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 Q8K0T4

Entry ID Method Resolution Chain Position Source
AF-Q8K0T4-F1 Predicted AlphaFoldDB

18 variants for Q8K0T4

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388812929 28 Y>* No EVA
rs3388815251 60 L>F No EVA
rs3388796462 61 E>K No EVA
rs3388813103 100 P>T No EVA
rs3388796439 107 H>R No EVA
rs3388815190 113 I>N No EVA
rs3396390221 129 A>E No EVA
rs3388810369 173 D>Y No EVA
rs864270107 182 A>T No EVA
rs3388812593 204 H>L No EVA
rs3388791861 277 S>Y No EVA
rs3388811336 331 L>I No EVA
rs3395985724 333 Q>H No EVA
rs3388812585 441 E>* No EVA
rs3396390219 470 V>A No EVA
rs3396133354 471 S>A No EVA
rs3396301897 472 A>E No EVA
rs3396439028 473 A>T No EVA

No associated diseases with Q8K0T4

5 regional properties for Q8K0T4

Type Name Position InterPro Accession
domain AAA+ ATPase domain 238 - 380 IPR003593
domain ATPase, AAA-type, core 242 - 378 IPR003959
conserved_site ATPase, AAA-type, conserved site 350 - 369 IPR003960
domain Spastin/Vps4, C-terminal 447 - 486 IPR015415
domain AAA ATPase, AAA+ lid domain 400 - 437 IPR041569

Functions

Description
EC Number 5.6.1.1 Enzymes altering polypeptide conformation or assembly
Subcellular Localization
  • Cytoplasm, cytoskeleton
  • Cytoplasm
  • Cytoplasm, cytoskeleton, spindle pole
  • Cytoplasm, cytoskeleton, spindle
  • Colocalizes with microtubules throughout the basal and adluminal compartments of Sertoli cells (PubMed:22654668)
  • Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
centrosome A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
katanin complex A complex possessing an activity that couples ATP hydrolysis to the severing of microtubules; usually a heterodimer comprising a catalytic subunit (often 60kDa) and a regulatory subunit (often 80 kDa).
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.
microtubule cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins.
spindle The array of microtubules and associated molecules that forms between opposite poles of a eukaryotic cell during mitosis or meiosis and serves to move the duplicated chromosomes apart.
spindle pole Either of the ends of a spindle, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules.

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
identical protein binding Binding to an identical protein or proteins.
isomerase activity Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
microtubule binding Binding to a microtubule, a filament composed of tubulin monomers.
microtubule severing ATPase activity Catalysis of the reaction: ATP + H2O = ADP + phosphate. Catalysis of the severing of a microtubule at a specific spot along its length, coupled to the hydrolysis of ATP.

2 GO annotations of biological process

Name Definition
microtubule severing The process in which a microtubule is broken down into smaller segments. Severing enzymes remove dimers from the middle of the filament to create new ends, unlike depolymerizing kinesins that use ATP to uncap microtubules at their ends.
spermatogenesis The developmental process by which male germ line stem cells self renew or give rise to successive cell types resulting in the development of a spermatozoa.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O75449 KATNA1 Katanin p60 ATPase-containing subunit A1 Homo sapiens (Human) PR
P46467 Vps4b Vacuolar protein sorting-associated protein 4B Mus musculus (Mouse) PR
Q8VEJ9 Vps4a Vacuolar protein sorting-associated protein 4A Mus musculus (Mouse) PR
A0JMA9 katnal2 Katanin p60 ATPase-containing subunit A-like 2 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
Q0IIR9 katna1 Katanin p60 ATPase-containing subunit A1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MNLAEICENA KKGREYALLG NYDSSMVYYQ GVIQQIQRHC QSLRDPATKA KWQQVRQELL
70 80 90 100 110 120
EEYEQVKSIV STLESFKMDK PPDFPVSCRD EPFRDPAVWP PPVPAEHRAP PQIRRPNREV
130 140 150 160 170 180
RPLRKDVGAG ARGLVGRAHQ ISKSDKPASR DKDYRARGRD DKARKNVQDG ASDSEIPKFD
190 200 210 220 230 240
GAGYDKDLVE ALERDIVSRN PSIHWDDIAD LEEAKKLLRE AVVLPMWMPD FFKGIRRPWK
250 260 270 280 290 300
GVLMVGPPGT GKTMLAKAVA TECGTTFFNV SSSTLTSKYR GESEKLVRLL FEMARFYAPT
310 320 330 340 350 360
TIFIDEIDSI CSRRGTSDEH EASRRVKSEL LIQMDGVGGA LENDDPSKMV MVLAATNFPW
370 380 390 400 410 420
DIDEALRRRL EKRIYIPLPT AKGRAELLKI SLREVELDPD VHLEDIADKT EGYSGADITN
430 440 450 460 470 480
ICRDASLMAM RRRINGLSPE EIRALSKEEL QMPVTRGDLE LALKKIAKSV SAADLEKYEK
WMVEFGSA