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O15269 (SPTC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SPTLC1
Synonyms:LCB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Catalytic activity

Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2. Ref.8

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Lipid metabolism; sphingolipid metabolism.

Subunit structure

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. Ref.8 Ref.10

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.

Tissue specificity

Widely expressed. Not detected in small intestine. Ref.7

Post-translational modification

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.9 Ref.16 Ref.17 Ref.18 Ref.19

Sequence similarities

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Caution

Variant Ala-387 has been originally thought to cause HSAN1A (Ref.13). Subsequently, it has been shown to be a rare, benign polymorphism found in homozygous state in a healthy individual (Ref.17).

Biophysicochemical properties

Kinetic parameters:

KM=0.75 mM for serine Ref.9

Vmax=1350 pmol/min/mg enzyme

Ontologies

Keywords
   Biological processLipid metabolism
Sphingolipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Neuropathy
   DomainTransmembrane
Transmembrane helix
   LigandPyridoxal phosphate
   Molecular functionAcyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processceramide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

sphinganine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

sphingolipid biosynthetic process

Traceable author statement Ref.8. Source: UniProtKB

sphingolipid metabolic process

Traceable author statement. Source: Reactome

sphingomyelin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

sphingosine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentSPOTS complex

Inferred from direct assay Ref.10. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

serine C-palmitoyltransferase complex

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionpyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

serine C-palmitoyltransferase activity

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15269-1)

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.
Isoform 2 (identifier: O15269-2)

The sequence of this isoform differs from the canonical sequence as follows:
     143-143: D → E
     144-473: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Serine palmitoyltransferase 1
PRO_0000163853

Regions

Topological domain1 – 1515Lumenal Potential
Transmembrane16 – 3621Helical; Potential
Topological domain37 – 473437Cytoplasmic Potential

Amino acid modifications

Modified residue1641Phosphotyrosine; by ABL Ref.12

Natural variations

Alternative sequence1431D → E in isoform 2.
VSP_043127
Alternative sequence144 – 473330Missing in isoform 2.
VSP_043128
Natural variant1331C → 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. Ref.2 Ref.9 Ref.17 Ref.19
VAR_011392
Natural variant1331C → Y in HSAN1A; reduced activity; does not interfere with SPT complex formation. Ref.2 Ref.17
VAR_011393
Natural variant1441V → D in HSAN1A; reduced activity; does not interfere with SPT complex formation. Ref.2 Ref.17
VAR_011394
Natural variant1511R → L. Ref.14
Corresponds to variant rs45461899 [ dbSNP | Ensembl ].
VAR_037889
Natural variant2391R → W in a breast cancer sample; somatic mutation. Ref.15
VAR_036610
Natural variant3101A → G Found in a patient with HSAN1A; uncertain pathological significance. Ref.19
VAR_068476
Natural variant3311S → F in HSAN1A; reduced activity. Ref.16 Ref.18
VAR_066245
Natural variant3521A → V in HSAN1A; reduced activity. Ref.16 Ref.18
VAR_066246
Natural variant3871G → A Rare polymorphism; does not affect activity; does not interfere with SPT complex formation. Ref.13 Ref.17
Corresponds to variant rs119482084 [ dbSNP | Ensembl ].
VAR_037890

Experimental info

Mutagenesis1641Y → F: Increased serine palmitoyltransferase activity and sphingolipid content. Ref.12

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: BA9E056A869D2EA2

FASTA47352,744
        10         20         30         40         50         60 
MATATEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLLF SKTYKLQERS DLTVKEKEEL 

        70         80         90        100        110        120 
IEEWQPEPLV PPVPKDHPAL NYNIVSGPPS HKTVVNGKEC INFASFNFLG LLDNPRVKAA 

       130        140        150        160        170        180 
ALASLKKYGV GTCGPRGFYG TFDVHLDLED RLAKFMKTEE AIIYSYGFAT IASAIPAYSK 

       190        200        210        220        230        240 
RGDIVFVDRA ACFAIQKGLQ ASRSDIKLFK HNDMADLERL LKEQEIEDQK NPRKARVTRR 

       250        260        270        280        290        300 
FIVVEGLYMN TGTICPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHYGINIDDI 

       310        320        330        340        350        360 
DLISANMENA LASIGGFCCG RSFVIDHQRL SGQGYCFSAS LPPLLAAAAI EALNIMEENP 

       370        380        390        400        410        420 
GIFAVLKEKC GQIHKALQGI SGLKVVGESL SPAFHLQLEE STGSREQDVR LLQEIVDQCM 

       430        440        450        460        470 
NRSIALTQAR YLEKEEKCLP PPSIRVVVTV EQTEEELERA ASTIKEVAQA VLL 

« Hide

Isoform 2 [UniParc].

