Q9BX95 (SGPP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sphingosine-1-phosphate phosphatase 1
Short name=SPPase1
Short name=Spp1
Short name=hSPP1
Short name=hSPPase1
EC=3.1.3.-

Alternative name(s):
Sphingosine-1-phosphatase 1

Gene names

Name:

SGPP1

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	441 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has enzymatic activity against both sphingosine 1-phosphate (S1P) and dihydro-S1P. Regulates intracellular and extracellular S1P levels. Ref.1
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1.
Tissue specificity	Ubiquitous, with the strongest level in placenta and kidney. Ref.1
Sequence similarities	Belongs to the type 2 lipid phosphate phosphatase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 441	441	Sphingosine-1-phosphate phosphatase 1		PRO_0000114477
Regions
	Transmembrane	132 – 152	21	Helical; Potential
	Transmembrane	163 – 183	21	Helical; Potential
	Transmembrane	204 – 224	21	Helical; Potential
	Transmembrane	227 – 247	21	Helical; Potential
	Transmembrane	257 – 277	21	Helical; Potential
	Transmembrane	290 – 310	21	Helical; Potential
	Transmembrane	322 – 342	21	Helical; Potential
	Transmembrane	359 – 379	21	Helical; Potential
	Transmembrane	420 – 440	21	Helical; Potential
Amino acid modifications
	Modified residue	101	1	Phosphoserine Ref.10 Ref.11 Ref.12
	Modified residue	112	1	Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14
	Modified residue	114	1	Phosphothreonine Ref.11
Experimental info
	Sequence conflict	146	1	L → P in AAK26660. Ref.1
	Sequence conflict	191	1	V → A in AAK26660. Ref.1
	Sequence conflict	282	1	D → G in AAK26660. Ref.1
	Sequence conflict	320	1	A → T in AAK26660. Ref.1
	Sequence conflict	371	1	I → V in AAK26660. Ref.1
	Sequence conflict	375	1	F → S in AAK26660. Ref.1
	Sequence conflict	410	1	E → G in AAK26660. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9BX95 [UniParc]. Last modified April 26, 2004. Version 2. Checksum: 86A018DDDA3A3019	FASTA	441	49,108
	10 20 30 40 50 60 MSLRQRLAQL VGRLQDPQKV ARFQRLCGVE APPRRSADRR EDEKAEAPLA GDPRLRGRQP 70 80 90 100 110 120 GAPGGPQPPG SDRNQCPAKP DGGGAPNGVR NGLAAELGPA SPRRAGALRR NSLTGEEGQL 130 140 150 160 170 180 ARVSNWPLYC LFCFGTELGN ELFYILFFPF WIWNLDPLVG RRLVVIWVLV MYLGQCTKDI 190 200 210 220 230 240 IRWPRPASPP VVKLEVFYNS EYSMPSTHAM SGTAIPISMV LLTYGRWQYP LIYGLILIPC 250 260 270 280 290 300 WCSLVCLSRI YMGMHSILDI IAGFLYTILI LAVFYPFVDL IDNFNQTHKY APFIIIGLHL 310 320 330 340 350 360 ALGIFSFTLD TWSTSRGDTA EILGSGAGIA CGSHVTYNMG LVLDPSLDTL PLAGPPITVT 370 380 390 400 410 420 LFGKAILRIL IGMVFVLIIR DVMKKITIPL ACKIFNIPCD DIRKARQHME VELPYRYITY 430 440 GMVGFSITFF VPYIFFFIGI S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Role of human sphingosine-1-phosphate phosphatase 1 in the regulation of intra- and extracellular sphingosine-1-phosphate levels and cell viability." Johnson K.R., Johnson K.Y., Becker K.P., Bielawski J., Mao C., Obeid L.M. J. Biol. Chem. 278:34541-34547(2003) [PubMed: 12815058] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION. Tissue: Fetal kidney.
[2]	"Cloning of human sphingosine-1-phosphatase." Van Veldhoven P.P. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thalamus.
[4]	"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].
[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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta and PNS.
[7]	"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-112, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-112, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-112 AND THR-114, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, MASS SPECTROMETRY.
[14]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF349315 mRNA. Translation: AAK26660.1. AJ293294 mRNA. Translation: CAC17772.1. AK314188 mRNA. Translation: BAG36867.1. AL161670 Genomic DNA. No translation available. CH471061 Genomic DNA. Translation: EAW80834.1. BC063839 mRNA. Translation: AAH63839.1. BC070060 mRNA. Translation: AAH70060.1.
IPI	IPI00306840.
RefSeq	NP_110418.1. NM_030791.2.
UniGene	Hs.24678.
3D structure databases
ProteinModelPortal	Q9BX95.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9BX95.
PTM databases
PhosphoSite	Q9BX95.
Polymorphism databases
DMDM	46577706.
Proteomic databases
PeptideAtlas	Q9BX95.
PRIDE	Q9BX95.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000247225; ENSP00000247225; ENSG00000126821.
GeneID	81537.
KEGG	hsa:81537.
NMPDR	fig|9606.3.peg.9708.
UCSC	uc001xgj.1. human.
Organism-specific databases
CTD	81537.
GeneCards	GC14M064150.
H-InvDB	HIX0037676.
HGNC	HGNC:17720. SGPP1.
MIM	612826. gene.
neXtProt	NX_Q9BX95.
PharmGKB	PA134884424.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16998.
GeneTree	ENSGT00390000017322.
HOGENOM	HBG713817.
HOVERGEN	HBG079185.
InParanoid	Q9BX95.
OMA	WVLVMYL.
OrthoDB	EOG4B8JD0.
PhylomeDB	Q9BX95.
Enzyme and pathway databases
Pathway_Interaction_DB	s1p_meta_pathway. Sphingosine 1-phosphate (S1P) pathway.
Reactome	REACT_22258. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	Q9BX95.
Bgee	Q9BX95.
CleanEx	HS_SGPP1.
Genevestigator	Q9BX95.
GermOnline	ENSG00000126821. Homo sapiens.
Family and domain databases
InterPro	IPR016118. P_Acid_Pase/Cl_peroxidase_N. IPR000326. P_Acid_Pase_2/haloperoxidase. [Graphical view]
Gene3D	G3DSA:1.20.144.10. P_Acid_Pase/Cl_peroxidase_N. 1 hit.
KO	K04716.
Pfam	PF01569. PAP2. 1 hit. [Graphical view]
SMART	SM00014. acidPPc. 1 hit. [Graphical view]
SUPFAM	SSF48317. AcPase_VanPerase. 1 hit.
ProtoNet	Search...
Other
NextBio	71763.
SOURCE	Search...

Entry information

Entry name

SGPP1_HUMAN

Accession

Primary (citable) accession number: Q9BX95
Secondary accession number(s): B2RAH0, Q9H189

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	April 26, 2004
Last modified:	January 25, 2012
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.