal of the cervix

  • spleen

  • left uterine tube

  • popliteal artery

  • ganglionic eminence

  • stromal cell of endometrium

  • right lung

  • ascending aorta
Top expressed in
  • granulocyte

  • lumbar spinal ganglion

  • ascending aorta

  • external carotid artery

  • intestinal villus

  • internal carotid artery

  • tunica media of zone of aorta

  • fossa

  • Paneth cell

  • sciatic nerve
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • SH3 domain binding
  • oxidoreductase activity
  • actin binding
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
  • FAD binding
  • protein binding
  • metal ion binding
  • protein kinase binding
  • monooxygenase activity
  • NAD(P)H oxidase H2O2-forming activity
  • actin filament binding
Cellular component
  • cytoplasm
  • cytoskeleton
  • intermediate filament
  • hippocampal mossy fiber expansion
  • cytosol
  • midbody
  • intercellular bridge
  • plasma membrane
  • actin cytoskeleton
Biological process
  • negative regulation of protein phosphorylation
  • actin filament depolymerization
  • sulfur oxidation
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
  • negative regulation of apoptotic process
  • cytoskeleton organization
  • signal transduction
  • regulation of regulated secretory pathway
  • blood coagulation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

64780

171580

Ensembl

n/a

ENSMUSG00000019823

UniProt

Q8TDZ2

Q8VDP3

RefSeq (mRNA)

NM_022765
NM_001159291
NM_001286613

NM_001164433
NM_138315
NM_001358838
NM_001358839

RefSeq (protein)

NP_001152763
NP_001273542
NP_073602

NP_001157905
NP_612188
NP_001345767
NP_001345768

Location (UCSC)n/aChr 10: 41.35 – 41.36 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

NEDD9-interacting protein with calponin homology and LIM domains is a protein that in humans is encoded by the MICAL1 gene.[4][5]

Interactions

MICAL1 has been shown to interact with NEDD9[4] and RAB1A.[6]

References

  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019823 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ a b Suzuki T, Nakamoto T, Ogawa S, Seo S, Matsumura T, Tachibana K, Morimoto C, Hirai H (Apr 2002). "MICAL, a novel CasL interacting molecule, associates with vimentin". J Biol Chem. 277 (17): 14933–41. doi:10.1074/jbc.M111842200. PMID 11827972.
  5. ^ "Entrez Gene: MICAL1 microtubule associated monoxygenase, calponin and LIM domain containing 1".
  6. ^ Weide, Thomas; Teuber Julia; Bayer Michael; Barnekow Angelika (Jun 2003). "MICAL-1 isoforms, novel rab1 interacting proteins". Biochem. Biophys. Res. Commun. 306 (1). United States: 79–86. doi:10.1016/S0006-291X(03)00918-5. ISSN 0006-291X. PMID 12788069.

Further reading

  • Iwata S, Ohashi Y, Kamiguchi K, Morimoto C (2000). "Beta 1-integrin-mediated cell signaling in T lymphocytes". J. Dermatol. Sci. 23 (2): 75–86. doi:10.1016/S0923-1811(99)00096-1. PMID 10808124.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Hattori A, Okumura K, Nagase T, et al. (2001). "Characterization of long cDNA clones from human adult spleen". DNA Res. 7 (6): 357–66. doi:10.1093/dnares/7.6.357. PMID 11214971.
  • Terman JR, Mao T, Pasterkamp RJ, et al. (2002). "MICALs, a family of conserved flavoprotein oxidoreductases, function in plexin-mediated axonal repulsion". Cell. 109 (7): 887–900. doi:10.1016/S0092-8674(02)00794-8. PMID 12110185.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Weide T, Teuber J, Bayer M, Barnekow A (2003). "MICAL-1 isoforms, novel rab1 interacting proteins". Biochem. Biophys. Res. Commun. 306 (1): 79–86. doi:10.1016/S0006-291X(03)00918-5. PMID 12788069.
  • Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. Bibcode:2003Natur.425..805M. doi:10.1038/nature02055. PMID 14574404.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Fischer J, Weide T, Barnekow A (2005). "The MICAL proteins and rab1: a possible link to the cytoskeleton?". Biochem. Biophys. Res. Commun. 328 (2): 415–23. doi:10.1016/j.bbrc.2004.12.182. PMID 15694364.
  • Bayer M, Fischer J, Kremerskothen J, et al. (2006). "Identification and characterization of Iporin as a novel interaction partner for rab1". BMC Cell Biol. 6 (1): 15. doi:10.1186/1471-2121-6-15. PMC 1079803. PMID 15796781.
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
  • Jin X, Zhang J, Dai H, et al. (2007). "Investigation of the four cooperative unfolding units existing in the MICAL-1 CH domain". Biophys. Chem. 129 (2–3): 269–78. doi:10.1016/j.bpc.2007.06.008. PMID 17662518.
  • v
  • t
  • e
  • 1wyl: Solution structure of the CH domain of human NEDD9 interacting protein with calponin homology and LIM domains
    1wyl: Solution structure of the CH domain of human NEDD9 interacting protein with calponin homology and LIM domains
  • 2bra: STRUCTURE OF N-TERMINAL FAD BINDING MOTIF OF MOUSE MICAL
    2bra: STRUCTURE OF N-TERMINAL FAD BINDING MOTIF OF MOUSE MICAL
  • 2bry: CRYSTAL STRUCTURE OF THE NATIVE MONOOXYGENASE DOMAIN OF MICAL AT 1.45 A RESOLUTION
    2bry: CRYSTAL STRUCTURE OF THE NATIVE MONOOXYGENASE DOMAIN OF MICAL AT 1.45 A RESOLUTION
  • 2c4c: CRYSTAL STRUCTURE OF THE NADPH-TREATED MONOOXYGENASE DOMAIN OF MICAL
    2c4c: CRYSTAL STRUCTURE OF THE NADPH-TREATED MONOOXYGENASE DOMAIN OF MICAL
  • 2co8: Solution structures of the LIM domain of human NEDD9 interacting protein with calponin homology and LIM domains
    2co8: Solution structures of the LIM domain of human NEDD9 interacting protein with calponin homology and LIM domains
  • 2dk9: Solution structure of Calponin Homology domain of Human MICAL-1
    2dk9: Solution structure of Calponin Homology domain of Human MICAL-1


Stub icon

This article on a gene on human chromosome 6 is a stub. You can help Wikipedia by expanding it.

  • v
  • t
  • e