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 Q8BHF7

Entry ID Method Resolution Chain Position Source
AF-Q8BHF7-F1 Predicted AlphaFoldDB

20 variants for Q8BHF7

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389221282 54 L>* No EVA
rs3389195832 54 L>F No EVA
rs3389221677 55 L>Q No EVA
rs3389216414 68 C>S No EVA
rs3389236184 70 C>Y No EVA
rs3389221654 71 P>S No EVA
rs13473066 113 I>T No EVA
rs3389231010 192 F>L No EVA
rs3389191184 213 I>L No EVA
rs3389191170 213 I>T No EVA
rs3389224009 325 S>I No EVA
rs13473068 371 T>M No EVA
rs3389236095 375 R>H No EVA
rs3389195767 379 V>F No EVA
rs3389218676 391 A>V No EVA
rs3389218713 399 T>S No EVA
rs3389218704 409 S>P No EVA
rs3389230999 442 S>N No EVA
rs3389224029 472 G>W No EVA
rs3389195840 541 W>* No EVA

No associated diseases with Q8BHF7

No regional properties for Q8BHF7

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q8BHF7

Functions

Description
EC Number 2.7.8.5 Transferases for other substituted phosphate groups
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
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.
organelle membrane A membrane that is one of the two lipid bilayers of an organelle envelope or the outermost membrane of single membrane bound organelle.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).

4 GO annotations of biological process

Name Definition
cardiolipin biosynthetic process The chemical reactions and pathways resulting in the formation of cardiolipin, 1,3-bis(3-phosphatidyl)glycerol.
diacylglycerol metabolic process The chemical reactions and pathways involving diacylglycerol, a glyceride in which any two of the R groups (positions not specified) are acyl groups while the remaining R group can be either H or an alkyl group.
phosphatidylglycerol biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidylglycerols, any of a class of phospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol.
phospholipid biosynthetic process The chemical reactions and pathways resulting in the formation of a phospholipid, a lipid containing phosphoric acid as a mono- or diester.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAAPAAGPVF WRRLLGLLPG RPGLAALLGR LSDRLGRSRE RRRRRSPWLL LAPLLSPTVP
70 80 90 100 110 120
QVTSPPCCLC PEGVHRFQWI RNLVPEFGVS SSHVRVLSSP AEFFELMKGQ IKIAKRRVVM
130 140 150 160 170 180
ASLYLGTGPL EQELVDCLES SLEKSLQAKF PSDLKVSILL DFTRGSRGRK NSRTMLLPLL
190 200 210 220 230 240
QRFPERVRVS LFHTPNLRGL LRLLIPERFN ETIGLQHIKV YLFDNNVILS GANLSDSYFT
250 260 270 280 290 300
NRQDRYVFLQ DCAEIADFFT ELVDAVGDVS LQLQGDDTVE VVDGMVHPYK GDRAAYCRAA
310 320 330 340 350 360
NKRVMDVIHS ARARQQMLHA QTFHSDSLLS QEEAAAAGDR RPAPDTWIYP LIQMKPFEIQ
370 380 390 400 410 420
IDEIVTETLL TEAERGAKVF LTTGYFNLTQ AYMDLVLGTR AEYQILLASP EVNGFFGAKG
430 440 450 460 470 480
VAGAIPAAYV HIERQFYSEV CSLGQQDRVQ LQEYWRRGWT FHAKGLWLYL AGSSLPCLTL
490 500 510 520 530 540
IGSPNFGYRS VHRDLEAQIA IVTESRSLQQ QLHQEQEQLY LRSGVVTSAT FEQPGRQVKL
550
WVKMVTPLIK NFF