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P34897

- GLYM_HUMAN

UniProt

P34897 - GLYM_HUMAN

Protein

Serine hydroxymethyltransferase, mitochondrial

Gene

SHMT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 3 (30 May 2000)
      Previous versions | rss
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    Functioni

    Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Interconversion of serine and glycine. Associates with mitochondrial DNA.1 Publication

    Catalytic activityi

    5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine.

    Cofactori

    Pyridoxal phosphate.

    Pathwayi

    GO - Molecular functioni

    1. amino acid binding Source: Ensembl
    2. chromatin binding Source: UniProtKB
    3. glycine hydroxymethyltransferase activity Source: UniProtKB
    4. L-allo-threonine aldolase activity Source: Ensembl
    5. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. glycine biosynthetic process from serine Source: Ensembl
    2. L-serine biosynthetic process Source: Ensembl
    3. one-carbon metabolic process Source: UniProtKB
    4. positive regulation of cell proliferation Source: Ensembl
    5. protein homotetramerization Source: Ensembl
    6. tetrahydrofolate interconversion Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00049-MONOMER.
    UniPathwayiUPA00193.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine hydroxymethyltransferase, mitochondrial (EC:2.1.2.1)
    Short name:
    SHMT
    Alternative name(s):
    Glycine hydroxymethyltransferase
    Serine methylase
    Gene namesi
    Name:SHMT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:10852. SHMT2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. microtubule cytoskeleton Source: HPA
    3. mitochondrial inner membrane Source: UniProtKB
    4. mitochondrial intermembrane space Source: Ensembl
    5. mitochondrial matrix Source: UniProtKB
    6. mitochondrial nucleoid Source: BHF-UCL
    7. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion nucleoid

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35755.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2929MitochondrionAdd
    BLAST
    Chaini30 – 504475Serine hydroxymethyltransferase, mitochondrialPRO_0000032562Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei103 – 1031N6-acetyllysine1 Publication
    Modified residuei181 – 1811N6-acetyllysine1 Publication
    Modified residuei196 – 1961N6-acetyllysine1 Publication
    Modified residuei280 – 2801N6-(pyridoxal phosphate)lysineBy similarity
    Modified residuei297 – 2971N6-acetyllysine1 Publication
    Modified residuei356 – 3561N6-acetyllysine1 Publication
    Modified residuei464 – 4641N6-acetyllysine1 Publication
    Modified residuei469 – 4691N6-acetyllysine1 Publication
    Modified residuei474 – 4741N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP34897.
    PaxDbiP34897.
    PRIDEiP34897.

    PTM databases

    PhosphoSiteiP34897.

    Expressioni

    Gene expression databases

    ArrayExpressiP34897.
    BgeeiP34897.
    CleanExiHS_SHMT2.
    GenevestigatoriP34897.

    Organism-specific databases

    HPAiHPA020543.
    HPA020549.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi112368. 44 interactions.
    IntActiP34897. 18 interactions.
    MINTiMINT-3013548.
    STRINGi9606.ENSP00000333667.

    Structurei

    Secondary structure

    1
    504
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi49 – 524
    Helixi54 – 6916
    Beta strandi70 – 723
    Helixi82 – 887
    Helixi91 – 933
    Helixi111 – 12616
    Turni131 – 1333
    Beta strandi134 – 1374
    Helixi143 – 15412
    Turni199 – 2013
    Helixi206 – 21611
    Beta strandi219 – 2235
    Helixi234 – 24411
    Beta strandi247 – 2515
    Helixi253 – 2553
    Helixi256 – 2605
    Helixi267 – 2693
    Beta strandi272 – 2809
    Beta strandi288 – 2936
    Beta strandi295 – 2995
    Beta strandi306 – 3083
    Helixi312 – 3198
    Turni320 – 3234
    Helixi329 – 34315
    Helixi345 – 36723
    Helixi373 – 3753
    Beta strandi378 – 3858
    Helixi387 – 3893
    Helixi393 – 40210
    Beta strandi408 – 4103
    Beta strandi418 – 4203
    Beta strandi422 – 4287
    Helixi429 – 4335
    Helixi438 – 46023
    Helixi465 – 47410
    Helixi476 – 49318

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OU5X-ray2.04A17-504[»]
    ProteinModelPortaliP34897.
    SMRiP34897. Positions 42-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP34897.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SHMT family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0112.
    HOGENOMiHOG000239405.
    HOVERGENiHBG002807.
    InParanoidiP34897.
    KOiK00600.
    OMAiPMFREYA.
    OrthoDBiEOG7327NN.
    PhylomeDBiP34897.
    TreeFamiTF314667.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_00051. SHMT.
    InterProiIPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR001085. Ser_HO-MeTrfase.
    IPR019798. Ser_HO-MeTrfase_PLP_BS.
    [Graphical view]
    PANTHERiPTHR11680. PTHR11680. 1 hit.
    PfamiPF00464. SHMT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000412. SHMT. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00096. SHMT. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P34897-1) [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

    MLYFSLFWAA RPLQRCGQLV RMAIRAQHSN AAQTQTGEAN RGWTGQESLS    50
    DSDPEMWELL QREKDRQCRG LELIASENFC SRAALEALGS CLNNKYSEGY 100
    PGKRYYGGAE VVDEIELLCQ RRALEAFDLD PAQWGVNVQP YSGSPANLAV 150
    YTALLQPHDR IMGLDLPDGG HLTHGYMSDV KRISATSIFF ESMPYKLNPK 200
    TGLIDYNQLA LTARLFRPRL IIAGTSAYAR LIDYARMREV CDEVKAHLLA 250
    DMAHISGLVA AKVIPSPFKH ADIVTTTTHK TLRGARSGLI FYRKGVKAVD 300
    PKTGREIPYT FEDRINFAVF PSLQGGPHNH AIAAVAVALK QACTPMFREY 350
    SLQVLKNARA MADALLERGY SLVSGGTDNH LVLVDLRPKG LDGARAERVL 400
    ELVSITANKN TCPGDRSAIT PGGLRLGAPA LTSRQFREDD FRRVVDFIDE 450
    GVNIGLEVKS KTAKLQDFKS FLLKDSETSQ RLANLRQRVE QFARAFPMPG 500
    FDEH 504
    Length:504
    Mass (Da):55,993
    Last modified:May 30, 2000 - v3
    Checksum:i7A13AF741C68FFD6
    GO
    Isoform 2 (identifier: P34897-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         199-208: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:494
    Mass (Da):54,863
    Checksum:iA304DE25F96E942E
    GO
    Isoform 3 (identifier: P34897-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: Missing.

    Show »
    Length:483
    Mass (Da):53,455
    Checksum:i9F8925E18D758E65
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti308 – 3081P → L in AAA63258. (PubMed:8505317)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2121Missing in isoform 3. 1 PublicationVSP_043844Add
    BLAST
    Alternative sequencei199 – 20810Missing in isoform 2. 1 PublicationVSP_043088

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK315916 mRNA. Translation: BAH14287.1.
    BT006866 mRNA. Translation: AAP35512.1.
    AC137834 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96994.1.
    CH471054 Genomic DNA. Translation: EAW96998.1.
    BC011911 mRNA. Translation: AAH11911.1.
    BC013677 mRNA. Translation: AAH13677.1.
    BC032584 mRNA. Translation: AAH32584.1.
    BC044211 mRNA. Translation: AAH44211.1.
    Y12331 Genomic DNA. Translation: CAA72999.1.
    U23143 Genomic DNA. Translation: AAA64572.1.
    L11932 mRNA. Translation: AAA63258.1.
    CCDSiCCDS53805.1. [P34897-3]
    CCDS55837.1. [P34897-2]
    CCDS8934.1. [P34897-1]
    PIRiB46746.
    RefSeqiNP_001159828.1. NM_001166356.1. [P34897-2]
    NP_001159829.1. NM_001166357.1. [P34897-3]
    NP_001159830.1. NM_001166358.1. [P34897-3]
    NP_001159831.1. NM_001166359.1. [P34897-3]
    NP_005403.2. NM_005412.5. [P34897-1]
    UniGeneiHs.741179.

    Genome annotation databases

    EnsembliENST00000328923; ENSP00000333667; ENSG00000182199. [P34897-1]
    ENST00000414700; ENSP00000406881; ENSG00000182199. [P34897-3]
    ENST00000449049; ENSP00000413770; ENSG00000182199. [P34897-3]
    ENST00000553474; ENSP00000452419; ENSG00000182199. [P34897-3]
    ENST00000557487; ENSP00000452315; ENSG00000182199. [P34897-2]
    GeneIDi6472.
    KEGGihsa:6472.
    UCSCiuc001snf.2. human. [P34897-1]
    uc009zpk.2. human. [P34897-2]

    Polymorphism databases

    DMDMi6226865.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK315916 mRNA. Translation: BAH14287.1 .
    BT006866 mRNA. Translation: AAP35512.1 .
    AC137834 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96994.1 .
    CH471054 Genomic DNA. Translation: EAW96998.1 .
    BC011911 mRNA. Translation: AAH11911.1 .
    BC013677 mRNA. Translation: AAH13677.1 .
    BC032584 mRNA. Translation: AAH32584.1 .
    BC044211 mRNA. Translation: AAH44211.1 .
    Y12331 Genomic DNA. Translation: CAA72999.1 .
    U23143 Genomic DNA. Translation: AAA64572.1 .
    L11932 mRNA. Translation: AAA63258.1 .
    CCDSi CCDS53805.1. [P34897-3 ]
    CCDS55837.1. [P34897-2 ]
    CCDS8934.1. [P34897-1 ]
    PIRi B46746.
    RefSeqi NP_001159828.1. NM_001166356.1. [P34897-2 ]
    NP_001159829.1. NM_001166357.1. [P34897-3 ]
    NP_001159830.1. NM_001166358.1. [P34897-3 ]
    NP_001159831.1. NM_001166359.1. [P34897-3 ]
    NP_005403.2. NM_005412.5. [P34897-1 ]
    UniGenei Hs.741179.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3OU5 X-ray 2.04 A 17-504 [» ]
    ProteinModelPortali P34897.
    SMRi P34897. Positions 42-504.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112368. 44 interactions.
    IntActi P34897. 18 interactions.
    MINTi MINT-3013548.
    STRINGi 9606.ENSP00000333667.

