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Protein

Serine palmitoyltransferase 1

Gene

SPTLC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference.1 Publication

Catalytic activityi

Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2.1 Publication

Cofactori

Kineticsi

  1. KM=0.75 mM for serine1 Publication
  1. Vmax=1350 pmol/min/mg enzyme1 Publication

Pathwayi

GO - Molecular functioni

  • pyridoxal phosphate binding Source: InterPro
  • serine C-palmitoyltransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS01673-MONOMER.
BRENDAi2.3.1.50. 2681.
ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.
UniPathwayiUPA00222.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine palmitoyltransferase 1 (EC:2.3.1.50)
Alternative name(s):
Long chain base biosynthesis protein 1
Short name:
LCB 1
Serine-palmitoyl-CoA transferase 1
Short name:
SPT 1
Short name:
SPT1
Gene namesi
Name:SPTLC1
Synonyms:LCB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:11277. SPTLC1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515LumenalSequence AnalysisAdd
BLAST
Transmembranei16 – 3621HelicalSequence AnalysisAdd
BLAST
Topological domaini37 – 473437CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: Reactome
  • integral component of membrane Source: UniProtKB-KW
  • serine C-palmitoyltransferase complex Source: UniProtKB
  • SPOTS complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Neuropathy, hereditary sensory and autonomic, 1A (HSAN1A)5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by prominent sensory abnormalities with a variable degree of motor and autonomic dysfunction. The neurological phenotype is often complicated by severe infections, osteomyelitis, and amputations. HSAN1A is an autosomal dominant axonal form with onset in the second or third decades. Initial symptoms are loss of pain, touch, heat, and cold sensation over the feet, followed by distal muscle wasting and weakness. Loss of pain sensation leads to chronic skin ulcers and distal amputations.

See also OMIM:162400
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti133 – 1331C → W in HSAN1A; inactive in the heterodimeric SPT complex; largely reduced activity with serine as substrate, but nearly no effect on serine affinity in the heterotrimeric SPT complex; in contrast to wild-type is able to use alanine as substrate leading to the formation of 1-deoxysphinganine (1-deoxySa); does not interfere with SPT complex formation. 4 Publications
VAR_011392
Natural varianti133 – 1331C → Y in HSAN1A; reduced activity; does not interfere with SPT complex formation. 2 Publications
VAR_011393
Natural varianti144 – 1441V → D in HSAN1A; reduced activity; does not interfere with SPT complex formation. 2 Publications
VAR_011394
Natural varianti310 – 3101A → G Found in a patient with HSAN1A; uncertain pathological significance. 1 Publication
VAR_068476
Natural varianti331 – 3311S → F in HSAN1A; severe form with early onset; reduced activity. 3 Publications
VAR_066245
Natural varianti352 – 3521A → V in HSAN1A; reduced activity. 2 Publications
VAR_066246

SPTLC1 mutations at Ser-331 are responsible for severe hereditary motor and sensory neuropathy (HMSN) forms, whose core features are severe, diffuse muscle wasting and hypotonia, motor and sensory disturbances, foot ulcers, amputations and/or burns, joint hypermobility, cataracts and considerable growth retardation.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi164 – 1641Y → F: Increased serine palmitoyltransferase activity and sphingolipid content. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

MIMi162400. phenotype.
Orphaneti36386. Hereditary sensory and autonomic neuropathy type 1.
PharmGKBiPA36106.

Chemistry

DrugBankiDB00133. L-Serine.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Serine palmitoyltransferase 1PRO_0000163853Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei164 – 1641Phosphotyrosine; by ABL1 Publication

Post-translational modificationi

Phosphorylation at Tyr-164 inhibits activity and promotes cell survival.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO15269.
PaxDbiO15269.
PeptideAtlasiO15269.
PRIDEiO15269.

PTM databases

PhosphoSiteiO15269.

Expressioni

Tissue specificityi

Widely expressed. Not detected in small intestine.1 Publication

Gene expression databases

BgeeiO15269.
CleanExiHS_SPTLC1.
ExpressionAtlasiO15269. baseline and differential.
GenevestigatoriO15269.

Organism-specific databases

HPAiCAB018747.
HPA010860.

