Q9HES9

EV
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)

895-927 (tail) EV

Target domain

9-342 (Kinesin motor domain)

Relief mechanism

Partner binding

Assay

Deletion assay

Accessory elements

No accessory elements

References

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

10 regional properties for Q9HES9

Type Name Position InterPro Accession
domain Protein kinase domain 552 - 808 IPR000719
domain Pleckstrin homology domain 398 - 512 IPR001849
domain Protein kinase C-like, phorbol ester/diacylglycerol-binding domain 138 - 189 IPR002219-1
domain Protein kinase C-like, phorbol ester/diacylglycerol-binding domain 265 - 315 IPR002219-2
active_site Serine/threonine-protein kinase, active site 671 - 683 IPR008271
binding_site Protein kinase, ATP binding site 558 - 581 IPR017441
domain Diacylglycerol/phorbol-ester binding 136 - 150 IPR020454-1
domain Diacylglycerol/phorbol-ester binding 152 - 161 IPR020454-2
domain Diacylglycerol/phorbol-ester binding 292 - 303 IPR020454-3
domain Diacylglycerol/phorbol-ester binding 304 - 316 IPR020454-4

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton
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