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Protein

Serine hydroxymethyltransferase, cytosolic

Gene

Shmt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Interconversion of serine and glycine.By similarity

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate1 Publication

Pathwayi: tetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.By similarity
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-MMU-196757. Metabolism of folate and pterines.
R-MMU-71262. Carnitine synthesis.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine hydroxymethyltransferase, cytosolic (EC:2.1.2.1By similarity)
Short name:
SHMT
Alternative name(s):
Glycine hydroxymethyltransferase
Serine methylase
Gene namesi
Name:Shmt1
Synonyms:Shmt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:98299. Shmt1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4396.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001135051 – 478Serine hydroxymethyltransferase, cytosolicAdd BLAST478

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei251N6-(pyridoxal phosphate)lysine1 Publication1

Proteomic databases

EPDiP50431.
MaxQBiP50431.
PaxDbiP50431.
PeptideAtlasiP50431.
PRIDEiP50431.

2D gel databases

REPRODUCTION-2DPAGEP50431.
SWISS-2DPAGEP50431.

PTM databases

iPTMnetiP50431.
PhosphoSitePlusiP50431.
SwissPalmiP50431.

Expressioni

Gene expression databases

BgeeiENSMUSG00000020534.
CleanExiMM_SHMT1.
ExpressionAtlasiP50431. baseline and differential.
GenevisibleiP50431. MM.

Interactioni

Subunit structurei

Homotetramer (PubMed:11063567). Identified in complex with FAM175B and the other subunits of the BRISC complex, at least composed of FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiP50431. 2 interactors.
MINTiMINT-1869579.
STRINGi10090.ENSMUSP00000018744.

Structurei

Secondary structure

1478
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Helixi6 – 15Combined sources10
Helixi20 – 23Combined sources4
Helixi25 – 39Combined sources15
Beta strandi40 – 43Combined sources4
Helixi53 – 59Combined sources7
Helixi62 – 65Combined sources4
Beta strandi72 – 74Combined sources3
Beta strandi76 – 78Combined sources3
Helixi81 – 97Combined sources17
Turni102 – 104Combined sources3
Beta strandi105 – 108Combined sources4
Helixi114 – 125Combined sources12
Beta strandi131 – 135Combined sources5
Helixi137 – 139Combined sources3
Helixi143 – 145Combined sources3
Helixi156 – 160Combined sources5
Beta strandi161 – 166Combined sources6
Turni170 – 172Combined sources3
Helixi177 – 187Combined sources11
Beta strandi190 – 194Combined sources5
Helixi205 – 214Combined sources10
Beta strandi218 – 222Combined sources5
Helixi224 – 226Combined sources3
Helixi227 – 231Combined sources5
Helixi238 – 240Combined sources3
Beta strandi243 – 250Combined sources8
Helixi251 – 253Combined sources3
Beta strandi259 – 264Combined sources6
Beta strandi266 – 270Combined sources5
Beta strandi277 – 280Combined sources4
Helixi282 – 290Combined sources9
Turni291 – 294Combined sources4
Helixi300 – 313Combined sources14
Helixi316 – 338Combined sources23
Beta strandi349 – 356Combined sources8
Helixi357 – 360Combined sources4
Helixi364 – 373Combined sources10
Beta strandi384 – 387Combined sources4
Beta strandi393 – 398Combined sources6
Helixi400 – 403Combined sources4
Turni404 – 406Combined sources3
Helixi409 – 431Combined sources23
Helixi439 – 447Combined sources9
Helixi453 – 467Combined sources15
Beta strandi474 – 476Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EJIX-ray2.90A/B/C/D1-478[»]
ProteinModelPortaliP50431.
SMRiP50431.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50431.

Family & Domainsi

Sequence similaritiesi

Belongs to the SHMT family.Curated

Phylogenomic databases

eggNOGiKOG2467. Eukaryota.
COG0112. LUCA.
GeneTreeiENSGT00390000002762.
HOGENOMiHOG000239405.
HOVERGENiHBG002807.
InParanoidiP50431.
KOiK00600.
OMAiDANNPAV.
OrthoDBiEOG091G05AU.
TreeFamiTF314667.

Family and domain databases

CDDicd00378. SHMT. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00051. SHMT. 1 hit.
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]

Sequencei

Sequence statusi: Complete.

