Autoinhibited structure

Activated structure

1 structures for P33175

Entry ID Method Resolution Chain Position Source
AF-P33175-F1 Predicted AlphaFoldDB

54 variants for P33175

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389104329 23 E>V No EVA
rs3389131086 37 D>N No EVA
rs3389071016 39 S>N No EVA
rs3389120442 65 A>T No EVA
rs3389127993 70 I>V No EVA
rs3389141192 108 I>N No EVA
rs3389123715 184 I>S No EVA
rs3389129798 186 E>G No EVA
rs3389071047 209 F>L No EVA
rs3389141206 215 Q>* No EVA
rs3412846132 238 K>N No EVA
rs3389129649 247 A>G No EVA
rs3389096653 302 I>V No EVA
rs3548449075 312 A>T No EVA
rs33857632 355 A>T No EVA
rs3389131043 456 L>R No EVA
rs3389131103 458 S>P No EVA
rs3389141753 460 R>Q No EVA
rs3389109133 463 N>K No EVA
rs3401551972 526 M>RGFEVRC* No EVA
rs3401748107 535 R>SAFAGVH* No EVA
rs3401414784 538 E>G No EVA
rs262744864 556 R>K No EVA
rs3389071105 562 S>R No EVA
rs3389132917 567 N>K No EVA
rs3389141145 575 E>* No EVA
rs3389096742 582 E>Q No EVA
rs3389137249 624 R>M No EVA
rs3389134581 629 C>S No EVA
rs3389131014 634 S>L No EVA
rs3401552034 641 R>C No EVA
rs3389128025 649 T>* No EVA
rs3389096687 649 T>S No EVA
rs3389071034 662 D>Y No EVA
rs3389104305 692 A>T No EVA
rs3389141143 703 M>L No EVA
rs3389129656 706 H>Q No EVA
rs3389129859 710 H>Y No EVA
rs3389123751 732 K>N No EVA
rs3389096737 766 L>M No EVA
rs3389129785 824 H>L No EVA
rs3389128006 838 E>V No EVA
rs3389129773 868 T>M No EVA
rs3389132864 896 E>K No EVA
rs3389129818 907 K>N No EVA
rs3389141715 909 S>F No EVA
rs3548358947 939 R>Q No EVA
rs3389123703 948 N>I No EVA
rs49422622 966 T>A No EVA
rs216030226 976 A>V No EVA
rs3389132857 982 L>S No EVA
rs3401764371 985 Y>* No EVA
rs3389109137 989 N>I No EVA
rs3401160995 1003 S>G No EVA

No associated diseases with P33175

2 regional properties for P33175

Type Name Position InterPro Accession
domain Kinesin motor domain 7 - 335 IPR001752
conserved_site Kinesin motor domain, conserved site 226 - 237 IPR019821

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, perinuclear region
  • Cytoplasm, cytoskeleton
  • Perikaryon
  • Concentrated in the cell body of the neurons, particularly in the perinuclear region
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

15 GO annotations of cellular component

Name Definition
apical dendrite A dendrite that emerges near the apical pole of a neuron. In bipolar neurons, apical dendrites are located on the opposite side of the soma from the axon.
axon The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter.
axon cytoplasm Any cytoplasm that is part of a axon.
central region of growth cone The center of the migrating motile tip of a growing nerve cell axon or dendrite.
ciliary rootlet A cytoskeleton-like structure, originating from the basal body at the proximal end of a cilium, and extending proximally toward the cell nucleus. Rootlets are typically 80-100 nm in diameter and contain cross striae distributed at regular intervals of approximately 55-70 nm.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
dendrite A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body.
dendrite cytoplasm All of the contents of a dendrite, excluding the surrounding plasma membrane.
kinesin complex Any complex that includes a dimer of molecules from the kinesin superfamily, a group of related proteins that contain an extended region of predicted alpha-helical coiled coil in the main chain that likely produces dimerization. The native complexes of several kinesin family members have also been shown to contain additional peptides, often designated light chains as all of the noncatalytic subunits that are currently known are smaller than the chain that contains the motor unit. Kinesin complexes generally possess a force-generating enzymatic activity, or motor, which converts the free energy of the gamma phosphate bond of ATP into mechanical work.
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.
neuron projection A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
neuronal cell body The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
P-body A focus in the cytoplasm where mRNAs may become inactivated by decapping or some other mechanism. Protein and RNA localized to these foci are involved in mRNA degradation, nonsense-mediated mRNA decay (NMD), translational repression, and RNA-mediated gene silencing.
perikaryon The portion of the cell soma (neuronal cell body) that excludes the nucleus.
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.

8 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
kinesin binding Interacting selectively and non-covalently and stoichiometrically with kinesin, a member of a superfamily of microtubule-based motor proteins that perform force-generating tasks such as organelle transport and chromosome segregation.
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.
plus-end-directed microtubule motor activity A motor activity that generates movement along a microtubule toward the plus end, driven by ATP hydrolysis.
protein-containing complex binding Binding to a macromolecular complex.
scaffold protein binding Binding to a scaffold protein. Scaffold proteins are crucial regulators of many key signaling pathways. Although not strictly defined in function, they are known to interact and/or bind with multiple members of a signaling pathway, tethering them into complexes.

