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Protein

Serine hydroxymethyltransferase, mitochondrial

Gene

SHMT2

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

Functioni

Contributes to the de novo mitochondrial thymidylate biosynthesis pathway via its role in glycine and tetrahydrofolate metabolism. Thymidylate biosynthesis is required to prevent uracil accumulation in mtDNA (PubMed:21876188). Interconversion of serine and glycine (PubMed:25619277). Associates with mitochondrial DNA (PubMed:18063578). Plays a role in the deubiquitination of target proteins as component of the BRISC complex (PubMed:24075985). Required for IFNAR1 deubiquitination by the BRISC complex (PubMed:24075985).4 Publications

Catalytic activityi

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine.2 Publications

Cofactori

pyridoxal 5'-phosphate1 Publication

Kineticsi

  1. KM=278 µM for L-serine1 Publication
  2. KM=23 µM for tetrahydrofolate1 Publication

    Pathwayi: tetrahydrofolate interconversion

    This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

    GO - Molecular functioni

    • amino acid binding Source: Ensembl
    • chromatin binding Source: UniProtKB
    • glycine hydroxymethyltransferase activity Source: UniProtKB
    • L-allo-threonine aldolase activity Source: Ensembl
    • pyridoxal phosphate binding Source: UniProtKB

    GO - Biological processi

    • folic acid metabolic process Source: Reactome
    • glycine biosynthetic process from serine Source: Ensembl
    • glycine metabolic process Source: UniProtKB
    • L-serine biosynthetic process Source: Ensembl
    • L-serine metabolic process Source: UniProtKB
    • one-carbon metabolic process Source: UniProtKB
    • positive regulation of cell proliferation Source: Ensembl
    • protein homotetramerization Source: Ensembl
    • protein K63-linked deubiquitination Source: UniProtKB
    • protein tetramerization Source: UniProtKB
    • response to type I interferon Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    • tetrahydrofolate interconversion Source: UniProtKB-UniPathway
    • tetrahydrofolate metabolic process Source: UniProtKB
    • vitamin metabolic process Source: Reactome
    • water-soluble vitamin metabolic process Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00049-MONOMER.
    ReactomeiR-HSA-196757. Metabolism of folate and pterines.
    UniPathwayiUPA00193.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine hydroxymethyltransferase, mitochondrial (EC:2.1.2.12 Publications)
    Short name:
    SHMT
    Alternative name(s):
    Glycine hydroxymethyltransferase
    Serine methylase
    Gene namesi
    Name:SHMT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:10852. SHMT2.

    Subcellular locationi

    GO - Cellular componenti

    • BRISC complex Source: UniProtKB
    • cytoplasm Source: BHF-UCL
    • extracellular exosome Source: UniProtKB
    • microtubule cytoskeleton Source: HPA
    • mitochondrial inner membrane Source: UniProtKB
    • mitochondrial intermembrane space Source: Ensembl
    • mitochondrial matrix Source: UniProtKB
    • mitochondrial nucleoid Source: BHF-UCL
    • mitochondrion Source: BHF-UCL
    • nucleus Source: BHF-UCL
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion nucleoid, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35755.

    Chemistry

    DrugBankiDB00145. Glycine.
    DB00116. Tetrahydrofolic acid.

    Polymorphism and mutation databases

    BioMutaiSHMT2.
    DMDMi6226865.

    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-acetyllysineCombined sources
    Modified residuei181 – 1811N6-acetyllysineCombined sources
    Modified residuei196 – 1961N6-acetyllysineCombined sources
    Modified residuei280 – 2801N6-(pyridoxal phosphate)lysineBy similarity
    Modified residuei297 – 2971N6-acetyllysineCombined sources
    Modified residuei356 – 3561N6-acetyllysineCombined sources
    Modified residuei464 – 4641N6-acetyllysineCombined sources
    Modified residuei469 – 4691N6-acetyllysineCombined sources
    Modified residuei474 – 4741N6-acetyllysineCombined sources

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiP34897.
    PaxDbiP34897.
    PRIDEiP34897.

    PTM databases

    iPTMnetiP34897.
    PhosphoSiteiP34897.
    SwissPalmiP34897.

