Q9HES9
Gene name |
kinA |
Protein name |
Kinesin-like protein |
Names |
|
Species |
Emericella nidulans (Aspergillus nidulans) |
KEGG Pathway |
|
EC number |
|
Protein Class |
CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED (PTHR47969) |
Descriptions
Kinesin-1 is a plus-end microtubule-based motor, and defects in kinesin-based transport are associated with diseases including neurodegeneration. Kinesin is autoinhibited through head-tail interactions. The autoinhibition is released upon cargo recruitment.
Autoinhibitory domains (AIDs)
Target domain |
9-342 (Kinesin motor domain) |
Relief mechanism |
Partner binding |
Assay |
Deletion assay |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q9HES9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9HES9-F1 | Predicted | AlphaFoldDB |
No variants for Q9HES9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9HES9 | |||||
No associated diseases with Q9HES9
No regional properties for Q9HES9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q9HES9 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | ||
| Subcellular Localization |
|
|
| PANTHER Family | PTHR47969 | CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED |
| PANTHER Subfamily | PTHR47969:SF29 | KINESIN-LIKE PROTEIN |
| PANTHER Protein Class |
cytoskeletal protein
microtubule binding motor protein microtubule or microtubule-binding cytoskeletal protein |
|
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| microtubule binding | Binding to a microtubule, a filament composed of tubulin monomers. |
| microtubule motor activity | A motor activity that generates movement along a microtubule, driven by ATP hydrolysis. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| microtubule-based movement | A microtubule-based process that results in the movement of organelles, other microtubules, or other cellular components. Examples include motor-driven movement along microtubules and movement driven by polymerization or depolymerization of microtubules. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASSTSNPSN | TIKVVARFRP | QNKVELASGG | QPIVEFENDE | TCSINSKEAS | GSFTFDRVFP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MDSKQTDVFN | YSIAPTVDDI | LNGYNGTVFA | YGQTGAGKSY | TMMGSDIDDE | VGKGIIPRIV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EQIFASILTS | PSNIEYTVRL | SYMEIYMERI | RDLLVPQNDN | LPVHEEKSRG | VYVKGLLEVY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VSSVQEVYEV | MRRGGNARAV | AATNMNQESS | RSHSIFVITV | TQKNLETGSA | KSGQLFLVDL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AGSEKVGKTG | ASGQTLEEAK | KINKSLSALG | MVINALTDGK | STHIPYRDSK | LTRILQESLG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GNSRTTLIIN | CSPSSYNDAE | TVSTLRFGVR | AKAIKNKAKV | NAELSPAELK | QLLRRAQSQV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TSFENYISAL | ESEVSSWRSG | ETVPREKWTP | ARNAEAVRGA | KAEARGPRPS | TPSRLHDVSR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SETPRPDSRI | GDRSSTPSIV | LEKDEREEFL | RRENELQDQI | AEKESHIATI | ERGLREARDE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LRTLKENSAR | SGKDNEKLNA | EVNELRMHLE | KVSYESKEAA | ITMDSLREAN | SELTAELDEV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KQQLLDVRMK | AKETTAALDE | KEKKKAEKMA | KMMAGFDLGG | EVFSDNERKL | QNLIQRVDSL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| HQIAEAGEVI | APDDLLELRA | SLSETQGFIR | QAELTVNDRS | ELNVLQDSRR | MELEQKLANL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EQDYESLLAR | NLGEEDLAEI | KERLEKVYIA | KKDVELAAAS | ELQQQLARKD | EELTKLQQSL |
| 730 | 740 | 750 | 760 | 770 | 780 |
| ADSQSRGSTN | GAASKSLQQQ | IAEFDAMKKS | LMRDLQNRCE | RVVELEISLD | DAREQYNNVL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| RSSNNRAQQK | KMAFLERNLE | QLTHVQRQLV | EQNSSLKKEV | AIAERKLIAR | NERISSLEAL |
| 850 | 860 | 870 | 880 | 890 | 900 |
| LQESQEKLTQ | ANHRFEAQLT | AVKERLEAAK | QGSTKGLPGM | DSNGGFSFAG | SRIAKPLRGG |
| 910 | 920 | ||||
| GGGNEPVAAV | QSQDTGTKRT | SWFFDRR |