7 GO annotations of biological process

Name Definition
anterograde axonal protein transport The directed movement of proteins along microtubules from the cell body toward the cell periphery in nerve cell axons.
anterograde dendritic transport of neurotransmitter receptor complex The directed movement of a neurotransmitter receptor complex along microtubules in nerve cell dendrites towards the postsynapse.
axon guidance The chemotaxis process that directs the migration of an axon growth cone to a specific target site in response to a combination of attractive and repulsive cues.
mitotic cell cycle Progression through the phases of the mitotic cell cycle, the most common eukaryotic cell cycle, which canonically comprises four successive phases called G1, S, G2, and M and includes replication of the genome and the subsequent segregation of chromosomes into daughter cells. In some variant cell cycles nuclear replication or nuclear division may not be followed by cell division, or G1 and G2 phases may be absent.
retrograde neuronal dense core vesicle transport The directed movement of neuronal dense core vesicles along axonal microtubules towards the cell body.
synaptic vesicle transport The directed movement of synaptic vesicles.
vesicle-mediated transport A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane.

16 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P17210 Khc Kinesin heavy chain Drosophila melanogaster (Fruit fly) EV
O60282 KIF5C Kinesin heavy chain isoform 5C Homo sapiens (Human) EV
P33176 KIF5B Kinesin-1 heavy chain Homo sapiens (Human) EV
Q12840 KIF5A Kinesin heavy chain isoform 5A Homo sapiens (Human) EV
P28738 Kif5c Kinesin heavy chain isoform 5C Mus musculus (Mouse) SS
Q61768 Kif5b Kinesin-1 heavy chain Mus musculus (Mouse) EV
Q99PW8 Kif17 Kinesin-like protein KIF17 Mus musculus (Mouse) SS
Q7M6Z4 Kif27 Kinesin-like protein KIF27 Mus musculus (Mouse) SS
Q9QXL2 Kif21a Kinesin-like protein KIF21A Mus musculus (Mouse) EV SS
Q9QXL1 Kif21b Kinesin-like protein KIF21B Mus musculus (Mouse) SS
Q9EQW7 Kif13a Kinesin-like protein KIF13A Mus musculus (Mouse) SS
B7ZNG0 Kif7 Kinesin-like protein KIF7 Mus musculus (Mouse) SS
Q2PQA9 Kif5b Kinesin-1 heavy chain Rattus norvegicus (Rat) SS
Q6QLM7 Kif5a Kinesin heavy chain isoform 5A Rattus norvegicus (Rat) SS
P34540 unc-116 Kinesin heavy chain Caenorhabditis elegans SS
Q9SV36 KINUC Kinesin-like protein KIN-UC Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAETNNECSI KVLCRFRPLN QAEILRGDKF IPIFQGDDSV IIGGKPYVFD RVFPPNTTQE
70 80 90 100 110 120
QVYHACAMQI VKDVLAGYNG TIFAYGQTSS GKTHTMEGKL HDPQLMGIIP RIARDIFNHI
130 140 150 160 170 180
YSMDENLEFH IKVSYFEIYL DKIRDLLDVT KTNLSVHEDK NRVPFVKGCT ERFVSSPEEI
190 200 210 220 230 240
LDVIDEGKSN RHVAVTNMNE HSSRSHSIFL INIKQENVET EQKLSGKLYL VDLAGSEKVS
250 260 270 280 290 300
KTGAEGAVLD EAKNINKSLS ALGNVISALA EGTKSYVPYR DSKMTRILQD SLGGNCRTTM
310 320 330 340 350 360
FICCSPSSYN DAETKSTLMF GQRAKTIKNT ASVNLELTAE QWKKKYEKEK EKTKAQKETI
370 380 390 400 410 420
AKLEAELSRW RNGENVPETE RLAGEDSALG AELCEETPVN DNSSIVVRIA PEERQKYEEE
430 440 450 460 470 480
IRRLYKQLDD KDDEINQQSQ LIEKLKQQML DQEELLVSTR GDNEKVQREL SHLQSENDAA
490 500 510 520 530 540
KDEVKEVLQA LEELAVNYDQ KSQEVEEKSQ QNQLLVDELS QKVATMLSLE SELQRLQEVS
550 560 570 580 590 600
GHQRKRIAEV LNGLMRDLSE FSVIVGNGEI KLPVEISGAI EEEFTVARLY ISKIKSEVKS
610 620 630 640 650 660
VVKRCRQLEN LQVECHRKME VTGRELSSCQ LLISQHEAKI RSLTEYMQTV ELKKRHLEES
670 680 690 700 710 720
YDSLSDELAR LQAHETVHEV ALKDKEPDTQ DAEEVKKALE LQMENHREAH HRQLARLRDE
730 740 750 760 770 780
INEKQKTIDE LKDLNQKLQL ELEKLQADYE RLKNEENEKS AKLQELTFLY ERHEQSKQDL
790 800 810 820 830 840
KGLEETVARE LQTLHNLRKL FVQDVTTRVK KSAEMEPEDS GGIHSQKQKI SFLENNLEQL
850 860 870 880 890 900
TKVHKQLVRD NADLRCELPK LEKRLRATAE RVKALEGALK EAKEGAMKDK RRYQQEVDRI
910 920 930 940 950 960
KEAVRYKSSG KRGHSAQIAK PVRPGHYPAS SPTNPYGTRS PECISYTNNL FQNYQNLHLQ
970 980 990 1000 1010 1020
AAPSSTSDMY FASSGATSVA PLASYQKANM DNGNATDIND NRSDLPCGYE AEDQAKLFPL
HQETAAS