Phosphatidylserine synthase 1 - Homo sapiens (Human)

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P48651 (PTSS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phosphatidylserine synthase 1
Short name=PSS-1
Short name=PtdSer synthase 1
EC=2.7.8.29

Alternative name(s):
Serine-exchange enzyme I

Gene names

Name:	PTDSS1
Synonyms:	KIAA0024, PSSA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. In membranes, PTDSS1 catalyzes mainly the conversion of phosphatidylcholine. Also converts, in vitro and to a lesser extent, phosphatidylethanolamine.
Catalytic activity	L-1-phosphatidylethanolamine + L-serine = L-1-phosphatidylserine + ethanolamine.
Enzyme regulation	Requires calcium ions. Activated by exogenous phosphatidylethanolamine. Ref.4 Ref.9
Pathway	Phospholipid metabolism; phosphatidylserine biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: Highly enriched in the mitochondria-associated membrane (MAM) By similarity.
Sequence similarities	Belongs to the phosphatidyl serine synthase family.
Biophysicochemical properties	Kinetic parameters: K_M=67 µM for serine (in the presence of 2 mM PC) Ref.9 K_M=24 µM for serine (in the presence of 1 mM PE) pH dependence: Optimum pH for both PC and PE is between 7.0 and 7.5.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phosphatidylserine biosynthetic process Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	transferase activity 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 – 473

473

Phosphatidylserine synthase 1

PRO_0000056829

Regions

Topological domain

1 – 35

Cytoplasmic Potential

Transmembrane

36 – 56

Helical; Potential

Topological domain

57 – 72

Lumenal Potential

Transmembrane

73 – 93

Helical; Potential

Topological domain

94 – 102

Cytoplasmic Potential

Transmembrane

103 – 123

Helical; Potential

Topological domain

124 – 186

Lumenal Potential

Transmembrane

187 – 207

Helical; Potential

Topological domain

208 – 216

Cytoplasmic Potential

Transmembrane

217 – 237

Helical; Potential

Topological domain

238 – 286

Lumenal Potential

Transmembrane

287 – 307

Helical; Potential

Topological domain

308 – 319

Cytoplasmic Potential

Transmembrane

320 – 342

Helical; Potential

Topological domain

343 – 355

Lumenal Potential

Transmembrane

356 – 376

Helical; Potential

Topological domain

377 – 383

Cytoplasmic Potential

Transmembrane

384 – 404

Helical; Potential

Topological domain

405 – 473

Lumenal Potential

Amino acid modifications

Modified residue

417

Phosphoserine Ref.8

Modified residue

425

Phosphoserine Ref.8

Modified residue

442

Phosphoserine Ref.7 Ref.10 Ref.11

Modified residue

454

Phosphoserine Ref.11

Natural variations

Natural variant

423

T → N.
Corresponds to variant rs7835798 [ dbSNP | Ensembl ].

VAR_048735

Sequences

Sequence

Length

Mass (Da)

Tools

P48651 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: CFC8F50A33CE038D
Show »

FASTA

473

55,528

        10         20         30         40         50         60 
MASCVGSRTL SKDDVNYKMH FRMINEQQVE DITIDFFYRP HTITLLSFTI VSLMYFAFTR 

        70         80         90        100        110        120 
DDSVPEDNIW RGILSVIFFF LIISVLAFPN GPFTRPHPAL WRMVFGLSVL YFLFLVFLLF 

       130        140        150        160        170        180 
LNFEQVKSLM YWLDPNLRYA TREADVMEYA VNCHVITWER IISHFDIFAF GHFWGWAMKA 

       190        200        210        220        230        240 
LLIRSYGLCW TISITWELTE LFFMHLLPNF AECWWDQVIL DILLCNGGGI WLGMVVCRFL 

       250        260        270        280        290        300 
EMRTYHWASF KDIHTTTGKI KRAVLQFTPA SWTYVRWFDP KSSFQRVAGV YLFMIIWQLT 

       310        320        330        340        350        360 
ELNTFFLKHI FVFQASHPLS WGRILFIGGI TAPTVRQYYA YLTDTQCKRV GTQCWVFGVI 

       370        380        390        400        410        420 
GFLEAIVCIK FGQDLFSKTQ ILYVVLWLLC VAFTTFLCLY GMIWYAEHYG HREKTYSECE 

       430        440        450        460        470 
DGTYSPEISW HHRKGTKGSE DSPPKHAGNN ESHSSRRRNR HSKSKVTNGV GKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1." Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S. DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[2]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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]. Tissue: Brain and Lymph.
[4]	"Control of phosphatidylserine biosynthesis through phosphatidylserine-mediated inhibition of phosphatidylserine synthase I in Chinese hamster ovary cells." Kuge O., Hasegawa K., Saito K., Nishijima M. Proc. Natl. Acad. Sci. U.S.A. 95:4199-4203(1998) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[5]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[6]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-425, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Purification and characterization of human phosphatidylserine synthases 1 and 2." Tomohiro S., Kawaguti A., Kawabe Y., Kitada S., Kuge O. Biochem. J. 418:421-429(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[10]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, MASS SPECTROMETRY.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442 AND SER-454, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	D14694 mRNA. Translation: BAA03520.1. AP003465 Genomic DNA. No translation available. BC004192 mRNA. Translation: AAH04192.1. BC004390 mRNA. Translation: AAH04390.1.
IPI	IPI00010746.
RefSeq	NP_055569.1. NM_014754.1.
UniGene	Hs.292579.
3D structure databases
ProteinModelPortal	P48651.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000337331.
PTM databases
PhosphoSite	P48651.
Polymorphism databases
DMDM	1346881.
Proteomic databases
PaxDb	P48651.
PeptideAtlas	P48651.
PRIDE	P48651.
Protocols and materials databases
DNASU	9791.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000517309; ENSP00000430548; ENSG00000156471.
GeneID	9791.
KEGG	hsa:9791.
UCSC	uc003yht.1. human.
Organism-specific databases
CTD	9791.
GeneCards	GC08P097343.
HGNC	HGNC:9587. PTDSS1.
HPA	HPA016852.
MIM	612792. gene.
neXtProt	NX_P48651.
PharmGKB	PA33939.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG264399.
HOVERGEN	HBG053765.
InParanoid	P48651.
KO	K08729.
OMA	WERIVSH.
OrthoDB	EOG4PNXGW.
PhylomeDB	P48651.
Enzyme and pathway databases
BioCyc	MetaCyc:HS08129-MONOMER.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00948.
Gene expression databases
ArrayExpress	P48651.
Bgee	P48651.
CleanEx	HS_PTDSS1.
Genevestigator	P48651.
Family and domain databases
InterPro	IPR004277. PSS. [Graphical view]
PANTHER	PTHR12615. PTHR12615. 1 hit.
Pfam	PF03034. PSS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00144. Phosphatidylserine.
GenomeRNAi	9791.
NextBio	36870.
SOURCE	Search...

Entry information

Entry name

PTSS1_HUMAN

Accession

Primary (citable) accession number: P48651

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 100 of the entry and version 1 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.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents