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 P48760

Entry ID Method Resolution Chain Position Source
AF-P48760-F1 Predicted AlphaFoldDB

32 variants for P48760

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388547568 28 A>V No EVA
rs3391485355 43 M>R No EVA
rs3388546475 75 Q>* No EVA
rs3391421983 128 F>L No EVA
rs3391432327 128 F>V No EVA
rs3388544261 178 F>Y No EVA
rs3388547237 186 F>Y No EVA
rs3388545167 191 Q>* No EVA
rs3388545164 192 E>D No EVA
rs3388545240 193 K>N No EVA
rs3391432364 262 P>L No EVA
rs3388541159 284 E>K No EVA
rs3388544180 311 Q>H No EVA
rs27208028 313 A>T No EVA
rs3388547257 327 E>D No EVA
rs3388544121 340 P>S No EVA
rs3388546667 381 T>S No EVA
rs27208033 409 H>Y No EVA
rs3388545150 429 Q>H No EVA
rs3388548607 433 F>L No EVA
rs3388549195 442 V>E No EVA
rs3388547269 451 A>E No EVA
rs3388545425 473 H>Y No EVA
rs3388544135 477 L>M No EVA
rs246461856 491 G>R No EVA
rs246461856 491 G>S No EVA
rs3388549153 497 P>R No EVA
rs3388541162 500 L>Q No EVA
rs3388538737 511 R>K No EVA
rs3388538659 524 L>* No EVA
rs3388548550 536 Q>* No EVA
rs3388543511 561 A>D No EVA

No associated diseases with P48760

10 regional properties for P48760

Type Name Position InterPro Accession
conserved_site Actinin-type actin-binding domain, conserved site 211 - 235 IPR001589-1
conserved_site Actinin-type actin-binding domain, conserved site 399 - 408 IPR001589-2
conserved_site Actinin-type actin-binding domain, conserved site 478 - 502 IPR001589-3
domain Calponin homology domain 123 - 239 IPR001715-1
domain Calponin homology domain 267 - 378 IPR001715-2
domain Calponin homology domain 397 - 506 IPR001715-3
domain Calponin homology domain 518 - 627 IPR001715-4
domain EF-hand domain 12 - 87 IPR002048
binding_site EF-Hand 1, calcium-binding site 25 - 37 IPR018247-1
binding_site EF-Hand 1, calcium-binding site 65 - 77 IPR018247-2

Functions

Description
EC Number 6.3.2.17 Acid--amino-acid ligases (peptide synthases)
Subcellular Localization
  • [Isoform 1]: Mitochondrion inner membrane
  • Mitochondrion matrix
  • ;
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.
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.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
tetrahydrofolylpolyglutamate synthase activity Catalysis of the reaction: ATP + tetrahydrofolyl-(Glu)(n) + L-glutamate = ADP + phosphate + tetrahydrofolyl-(Glu)(n+1).

9 GO annotations of biological process

Name Definition
animal organ regeneration The regrowth of a lost or destroyed animal organ.
brain development The process whose specific outcome is the progression of the brain over time, from its formation to the mature structure. Brain development begins with patterning events in the neural tube and ends with the mature structure that is the center of thought and emotion. The brain is responsible for the coordination and control of bodily activities and the interpretation of information from the senses (sight, hearing, smell, etc.).
cell population proliferation The multiplication or reproduction of cells, resulting in the expansion of a cell population.
folic acid-containing compound biosynthetic process The chemical reactions and pathways resulting in the formation of folic acid and its derivatives.
folic acid-containing compound metabolic process The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units.
glutamate metabolic process The chemical reactions and pathways involving glutamate, the anion of 2-aminopentanedioic acid.
liver development The process whose specific outcome is the progression of the liver over time, from its formation to the mature structure. The liver is an exocrine gland which secretes bile and functions in metabolism of protein and carbohydrate and fat, synthesizes substances involved in the clotting of the blood, synthesizes vitamin A, detoxifies poisonous substances, stores glycogen, and breaks down worn-out erythrocytes.
one-carbon metabolic process The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
tetrahydrofolylpolyglutamate biosynthetic process The chemical reactions and pathways resulting in the formation of tetrahydrofolylpolyglutamate, a folate derivative comprising tetrahydrofolate attached to a chain of glutamate residues.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q05932 FPGS Folylpolyglutamate synthase, mitochondrial Homo sapiens (Human) PR
10 20 30 40 50 60
MSWARSRLCS TLSLAAVSAR GATTEGAARR GMSAWPAPQE PGMEYQDAVR TLNTLQTNAS
70 80 90 100 110 120
YLEQVKRQRS DPQAQLEAME MYLARSGLQV EDLNRLNIIH VTGTKGKGST CAFTERILRN
130 140 150 160 170 180
YGLKTGFFSS PHMVQVRERI RINGKPISPE LFTKHFWCLY NQLEEFKDDS HVSMPSYFRF
190 200 210 220 230 240
LTLMAFHVFL QEKVDLAVVE VGIGGAFDCT NIIRKPVVCG VSSLGIDHTS LLGDTVEKIA
250 260 270 280 290 300
WQKGGIFKPG VPAFTVVQPE GPLAVLRDRA QQIGCPLYLC PPLEALEEVG LPLSLGLEGA
310 320 330 340 350 360
HQRSNAALAL QLAHCWLERQ DHQDIQELKV SRPSIRWQLP LAPVFRPTPH MRRGLRDTVW
370 380 390 400 410 420
PGRTQILQRG PLTWYLDGAH TTSSVQACVH WYRQSLERSK RTDGGSEVHI LLFNSTGDRD
430 440 450 460 470 480
SAALLKLLQP CQFDYAVFCP NVTEVSSIGN ADQQNFTVTL DQVLLRCLQH QQHWNGLAEK
490 500 510 520 530 540
QASSNLWSSC GPDPAGPGSL LLAPHPPQPT RTSSLVFSCI SHALLWISQG RDPIFQPQSL
550 560 570 580
PRNLLNHPTA NSGASILREA AAIHVLVTGS LHLVGGVLKL LDPSMSQ