Interactioni

Subunit structurei

Heterodimer with SPTLC2 or SPTLC3. Component of the serine palmitoyltransferase (SPT) complex, composed of SPTLC1, either SPTLC2 or SPTLC3, and either SPTSSA or SPTSSB. Interacts with SPTSSA and SPTSSB; the interaction is direct. Interacts with ORMDL3.2 Publications

Protein-protein interaction databases

BioGridi115809. 14 interactions.
DIPiDIP-45626N.
IntActiO15269. 8 interactions.
STRINGi9606.ENSP00000262554.

Structurei

3D structure databases

ProteinModelPortaliO15269.
SMRiO15269. Positions 59-471.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0156.
GeneTreeiENSGT00550000074872.
HOGENOMiHOG000216602.
HOVERGENiHBG003992.
InParanoidiO15269.
KOiK00654.
OMAiGLQISRC.
OrthoDBiEOG786H30.
PhylomeDBiO15269.
TreeFamiTF314877.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15269-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MATATEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLLF SKTYKLQERS
60 70 80 90 100
DLTVKEKEEL IEEWQPEPLV PPVPKDHPAL NYNIVSGPPS HKTVVNGKEC
110 120 130 140 150
INFASFNFLG LLDNPRVKAA ALASLKKYGV GTCGPRGFYG TFDVHLDLED
160 170 180 190 200
RLAKFMKTEE AIIYSYGFAT IASAIPAYSK RGDIVFVDRA ACFAIQKGLQ
210 220 230 240 250
ASRSDIKLFK HNDMADLERL LKEQEIEDQK NPRKARVTRR FIVVEGLYMN
260 270 280 290 300
TGTICPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHYGINIDDI
310 320 330 340 350
DLISANMENA LASIGGFCCG RSFVIDHQRL SGQGYCFSAS LPPLLAAAAI
360 370 380 390 400
EALNIMEENP GIFAVLKEKC GQIHKALQGI SGLKVVGESL SPAFHLQLEE
410 420 430 440 450
STGSREQDVR LLQEIVDQCM NRSIALTQAR YLEKEEKCLP PPSIRVVVTV
460 470
EQTEEELERA ASTIKEVAQA VLL
Length:473
Mass (Da):52,744
Last modified:January 1, 1998 - v1
Checksum:iBA9E056A869D2EA2
GO
Isoform 2 (identifier: O15269-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     143-143: D → E
     144-473: Missing.

Note: No experimental confirmation available.

Show »
Length:143
Mass (Da):16,073
Checksum:iED13F62F871136BF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti133 – 1331C → W in HSAN1A; inactive in the heterodimeric SPT complex; largely reduced activity with serine as substrate, but nearly no effect on serine affinity in the heterotrimeric SPT complex; in contrast to wild-type is able to use alanine as substrate leading to the formation of 1-deoxysphinganine (1-deoxySa); does not interfere with SPT complex formation. 4 Publications
VAR_011392
Natural varianti133 – 1331C → Y in HSAN1A; reduced activity; does not interfere with SPT complex formation. 2 Publications
VAR_011393
Natural varianti144 – 1441V → D in HSAN1A; reduced activity; does not interfere with SPT complex formation. 2 Publications
VAR_011394
Natural varianti151 – 1511R → L.1 Publication
Corresponds to variant rs45461899 [ dbSNP | Ensembl ].
VAR_037889
Natural varianti239 – 2391R → W in a breast cancer sample; somatic mutation. 1 Publication
VAR_036610
Natural varianti310 – 3101A → G Found in a patient with HSAN1A; uncertain pathological significance. 1 Publication
VAR_068476
Natural varianti331 – 3311S → F in HSAN1A; severe form with early onset; reduced activity. 3 Publications
VAR_066245
Natural varianti331 – 3311S → Y Probable disease-associated mutation found in severe HMSN; reduced activity. 1 Publication
VAR_073294
Natural varianti352 – 3521A → V in HSAN1A; reduced activity. 2 Publications
VAR_066246
Natural varianti387 – 3871G → A Rare polymorphism; does not affect activity; does not interfere with SPT complex formation. 2 Publications
Corresponds to variant rs119482084 [ dbSNP | Ensembl ].
VAR_037890

