Reviewed, UniProtKB/Swiss-Prot O15270 (SPTC2_HUMAN)

Names and origin

Protein names

Recommended name:
    Serine palmitoyltransferase 2
    EC=2.3.1.50
Alternative name(s):
    Serine-palmitoyl-CoA transferase 2
      Short name=SPT 2
    Long chain base biosynthesis protein 2
      Short name=LCB 2

Gene names

Name:	SPTLC2
Synonyms:	KIAA0526, LCB2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Lipid metabolism; sphingolipid metabolism.
Subunit structure	SPTLC1, SPTLC2 and SPTLC3 may encode subunits of the enzyme.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.
Tissue specificity	Widely expressed. Ref.7
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	Pyridoxal phosphate
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	sphingolipid biosynthetic process Traceable author statement. Source: UniProtKB
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW serine C-palmitoyltransferase complex Inferred from direct assay. Source: UniProtKB
Molecular function	pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro serine C-palmitoyltransferase activity Ref.1 Inferred from direct assay. Source: UniProtKB transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 562	562	Serine palmitoyltransferase 2		PRO_0000163858
Regions
	Transmembrane	67 – 87	21	Potential
Amino acid modifications
	Modified residue	379	1	N6-(pyridoxal phosphate)lysine By similarity
	Modified residue	384	1	Phosphoserine Ref.8
	Modified residue	387	1	Phosphotyrosine Ref.8
Experimental info
	Sequence conflict	61 – 64	4	EAFE → TLAR in AAC50871. Ref.5
	Sequence conflict	436 – 469	34	KECVQ…DSPVV → NGITIHEVVQTRNTYHRFSP LSPVFSHQCLWIML Ref.5

Sequences

	Sequence		Length	Mass (Da)
	O15270-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 0C1AA1E233DE36F1	FASTA	562	62,924
	10 20 30 40 50 60 MRPEPGGCCC RRTVRANGCV ANGEVRNGYV RSSAAAAAAA AAGQIHHVTQ NGGLYKRPFN 70 80 90 100 110 120 EAFEETPMLV AVLTYVGYGV LTLFGYLRDF LRYWRIEKCH HATEREEQKD FVSLYQDFEN 130 140 150 160 170 180 FYTRNLYMRI RDNWNRPICS VPGARVDIME RQSHDYNWSF KYTGNIIKGV INMGSYNYLG 190 200 210 220 230 240 FARNTGSCQE AAAKVLEEYG AGVCSTRQEI GNLDKHEELE ELVARFLGVE AAMAYGMGFA 250 260 270 280 290 300 TNSMNIPALV GKGCLILSDE LNHASLVLGA RLSGATIRIF KHNNMQSLEK LLKDAIVYGQ 310 320 330 340 350 360 PRTRRPWKKI LILVEGIYSM EGSIVRLPEV IALKKKYKAY LYLDEAHSIG ALGPTGRGVV 370 380 390 400 410 420 EYFGLDPEDV DVMMGTFTKS FGASGGYIGG KKELIDYLRT HSHSAVYATS LSPPVVEQII 430 440 450 460 470 480 TSMKCIMGQD GTSLGKECVQ QLAENTRYFR RRLKEMGFII YGNEDSPVVP LMLYMPAKIG 490 500 510 520 530 540 AFGREMLKRN IGVVVVGFPA TPIIESRARF CLSAAHTKEI LDTALKEIDE VGDLLQLKYS 550 560 RHRLVPLLDR PFDETTYEET ED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human and murine serine-palmitoyl-CoA transferase. Cloning, expression and characterization of the key enzyme in sphingolipid synthesis." Weiss B., Stoffel W. Eur. J. Biochem. 249:239-247(1997) [PubMed: 9363775] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pancreas.
[2]	"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." Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:31-39(1998) [PubMed: 9628581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed: 12508121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph.
[5]	"Sphingolipid synthesis: identification and characterization of mammalian cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase." Nagiec M.M., Lester R.L., Dickson R.C. Gene 177:237-241(1996) [PubMed: 8921873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-470. Tissue: Pancreatic islet.
[6]	"A molecular inventory of human pancreatic islets: sequence analysis of 1000 cDNA clones." Takeda J., Yano H., Eng S., Zeng Y., Bell G.I. Hum. Mol. Genet. 2:1793-1798(1993) [PubMed: 7506601] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 68-144. Tissue: Pancreatic islet.
[7]	"Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase." Hornemann T., Richard S., Ruetti M.F., Wei Y., von Eckardstein A. J. Biol. Chem. 281:37275-37281(2006) [PubMed: 17023427] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND TYR-387, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y08686 mRNA. Translation: CAA69942.1. AB011098 mRNA. Translation: BAA25452.2. Different initiation. AF111168 Genomic DNA. Translation: AAD09621.1. BC005123 mRNA. Translation: AAH05123.1. U15555 mRNA. Translation: AAC50871.1.
IPI	IPI00005751.
PIR	I38873.
RefSeq	NP_004854.1.
UniGene	Hs.435661
3D structure databases
HSSP	HSSP built from PDB template 1FC4 based on UniProtKB P07912.
ModBase	Search...
PTM databases
PhosphoSite	O15270.
Proteomic databases
PeptideAtlas	O15270.
PRIDE	O15270.
Genome annotation databases
Ensembl	ENSG00000100596. Homo sapiens. [Contig view]
GeneID	9517.
KEGG	hsa:9517.
NMPDR	fig|9606.3.peg.9944.
Organism-specific databases
GeneCards	GC14M077043.
H-InvDB	HIX0011853.
HGNC	HGNC:11278. SPTLC2.
MIM	605713. gene.
PharmGKB	PA36107.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O15270.
HOVERGEN	O15270.
OMA	O15270. KYKCYLF.
Enzyme and pathway databases
BRENDA	2.3.1.50. 247.
Gene expression databases
ArrayExpress	O15270.
Bgee	O15270.
CleanEx	HS_SPTLC2.
GermOnline	ENSG00000100596. Homo sapiens.
Family and domain databases
InterPro	IPR004839. Aminotrans_I/II. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00133. L-Serine. DB00114. Pyridoxal Phosphate.
NextBio	35666.
SOURCE	Search...

Entry information

Entry name

SPTC2_HUMAN

Accession

Primary (citable) accession number: O15270
Secondary accession number(s): Q16685

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)