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Protein

Phosphatidylserine decarboxylase proenzyme

Gene

PISD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Phosphatidyl-L-serine = phosphatidylethanolamine + CO2.

Cofactori

pyruvateBy similarityNote: Binds 1 pyruvoyl group covalently per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei377 – 3782Cleavage (non-hydrolytic)By similarity

GO - Molecular functioni

  1. phosphatidylserine decarboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycerophospholipid biosynthetic process Source: Reactome
  2. phosphatidylethanolamine biosynthetic process Source: Reactome
  3. phospholipid metabolic process Source: Reactome
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

Pyruvate

Enzyme and pathway databases

BioCyciMetaCyc:HS01985-MONOMER.
ReactomeiREACT_120919. Synthesis of PE.
UniPathwayiUPA00558; UER00616.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylserine decarboxylase proenzyme (EC:4.1.1.65)
Cleaved into the following 2 chains:
Gene namesi
Name:PISD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:8999. PISD.

Subcellular locationi

  1. Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
  2. nucleus Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33333.

Chemistry

DrugBankiDB00144. Phosphatidylserine.

Polymorphism and mutation databases

BioMutaiPISD.
DMDMi311033492.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Phosphatidylserine decarboxylase beta chainPRO_0000029835Add
BLAST
Chaini378 – 40932Phosphatidylserine decarboxylase alpha chainPRO_0000029836Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei378 – 3781Pyruvic acid (Ser)By similarity

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiQ9UG56.
PaxDbiQ9UG56.
PRIDEiQ9UG56.

PTM databases

PhosphoSiteiQ9UG56.

Expressioni

Gene expression databases

BgeeiQ9UG56.
CleanExiHS_PISD.
ExpressionAtlasiQ9UG56. baseline and differential.
GenevestigatoriQ9UG56.

Organism-specific databases

HPAiHPA031090.
HPA031091.

Interactioni

Subunit structurei

Heterodimer.By similarity

Protein-protein interaction databases

BioGridi117262. 5 interactions.
IntActiQ9UG56. 2 interactions.
STRINGi9606.ENSP00000266095.

Structurei

3D structure databases

ProteinModelPortaliQ9UG56.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0688.
GeneTreeiENSGT00390000013484.
HOVERGENiHBG039630.
InParanoidiQ9UG56.
KOiK01613.
OMAiSTELYQC.
OrthoDBiEOG76T9RH.
PhylomeDBiQ9UG56.
TreeFamiTF313148.

Family and domain databases

InterProiIPR003817. PS_Dcarbxylase.
[Graphical view]
PANTHERiPTHR10067. PTHR10067. 1 hit.
PfamiPF02666. PS_Dcarbxylase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00163. PS_decarb. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UG56-3) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MATSVGHRCL GLLHGVAPWR SSLHPCEITA LSQSLQPLRK LPFRAFRTDA
60 70 80 90 100
RKIHTAPART MFLLRPLPIL LVTGGGYAGY RQYEKYRERE LEKLGLEIPP
110 120 130 140 150
KLAGHWEVAL YKSVPTRLLS RAWGRLNQVE LPHWLRRPVY SLYIWTFGVN
160 170 180 190 200
MKEAAVEDLH HYRNLSEFFR RKLKPQARPV CGLHSVISPS DGRILNFGQV
210 220 230 240 250
KNCEVEQVKG VTYSLESFLG PRMCTEDLPF PPAASCDSFK NQLVTREGNE
260 270 280 290 300
LYHCVIYLAP GDYHCFHSPT DWTVSHRRHF PGSLMSVNPG MARWIKELFC
310 320 330 340 350
HNERVVLTGD WKHGFFSLTA VGATNVGSIR IYFDRDLHTN SPRHSKGSYN
360 370 380 390 400
DFSFVTHTNR EGVPMRKGEH LGEFNLGSTI VLIFEAPKDF NFQLKTGQKI

RFGEALGSL
Length:409
Mass (Da):46,672
Last modified:November 2, 2010 - v4
Checksum:i6A5148265369D9DF
GO
Isoform 2 (identifier: Q9UG56-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-107: MATSVGHRCL...IPPKLAGHWE → MMCQSEARQG...SRVGWRPVSR

Note: No experimental confirmation available.

Show »
Length:375
Mass (Da):43,047
Checksum:i4ED283AD1944C3C9
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 107107MATSV…AGHWE → MMCQSEARQGPELRAAKWLH FPQLALRRRLGQLSCMSRPA LKLRSWPLTVLYYLLPFGAL RPLSRVGWRPVSR in isoform 2. 1 PublicationVSP_007540Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR456540 mRNA. Translation: CAG30426.1.
AL050371 Transcribed RNA. Translation: CAB43678.2. Sequence problems.
AL096768 Genomic DNA. Translation: CAB56394.1.
AL096768, AL031255 Genomic DNA. Translation: CAI23032.1.
AL031255, AL096768 Genomic DNA. Translation: CAI22447.1.
CH471095 Genomic DNA. Translation: EAW59984.1.
BC001482 mRNA. Translation: AAH01482.1.
BC009315 mRNA. Translation: AAH09315.1.
AF035304 mRNA. Translation: AAB88186.1.
CCDSiCCDS13899.1. [Q9UG56-2]
RefSeqiNP_055153.1. NM_014338.3. [Q9UG56-2]
XP_005261512.1. XM_005261455.1. [Q9UG56-3]
XP_005261513.1. XM_005261456.1. [Q9UG56-2]
XP_005261514.1. XM_005261457.3. [Q9UG56-2]
XP_005261515.1. XM_005261458.1. [Q9UG56-2]
XP_005261516.1. XM_005261459.1. [Q9UG56-2]
XP_005261517.1. XM_005261460.3. [Q9UG56-2]
XP_005261518.1. XM_005261461.3. [Q9UG56-2]
XP_006724263.1. XM_006724200.2. [Q9UG56-2]
XP_006724264.1. XM_006724201.2. [Q9UG56-2]
XP_006724265.1. XM_006724202.2. [Q9UG56-2]
UniGeneiHs.420559.
Hs.732339.