    Expressioni

    Gene expression databases

    BgeeiP34897.
    CleanExiHS_SHMT2.
    ExpressionAtlasiP34897. baseline and differential.
    GenevisibleiP34897. HS.

    Organism-specific databases

    HPAiHPA020543.
    HPA020549.

    Interactioni

    Subunit structurei

    Homotetramer; in the presence of bound pyridoxal 5'-phosphate. Homodimer; in the absence of bound pyridoxal 5'-phosphate. Pyridoxal 5'-phosphate binding mediates an important conformation change that is required for tetramerization (PubMed:25619277). Interacts with FAM175B; the interaction is direct. Identified in a complex with FAM175B and the other subunits of the BRISC complex, at least composed of the FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1. Identified in a complex with FAM175B and INAR1 (PubMed:24075985). Interacts with KIRREL3 (PubMed:25902260).3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARL6IP1Q150413EBI-352908,EBI-714543
    CMTM5Q96DZ93EBI-352908,EBI-2548702

    Protein-protein interaction databases

    BioGridi112368. 432 interactions.
    IntActiP34897. 37 interactions.
    MINTiMINT-3013548.
    STRINGi9606.ENSP00000333667.

    Structurei

    Secondary structure

    1
    504
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi49 – 524Combined sources
    Helixi54 – 6916Combined sources
    Beta strandi70 – 723Combined sources
    Helixi82 – 887Combined sources
    Helixi91 – 933Combined sources
    Beta strandi103 – 1075Combined sources
    Helixi111 – 12616Combined sources
    Turni131 – 1333Combined sources
    Beta strandi134 – 1374Combined sources
    Helixi143 – 15412Combined sources
    Beta strandi160 – 1645Combined sources
    Helixi166 – 1683Combined sources
    Helixi172 – 1743Combined sources
    Helixi186 – 1894Combined sources
    Beta strandi190 – 1956Combined sources
    Turni199 – 2013Combined sources
    Beta strandi202 – 2043Combined sources
    Helixi206 – 21611Combined sources
    Beta strandi219 – 2235Combined sources
    Helixi234 – 24411Combined sources
    Beta strandi247 – 2515Combined sources
    Helixi253 – 2553Combined sources
    Helixi256 – 2605Combined sources
    Helixi267 – 2693Combined sources
    Beta strandi272 – 2809Combined sources
    Beta strandi288 – 2936Combined sources
    Beta strandi295 – 2995Combined sources
    Beta strandi306 – 3083Combined sources
    Helixi312 – 3198Combined sources
    Turni320 – 3234Combined sources
    Helixi329 – 34315Combined sources
    Helixi345 – 36723Combined sources
    Helixi373 – 3753Combined sources
    Beta strandi378 – 3858Combined sources
    Helixi387 – 3893Combined sources
    Helixi393 – 40210Combined sources
    Beta strandi408 – 4103Combined sources
    Beta strandi418 – 4203Combined sources
    Beta strandi422 – 4287Combined sources
    Helixi429 – 4335Combined sources
    Helixi438 – 46023Combined sources
    Helixi465 – 47410Combined sources
    Helixi476 – 49318Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OU5X-ray2.04A17-504[»]
    4PVFX-ray2.60A/B22-504[»]
    ProteinModelPortaliP34897.
    SMRiP34897. Positions 43-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP34897.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SHMT family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG2467. Eukaryota.
    COG0112. LUCA.
    GeneTreeiENSGT00390000002762.
    HOGENOMiHOG000239405.
    HOVERGENiHBG002807.
    InParanoidiP34897.
    KOiK00600.
    OMAiMAIRCQH.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MLYFSLFWAA RPLQRCGQLV RMAIRAQHSN AAQTQTGEAN RGWTGQESLS
    60 70 80 90 100
    DSDPEMWELL QREKDRQCRG LELIASENFC SRAALEALGS CLNNKYSEGY
    110 120 130 140 150
    PGKRYYGGAE VVDEIELLCQ RRALEAFDLD PAQWGVNVQP YSGSPANLAV
    160 170 180 190 200
    YTALLQPHDR IMGLDLPDGG HLTHGYMSDV KRISATSIFF ESMPYKLNPK
    210 220 230 240 250
    TGLIDYNQLA LTARLFRPRL IIAGTSAYAR LIDYARMREV CDEVKAHLLA
    260 270 280 290 300
    DMAHISGLVA AKVIPSPFKH ADIVTTTTHK TLRGARSGLI FYRKGVKAVD
    310 320 330 340 350
    PKTGREIPYT FEDRINFAVF PSLQGGPHNH AIAAVAVALK QACTPMFREY
    360 370 380 390 400
    SLQVLKNARA MADALLERGY SLVSGGTDNH LVLVDLRPKG LDGARAERVL
    410 420 430 440 450
    ELVSITANKN TCPGDRSAIT PGGLRLGAPA LTSRQFREDD FRRVVDFIDE
    460 470 480 490 500
    GVNIGLEVKS KTAKLQDFKS FLLKDSETSQ RLANLRQRVE QFARAFPMPG

