SPTLC2

Serine palmitoyltransferase, long chain base subunit 2, also known as SPTLC2, is a protein which in humans is encoded by the SPTLC2 gene.[5][6][7]

SPTLC2
Identifiers
Aliases	SPTLC2, HSN1C, LCB2, LCB2A, NSAN1C, SPT2, hLCB2a, serine palmitoyltransferase long chain base subunit 2
External IDs	OMIM: 605713 MGI: 108074 HomoloGene: 21610 GeneCards: SPTLC2
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q24.3 Start 77,505,997 bp[1] End 77,616,773 bp[1]
Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band 12|12 D2 Start 87,305,058 bp[2] End 87,388,355 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • catalytic activity • serine C-palmitoyltransferase activity • pyridoxal phosphate binding • transferase activity, transferring acyl groups Cellular component • integral component of membrane • serine C-palmitoyltransferase complex • endoplasmic reticulum membrane • membrane • endoplasmic reticulum • mitochondrion Biological process • lipid metabolism • sphinganine biosynthetic process • sphingosine biosynthetic process • sphingolipid biosynthetic process • biosynthetic process • sphingomyelin biosynthetic process • positive regulation of lipophagy • metabolism • ceramide biosynthetic process • sphingolipid metabolic process • adipose tissue development Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9517	20773
Ensembl	ENSG00000100596	ENSMUSG00000021036
UniProt	O15270	P97363
RefSeq (mRNA)	NM_004863	NM_011479
RefSeq (protein)	NP_004854 NP_004854.1	NP_035609
Location (UCSC)	Chr 14: 77.51 – 77.62 Mb	Chr 12: 87.31 – 87.39 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

This gene encodes a long chain base subunit of serine palmitoyltransferase. Serine palmitoyltransferase, which consists of two different subunits, is the initial enzyme in sphingolipid biosynthesis. It catalyzes the pyridoxal 5'-phosphate dependent condensation of L-serine and palmitoyl CoA to 3-oxosphinganine. Mutations in this gene were identified in patients with hereditary sensory neuropathy type I. Alternatively spliced variants encoding different isoforms have been identified.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000100596 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000021036 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: SPTLC2 serine palmitoyltransferase, long chain base subunit 2".
6. Nagiec MM, Lester RL, Dickson RC (October 1996). "Sphingolipid synthesis: identification and characterization of mammalian cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase". Gene. 177 (1–2): 237–41. doi:10.1016/0378-1119(96)00309-5. PMID 8921873.
7. Weiss B, Stoffel W (October 1997). "Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis". European Journal of Biochemistry / FEBS. 249 (1): 239–47. doi:10.1111/j.1432-1033.1997.00239.x. PMID 9363775.

Further reading

• Takeda J, Yano H, Eng S, Zeng Y, Bell GI (November 1993). "A molecular inventory of human pancreatic islets: sequence analysis of 1000 cDNA clones". Human Molecular Genetics. 2 (11): 1793–8. doi:10.1093/hmg/2.11.1793. PMID 7506601.
• Hillier LD, Lennon G, Becker M, Bonaldo MF, Chiapelli B, Chissoe S, Dietrich N, DuBuque T, Favello A, Gish W, Hawkins M, Hultman M, Kucaba T, Lacy M, Le M, Le N, Mardis E, Moore B, Morris M, Parsons J, Prange C, Rifkin L, Rohlfing T, Schellenberg K, Bento Soares M, Tan F, Thierry-Meg J, Trevaskis E, Underwood K, Wohldman P, Waterston R, Wilson R, Marra M (September 1996). "Generation and analysis of 280,000 human expressed sequence tags". Genome Research. 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID 8889549.
• Nagiec MM, Lester RL, Dickson RC (October 1996). "Sphingolipid synthesis: identification and characterization of mammalian cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase". Gene. 177 (1–2): 237–41. doi:10.1016/0378-1119(96)00309-5. PMID 8921873.
• Weiss B, Stoffel W (October 1997). "Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis". European Journal of Biochemistry / FEBS. 249 (1): 239–47. doi:10.1111/j.1432-1033.1997.00239.x. PMID 9363775.
• Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (February 1998). "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Research. 5 (1): 31–9. doi:10.1093/dnares/5.1.31. PMID 9628581.
• Hanada K, Hara T, Nishijima M (March 2000). "Purification of the serine palmitoyltransferase complex responsible for sphingoid base synthesis by using affinity peptide chromatography techniques". The Journal of Biological Chemistry. 275 (12): 8409–15. doi:10.1074/jbc.275.12.8409. PMID 10722674.
• Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W, Zago MA, Bordin S, Costa FF, Goldman GH, Carvalho AF, Matsukuma A, Baia GS, Simpson DH, Brunstein A, de Oliveira PS, Bucher P, Jongeneel CV, O'Hare MJ, Soares F, Brentani RR, Reis LF, de Souza SJ, Simpson AJ (March 2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proceedings of the National Academy of Sciences of the United States of America. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
• Dawkins JL, Brahmbhatt S, Auer-Grumbach M, Wagner K, Hartung HP, Verhoeven K, Timmerman V, De Jonghe P, Kennerson M, LeGuern E, Nicholson GA (October 2002). "Exclusion of serine palmitoyltransferase long chain base subunit 2 (SPTLC2) as a common cause for hereditary sensory neuropathy". Neuromuscular Disorders. 12 (7–8): 656–8. doi:10.1016/S0960-8966(02)00015-9. PMID 12207934.
• Stachowitz S, Alessandrini F, Abeck D, Ring J, Behrendt H (November 2002). "Permeability barrier disruption increases the level of serine palmitoyltransferase in human epidermis". The Journal of Investigative Dermatology. 119 (5): 1048–52. doi:10.1046/j.1523-1747.2002.19524.x. PMID 12445191.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 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.
• Chen M, Han G, Dietrich CR, Dunn TM, Cahoon EB (December 2006). "The essential nature of sphingolipids in plants as revealed by the functional identification and characterization of the Arabidopsis LCB1 subunit of serine palmitoyltransferase". The Plant Cell. 18 (12): 3576–93. doi:10.1105/tpc.105.040774. PMC 1785403. PMID 17194770.
• Hornemann T, Wei Y, von Eckardstein A (July 2007). "Is the mammalian serine palmitoyltransferase a high-molecular-mass complex?". The Biochemical Journal. 405 (1): 157–64. doi:10.1042/BJ20070025. PMC 1925250. PMID 17331073.