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 A2APC3

Entry ID Method Resolution Chain Position Source
AF-A2APC3-F1 Predicted AlphaFoldDB

32 variants for A2APC3

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388592624 5 K>N No EVA
rs27387591 11 G>S No EVA
rs3388592115 22 Q>* No EVA
rs3388601827 33 M>V No EVA
rs3388586548 34 N>S No EVA
rs3388602654 69 F>Y No EVA
rs3388593284 110 S>L No EVA
rs3388586600 124 T>I No EVA
rs3388601264 177 G>W No EVA
rs3388603415 180 P>L No EVA
rs261877142 188 A>T No EVA
rs27387527 192 M>V No EVA
rs253567573 200 T>S No EVA
rs3388599124 201 R>G No EVA
rs3388597760 218 Q>* No EVA
rs3392469514 238 V>A No EVA
rs3392395877 239 L>Q No EVA
rs3392308750 255 F>I No EVA
rs3392387131 255 F>L No EVA
rs3392469506 255 F>Y No EVA
rs224514252 286 D>H No EVA
rs3388601243 291 K>Q No EVA
rs3392395899 309 G>K No EVA
rs3392389239 372 S>R No EVA
rs3392108243 380 T>S No EVA
rs3388592654 381 C>W No EVA
rs3388597792 383 L>R No EVA
rs3388603380 427 M>I No EVA
rs3388603484 432 T>S No EVA
rs3392248032 451 R>L No EVA
rs218634172 451 R>Q No EVA
rs237094414 457 R>K No EVA

No associated diseases with A2APC3

No regional properties for A2APC3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for A2APC3

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton, cilium basal body
  • Cytoplasm, cytoskeleton
  • Cytoplasm, cytoskeleton, flagellum axoneme
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
ciliary basal body A membrane-tethered, short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum) that is similar in structure to a centriole and derives from it. The cilium basal body is the site of assembly and remodelling of the cilium and serves as a nucleation site for axoneme growth. As well as anchoring the cilium, it is thought to provide a selective gateway regulating the entry of ciliary proteins and vesicles by intraflagellar transport.
cilium A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.
motile cilium A cilium which may have a variable arrangement of axonemal microtubules and also contains molecular motors. It may beat with a whip-like pattern that promotes cell motility or transport of fluids and other cells across a cell surface, such as on epithelial cells that line the lumenal ducts of various tissues; or they may display a distinct twirling motion that directs fluid flow asymmetrically across the cellular surface to affect asymmetric body plan organization. Motile cilia can be found in single as well as multiple copies per cell.

4 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.
tubulin binding Binding to monomeric or multimeric forms of tubulin, including microtubules.
tubulin-glutamic acid ligase activity Catalysis of the posttranslational transfer of one or more glutamate residues to the gamma-carboxyl group(s) of one or more specific glutamate residues on a tubulin molecule.

3 GO annotations of biological process

Name Definition
flagellated sperm motility The directed, self-propelled movement of a cilium (aka flagellum) that contributes to the movement of a flagellated sperm.
microtubule cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising microtubules and their associated proteins.
protein polyglutamylation The addition of one or more alpha-linked glutamyl units to the gamma carboxyl group of peptidyl-glutamic acid.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3SZH6 TTLL9 Probable tubulin polyglutamylase TTLL9 Bos taurus (Bovine) PR
Q9BWV7 TTLL2 Probable tubulin polyglutamylase TTLL2 Homo sapiens (Human) PR
Q3SXZ7 TTLL9 Probable tubulin polyglutamylase TTLL9 Homo sapiens (Human) PR
A4Q9F4 Ttll11 Tubulin polyglutamylase TTLL11 Mus musculus (Mouse) PR
A4Q9F0 Ttll7 Tubulin polyglutamylase TTLL7 Mus musculus (Mouse) PR
10 20 30 40 50 60
MSRQKNQNSK GHGVSKGKER EQRTLIRFKT TLMNTLMDVL RHRPGWVEVK DEGEWDFYWC
70 80 90 100 110 120
DVSWLRENFD HTYMDEHVRI SHFRNHYELT RKNYMVKNLK RFRKYLERES GKTEAAKCDF
130 140 150 160 170 180
FPKTFEMPCE YHLFVEEFRK NPGITWIMKP VARSQGKGIF LFRRLKDIMD WRKGTSGKKP
190 200 210 220 230 240
TGVETQPARA NMNPSGSHDT RSSDDQKDDL PVENYVAQRY VENPYLIGGR KFDLRVYVLV
250 260 270 280 290 300
MSYIPLRAWL YRDGFARFSN TRFTLNSIDD HYVHLTNVAV QKTSPDYHLK KGCKWMLQRF
310 320 330 340 350 360
RQYLASKHGP KAVETLFSDM DNIFIKSLQS VQKVIISDKH CFELYGYDIL IDQDLKPWLL
370 380 390 400 410 420
EVNASPSLTA SSQEDYELKT CLLEDTLHVV DMEARLTGKE KRVGGFDLMW NDGPVSREDG
430 440 450 460
PSDLSGMGNF VTNTHLGCVN DRKEQLRQLF RSLQAQRKAP S