Checksum: ED13F62F871136BF
Show »

FASTA14316,073

References

« Hide '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] [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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Orm family proteins mediate sphingolipid homeostasis."
Breslow D.K., Collins S.R., Bodenmiller B., Aebersold R., Simons K., Shevchenko A., Ejsing C.S., Weissman J.S.
Nature 463:1048-1053(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ORMDL3.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"SPTLC1 mutation in twin sisters with hereditary sensory neuropathy type I."
Verhoeven K., Coen K., De Vriendt E., Jacobs A., Van Gerwen V., Smouts I., Pou-Serradell A., Martin J.-J., Timmerman V., De Jonghe P.
Neurology 62:1001-1002(2004) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-239.
[16]"Genes for hereditary sensory and autonomic neuropathies: a genotype-phenotype correlation."
Rotthier A., Baets J., De Vriendt E., Jacobs A., Auer-Grumbach M., Levy N., Bonello-Palot N., Kilic S.S., Weis J., Nascimento A., Swinkels M., Kruyt M.C., Jordanova A., De Jonghe P., Timmerman V.
Brain 132:2699-2711(2009) [PubMed] [Europe PMC] [Abstract]
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]"Frequency of mutations in the genes associated with hereditary sensory and autonomic neuropathy in a UK cohort."
Davidson G.L., Murphy S.M., Polke J.M., Laura M., Salih M.A., Muntoni F., Blake J., Brandner S., Davies N., Horvath R., Price S., Donaghy M., Roberts M., Foulds N., Ramdharry G., Soler D., Lunn M.P., Manji H. expand/collapse author list , Davis M.B., Houlden H., Reilly M.M.
J. Neurol. 259:1673-1685(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HSAN1A TRP-133, VARIANT GLY-310.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y08685 mRNA. Translation: CAA69941.1.
AF286717 expand/collapse EMBL AC list , 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.
RefSeqNP_001268232.1. NM_001281303.1.
NP_006406.1. NM_006415.3.
NP_847894.1. NM_178324.2.
UniGeneHs.90458.

3D structure databases

ProteinModelPortalO15269.
SMRO15269. Positions 54-471.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115809. 16 interactions.
DIPDIP-45626N.
IntActO15269. 7 interactions.
STRING9606.ENSP00000262554.

Chemistry

BindingDBO15269.
ChEMBLCHEMBL1250343.
DrugBankDB00133. L-Serine.
DB00114. Pyridoxal Phosphate.
GuidetoPHARMACOLOGY2509.

PTM databases

PhosphoSiteO15269.

Proteomic databases

PaxDbO15269.
PeptideAtlasO15269.
PRIDEO15269.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262554; ENSP00000262554; ENSG00000090054. [O15269-1]
ENST00000337841; ENSP00000337635; ENSG00000090054. [O15269-2]
GeneID10558.
KEGGhsa:10558.
UCSCuc004arl.1. human. [O15269-1]
uc004arn.1. human. [O15269-2]

Organism-specific databases

CTD10558.
GeneCardsGC09M094793.
H-InvDBHIX0034871.
HGNCHGNC:11277. SPTLC1.
HPACAB018747.
HPA010860.
MIM162400. phenotype.
605712. gene.
neXtProtNX_O15269.
Orphanet36386. Hereditary sensory and autonomic neuropathy type 1.
PharmGKBPA36106.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000216602.
HOVERGENHBG003992.
InParanoidO15269.
KOK00654.
OMAVNHQRIN.
OrthoDBEOG786H30.
PhylomeDBO15269.
TreeFamTF314877.

Enzyme and pathway databases

BioCycMetaCyc:HS01673-MONOMER.
BRENDA2.3.1.50. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00222.

Gene expression databases

ArrayExpressO15269.
BgeeO15269.
CleanExHS_SPTLC1.
GenevestigatorO15269.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSPTLC1. human.
GeneWikiSPTLC1.
GenomeRNAi10558.
NextBio40067.
PROO15269.
SOURCESearch...

Entry information

Entry nameSPTC1_HUMAN
AccessionPrimary (citable) accession number: O15269
Secondary accession number(s): A8K681, Q5VWB4, Q96IX6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM