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 Q61235

Entry ID Method Resolution Chain Position Source
AF-Q61235-F1 Predicted AlphaFoldDB

23 variants for Q61235

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3399669582 104 G>A No EVA
rs3389007119 187 P>T No EVA
rs3389000500 204 S>G No EVA
rs3399560328 215 K>* No EVA
rs226217758 225 V>I No EVA
rs3389009853 267 T>I No EVA
rs3389000540 288 A>T No EVA
rs3399604835 288 A>V No EVA
rs3399392564 292 A>G No EVA
rs3389006096 296 A>V No EVA
rs3398649911 297 T>A No EVA
rs3389007057 298 S>N No EVA
rs3388985470 365 V>F No EVA
rs3389014847 385 R>S No EVA
rs3388989511 388 S>P No EVA
rs3389010105 394 M>I No EVA
rs3388985479 410 R>I No EVA
rs248714286 456 A>T No EVA
rs3389013982 475 G>E No EVA
rs3389011159 483 F>L No EVA
rs3389002102 492 M>I No EVA
rs3389002042 501 I>N No EVA
rs3388959992 512 K>N No EVA

No associated diseases with Q61235

4 regional properties for Q61235

Type Name Position InterPro Accession
domain PDZ domain 95 - 178 IPR001478
domain Pleckstrin homology domain 144 - 282 IPR001849-1
domain Pleckstrin homology domain 305 - 419 IPR001849-2
domain Syntrophin, split Pleckstrin homology (PH) domain 220 - 281 IPR041428

Functions

Description
EC Number
Subcellular Localization
  • Membrane
  • Cytoplasmic vesicle, secretory vesicle membrane ; Peripheral membrane protein
  • Cell junction
  • Cytoplasm, cytoskeleton
  • Membrane-associated
  • In insulinoma cell line, it is enriched in secretory granules (By similarity)
  • In muscle, it is exclusively localized at the neuromuscular junction
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

10 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.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
dystrophin-associated glycoprotein complex A multiprotein complex that forms a strong mechanical link between the cytoskeleton and extracellular matrix; typical of, but not confined to, muscle cells. The complex is composed of transmembrane, cytoplasmic, and extracellular proteins, including dystrophin, sarcoglycans, dystroglycan, dystrobrevins, syntrophins, sarcospan, caveolin-3, and NO synthase.
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
microtubule Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
synapse The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.
transport vesicle membrane The lipid bilayer surrounding a transport vesicle.

3 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
calmodulin binding Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
structural molecule activity The action of a molecule that contributes to the structural integrity of a complex or its assembly within or outside a cell.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q13424 SNTA1 Alpha-1-syntrophin Homo sapiens (Human) PR
Q61234 Snta1 Alpha-1-syntrophin Mus musculus (Mouse) PR
Q925E0 Sntg2 Gamma-2-syntrophin Mus musculus (Mouse) PR
10 20 30 40 50 60
MAVWTRATKA GLVELLLRER WVRVVAELSG ESLSLTGDAA AVEPEPPAAA FNGLPNGGGG
70 80 90 100 110 120
ESLPGSPNRG LGPPSPPAPP RGPAGEASAS PPVRRVRVVK QEAGGLGISI KGGRENRMPI
130 140 150 160 170 180
LISKIFPGLA ADQSRALRLG DAILSVNGTD LRQATHDQAV QALKRAGKEV LLEVKFIREV
190 200 210 220 230 240
TPYIKKPSLV SDLPWEGASP QSPSFSGSED SGSPKHQNTT KDRKVIPLKM CFAARNLSMP
250 260 270 280 290 300
DLENRLIELH SPDSRNTLIL RCKDTATAHS WFVAIHTNIM ALLPQVLAEL NAMLGATSTA
310 320 330 340 350 360
GGSKEVKHIA WLAEQAKLDG GRQQWRPVLM AVTEKDLLLY DCMPWTRDAW ASPCHSYPLV
370 380 390 400 410 420
ATRLVHSGSG CRSPSLGSDL TFATRTGSRQ GIEMHLFRVE THRDLSTWTR ILVQGCHAAA
430 440 450 460 470 480
ELIKEVSLGC TLSGQEVRFT VHYEHGFTIT RDNGGASSIL YRYPFERLKM SADDGIRNLY
490 500 510
LDFGGPEGEL TMDLHSCPKP IVFVLHTFLS AKVTRMGLLV