SPTSB_HUMAN
ID SPTSB_HUMAN Reviewed; 76 AA.
AC Q8NFR3; B2R5D3; D3DNM8; Q0P5S6;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Serine palmitoyltransferase small subunit B;
DE AltName: Full=Protein ADMP;
DE AltName: Full=Small subunit of serine palmitoyltransferase B;
DE Short=ssSPTb;
GN Name=SPTSSB; Synonyms=ADMP, C3orf57, SSSPTB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Zan Q., Guo J.H., Yu L.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15777716; DOI=10.1016/j.gene.2004.12.047;
RA Singh J., Young L., Handelsman D.J., Dong Q.;
RT "Molecular cloning and characterization of a novel androgen repressible
RT gene expressed in the prostate epithelium.";
RL Gene 348:55-63(2005).
RN [6]
RP FUNCTION, TOPOLOGY, IDENTIFICATION IN THE SPT COMPLEX, AND INTERACTION WITH
RP SPTLC1.
RX PubMed=19416851; DOI=10.1073/pnas.0811269106;
RA Han G., Gupta S.D., Gable K., Niranjanakumari S., Moitra P., Eichler F.,
RA Brown R.H. Jr., Harmon J.M., Dunn T.M.;
RT "Identification of small subunits of mammalian serine palmitoyltransferase
RT that confer distinct acyl-CoA substrate specificities.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8186-8191(2009).
CC -!- FUNCTION: Stimulates the activity of serine palmitoyltransferase (SPT).
CC The composition of the serine palmitoyltransferase (SPT) complex
CC determines the substrate preference, complexes with this subunit
CC showing a clear preference for longer acyl-CoAs. The SPTLC1-SPTLC2-
CC SPTSSB complex shows a strong preference for C18-CoA substrate, while
CC the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader
CC range of acyl-CoAs, without apparent preference. May play a role in
CC signal transduction. {ECO:0000269|PubMed:19416851}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBUNIT: Interacts with SPTLC1; the interaction is direct. Component of
CC the serine palmitoyltransferase (SPT) complex, composed of SPTLC1,
CC either SPTLC2 or SPTLC3, and either SPTSSA or SPTSSB.
CC {ECO:0000269|PubMed:19416851}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expression is seen predominantly in the prostate
CC epithelium with weaker expression in the fibroblasts and endothelial
CC cells. {ECO:0000269|PubMed:15777716}.
CC -!- INDUCTION: Expression is suppressed by androgens in the androgen-
CC sensitive LNCaP cell line. {ECO:0000269|PubMed:15777716}.
CC -!- SIMILARITY: Belongs to the SPTSS family. SPTSSB subfamily.
CC {ECO:0000305}.
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DR EMBL; AF458592; AAM49720.1; -; mRNA.
DR EMBL; AK312144; BAG35080.1; -; mRNA.
DR EMBL; CH471052; EAW78616.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78617.1; -; Genomic_DNA.
DR EMBL; BC065208; AAH65208.1; -; mRNA.
DR EMBL; BC071875; AAH71875.1; -; mRNA.
DR EMBL; BC107756; AAI07757.1; -; mRNA.
DR CCDS; CCDS33887.1; -.
DR RefSeq; NP_001035189.1; NM_001040100.1.
DR RefSeq; NP_001307608.1; NM_001320679.1.
DR AlphaFoldDB; Q8NFR3; -.
DR SMR; Q8NFR3; -.
DR ComplexPortal; CPX-6664; Serine palmitoyltransferase complex, SPTLC1-SPTLC2-SPTSSB variant.
DR ComplexPortal; CPX-6681; Serine palmitoyltransferase complex, SPTLC1-SPTLC3-SPTSSB variant.
DR CORUM; Q8NFR3; -.
DR DIP; DIP-60755N; -.
DR IntAct; Q8NFR3; 3.
DR STRING; 9606.ENSP00000352097; -.
DR GuidetoPHARMACOLOGY; 2513; -.
DR iPTMnet; Q8NFR3; -.
DR PhosphoSitePlus; Q8NFR3; -.
DR BioMuta; SPTSSB; -.
DR DMDM; 74730296; -.
DR MassIVE; Q8NFR3; -.
DR MaxQB; Q8NFR3; -.
DR PaxDb; Q8NFR3; -.
DR PeptideAtlas; Q8NFR3; -.
DR PRIDE; Q8NFR3; -.
DR ProteomicsDB; 73338; -.
DR Antibodypedia; 77962; 4 antibodies from 4 providers.
DR DNASU; 165679; -.
DR Ensembl; ENST00000359175.9; ENSP00000352097.4; ENSG00000196542.9.
DR Ensembl; ENST00000497137.1; ENSP00000420115.1; ENSG00000196542.9.
DR Ensembl; ENST00000620149.2; ENSP00000480827.1; ENSG00000196542.9.
DR GeneID; 165679; -.
DR KEGG; hsa:165679; -.
DR MANE-Select; ENST00000620149.2; ENSP00000480827.1; NM_001040100.2; NP_001035189.1.
DR UCSC; uc003fee.4; human.
DR CTD; 165679; -.
DR DisGeNET; 165679; -.
DR GeneCards; SPTSSB; -.
DR HGNC; HGNC:24045; SPTSSB.
DR HPA; ENSG00000196542; Tissue enhanced (skin, stomach, urinary bladder).
DR MIM; 610412; gene.
DR neXtProt; NX_Q8NFR3; -.
DR OpenTargets; ENSG00000196542; -.
DR PharmGKB; PA143485333; -.
DR VEuPathDB; HostDB:ENSG00000196542; -.
DR eggNOG; ENOG502S4Q9; Eukaryota.
DR GeneTree; ENSGT00390000002766; -.
DR HOGENOM; CLU_187811_0_0_1; -.
DR InParanoid; Q8NFR3; -.
DR OMA; WEFFSEI; -.
DR OrthoDB; 1290556at2759; -.
DR PhylomeDB; Q8NFR3; -.
DR TreeFam; TF328418; -.
DR BioCyc; MetaCyc:MON66-34372; -.
DR PathwayCommons; Q8NFR3; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR SignaLink; Q8NFR3; -.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 165679; 8 hits in 1029 CRISPR screens.
DR GenomeRNAi; 165679; -.
DR Pharos; Q8NFR3; Tdark.
DR PRO; PR:Q8NFR3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8NFR3; protein.
DR Bgee; ENSG00000196542; Expressed in skin of abdomen and 138 other tissues.
DR ExpressionAtlas; Q8NFR3; baseline and differential.
DR Genevisible; Q8NFR3; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017059; C:serine C-palmitoyltransferase complex; IDA:UniProtKB.
DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; IEA:Ensembl.
DR GO; GO:0046513; P:ceramide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR GO; GO:1904220; P:regulation of serine C-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IDA:ComplexPortal.
DR InterPro; IPR024512; Ser_palmitoyltrfase_ssu-like.
DR Pfam; PF11779; SPT_ssu-like; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; Reference proteome;
KW Sphingolipid metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..76
FT /note="Serine palmitoyltransferase small subunit B"
FT /id="PRO_0000239719"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..36
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 76 AA; 9198 MW; F43280DBC07B5A0E CRC64;
MDLRRVKEYF SWLYYQYQII SCCAVLEPWE RSMFNTILLT IIAMVVYTAY VFIPIHIRLA
WEFFSKICGY HSTISN