    Chemistry

    DrugBanki DB00145. Glycine.
    DB00114. Pyridoxal Phosphate.
    DB00116. Tetrahydrofolic acid.

    PTM databases

    PhosphoSitei P34897.

    Polymorphism databases

    DMDMi 6226865.

    Proteomic databases

    MaxQBi P34897.
    PaxDbi P34897.
    PRIDEi P34897.

    Protocols and materials databases

    DNASUi 6472.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000328923 ; ENSP00000333667 ; ENSG00000182199 . [P34897-1 ]
    ENST00000414700 ; ENSP00000406881 ; ENSG00000182199 . [P34897-3 ]
    ENST00000449049 ; ENSP00000413770 ; ENSG00000182199 . [P34897-3 ]
    ENST00000553474 ; ENSP00000452419 ; ENSG00000182199 . [P34897-3 ]
    ENST00000557487 ; ENSP00000452315 ; ENSG00000182199 . [P34897-2 ]
    GeneIDi 6472.
    KEGGi hsa:6472.
    UCSCi uc001snf.2. human. [P34897-1 ]
    uc009zpk.2. human. [P34897-2 ]

    Organism-specific databases

    CTDi 6472.
    GeneCardsi GC12P057623.
    HGNCi HGNC:10852. SHMT2.
    HPAi HPA020543.
    HPA020549.
    MIMi 138450. gene.
    neXtProti NX_P34897.
    PharmGKBi PA35755.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0112.
    HOGENOMi HOG000239405.
    HOVERGENi HBG002807.
    InParanoidi P34897.
    KOi K00600.
    OMAi PMFREYA.
    OrthoDBi EOG7327NN.
    PhylomeDBi P34897.
    TreeFami TF314667.

    Enzyme and pathway databases

    UniPathwayi UPA00193 .
    BioCyci MetaCyc:HS00049-MONOMER.

    Miscellaneous databases

    ChiTaRSi SHMT2. human.
    EvolutionaryTracei P34897.
    GenomeRNAii 6472.
    NextBioi 25141.
    PROi P34897.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P34897.
    Bgeei P34897.
    CleanExi HS_SHMT2.
    Genevestigatori P34897.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPi MF_00051. SHMT.
    InterProi IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR001085. Ser_HO-MeTrfase.
    IPR019798. Ser_HO-MeTrfase_PLP_BS.
    [Graphical view ]
    PANTHERi PTHR11680. PTHR11680. 1 hit.
    Pfami PF00464. SHMT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000412. SHMT. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    PROSITEi PS00096. SHMT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 3).
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [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] (ISOFORMS 1 AND 2).
      Tissue: Lymph, Muscle, Ovary and Uterus.
    6. "The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase."
      Snell K., Baumann U., Byrne P.C., Chave K.J., Renwick S.B., Sanders P.G., Whitehouse S.K.
      Adv. Enzyme Regul. 40:353-403(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
    7. "Molecular cloning, characterization, and regulation of the human mitochondrial serine hydroxymethyltransferase gene."
      Stover P.J., Chen L.H., Suh J.R., Stover D.M., Keyomarsi K., Shane B.
      J. Biol. Chem. 272:1842-1848(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-504.
    8. "Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization."
      Garrow T.A., Brenner A.A., Whitehead M.V., Chen X.-N., Duncan R.G., Korenberg J.R., Shane B.
      J. Biol. Chem. 268:11910-11916(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-504 (ISOFORM 1).
    9. "The layered structure of human mitochondrial DNA nucleoids."
      Bogenhagen D.F., Rousseau D., Burke S.
      J. Biol. Chem. 283:3665-3675(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH MITOCHONDRIAL DNA, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103; LYS-181; LYS-196; LYS-297; LYS-356; LYS-464; LYS-469 AND LYS-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Identification of a de novo thymidylate biosynthesis pathway in mammalian mitochondria."
      Anderson D.D., Quintero C.M., Stover P.J.
      Proc. Natl. Acad. Sci. U.S.A. 108:15163-15168(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Crystal structure of human mitochondrial serine hydroxymethyltransferase 2."
      Structural genomics consortium (SGC)
      Submitted (OCT-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 17-504.

    Entry informationi

    Entry nameiGLYM_HUMAN
    AccessioniPrimary (citable) accession number: P34897
    Secondary accession number(s): B7Z9F1
    , E7EQ19, E7EU43, O00740, Q8N1A5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 154 of the entry and version 3 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

    Miscellaneous

    In eukaryotes there are two forms of the enzymes: a cytosolic one and a mitochondrial one.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3