P50431-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADRDATLWA SHEKMLSQPL KDSDAEVYSI IKKESNRQRV GLELIASENF
60 70 80 90 100
ASRAVLEALG SCLNNKYSEG YPGQRYYGGT EFIDELEMLC QKRALQAYHL
110 120 130 140 150
DPQCWGVNVQ PYSGSPANFA VYTALVEPHG RIMGLDLPDG GHLTHGFMTD
160 170 180 190 200
KKKISATSIF FESMPYKVYP ETGYINYDQL EENASLFHPK LIIAGTSCYS
210 220 230 240 250
RNLDYARLRK IADDNGAYLM ADMAHISGLV AAGVVPSPFE HCHVVTTTTH
260 270 280 290 300
KTLRGCRAGM IFYRKGVRSV DPKTGKETYY ELESLINSAV FPGLQGGPHN
310 320 330 340 350
HAIAGVAVAL KQAMTTEFKI YQLQVLANCR ALSDALTELG YKIVTGGSDN
360 370 380 390 400
HLILMDLRSK GTDGGRAEKV LEACSIACNK NTCPGDKSAL RPSGLRLGTP
410 420 430 440 450
ALTSRGLLEE DFQKVAHFIH RGIELTLQIQ SHMATKATLK EFKEKLAGDE
460 470
KIQSAVATLR EEVENFASNF SLPGLPDF
Length:478
Mass (Da):52,601
Last modified:July 27, 2011 - v3
Checksum:i780C764C5AA3CEA3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti62C → S in AAK15040 (PubMed:11063567).Curated1
Sequence conflicti62C → S in CAA64225 (PubMed:8863732).Curated1
Sequence conflicti62C → S in CAA64226 (PubMed:8863732).Curated1
Sequence conflicti267 – 309VRSVD…GVAVA → KFPYAGTDSVGSHFLCGRDW ENSGLSLLGKIGALALEELL RKK in CAA64225 (PubMed:8863732).CuratedAdd BLAST43
Sequence conflicti304A → R in CAA64226 (PubMed:8863732).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237702 mRNA. Translation: AAK15040.1.
AL596215 Genomic DNA. Translation: CAI35264.1.
BC026055 mRNA. Translation: AAH26055.1.
X94478 mRNA. Translation: CAA64225.1.
X94479 mRNA. Translation: CAA64226.1.
CCDSiCCDS24799.1.
PIRiJC4959.
RefSeqiNP_033197.2. NM_009171.2.
XP_006532707.1. XM_006532644.3.
UniGeneiMm.364956.

Genome annotation databases

EnsembliENSMUST00000018744; ENSMUSP00000018744; ENSMUSG00000020534.
GeneIDi20425.
KEGGimmu:20425.
UCSCiuc007jgo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237702 mRNA. Translation: AAK15040.1.
AL596215 Genomic DNA. Translation: CAI35264.1.
BC026055 mRNA. Translation: AAH26055.1.
X94478 mRNA. Translation: CAA64225.1.
X94479 mRNA. Translation: CAA64226.1.
CCDSiCCDS24799.1.
PIRiJC4959.
RefSeqiNP_033197.2. NM_009171.2.
XP_006532707.1. XM_006532644.3.
UniGeneiMm.364956.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EJIX-ray2.90A/B/C/D1-478[»]
ProteinModelPortaliP50431.
SMRiP50431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP50431. 2 interactors.
MINTiMINT-1869579.
STRINGi10090.ENSMUSP00000018744.

Chemistry databases

ChEMBLiCHEMBL4396.

PTM databases

iPTMnetiP50431.
PhosphoSitePlusiP50431.
SwissPalmiP50431.

2D gel databases

REPRODUCTION-2DPAGEP50431.
SWISS-2DPAGEP50431.

Proteomic databases

EPDiP50431.
MaxQBiP50431.
PaxDbiP50431.
PeptideAtlasiP50431.
PRIDEiP50431.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018744; ENSMUSP00000018744; ENSMUSG00000020534.
GeneIDi20425.
KEGGimmu:20425.
UCSCiuc007jgo.1. mouse.

Organism-specific databases

CTDi6470.
MGIiMGI:98299. Shmt1.

Phylogenomic databases

eggNOGiKOG2467. Eukaryota.
COG0112. LUCA.
GeneTreeiENSGT00390000002762.
HOGENOMiHOG000239405.
HOVERGENiHBG002807.
InParanoidiP50431.
KOiK00600.
OMAiDANNPAV.
OrthoDBiEOG091G05AU.
TreeFamiTF314667.

Enzyme and pathway databases

UniPathwayiUPA00193.
ReactomeiR-MMU-196757. Metabolism of folate and pterines.
R-MMU-71262. Carnitine synthesis.

Miscellaneous databases

EvolutionaryTraceiP50431.
PROiP50431.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020534.
CleanExiMM_SHMT1.
ExpressionAtlasiP50431. baseline and differential.
GenevisibleiP50431. MM.

Family and domain databases

CDDicd00378. SHMT. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00051. SHMT. 1 hit.
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...

Entry informationi

Entry nameiGLYC_MOUSE
AccessioniPrimary (citable) accession number: P50431
Secondary accession number(s): Q64508, Q8R0X9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.