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O43175

- SERA_HUMAN

UniProt

O43175 - SERA_HUMAN

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Protein

D-3-phosphoglycerate dehydrogenase

Gene

PHGDH

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

Functioni

Catalytic activityi

3-phospho-D-glycerate + NAD+ = 3-phosphonooxypyruvate + NADH.1 Publication
2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH.1 Publication

Kineticsi

  1. KM=21.6 µM for 3-phosphohydroxypyruvate1 Publication

Vmax=35 nmol/min/mg enzyme with 3-phosphohydroxypyruvate as substrate (in patient-derived fibroblasts)1 Publication

Vmax=168 nmol/min/mg enzyme with 3-phosphohydroxypyruvate as substrate (in 3-PGDH overexpressed cells)1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781NAD1 Publication
Binding sitei175 – 1751NAD1 Publication
Binding sitei207 – 2071NAD; via carbonyl oxygen1 Publication
Active sitei236 – 2361
Binding sitei260 – 2601NAD1 Publication
Active sitei265 – 2651By similarity
Active sitei283 – 2831Proton donor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi155 – 1562NAD1 Publication
Nucleotide bindingi234 – 2363NAD1 Publication
Nucleotide bindingi283 – 2864NAD1 Publication

GO - Molecular functioni

  1. electron carrier activity Source: UniProtKB
  2. NAD binding Source: InterPro
  3. phosphoglycerate dehydrogenase activity Source: Reactome

GO - Biological processi

  1. brain development Source: ProtInc
  2. cellular amino acid biosynthetic process Source: Reactome
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. G1 to G0 transition Source: Ensembl
  5. gamma-aminobutyric acid metabolic process Source: Ensembl
  6. glial cell development Source: Ensembl
  7. glutamine metabolic process Source: Ensembl
  8. glycine metabolic process Source: Ensembl
  9. L-serine biosynthetic process Source: Reactome
  10. neural tube development Source: Ensembl
  11. neuron projection development Source: Ensembl
  12. regulation of gene expression Source: Ensembl
  13. small molecule metabolic process Source: Reactome
  14. spinal cord development Source: Ensembl
  15. taurine metabolic process Source: Ensembl
  16. threonine metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Serine biosynthesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS01776-MONOMER.
ReactomeiREACT_115789. Serine biosynthesis.
UniPathwayiUPA00135; UER00196.

Names & Taxonomyi

Protein namesi
Recommended name:
D-3-phosphoglycerate dehydrogenase (EC:1.1.1.95)
Short name:
3-PGDH
Gene namesi
Name:PHGDH
Synonyms:PGDH3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:8923. PHGDH.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Phosphoglycerate dehydrogenase deficiency (PHGDH deficiency) [MIM:601815]: Characterized by congenital microcephaly, psychomotor retardation, and seizures.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti135 – 1351R → W in PHGDH deficiency; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity. 1 Publication
VAR_059026
Natural varianti261 – 2611V → M in PHGDH deficiency; results in a four-fold decrease in substrate affinity and a slight increase in maximal enzyme activity with 3-phosphohydroxypyruvate. 1 Publication
VAR_059027
Natural varianti373 – 3731A → T in PHGDH deficiency; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate. 1 Publication
VAR_059028
Natural varianti377 – 3771G → S in PHGDH deficiency; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity. 1 Publication
VAR_059029
Natural varianti425 – 4251V → M in PHGDH deficiency; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate. 1 Publication
VAR_013461
Natural varianti490 – 4901V → M in PHGDH deficiency; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate. 2 Publications
Corresponds to variant rs121907987 [ dbSNP | Ensembl ].
VAR_059030
Neu-Laxova syndrome (NLS) [MIM:256520]: A lethal, autosomal recessive multiple malformation syndrome characterized by ichthyosis, marked intrauterine growth restriction, microcephaly, short neck, limb deformities, hypoplastic lungs, edema, and central nervous system anomalies including lissencephaly, cerebellar hypoplasia and/or abnormal/agenesis of the corpus callosum. Abnormal facial features include severe proptosis with ectropion, hypertelorism, micrognathia, flattened nose, and malformed ears.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti140 – 1401G → R in NLS. 1 Publication
VAR_071819
Natural varianti163 – 1631R → Q in NLS. 1 Publication
VAR_071820

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi256520. phenotype.
601815. phenotype.
Orphaneti79351. 3-phosphoglycerate dehydrogenase deficiency.
2671. Neu-Laxova syndrome.
PharmGKBiPA33264.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 533532D-3-phosphoglycerate dehydrogenasePRO_0000076012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei21 – 211N6-acetyllysineBy similarity
Modified residuei58 – 581N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO43175.
PaxDbiO43175.
PeptideAtlasiO43175.
PRIDEiO43175.

