P14519

PR
Gene name
SHMT2
Protein name
Serine hydroxymethyltransferase, mitochondrial
Names
SHMT, Glycine hydroxymethyltransferase, Serine methylase
Species
Oryctolagus cuniculus (Rabbit)
KEGG Pathway
ocu:100009293
EC number
2.1.2.1: Hydroxymethyl-, formyl- and related transferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-85 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P14519

Entry ID Method Resolution Chain Position Source
AF-P14519-F1 Predicted AlphaFoldDB

No variants for P14519

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P14519

No associated diseases with P14519

2 regional properties for P14519

Type Name Position InterPro Accession
binding_site Serine hydroxymethyltransferase, pyridoxal phosphate binding site 272 - 288 IPR019798
domain Serine hydroxymethyltransferase-like domain 49 - 448 IPR039429

Functions

Description
EC Number 2.1.2.1 Hydroxymethyl-, formyl- and related transferases
Subcellular Localization
  • Mitochondrion
  • Mitochondrion matrix, mitochondrion nucleoid
  • Mitochondrion inner membrane
  • Cytoplasm
  • Nucleus
  • Mainly localizes in the mitochondrion
  • Also found in the cytoplasm and nucleus as part of the BRISC complex
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
BRISC complex A protein complex that contains the FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and MERIT40/NBA1 proteins, and specifically cleaves K63-linked polyubiquitin chains.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitochondrial nucleoid The region of a mitochondrion to which the DNA is confined.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

3 GO annotations of molecular function

Name Definition
chromatin binding Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
glycine hydroxymethyltransferase activity Catalysis of the reaction: 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine.
pyridoxal phosphate binding Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.

13 GO annotations of biological process

Name Definition
glycine biosynthetic process from serine The chemical reactions and pathways resulting in the formation of glycine from other compounds, including serine.
glycine metabolic process The chemical reactions and pathways involving glycine, aminoethanoic acid.
L-serine metabolic process The chemical reactions and pathways involving L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
one-carbon metabolic process The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
protein homotetramerization The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.
protein K63-linked deubiquitination A protein deubiquitination process in which a K63-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is removed from a protein.
protein tetramerization The formation of a protein tetramer, a macromolecular structure consisting of four noncovalently associated identical or nonidentical subunits.
regulation of aerobic respiration Any process that modulates the frequency, rate or extent of aerobic respiration.
regulation of mitochondrial translation Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA in a mitochondrion.
regulation of oxidative phosphorylation Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis.
response to type I interferon Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
tetrahydrofolate interconversion The chemical reactions and pathways by which one-carbon (C1) units are transferred between tetrahydrofolate molecules, to synthesise other tetrahydrofolate molecules.
tetrahydrofolate metabolic process The chemical reactions and pathways involving tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLPFSLLWAV RPLQRCGPLV RTAVRAQHGK AAQTQTGEAS RGWTGQESLS DTDPEMWELL
70 80 90 100 110 120
QREKDRQCRG LELIASENFC IRAALEALGS CLNNKYSEGY PGKRYYGGAE VVDEIELLCQ
130 140 150 160 170 180
RRALEAFDLD PAQWGVNVQP YSGSPANLAA YTALLQPHDR IMGLDLPDGG HLTHGYMSDV
190 200 210 220 230 240
KRVSATSIFF ESMPYKLNPQ TGLIDYEQLA LTARLFRPRL IIAGTSAYAR LIDYARMREV
250 260 270 280 290 300
CDEVKAHLLA DMAHISGLVA AKVIPSPFKH ADVVTTTTHK TLRGARSGLI FYRKGVRTVD
310 320 330 340 350 360
PKTGQEIPYT FEDRINFAVF PSLQGGPHNH AIAAVAVALK QACTPMFREY SLQVLKNARA
370 380 390 400 410 420
MADALLERGY SLVSGGTDNH LVLVDLRPKG LDGARAERVL ELVSITANKN TCPGDRSAIT
430 440 450 460 470 480
PGGLRLGAPA LTSRQFREDD FRRVVDFIDE GVNIGLEVKR KTAKLQDFKS FLLKDPETSQ
490 500
HLADLRRRVQ QFARAFPMPG FPEH