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Pyridoxal phosphate homeostasis protein (PLP homeostasis protein) (Proline synthase co-transcribed bacterial homolog protein) (Pyridoxal phosphate-binding protein)

 PLPHP_HUMAN             Reviewed;         275 AA.
O94903; Q6FI94;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
07-NOV-2018, entry version 162.
RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000255|HAMAP-Rule:MF_03225};
Short=PLP homeostasis protein {ECO:0000255|HAMAP-Rule:MF_03225};
AltName: Full=Proline synthase co-transcribed bacterial homolog protein {ECO:0000255|HAMAP-Rule:MF_03225};
AltName: Full=Pyridoxal phosphate-binding protein {ECO:0000312|HGNC:HGNC:9457};
Name=PLPBP {ECO:0000255|HAMAP-Rule:MF_03225,
ECO:0000312|HGNC:HGNC:9457};
Synonyms=PROSC {ECO:0000255|HAMAP-Rule:MF_03225,
ECO:0000312|HGNC:HGNC:9457};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10496079; DOI=10.1007/s100380050172;
Ikegawa S., Isomura M., Koshizuka Y., Nakamura Y.;
"Cloning and characterization of human and mouse PROSC (proline
synthetase co-transcribed) genes.";
J. Hum. Genet. 44:337-342(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-244, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-244, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[9]
INVOLVEMENT IN EPVB6D, FUNCTION, VARIANTS EPVB6D 71-GLN--HIS-275 DEL;
78-SER--HIS-275 DEL; LEU-87; PRO-175 AND GLN-241, AND CHARACTERIZATION
OF VARIANTS EPVB6D 78-SER--HIS-275 DEL AND PRO-175.
PubMed=27912044; DOI=10.1016/j.ajhg.2016.10.011;
Darin N., Reid E., Prunetti L., Samuelsson L., Husain R.A., Wilson M.,
El Yacoubi B., Footitt E., Chong W.K., Wilson L.C., Prunty H.,
Pope S., Heales S., Lascelles K., Champion M., Wassmer E.,
Veggiotti P., de Crecy-Lagard V., Mills P.B., Clayton P.T.;
"Mutations in PROSC disrupt cellular pyridoxal phosphate homeostasis
and cause vitamin-B6-dependent epilepsy.";
Am. J. Hum. Genet. 99:1325-1337(2016).
-!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which may
be involved in intracellular homeostatic regulation of pyridoxal
5'-phosphate (PLP), the active form of vitamin B6.
{ECO:0000255|HAMAP-Rule:MF_03225, ECO:0000269|PubMed:27912044}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DISEASE: Epilepsy, early-onset, vitamin B6-dependent (EPVB6D)
[MIM:617290]: An autosomal recessive neurologic disorder
characterized by seizures responsive to treatment with activated
vitamin B6 and/or pyridoxine. Most patients show delayed
psychomotor development, mental retardation and learning
disability. Seizures onset is in the first days or months of life.
{ECO:0000269|PubMed:27912044}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
YggS/PROSC family. {ECO:0000255|HAMAP-Rule:MF_03225}.
-----------------------------------------------------------------------
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EMBL; AB018566; BAA36842.1; -; Genomic_DNA.
EMBL; AL136616; CAB66551.1; -; mRNA.
EMBL; CR533532; CAG38563.1; -; mRNA.
EMBL; BC012334; AAH12334.1; -; mRNA.
CCDS; CCDS6096.1; -.
RefSeq; NP_009129.1; NM_007198.3.
UniGene; Hs.304792; -.
UniGene; Hs.608177; -.
ProteinModelPortal; O94903; -.
SMR; O94903; -.
BioGrid; 116381; 66.
IntAct; O94903; 14.
STRING; 9606.ENSP00000333551; -.
DrugBank; DB00172; L-Proline.
DrugBank; DB00114; Pyridoxal Phosphate.
iPTMnet; O94903; -.
PhosphoSitePlus; O94903; -.
BioMuta; PROSC; -.
UCD-2DPAGE; O94903; -.
EPD; O94903; -.
MaxQB; O94903; -.
PaxDb; O94903; -.
PeptideAtlas; O94903; -.
PRIDE; O94903; -.
ProteomicsDB; 50537; -.
DNASU; 11212; -.
Ensembl; ENST00000328195; ENSP00000333551; ENSG00000147471.
GeneID; 11212; -.
KEGG; hsa:11212; -.
