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

2 structures for Q3USJ8

Entry ID Method Resolution Chain Position Source
7WEG X-ray 200 A C/D 728-740 PDB
AF-Q3USJ8-F1 Predicted AlphaFoldDB

28 variants for Q3USJ8

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388902578 46 K>E No EVA
rs3388935068 50 E>G No EVA
rs223951513 51 R>K No EVA
rs1133158509 104 I>V No EVA
rs3388935099 286 F>Y No EVA
rs3388902646 292 V>I No EVA
rs3388931597 302 Q>H No EVA
rs3388931090 341 N>I No EVA
rs3388931418 371 I>K No EVA
rs3388931603 410 M>I No EVA
rs3388935058 419 N>Y No EVA
rs3388926473 473 T>I No EVA
rs3388912047 474 C>F No EVA
rs3388931366 480 Y>* No EVA
rs3413101006 498 V>M No EVA
rs3388907589 546 R>Q No EVA
rs3388935140 575 L>I No EVA
rs3388887388 582 T>A No EVA
rs3388902642 601 N>K No EVA
rs3388917118 602 Q>H No EVA
rs3397940166 604 D>A No EVA
rs3388923856 607 F>I No EVA
rs3388907618 672 K>N No EVA
rs3388926634 682 P>L No EVA
rs3388926621 684 A>D No EVA
rs244931940 726 R>L No EVA
rs3388935103 727 R>Q No EVA
rs3397940147 739 L>P No EVA

No associated diseases with Q3USJ8

3 regional properties for Q3USJ8

Type Name Position InterPro Accession
domain Phenylalanyl-tRNA synthetase 92 - 326 IPR002319
domain Phenylalanine-tRNA ligase, class II, N-terminal 20 - 87 IPR004188
domain Aminoacyl-tRNA synthetase, class II 116 - 305 IPR006195

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cell junction
  • Membrane, clathrin-coated pit
  • Cell membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Cell projection, stereocilium
  • Partially localized at clathrin-coated pits at the cell membrane
  • Detected at the cell membrane at sites around clathrin-coated pits, very close to the clathrin-coated pits but not an intrinsic part of the clathrin-coated pits
  • Colocalizes at cell-cell contacts with CDH1, but is not detected at tight junctions
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
anchoring junction A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix.
clathrin-coated pit A part of the endomembrane system in the form of an invagination of a membrane upon which a clathrin coat forms, and that can be converted by vesicle budding into a clathrin-coated vesicle. Coated pits form on the plasma membrane, where they are involved in receptor-mediated selective transport of many proteins and other macromolecules across the cell membrane, in the trans-Golgi network, and on some endosomes.
neuromuscular junction The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
recycling endosome An organelle consisting of a network of tubules that functions in targeting molecules, such as receptors transporters and lipids, to the plasma membrane.
stereocilium shaft The shaft comprises the majority of the length of the stereocilium. This region is notable for the extreme stability of actin filaments, which are highly crosslinked into a parallel bundle.

2 GO annotations of molecular function

Name Definition
phosphatidylinositol-3,4,5-trisphosphate binding Binding to phosphatidylinositol-3,4,5-trisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3', 4' and 5' positions.
phosphatidylinositol-3,4-bisphosphate binding Binding to phosphatidylinositol-3,4-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' and 4' positions.

7 GO annotations of biological process

Name Definition
clathrin-dependent endocytosis An endocytosis process that begins when material is taken up into clathrin-coated pits, which then pinch off to form clathrin-coated endocytic vesicles.
membrane organization A process which results in the assembly, arrangement of constituent parts, or disassembly of a membrane. A membrane is a double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins.
neuromuscular synaptic transmission The process of synaptic transmission from a neuron to a muscle, across a synapse.
positive regulation of actin filament polymerization Any process that activates or increases the frequency, rate or extent of actin polymerization.
positive regulation of Arp2/3 complex-mediated actin nucleation Any process that activates or increases the frequency, rate or extent of Arp2/3 complex-mediated actin nucleation.
protein transport The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
regulation of actin filament polymerization Any process that modulates the frequency, rate or extent of the assembly of actin filaments by the addition of actin monomers to a filament.

15 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5T0N5 FNBP1L Formin-binding protein 1-like Homo sapiens (Human) PR
Q7Z6B7 SRGAP1 SLIT-ROBO Rho GTPase-activating protein 1 Homo sapiens (Human) PR
Q96RU3 FNBP1 Formin-binding protein 1 Homo sapiens (Human) PR
O75044 SRGAP2 SLIT-ROBO Rho GTPase-activating protein 2 Homo sapiens (Human) PR
O94868 FCHSD2 F-BAR and double SH3 domains protein 2 Homo sapiens (Human) PR
Q91Z69 Srgap1 SLIT-ROBO Rho GTPase-activating protein 1 Mus musculus (Mouse) PR
Q812A2 Srgap3 SLIT-ROBO Rho GTPase-activating protein 3 Mus musculus (Mouse) PR
Q91Z67 Srgap2 SLIT-ROBO Rho GTPase-activating protein 2 Mus musculus (Mouse) PR
Q80TY0 Fnbp1 Formin-binding protein 1 Mus musculus (Mouse) PR
Q8CJ53 Trip10 Cdc42-interacting protein 4 Mus musculus (Mouse) PR
Q6PFY1 Fchsd1 F-BAR and double SH3 domains protein 1 Mus musculus (Mouse) PR
Q8K012 Fnbp1l Formin-binding protein 1-like Mus musculus (Mouse) PR
D4A208 Srgap2 SLIT-ROBO Rho GTPase-activating protein 2 Rattus norvegicus (Rat) PR
Q8R511 Fnbp1 Formin-binding protein 1 Rattus norvegicus (Rat) PR
Q2HWF0 Fnbp1l Formin-binding protein 1-like Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MQPPPRKVKV TQELRNIQGE QMTKLQAKHQ AECDLLEDMR TFSQKKAAIE REYAQGIQKL
70 80 90 100 110 120
ASQYLKRDWP GIKTDDRNDY RSMYPVWKSF LEGTMQVAQS RINICENYKN FISEPARAVR
130 140 150 160 170 180
SLKEQQLKRC VDQLTKIQTE LQETVKDLVK GKKKYFETEQ MAHAVREKAD IEAKSKLSLF
190 200 210 220 230 240
QSRISLQKAS VKLKARRSEC NTKATHARND YLLTLAAANA HQDRYYQTDL VNIMKALDGN
250 260 270 280 290 300
VYDHLKDYLI AFSRTELETC QAIQNTFQFL LENSSKVVRD YNLQLFLQEN AVFHKPQPFQ
310 320 330 340 350 360
FQPCDSDTSR QLESETGTTE EHSLNKEARK WATRVAREHK NIVHQQRVLN ELECHGVALS
370 380 390 400 410 420
EQSRAELEQK IDEARESIRK AEIIKLKAEA RLDLLKQIGV SVDTWLKSAM NQVMEELENE
430 440 450 460 470 480
RWARPPAVTS NGTLHSLNAD AEREEGEEFE DNMDVFDDSS SSPSGTLRNY PLTCKVVYSY
490 500 510 520 530 540
KASQPDELTI EEHEVLEVIE DGDMEDWVKA RNKVGQVGYV PEKYLQFPTS NSLLSMLQSL
550 560 570 580 590 600
AALDSRSHTS SNSTEAELVS GSLNGDASVC FVKALYDYEG QTDDELSFPE GAIIRILNKE
610 620 630 640 650 660
NQDDDGFWEG EFSGRIGVFP SVLVEELSAS ENGDTPWTRE IQISPSPKPH TSLPPLPLYD
670 680 690 700 710 720
QPPSSPYPSP DKRSSQFFPR SPSANENSLH AESPGFSQAS RQTPDTSYGK LRPVRAAPPP
730
PTQNHRRTTE KMEDVEITLV