PTM databases

PhosphoSiteiO43175.

Expressioni

Inductioni

Induced by 17-beta-estradiol (estrogenic ligand) and 4-hydroxytamoxifen (agonist/antagonist ligand). Positively regulated by the transcription factors SP1 and NF-Y.2 Publications

Gene expression databases

BgeeiO43175.
CleanExiHS_PHGDH.
ExpressionAtlasiO43175. baseline and differential.
GenevestigatoriO43175.

Organism-specific databases

HPAiCAB003681.
HPA021241.
HPA024031.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi117618. 71 interactions.
IntActiO43175. 25 interactions.
MINTiMINT-4999739.
STRINGi9606.ENSP00000358417.

Structurei

Secondary structure

1
533
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114Combined sources
Helixi18 – 269Combined sources
Beta strandi29 – 324Combined sources
Helixi38 – 447Combined sources
Helixi45 – 473Combined sources
Beta strandi49 – 535Combined sources
Beta strandi55 – 573Combined sources
Helixi61 – 666Combined sources
Beta strandi72 – 798Combined sources
Helixi85 – 917Combined sources
Beta strandi94 – 963Combined sources
Helixi103 – 11917Combined sources
Helixi121 – 1299Combined sources
Helixi136 – 1383Combined sources
Beta strandi147 – 1515Combined sources
Helixi155 – 16511Combined sources
Turni166 – 1683Combined sources
Beta strandi170 – 1745Combined sources
Beta strandi176 – 1783Combined sources
Helixi180 – 1856Combined sources
Helixi193 – 1964Combined sources
Helixi197 – 1993Combined sources
Beta strandi201 – 2055Combined sources
Turni211 – 2155Combined sources
Helixi219 – 2224Combined sources
Beta strandi229 – 2335Combined sources
Helixi242 – 25110Combined sources
Beta strandi252 – 2609Combined sources
Beta strandi263 – 2664Combined sources
Helixi271 – 2744Combined sources
Beta strandi278 – 2803Combined sources
Helixi289 – 30618Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G76X-ray1.70A/B4-315[»]
ProteinModelPortaliO43175.
SMRiO43175. Positions 6-307.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43175.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0111.
GeneTreeiENSGT00530000063021.
HOGENOMiHOG000136693.
HOVERGENiHBG054241.
InParanoidiO43175.
KOiK00058.
OMAiDNTFAQC.
OrthoDBiEOG7JT6WT.
PhylomeDBiO43175.
TreeFamiTF314548.

Family and domain databases

Gene3Di3.30.1330.90. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR029009. ASB_dom.
IPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR006236. PGDH.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF143548. SSF143548. 1 hit.
TIGRFAMsiTIGR01327. PGDH. 1 hit.
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O43175-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFANLRKVL ISDSLDPCCR KILQDGGLQV VEKQNLSKEE LIAELQDCEG
60 70 80 90 100
LIVRSATKVT ADVINAAEKL QVVGRAGTGV DNVDLEAATR KGILVMNTPN
110 120 130 140 150
GNSLSAAELT CGMIMCLARQ IPQATASMKD GKWERKKFMG TELNGKTLGI
160 170 180 190 200
LGLGRIGREV ATRMQSFGMK TIGYDPIISP EVSASFGVQQ LPLEEIWPLC
210 220 230 240 250
DFITVHTPLL PSTTGLLNDN TFAQCKKGVR VVNCARGGIV DEGALLRALQ
260 270 280 290 300
SGQCAGAALD VFTEEPPRDR ALVDHENVIS CPHLGASTKE AQSRCGEEIA
310 320 330 340 350
VQFVDMVKGK SLTGVVNAQA LTSAFSPHTK PWIGLAEALG TLMRAWAGSP
360 370 380 390 400
KGTIQVITQG TSLKNAGNCL SPAVIVGLLK EASKQADVNL VNAKLLVKEA
410 420 430 440 450
GLNVTTSHSP AAPGEQGFGE CLLAVALAGA PYQAVGLVQG TTPVLQGLNG
460 470 480 490 500
AVFRPEVPLR RDLPLLLFRT QTSDPAMLPT MIGLLAEAGV RLLSYQTSLV
510 520 530
SDGETWHVMG ISSLLPSLEA WKQHVTEAFQ FHF
Length:533
Mass (Da):56,651
Last modified:January 23, 2007 - v4
Checksum:iC58EB72275C45B35
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251D → E in AAB88664. (PubMed:10713460)Curated
Sequence conflicti25 – 251D → E in AAD51415. (PubMed:10713460)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti135 – 1351R → W in PHGDH deficiency; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity. 1 Publication
VAR_059026
Natural varianti140 – 1401G → R in NLS. 1 Publication
VAR_071819
Natural varianti163 – 1631R → Q in NLS. 1 Publication
VAR_071820
Natural varianti261 – 2611V → M in PHGDH deficiency; results in a four-fold decrease in substrate affinity and a slight increase in maximal enzyme activity with 3-phosphohydroxypyruvate. 1 Publication
VAR_059027
Natural varianti373 – 3731A → T in PHGDH deficiency; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate. 1 Publication
VAR_059028
Natural varianti377 – 3771G → S in PHGDH deficiency; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity. 1 Publication
VAR_059029
Natural varianti425 – 4251V → M in PHGDH deficiency; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate. 1 Publication
VAR_013461
Natural varianti490 – 4901V → M in PHGDH deficiency; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate. 2 Publications
Corresponds to variant rs121907987 [ dbSNP | Ensembl ].
VAR_059030

