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O15269

- SPTC1_HUMAN

UniProt

O15269 - SPTC1_HUMAN

Protein

Serine palmitoyltransferase 1

Gene

SPTLC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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

    Pyridoxal phosphate.By similarity

    Kineticsi

    1. KM=0.75 mM for serine1 Publication

    Vmax=1350 pmol/min/mg enzyme1 Publication

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. pyridoxal phosphate binding Source: InterPro
    3. serine C-palmitoyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. ceramide biosynthetic process Source: Ensembl
    2. small molecule metabolic process Source: Reactome
    3. sphinganine biosynthetic process Source: Ensembl
    4. sphingolipid biosynthetic process Source: UniProtKB
    5. sphingolipid metabolic process Source: Reactome
    6. sphingomyelin biosynthetic process Source: Ensembl
    7. sphingosine biosynthetic process Source: Ensembl

    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: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:11277. SPTLC1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW
    3. serine C-palmitoyltransferase complex Source: UniProtKB
    4. SPOTS complex Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Neuropathy, hereditary sensory and autonomic, 1A (HSAN1A) [MIM:162400]: A 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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 2 Publications
    VAR_011392
    Natural varianti133 – 1331C → Y in HSAN1A; reduced activity; does not interfere with SPT complex formation. 1 Publication
    VAR_011393
    Natural varianti144 – 1441V → D in HSAN1A; reduced activity; does not interfere with SPT complex formation. 1 Publication
    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; reduced activity. 2 Publications
    VAR_066245
    Natural varianti352 – 3521A → V in HSAN1A; reduced activity. 1 Publication
    VAR_066246

    Mutagenesis

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

    Keywords - Diseasei

    Disease mutation, Neuropathy

    Organism-specific databases

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

    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

    ArrayExpressiO15269.
    BgeeiO15269.
    CleanExiHS_SPTLC1.
    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. 15 interactions.
    DIPiDIP-45626N.
    IntActiO15269. 8 interactions.
    STRINGi9606.ENSP00000262554.

    Structurei

    3D structure databases

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

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei16 – 3621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0156.
    HOGENOMiHOG000216602.
    HOVERGENiHBG003992.
    InParanoidiO15269.
    KOiK00654.
    OMAiVNHQRIN.
    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. Align

    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

    MATATEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLLF SKTYKLQERS    50
    DLTVKEKEEL IEEWQPEPLV PPVPKDHPAL NYNIVSGPPS HKTVVNGKEC 100
    INFASFNFLG LLDNPRVKAA ALASLKKYGV GTCGPRGFYG TFDVHLDLED 150
    RLAKFMKTEE AIIYSYGFAT IASAIPAYSK RGDIVFVDRA ACFAIQKGLQ 200
    ASRSDIKLFK HNDMADLERL LKEQEIEDQK NPRKARVTRR FIVVEGLYMN 250
    TGTICPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHYGINIDDI 300
    DLISANMENA LASIGGFCCG RSFVIDHQRL SGQGYCFSAS LPPLLAAAAI 350
    EALNIMEENP GIFAVLKEKC GQIHKALQGI SGLKVVGESL SPAFHLQLEE 400
    STGSREQDVR LLQEIVDQCM NRSIALTQAR YLEKEEKCLP PPSIRVVVTV 450
    EQTEEELERA ASTIKEVAQA VLL 473
    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. 2 Publications
    VAR_011392
    Natural varianti133 – 1331C → Y in HSAN1A; reduced activity; does not interfere with SPT complex formation. 1 Publication
    VAR_011393
    Natural varianti144 – 1441V → D in HSAN1A; reduced activity; does not interfere with SPT complex formation. 1 Publication
    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; reduced activity. 2 Publications
    VAR_066245
    Natural varianti352 – 3521A → V in HSAN1A; reduced activity. 1 Publication
    VAR_066246
    Natural varianti387 – 3871G → A Rare polymorphism; does not affect activity; does not interfere with SPT complex formation. 1 Publication
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6692.1. [O15269-1 ]
    CCDS6693.1. [O15269-2 ]
    RefSeqi NP_001268232.1. NM_001281303.1.
    NP_006406.1. NM_006415.3. [O15269-1 ]
    NP_847894.1. NM_178324.2. [O15269-2 ]
    UniGenei Hs.90458.

    3D structure databases

    ProteinModelPortali O15269.
    SMRi O15269. Positions 59-471.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115809. 15 interactions.
    DIPi DIP-45626N.
    IntActi O15269. 8 interactions.
    STRINGi 9606.ENSP00000262554.

    Chemistry

    BindingDBi O15269.
    ChEMBLi CHEMBL1250343.
    DrugBanki DB00133. L-Serine.
    GuidetoPHARMACOLOGYi 2509.

    PTM databases

    PhosphoSitei O15269.

    Proteomic databases

    MaxQBi O15269.
    PaxDbi O15269.
    PeptideAtlasi O15269.
    PRIDEi O15269.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262554 ; ENSP00000262554 ; ENSG00000090054 . [O15269-1 ]
    ENST00000337841 ; ENSP00000337635 ; ENSG00000090054 . [O15269-2 ]
    GeneIDi 10558.
    KEGGi hsa:10558.
    UCSCi uc004arl.1. human. [O15269-1 ]
    uc004arn.1. human. [O15269-2 ]

    Organism-specific databases

    CTDi 10558.
    GeneCardsi GC09M094793.
    GeneReviewsi SPTLC1.
    H-InvDB HIX0034871.
    HGNCi HGNC:11277. SPTLC1.
    HPAi CAB018747.
    HPA010860.
    MIMi 162400. phenotype.
    605712. gene.
    neXtProti NX_O15269.
    Orphaneti 36386. Hereditary sensory and autonomic neuropathy type 1.
    PharmGKBi PA36106.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0156.
    HOGENOMi HOG000216602.
    HOVERGENi HBG003992.
    InParanoidi O15269.
    KOi K00654.
    OMAi VNHQRIN.
    OrthoDBi EOG786H30.
    PhylomeDBi O15269.
    TreeFami TF314877.

    Enzyme and pathway databases

    UniPathwayi UPA00222 .
    BioCyci MetaCyc:HS01673-MONOMER.
    BRENDAi 2.3.1.50. 2681.
    Reactomei REACT_115810. Sphingolipid de novo biosynthesis.

    Miscellaneous databases

    ChiTaRSi SPTLC1. human.
    GeneWikii SPTLC1.
    GenomeRNAii 10558.
    NextBioi 40067.
    PROi O15269.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15269.
    Bgeei O15269.
    CleanExi HS_SPTLC1.
    Genevestigatori O15269.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR004839. Aminotransferase_I/II.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    Pfami PF00155. Aminotran_1_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 138 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

    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