UCSC; uc003xkh.4; human.
CTD; 11212; -.
DisGeNET; 11212; -.
EuPathDB; HostDB:ENSG00000147471.11; -.
GeneCards; PLPBP; -.
HGNC; HGNC:9457; PLPBP.
HPA; CAB017033; -.
HPA; HPA023646; -.
HPA; HPA023733; -.
MalaCards; PLPBP; -.
MIM; 604436; gene.
MIM; 617290; phenotype.
neXtProt; NX_O94903; -.
OpenTargets; ENSG00000147471; -.
Orphanet; 3006; Pyridoxine-dependent epilepsy.
PharmGKB; PA33810; -.
eggNOG; KOG3157; Eukaryota.
eggNOG; COG0325; LUCA.
GeneTree; ENSGT00390000004928; -.
HOVERGEN; HBG053692; -.
InParanoid; O94903; -.
KO; K06997; -.
OMA; LQWHFIG; -.
OrthoDB; EOG091G0IMD; -.
PhylomeDB; O94903; -.
TreeFam; TF314637; -.
ChiTaRS; PROSC; human.
GeneWiki; PROSC; -.
GenomeRNAi; 11212; -.
PRO; PR:O94903; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000147471; Expressed in 241 organ(s), highest expression level in upper lobe of lung.
CleanEx; HS_PROSC; -.
ExpressionAtlas; O94903; baseline and differential.
Genevisible; O94903; HS.
GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
Gene3D; 3.20.20.10; -; 1.
HAMAP; MF_02087; PLP_homeostasis; 1.
InterPro; IPR001608; Ala_racemase_N.
InterPro; IPR029066; PLP-binding_barrel.
InterPro; IPR011078; PyrdxlP_homeostasis.
PANTHER; PTHR10146; PTHR10146; 1.
Pfam; PF01168; Ala_racemase_N; 1.
PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1.
SUPFAM; SSF51419; SSF51419; 1.
TIGRFAMs; TIGR00044; TIGR00044; 1.
PROSITE; PS01211; UPF0001; 1.
1: Evidence at protein level;
Complete proteome; Disease mutation; Epilepsy; Phosphoprotein;
Polymorphism; Pyridoxal phosphate; Reference proteome.
CHAIN 1 275 Pyridoxal phosphate homeostasis protein.
/FTId=PRO_0000163210.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 47 47 N6-(pyridoxal phosphate)lysine.
{ECO:0000255|HAMAP-Rule:MF_03225}.
MOD_RES 69 69 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9Z2Y8}.
MOD_RES 125 125 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9Z2Y8}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 244 244 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VARIANT 24 24 V -> M (in dbSNP:rs35423325).
/FTId=VAR_052476.
VARIANT 71 275 Missing (in EPVB6D).
{ECO:0000269|PubMed:27912044}.
/FTId=VAR_078004.
VARIANT 78 275 Missing (in EPVB6D; decreased expression
at the mRNA level; undetectable at the
protein level in patient's fibroblasts).
{ECO:0000269|PubMed:27912044}.
/FTId=VAR_078005.
VARIANT 87 87 P -> L (in EPVB6D; dbSNP:rs755946598).
{ECO:0000269|PubMed:27912044}.
/FTId=VAR_078006.
VARIANT 175 175 L -> P (in EPVB6D; decreased expression
at the mRNA level; undetectable at the
protein level in patient's fibroblasts;
dbSNP:rs752753379).
{ECO:0000269|PubMed:27912044}.
/FTId=VAR_078007.
VARIANT 241 241 R -> Q (in EPVB6D; dbSNP:rs760609867).
{ECO:0000269|PubMed:27912044}.
/FTId=VAR_078008.
SEQUENCE 275 AA; 30344 MW; A81049432B1A8732 CRC64;
MWRAGSMSAE LGVGCALRAV NERVQQAVAR RPRDLPAIQP RLVAVSKTKP ADMVIEAYGH
GQRTFGENYV QELLEKASNP KILSLCPEIK WHFIGHLQKQ NVNKLMAVPN LFMLETVDSV
KLADKVNSSW QRKGSPERLK VMVQINTSGE ESKHGLPPSE TIAIVEHINA KCPNLEFVGL
MTIGSFGHDL SQGPNPDFQL LLSLREELCK KLNIPADQVE LSMGMSADFQ HAVEVGSTNV
RIGSTIFGER DYSKKPTPDK CAADVKAPLE VAQEH


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