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006043 mRNA. Translation: AAB88664.1.
AF171237 mRNA. Translation: AAD51415.1.
CR456795 mRNA. Translation: CAG33076.1.
AK315360 mRNA. Translation: BAG37755.1.
AL589734, AL139251 Genomic DNA. Translation: CAI22407.1.
AL139251, AL589734 Genomic DNA. Translation: CAI22212.1.
CH471122 Genomic DNA. Translation: EAW56708.1.
BC000303 mRNA. Translation: AAH00303.1.
BC001349 mRNA. Translation: AAH01349.1.
BC011262 mRNA. Translation: AAH11262.1.
CCDSiCCDS904.1.
RefSeqiNP_006614.2. NM_006623.3.
UniGeneiHs.487296.

Genome annotation databases

EnsembliENST00000369409; ENSP00000358417; ENSG00000092621.
GeneIDi26227.
KEGGihsa:26227.
UCSCiuc001ehz.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006043 mRNA. Translation: AAB88664.1 .
AF171237 mRNA. Translation: AAD51415.1 .
CR456795 mRNA. Translation: CAG33076.1 .
AK315360 mRNA. Translation: BAG37755.1 .
AL589734 , AL139251 Genomic DNA. Translation: CAI22407.1 .
AL139251 , AL589734 Genomic DNA. Translation: CAI22212.1 .
CH471122 Genomic DNA. Translation: EAW56708.1 .
BC000303 mRNA. Translation: AAH00303.1 .
BC001349 mRNA. Translation: AAH01349.1 .
BC011262 mRNA. Translation: AAH11262.1 .
CCDSi CCDS904.1.
RefSeqi NP_006614.2. NM_006623.3.
UniGenei Hs.487296.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2G76 X-ray 1.70 A/B 4-315 [» ]
ProteinModelPortali O43175.
SMRi O43175. Positions 6-307.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117618. 71 interactions.
IntActi O43175. 25 interactions.
MINTi MINT-4999739.
STRINGi 9606.ENSP00000358417.

Chemistry

ChEMBLi CHEMBL2311243.

PTM databases

PhosphoSitei O43175.

Proteomic databases

MaxQBi O43175.
PaxDbi O43175.
PeptideAtlasi O43175.
PRIDEi O43175.

Protocols and materials databases

DNASUi 26227.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369409 ; ENSP00000358417 ; ENSG00000092621 .
GeneIDi 26227.
KEGGi hsa:26227.
UCSCi uc001ehz.3. human.

Organism-specific databases

CTDi 26227.
GeneCardsi GC01P120202.
HGNCi HGNC:8923. PHGDH.
HPAi CAB003681.
HPA021241.
HPA024031.
MIMi 256520. phenotype.
601815. phenotype.
606879. gene.
neXtProti NX_O43175.
Orphaneti 79351. 3-phosphoglycerate dehydrogenase deficiency.
2671. Neu-Laxova syndrome.
PharmGKBi PA33264.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0111.
GeneTreei ENSGT00530000063021.
HOGENOMi HOG000136693.
HOVERGENi HBG054241.
InParanoidi O43175.
KOi K00058.
OMAi DNTFAQC.
OrthoDBi EOG7JT6WT.
PhylomeDBi O43175.
TreeFami TF314548.