    FDEH
    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:
    EMBLi
    GenBanki
    DDBJi
    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.
    UCSCiuc001sni.3. human. [P34897-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OU5X-ray2.04A17-504[»]
    4PVFX-ray2.60A/B22-504[»]
    ProteinModelPortaliP34897.
    SMRiP34897. Positions 43-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi112368. 432 interactions.
    IntActiP34897. 37 interactions.
    MINTiMINT-3013548.
    STRINGi9606.ENSP00000333667.

    Chemistry

    DrugBankiDB00145. Glycine.
    DB00116. Tetrahydrofolic acid.

    PTM databases

    iPTMnetiP34897.
    PhosphoSiteiP34897.
    SwissPalmiP34897.

    Polymorphism and mutation databases

    BioMutaiSHMT2.
    DMDMi6226865.

    Proteomic databases

    EPDiP34897.
    PaxDbiP34897.
    PRIDEiP34897.

    Protocols and materials databases

    DNASUi6472.
    Structural Biology KnowledgebaseSearch...

    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.
    UCSCiuc001sni.3. human. [P34897-1]

    Organism-specific databases

    CTDi6472.
    GeneCardsiSHMT2.
    HGNCiHGNC:10852. SHMT2.
    HPAiHPA020543.
    HPA020549.
    MIMi138450. gene.
    neXtProtiNX_P34897.
    PharmGKBiPA35755.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG2467. Eukaryota.
    COG0112. LUCA.
    GeneTreeiENSGT00390000002762.
    HOGENOMiHOG000239405.
    HOVERGENiHBG002807.
    InParanoidiP34897.
    KOiK00600.
    OMAiMAIRCQH.
    OrthoDBiEOG7327NN.
    PhylomeDBiP34897.
    TreeFamiTF314667.

    Enzyme and pathway databases

    UniPathwayiUPA00193.
    BioCyciMetaCyc:HS00049-MONOMER.
    ReactomeiR-HSA-196757. Metabolism of folate and pterines.

    Miscellaneous databases

    ChiTaRSiSHMT2. human.
    EvolutionaryTraceiP34897.
    GenomeRNAii6472.
    NextBioi25141.
    PROiP34897.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP34897.
    CleanExiHS_SHMT2.
    ExpressionAtlasiP34897. baseline and differential.
    GenevisibleiP34897. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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, FUNCTION IN 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. Cited for: IDENTIFICATION IN THE BRISC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FAM175B, CATALYTIC ACTIVITY, IDENTIFICATION IN A COMPLEX WITH FAM175B AND INAR1, SUBCELLULAR LOCATION.
    14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    15. "Autism and intellectual disability-associated KIRREL3 interacts with neuronal proteins MAP1B and MYO16 with potential roles in neurodevelopment."
      Liu Y.F., Sowell S.M., Luo Y., Chaubey A., Cameron R.S., Kim H.G., Srivastava A.K.
      PLoS ONE 10:E0123106-E0123106(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIRREL3.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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.
    18. "How pyridoxal 5'-phosphate differentially regulates human cytosolic and mitochondrial serine hydroxymethyltransferase oligomeric state."
      Giardina G., Brunotti P., Fiascarelli A., Cicalini A., Costa M.G., Buckle A.M., di Salvo M.L., Giorgi A., Marani M., Paone A., Rinaldo S., Paiardini A., Contestabile R., Cutruzzola F.
      FEBS J. 282:1225-1241(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 22-504, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR.

    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: April 13, 2016
    This is version 171 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.