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Showing Protein Ninjurin-1 (HMDBP13748)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP13748
Secondary Accession Numbers None
Name Ninjurin-1
Synonyms
  1. Nerve injury-induced protein 1
Gene Name NINJ1
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Homophilic transmembrane adhesion molecule involved in various processes such as inflammation, cell death, axonal growth, cell chemotaxis and angiogenesis (PubMed:8780658, PubMed:9261151, PubMed:33472215). Promotes cell adhesion by mediating homophilic interactions via its extracellular N-terminal adhesion motif (N-NAM) (PubMed:33028854). Involved in the progression of the inflammatory stress by promoting cell-to-cell interactions between immune cells and endothelial cells (PubMed:22162058, PubMed:26677008, PubMed:32147432). Involved in leukocyte migration during inflammation by promoting transendothelial migration of macrophages via homotypic binding (By similarity). Promotes the migration of monocytes across the brain endothelium to central nervous system inflammatory lesions (PubMed:22162058). Acts as a regulator of Toll-like receptor 4 (TLR4) signaling triggered by lipopolysaccharide (LPS) during systemic inflammation; directly binds LPS (PubMed:26677008). Acts as a mediator of both programmed and necrotic cell death (PubMed:33472215). Plays a key role in the induction of plasma membrane rupture during programmed and necrotic cell death: oligomerizes in response to death stimuli to mediate plasma membrane rupture (cytolysis), leading to release intracellular molecules named damage-associated molecular patterns (DAMPs) that propagate the inflammatory response (PubMed:33472215). Plays a role in nerve regeneration by promoting maturation of Schwann cells (PubMed:8780658, PubMed:9261151). Acts as a regulator of angiogenesis (PubMed:33028854). Promotes the formation of new vessels by mediating the interaction between capillary pericyte cells and endothelial cells (By similarity). Promotes osteoclasts development by enhancing the survival of prefusion osteoclasts (By similarity). Also involved in striated muscle growth and differentiation (By similarity).Secreted form generated by cleavage, which has chemotactic activity (By similarity). Acts as an anti-inflammatory mediator by promoting monocyte recruitment, thereby ameliorating atherosclerosis (PubMed:32883094).
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
cell adhesion
nervous system development
tissue regeneration
Cellular Component
integral to membrane
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 152
Molecular Weight 16344.955
Theoretical pI 6.277
Pfam Domain Function
Signals Not Available
Transmembrane Regions
  • 81-101;121-141;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q92982
UniProtKB/Swiss-Prot Entry Name NINJ1_HUMAN
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed:15164053 ]
  3. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [PubMed:22814378 ]
  4. Chadwick BP, Heath SK, Williamson J, Obermayr F, Patel L, Sheer D, Frischauf AM: The human homologue of the ninjurin gene maps to the candidate region of hereditary sensory neuropathy type I (HSNI). Genomics. 1998 Jan 1;47(1):58-63. doi: 10.1006/geno.1997.5084. [PubMed:9465296 ]
  5. Shin MW, Bae SJ, Wee HJ, Lee HJ, Ahn BJ, Le H, Lee EJ, Kim RH, Lee HS, Seo JH, Park JH, Kim KW: Ninjurin1 regulates lipopolysaccharide-induced inflammation through direct binding. Int J Oncol. 2016 Feb;48(2):821-8. doi: 10.3892/ijo.2015.3296. Epub 2015 Dec 15. [PubMed:26677008 ]
  6. Jeon S, Kim TK, Jeong SJ, Jung IH, Kim N, Lee MN, Sonn SK, Seo S, Jin J, Kweon HY, Kim S, Shim D, Park YM, Lee SH, Kim KW, Cybulsky MI, Shim H, Roh TY, Park WY, Lee HO, Choi JH, Park SH, Oh GT: Anti-Inflammatory Actions of Soluble Ninjurin-1 Ameliorate Atherosclerosis. Circulation. 2020 Nov 3;142(18):1736-1751. doi: 10.1161/CIRCULATIONAHA.120.046907. Epub 2020 Sep 4. [PubMed:32883094 ]
  7. Kayagaki N, Kornfeld OS, Lee BL, Stowe IB, O'Rourke K, Li Q, Sandoval W, Yan D, Kang J, Xu M, Zhang J, Lee WP, McKenzie BS, Ulas G, Payandeh J, Roose-Girma M, Modrusan Z, Reja R, Sagolla M, Webster JD, Cho V, Andrews TD, Morris LX, Miosge LA, Goodnow CC, Bertram EM, Dixit VM: NINJ1 mediates plasma membrane rupture during lytic cell death. Nature. 2021 Mar;591(7848):131-136. doi: 10.1038/s41586-021-03218-7. Epub 2021 Jan 20. [PubMed:33472215 ]
  8. Araki T, Milbrandt J: Ninjurin, a novel adhesion molecule, is induced by nerve injury and promotes axonal growth. Neuron. 1996 Aug;17(2):353-61. doi: 10.1016/s0896-6273(00)80166-x. [PubMed:8780658 ]
  9. Araki T, Zimonjic DB, Popescu NC, Milbrandt J: Mechanism of homophilic binding mediated by ninjurin, a novel widely expressed adhesion molecule. J Biol Chem. 1997 Aug 22;272(34):21373-80. doi: 10.1074/jbc.272.34.21373. [PubMed:9261151 ]
  10. Ifergan I, Kebir H, Terouz S, Alvarez JI, Lecuyer MA, Gendron S, Bourbonniere L, Dunay IR, Bouthillier A, Moumdjian R, Fontana A, Haqqani A, Klopstein A, Prinz M, Lopez-Vales R, Birchler T, Prat A: Role of Ninjurin-1 in the migration of myeloid cells to central nervous system inflammatory lesions. Ann Neurol. 2011 Nov;70(5):751-63. doi: 10.1002/ana.22519. [PubMed:22162058 ]
  11. Toma L, Sanda GM, Raileanu M, Stancu CS, Niculescu LS, Sima AV: Ninjurin-1 upregulated by TNFalpha receptor 1 stimulates monocyte adhesion to human TNFalpha-activated endothelial cells; benefic effects of amlodipine. Life Sci. 2020 May 15;249:117518. doi: 10.1016/j.lfs.2020.117518. Epub 2020 Mar 6. [PubMed:32147432 ]
  12. Kim SW, Lee HK, Seol SI, Davaanyam D, Lee H, Lee JK: Ninjurin 1 dodecamer peptide containing the N-terminal adhesion motif (N-NAM) exerts proangiogenic effects in HUVECs and in the postischemic brain. Sci Rep. 2020 Oct 7;10(1):16656. doi: 10.1038/s41598-020-73340-5. [PubMed:33028854 ]