Genome annotation databases

EnsembliENST00000266095; ENSP00000266095; ENSG00000241878. [Q9UG56-2]
ENST00000382151; ENSP00000371586; ENSG00000241878. [Q9UG56-2]
ENST00000439502; ENSP00000391739; ENSG00000241878. [Q9UG56-3]
GeneIDi23761.
KEGGihsa:23761.
UCSCiuc003alk.2. human. [Q9UG56-2]
uc003alm.4. human. [Q9UG56-3]

Polymorphism and mutation databases

BioMutaiPISD.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR456540 mRNA. Translation: CAG30426.1.
AL050371 Transcribed RNA. Translation: CAB43678.2. Sequence problems.
AL096768 Genomic DNA. Translation: CAB56394.1.
AL096768, AL031255 Genomic DNA. Translation: CAI23032.1.
AL031255, AL096768 Genomic DNA. Translation: CAI22447.1.
CH471095 Genomic DNA. Translation: EAW59984.1.
BC001482 mRNA. Translation: AAH01482.1.
BC009315 mRNA. Translation: AAH09315.1.
AF035304 mRNA. Translation: AAB88186.1.
CCDSiCCDS13899.1. [Q9UG56-2]
RefSeqiNP_055153.1. NM_014338.3. [Q9UG56-2]
XP_005261512.1. XM_005261455.1. [Q9UG56-3]
XP_005261513.1. XM_005261456.1. [Q9UG56-2]
XP_005261514.1. XM_005261457.3. [Q9UG56-2]
XP_005261515.1. XM_005261458.1. [Q9UG56-2]
XP_005261516.1. XM_005261459.1. [Q9UG56-2]
XP_005261517.1. XM_005261460.3. [Q9UG56-2]
XP_005261518.1. XM_005261461.3. [Q9UG56-2]
XP_006724263.1. XM_006724200.2. [Q9UG56-2]
XP_006724264.1. XM_006724201.2. [Q9UG56-2]
XP_006724265.1. XM_006724202.2. [Q9UG56-2]
UniGeneiHs.420559.
Hs.732339.

3D structure databases

ProteinModelPortaliQ9UG56.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117262. 5 interactions.
IntActiQ9UG56. 2 interactions.
STRINGi9606.ENSP00000266095.

Chemistry

DrugBankiDB00144. Phosphatidylserine.

PTM databases

PhosphoSiteiQ9UG56.

Polymorphism and mutation databases

BioMutaiPISD.
DMDMi311033492.

Proteomic databases

MaxQBiQ9UG56.
PaxDbiQ9UG56.
PRIDEiQ9UG56.

Protocols and materials databases

DNASUi23761.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266095; ENSP00000266095; ENSG00000241878. [Q9UG56-2]
ENST00000382151; ENSP00000371586; ENSG00000241878. [Q9UG56-2]
ENST00000439502; ENSP00000391739; ENSG00000241878. [Q9UG56-3]
GeneIDi23761.
KEGGihsa:23761.
UCSCiuc003alk.2. human. [Q9UG56-2]
uc003alm.4. human. [Q9UG56-3]

Organism-specific databases

CTDi23761.
GeneCardsiGC22M032014.
HGNCiHGNC:8999. PISD.
HPAiHPA031090.
HPA031091.
MIMi612770. gene.
neXtProtiNX_Q9UG56.
PharmGKBiPA33333.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0688.
GeneTreeiENSGT00390000013484.
HOVERGENiHBG039630.
InParanoidiQ9UG56.
KOiK01613.
OMAiSTELYQC.
OrthoDBiEOG76T9RH.
PhylomeDBiQ9UG56.
TreeFamiTF313148.

Enzyme and pathway databases

UniPathwayiUPA00558; UER00616.
BioCyciMetaCyc:HS01985-MONOMER.
ReactomeiREACT_120919. Synthesis of PE.

Miscellaneous databases

ChiTaRSiPISD. human.
GeneWikiiPISD_(gene).
GenomeRNAii23761.
NextBioi46711.
PROiQ9UG56.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UG56.
CleanExiHS_PISD.
ExpressionAtlasiQ9UG56. baseline and differential.
GenevestigatoriQ9UG56.

Family and domain databases

InterProiIPR003817. PS_Dcarbxylase.
[Graphical view]
PANTHERiPTHR10067. PTHR10067. 1 hit.
PfamiPF02666. PS_Dcarbxylase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00163. PS_decarb. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Neuroblastoma and Rhabdomyosarcoma.
  6. Yu W., Sarginson J., Gibbs R.A.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 333-409.
    Tissue: Brain.

Entry informationi

Entry nameiPISD_HUMAN
AccessioniPrimary (citable) accession number: Q9UG56
Secondary accession number(s): B1AKM7
, O43207, O95535, Q6IC28, Q96GQ2, Q9UGA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: November 2, 2010
Last modified: April 29, 2015
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.