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O43175

- SERA_HUMAN

UniProt

O43175 - SERA_HUMAN

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Protein

D-3-phosphoglycerate dehydrogenase

Gene
PHGDH, PGDH3
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)

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

Pathwayi

Sites

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

Regions

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

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: UniProt
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Phosphoglycerate dehydrogenase deficiency (PHGDH deficiency) [MIM:601815]: Characterized by congenital microcephaly, psychomotor retardation, and seizures.
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. 2 Publications
VAR_013461
Natural varianti490 – 4901V → M in PHGDH deficiency; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate. 3 Publications
Corresponds to variant rs121907987 [ dbSNP | Ensembl ].
VAR_059030

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi601815. phenotype.
Orphaneti79351. 3-phosphoglycerate dehydrogenase deficiency.
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-acetyllysine By similarity
Modified residuei58 – 581N6-acetyllysine By 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

ArrayExpressiO43175.
BgeeiO43175.
CleanExiHS_PHGDH.
GenevestigatoriO43175.

Organism-specific databases

HPAiCAB003681.
HPA021241.
HPA024031.

Interactioni

Subunit structurei

Homotetramer By similarity.

Protein-protein interaction databases

BioGridi117618. 65 interactions.
IntActiO43175. 21 interactions.
MINTiMINT-4999739.
STRINGi9606.ENSP00000358417.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G76X-ray1.70A/B4-315[»]
ProteinModelPortaliO43175.
SMRiO43175. Positions 6-307.

Miscellaneous databases

EvolutionaryTraceiO43175.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0111.
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.
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

MAFANLRKVL ISDSLDPCCR KILQDGGLQV VEKQNLSKEE LIAELQDCEG    50
LIVRSATKVT ADVINAAEKL QVVGRAGTGV DNVDLEAATR KGILVMNTPN 100
GNSLSAAELT CGMIMCLARQ IPQATASMKD GKWERKKFMG TELNGKTLGI 150
LGLGRIGREV ATRMQSFGMK TIGYDPIISP EVSASFGVQQ LPLEEIWPLC 200
DFITVHTPLL PSTTGLLNDN TFAQCKKGVR VVNCARGGIV DEGALLRALQ 250
SGQCAGAALD VFTEEPPRDR ALVDHENVIS CPHLGASTKE AQSRCGEEIA 300
VQFVDMVKGK SLTGVVNAQA LTSAFSPHTK PWIGLAEALG TLMRAWAGSP 350
KGTIQVITQG TSLKNAGNCL SPAVIVGLLK EASKQADVNL VNAKLLVKEA 400
GLNVTTSHSP AAPGEQGFGE CLLAVALAGA PYQAVGLVQG TTPVLQGLNG 450
AVFRPEVPLR RDLPLLLFRT QTSDPAMLPT MIGLLAEAGV RLLSYQTSLV 500
SDGETWHVMG ISSLLPSLEA WKQHVTEAFQ FHF 533
Length:533
Mass (Da):56,651
Last modified:January 23, 2007 - v4
Checksum:iC58EB72275C45B35
GO

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 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. 2 Publications
VAR_013461
Natural varianti490 – 4901V → M in PHGDH deficiency; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate. 3 Publications
Corresponds to variant rs121907987 [ dbSNP | Ensembl ].
VAR_059030

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251D → E in AAB88664. 1 Publication
Sequence conflicti25 – 251D → E in AAD51415. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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. 65 interactions.
IntActi O43175. 21 interactions.
MINTi MINT-4999739.
STRINGi 9606.ENSP00000358417.

Chemistry

ChEMBLi CHEMBL2311243.
DrugBanki DB00157. NADH.

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 601815. phenotype.
606879. gene.
neXtProti NX_O43175.
Orphaneti 79351. 3-phosphoglycerate dehydrogenase deficiency.
PharmGKBi PA33264.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0111.
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

ArrayExpressi O43175.
Bgeei O43175.
CleanExi HS_PHGDH.
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.
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.

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: September 3, 2014
This is version 150 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

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