Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O43175

- SERA_HUMAN

UniProt

O43175 - SERA_HUMAN

Protein

D-3-phosphoglycerate dehydrogenase

Gene

PHGDH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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

    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-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

    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. 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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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 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:
    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. 25 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

    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: October 1, 2014
    This is version 151 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