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P48651 (PTSS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
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

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:

KM=67 µM for serine (in the presence of 2 mM PC) Ref.9

KM=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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Phosphatidylserine synthase 1
PRO_0000056829

Regions

Topological domain1 – 3535Cytoplasmic Potential
Transmembrane36 – 5621Helical; Potential
Topological domain57 – 7216Lumenal Potential
Transmembrane73 – 9321Helical; Potential
Topological domain94 – 1029Cytoplasmic Potential
Transmembrane103 – 12321Helical; Potential
Topological domain124 – 18663Lumenal Potential
Transmembrane187 – 20721Helical; Potential
Topological domain208 – 2169Cytoplasmic Potential
Transmembrane217 – 23721Helical; Potential
Topological domain238 – 28649Lumenal Potential
Transmembrane287 – 30721Helical; Potential
Topological domain308 – 31912Cytoplasmic Potential
Transmembrane320 – 34223Helical; Potential
Topological domain343 – 35513Lumenal Potential
Transmembrane356 – 37621Helical; Potential
Topological domain377 – 3837Cytoplasmic Potential
Transmembrane384 – 40421Helical; Potential
Topological domain405 – 47369Lumenal Potential

Amino acid modifications

Modified residue4171Phosphoserine Ref.8
Modified residue4251Phosphoserine Ref.8
Modified residue4421Phosphoserine Ref.7 Ref.10 Ref.11
Modified residue4541Phosphoserine Ref.11

Natural variations

Natural variant4231T → N.
Corresponds to variant rs7835798 [ dbSNP | Ensembl ].
VAR_048735

Sequences

Sequence LengthMass (Da)Tools
P48651 [UniParc].

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

FASTA47355,528
        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' 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. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
RefSeqNP_055569.1. NM_014754.1.
UniGeneHs.292579.

3D structure databases

ProteinModelPortalP48651.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115135. 2 interactions.
IntActP48651. 1 interaction.
STRING9606.ENSP00000337331.

Chemistry

DrugBankDB00144. Phosphatidylserine.

PTM databases

PhosphoSiteP48651.

Polymorphism databases

DMDM1346881.

Proteomic databases

PaxDbP48651.
PeptideAtlasP48651.
PRIDEP48651.

Protocols and materials databases

DNASU9791.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000517309; ENSP00000430548; ENSG00000156471.
GeneID9791.
KEGGhsa:9791.
UCSCuc003yht.1. human.

Organism-specific databases

CTD9791.
GeneCardsGC08P097343.
HGNCHGNC:9587. PTDSS1.
HPAHPA016852.
MIM612792. gene.
neXtProtNX_P48651.
PharmGKBPA33939.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264399.
HOVERGENHBG053765.
InParanoidP48651.
KOK08729.
OMASGNNESH.
OrthoDBEOG7CRTQC.
PhylomeDBP48651.
TreeFamTF300012.

Enzyme and pathway databases

BioCycMetaCyc:HS08129-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00948.

Gene expression databases

ArrayExpressP48651.
BgeeP48651.
CleanExHS_PTDSS1.
GenevestigatorP48651.

Family and domain databases

InterProIPR004277. PSS.
[Graphical view]
PANTHERPTHR12615. PTHR12615. 1 hit.
PfamPF03034. PSS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi9791.
NextBio36870.
PROP48651.
SOURCESearch...

Entry information

Entry namePTSS1_HUMAN
AccessionPrimary (citable) accession number: P48651
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 107 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 8

Human chromosome 8: entries, gene names and cross-references to MIM