Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q7T3T4

Entry ID Method Resolution Chain Position Source
AF-Q7T3T4-F1 Predicted AlphaFoldDB

No variants for Q7T3T4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7T3T4

No associated diseases with Q7T3T4

3 regional properties for Q7T3T4

Type Name Position InterPro Accession
domain Sterile alpha motif domain 11 - 74 IPR001660
domain Sphingomyelin synthase-like domain 280 - 353 IPR025749
domain SAM domain 12 - 50 IPR041418

Functions

Description
EC Number 2.7.8.27 Transferases for other substituted phosphate groups
Subcellular Localization
  • Golgi apparatus membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
integral component of endoplasmic reticulum membrane The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
integral component of Golgi membrane The component of the Golgi membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
integral component of plasma membrane The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

3 GO annotations of molecular function

Name Definition
ceramide cholinephosphotransferase activity Catalysis of the reaction: CDP-choline + ceramide = CMP + H(+) + sphingomyelin.
kinase activity Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
sphingomyelin synthase activity Catalysis of the reaction: 1,2-diacyl-sn-glycero-3-phosphocholine + ceramide = 1,2-diacyl-sn-glycerol + sphingomyelin.

6 GO annotations of biological process

Name Definition
apoptotic process A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
ceramide biosynthetic process The chemical reactions and pathways resulting in the formation of ceramides, any N-acylated sphingoid.
inflammatory response The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages.
negative regulation of apoptotic process Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
sphingomyelin biosynthetic process The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSGRMKEVVS WSPEEVTNWL MENAVPEYCE PLKSFTGQDL INLTEEDFKK TPLSRVSSDS
70 80 90 100 110 120
GQQLLHMIET LKMAHHIEAH KNGHVNGHIH VSVNNTAHEN GFSSKTKLNG VPNGYKKEMI
130 140 150 160 170 180
KIPMPEPERL QYPMEWGKTF LAFIYALFCF IFTTVTISVV HERVPPKEVQ PPLPDAFFDR
190 200 210 220 230 240
FDRVQWAFSI CEINGMILVG LWLVQWLLLK YKSIISRRFF CIVCTLYLYR CITMYVTTLP
250 260 270 280 290 300
VPGMHFKCSP KLFGDWESHL RRIMKLIAGG GLSITGSHNM CGDYLYSGHT VILTLTYLFI
310 320 330 340 350 360
KEYSPRRLWW YHWLCWTLSM VGMFCILLAH DHYTVDVVVA YYITTRLFWW YHTMANQQVL
370 380 390 400 410
KEASQTNLLA RVWWYKPFQY FEKNVQGIVP RSYHWPFPWP VLHRGRQVKY SRLVNDT