Enzyme and pathway databases

UniPathwayi UPA00135 ; UER00196 .
BioCyci MetaCyc:HS01776-MONOMER.
Reactomei REACT_115789. Serine biosynthesis.

Miscellaneous databases

ChiTaRSi PHGDH. human.
EvolutionaryTracei O43175.
GeneWikii Phosphoglycerate_dehydrogenase.
GenomeRNAii 26227.
NextBioi 48383.
PROi O43175.
SOURCEi Search...

Gene expression databases

Bgeei O43175.
CleanExi HS_PHGDH.
ExpressionAtlasi O43175. baseline and differential.
Genevestigatori O43175.

Family and domain databases

Gene3Di 3.30.1330.90. 1 hit.
3.40.50.720. 2 hits.
InterProi IPR029009. ASB_dom.
IPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR006236. PGDH.
[Graphical view ]
Pfami PF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view ]
SUPFAMi SSF143548. SSF143548. 1 hit.
TIGRFAMsi TIGR01327. PGDH. 1 hit.
PROSITEi PS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and differential expression of the human 3-phosphoglycerate dehydrogenase gene."
    Cho H.M., Jun D.Y., Bae M.A., Ahn J.D., Kim Y.H.
    Gene 245:193-201(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular characterization of 3-phosphoglycerate dehydrogenase deficiency -- a neurometabolic disorder associated with reduced L-serine biosynthesis."
    Klomp L.W.J., de Koning T.J., Malingre H.E.M., van Beurden E.A.C.M., Brink M., Opdam F.L., Duran M., Jaeken J., Pineda M., van Maldergem L., Poll-The B.T., van den Berg I.E.T., Berger R.
    Am. J. Hum. Genet. 67:1389-1399(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS PHGDH DEFICIENCY MET-425 AND MET-490.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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, Lung and Muscle.
  8. Bienvenut W.V.
    Submitted (JAN-2010) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-54; 59-69; 76-119; 138-155; 237-289; 295-308; 352-380; 385-394; 462-491 AND 523-533, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma and Ovarian carcinoma.
  9. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 9-20; 22-33; 76-90; 248-268 AND 271-289.
    Tissue: Fetal brain cortex.
  10. "V490M, a common mutation in 3-phosphoglycerate dehydrogenase deficiency, causes enzyme deficiency by decreasing the yield of mature enzyme."
    Pind S., Slominski E., Mauthe J., Pearlman K., Swoboda K.J., Wilkins J.A., Sauder P., Natowicz M.R.
    J. Biol. Chem. 277:7136-7143(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, VARIANT MET-490.
  11. "Identification of novel proteins induced by estradiol, 4-hydroxytamoxifen and acolbifene in T47D breast cancer cells."
    Al-Dhaheri M.H., Shah Y.M., Basrur V., Pind S., Rowan B.G.
    Steroids 71:966-978(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION BY 17-BETA-ESTRADIOL AND 4-HYDROXYTAMOXIFEN.
  12. "Positive regulation of promoter activity of human 3-phosphoglycerate dehydrogenase (PHGDH) gene is mediated by transcription factors Sp1 and NF-Y."
    Jun D.Y., Park H.S., Lee J.Y., Baek J.Y., Park H.-K., Fukui K., Kim Y.H.
    Gene 414:106-114(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY SP1 AND NF-Y.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Crystal structure of human 3-phosphoglycerate dehydrogenase."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 4-314 IN COMPLEX WITH NAD AND SUBSTRATE.
  16. "Novel mutations in 3-phosphoglycerate dehydrogenase (PHGDH) are distributed throughout the protein and result in altered enzyme kinetics."
    Tabatabaie L., de Koning T.J., Geboers A.J.J.M., van den Berg I.E.T., Berger R., Klomp L.W.J.
    Hum. Mutat. 30:749-756(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PHGDH DEFICIENCY TRP-135; MET-261; THR-373 AND SER-377, CHARACTERIZATION OF VARIANTS PHGDH DEFICIENCY TRP-135; MET-261; THR-373; SER-377; MET-425 AND MET-490, BIOPHYSICOCHEMICAL PROPERTIES.
  17. Cited for: INVOLVEMENT IN NLS, VARIANTS NLS ARG-140 AND GLN-163.

Entry informationi

Entry nameiSERA_HUMAN
AccessioniPrimary (citable) accession number: O43175
Secondary accession number(s): B2RD08, Q5SZU3, Q9BQ01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 153 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3