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei143 – 1431D → E in isoform 2. 1 PublicationVSP_043127
Alternative sequencei144 – 473330Missing in isoform 2. 1 PublicationVSP_043128Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08685 mRNA. Translation: CAA69941.1.
AF286717
, AF286703, AF286704, AF286705, AF286706, AF286707, AF286708, AF286709, AF286710, AF286711, AF286712, AF286713, AF286714, AF286715, AF286716 Genomic DNA. Translation: AAK29328.1.
AK291546 mRNA. Translation: BAF84235.1.
AL391219, AL354751 Genomic DNA. Translation: CAH70209.1.
AL354751 Genomic DNA. Translation: CAH69923.1.
AL354751, AL391219 Genomic DNA. Translation: CAH69924.1.
CH471089 Genomic DNA. Translation: EAW62804.1.
BC007085 mRNA. Translation: AAH07085.1.
CCDSiCCDS6692.1. [O15269-1]
CCDS6693.1. [O15269-2]
RefSeqiNP_001268232.1. NM_001281303.1.
NP_006406.1. NM_006415.3. [O15269-1]
NP_847894.1. NM_178324.2. [O15269-2]
UniGeneiHs.90458.

Genome annotation databases

EnsembliENST00000262554; ENSP00000262554; ENSG00000090054. [O15269-1]
ENST00000337841; ENSP00000337635; ENSG00000090054. [O15269-2]
GeneIDi10558.
KEGGihsa:10558.
UCSCiuc004arl.1. human. [O15269-1]
uc004arn.1. human. [O15269-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08685 mRNA. Translation: CAA69941.1.
AF286717
, AF286703, AF286704, AF286705, AF286706, AF286707, AF286708, AF286709, AF286710, AF286711, AF286712, AF286713, AF286714, AF286715, AF286716 Genomic DNA. Translation: AAK29328.1.
AK291546 mRNA. Translation: BAF84235.1.
AL391219, AL354751 Genomic DNA. Translation: CAH70209.1.
AL354751 Genomic DNA. Translation: CAH69923.1.
AL354751, AL391219 Genomic DNA. Translation: CAH69924.1.
CH471089 Genomic DNA. Translation: EAW62804.1.
BC007085 mRNA. Translation: AAH07085.1.
CCDSiCCDS6692.1. [O15269-1]
CCDS6693.1. [O15269-2]
RefSeqiNP_001268232.1. NM_001281303.1.
NP_006406.1. NM_006415.3. [O15269-1]
NP_847894.1. NM_178324.2. [O15269-2]
UniGeneiHs.90458.

3D structure databases

ProteinModelPortaliO15269.
SMRiO15269. Positions 59-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115809. 14 interactions.
DIPiDIP-45626N.
IntActiO15269. 8 interactions.
STRINGi9606.ENSP00000262554.

Chemistry

BindingDBiO15269.
ChEMBLiCHEMBL1250343.
DrugBankiDB00133. L-Serine.
GuidetoPHARMACOLOGYi2509.

PTM databases

PhosphoSiteiO15269.

Proteomic databases

MaxQBiO15269.
PaxDbiO15269.
PeptideAtlasiO15269.
PRIDEiO15269.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262554; ENSP00000262554; ENSG00000090054. [O15269-1]
ENST00000337841; ENSP00000337635; ENSG00000090054. [O15269-2]
GeneIDi10558.
KEGGihsa:10558.
UCSCiuc004arl.1. human. [O15269-1]
uc004arn.1. human. [O15269-2]

Organism-specific databases

CTDi10558.
GeneCardsiGC09M094793.
GeneReviewsiSPTLC1.
H-InvDBHIX0034871.
HGNCiHGNC:11277. SPTLC1.
HPAiCAB018747.
HPA010860.
MIMi162400. phenotype.
605712. gene.
neXtProtiNX_O15269.
Orphaneti36386. Hereditary sensory and autonomic neuropathy type 1.
PharmGKBiPA36106.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0156.
GeneTreeiENSGT00550000074872.
HOGENOMiHOG000216602.
HOVERGENiHBG003992.
InParanoidiO15269.
KOiK00654.
OMAiGLQISRC.
OrthoDBiEOG786H30.
PhylomeDBiO15269.
TreeFamiTF314877.

Enzyme and pathway databases

UniPathwayiUPA00222.
BioCyciMetaCyc:HS01673-MONOMER.
BRENDAi2.3.1.50. 2681.
ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.

Miscellaneous databases

ChiTaRSiSPTLC1. human.
GeneWikiiSPTLC1.
GenomeRNAii10558.
NextBioi40067.
PROiO15269.
SOURCEiSearch...

Gene expression databases

BgeeiO15269.
CleanExiHS_SPTLC1.
ExpressionAtlasiO15269. baseline and differential.
GenevestigatoriO15269.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  2. "Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1, cause hereditary sensory neuropathy type I."
    Dawkins J.L., Hulme D.J., Brahmbhatt S.B., Auer-Grumbach M., Nicholson G.A.
    Nat. Genet. 27:309-312(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS HSAN1A TRP-133; TYR-133 AND ASP-144.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Identification of small subunits of mammalian serine palmitoyltransferase that confer distinct acyl-CoA substrate specificities."
    Han G., Gupta S.D., Gable K., Niranjanakumari S., Moitra P., Eichler F., Brown R.H. Jr., Harmon J.M., Dunn T.M.
    Proc. Natl. Acad. Sci. U.S.A. 106:8186-8191(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE SPT COMPLEX, INTERACTION WITH SPTSSA AND SPTSSB.
  9. "A disease-causing mutation in the active site of serine palmitoyltransferase causes catalytic promiscuity."
    Gable K., Gupta S.D., Han G., Niranjanakumari S., Harmon J.M., Dunn T.M.
    J. Biol. Chem. 285:22846-22852(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANT HSAN1A TRP-133.
  10. Cited for: INTERACTION WITH ORMDL3.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Phosphorylation of serine palmitoyltransferase long chain-1 (SPTLC1) on tyrosine 164 inhibits its activity and promotes cell survival."
    Taouji S., Higa A., Delom F., Palcy S., Mahon F.X., Pasquet J.M., Bosse R., Segui B., Chevet E.
    J. Biol. Chem. 288:17190-17201(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-164, MUTAGENESIS OF TYR-164.
  13. Cited for: VARIANT ALA-387.
  14. "Charcot-Marie-Tooth disease due to a de novo mutation of the RAB7 gene."
    Meggouh F., Bienfait H.M.E., Weterman M.A.J., de Visser M., Baas F.
    Neurology 67:1476-1478(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-151.
  15. Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-239.
  16. Cited for: VARIANTS HSAN1A PHE-331 AND VAL-352.
  17. "A systematic comparison of all mutations in hereditary sensory neuropathy type I (HSAN I) reveals that the G387A mutation is not disease associated."
    Hornemann T., Penno A., Richard S., Nicholson G., van Dijk F.S., Rotthier A., Timmerman V., von Eckardstein A.
    Neurogenetics 10:135-143(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS HSAN1A TYR-133; TRP-133 AND ASP-144, CHARACTERIZATION OF VARIANT ALA-387, LACK OF ASSOCIATION OF VARIANT ALA-387 WITH HSAN1A.
  18. "Characterization of two mutations in the SPTLC1 subunit of serine palmitoyltransferase associated with hereditary sensory and autonomic neuropathy type I."
    Rotthier A., Penno A., Rautenstrauss B., Auer-Grumbach M., Stettner G.M., Asselbergh B., Van Hoof K., Sticht H., Levy N., Timmerman V., Hornemann T., Janssens K.
    Hum. Mutat. 32:E2211-E2225(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HSAN1A PHE-331, CHARACTERIZATION OF VARIANTS HSAN1A PHE-331 AND VAL-352.
  19. Cited for: VARIANT HSAN1A TRP-133, VARIANT GLY-310.
  20. "Mutations at Ser331 in the HSN type I gene SPTLC1 are associated with a distinct syndromic phenotype."
    Auer-Grumbach M., Bode H., Pieber T.R., Schabhuettl M., Fischer D., Seidl R., Graf E., Wieland T., Schuh R., Vacariu G., Grill F., Timmerman V., Strom T.M., Hornemann T.
    Eur. J. Med. Genet. 56:266-269(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN HMSN, VARIANT TYR-331, CHARACTERIZATION OF VARIANT TYR-331.
  21. "Early-onset severe hereditary sensory and autonomic neuropathy type 1 with S331F SPTLC1 mutation."
    Suh B.C., Hong Y.B., Nakhro K., Nam S.H., Chung K.W., Choi B.O.
    Mol. Med. Report. 9:481-486(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HSAN1A PHE-331.

Entry informationi

Entry nameiSPTC1_HUMAN
AccessioniPrimary (citable) accession number: O15269
Secondary accession number(s): A8K681, Q5VWB4, Q96IX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: May 27, 2015
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Caution

Variant Ala-387 has been originally thought to cause HSAN1A (PubMed:15037712). Subsequently, it has been shown to be a rare, benign polymorphism found in homozygous state in a healthy individual (PubMed:19132419).2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.