Descriptions

Kinesin (KIF) motor proteins play a major role in the transport of intracellular cargo and in the regulation of microtubule (MT) organization and dynamics in an ATP-dependent fashion. A prototypic kinesin includes a conserved globular N-terminal motor domain, which binds to MTs, hydrolyses ATP and converts its chemical energy to mechanical work. The kinesin motor domain is typically followed by a stalk domain often consisting of α-helical coiled-coil regions that are important for dimerization and a tail domain containing the binding sites for cargo or kinesin-regulatory proteins.
In human KIF21A, the intramolecular antiparallel coiled coil in the stalk domain autoinhibits the kinesin motor domain, preventing its interaction with microtubules (MTs) and ATP hydrolysis, thus regulating intracellular transport and MT dynamics. Interaction of the KIF21A regulatory domain with the KIF21B motor domain and sequence similarities to KIF7 and KIF27 strongly suggest a conservation of this regulatory mechanism in other kinesin-4 family members.

Autoinhibitory domains (AIDs)

Target domain

7-379 (Kinesin motor domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

0 structures for A0A8V0XS96

Entry ID Method Resolution Chain Position Source

14 variants for A0A8V0XS96

Variant ID(s) Position Change Description Diseaes Association Provenance
rs735116450 213 T>P No EVA
rs733481110 214 T>P No EVA
rs80678074 599 E>D No EVA
rs739093380 831 V>E No EVA
rs735808068 832 S>G No EVA
rs736463422 835 L>P No EVA
rs3555183949 1122 G>S No EVA
rs732545094 1228 T>A No EVA
rs15193535 1232 T>A No EVA
rs317786474 1232 T>I No EVA
rs80583501 1241 D>N No EVA
rs315056178 1244 I>T No EVA
rs740959036 1248 S>N No EVA
rs734053691 1583 L>V No EVA

No associated diseases with A0A8V0XS96

9 regional properties for A0A8V0XS96

Type Name Position InterPro Accession
repeat WD40 repeat 1311 - 1389 IPR001680-1
repeat WD40 repeat 1415 - 1453 IPR001680-2
repeat WD40 repeat 1456 - 1498 IPR001680-3
repeat WD40 repeat 1506 - 1544 IPR001680-4
repeat WD40 repeat 1547 - 1590 IPR001680-5
repeat WD40 repeat 1590 - 1630 IPR001680-6
domain Kinesin motor domain 7 - 379 IPR001752
conserved_site WD40 repeat, conserved site 1335 - 1349 IPR019775
conserved_site Kinesin motor domain, conserved site 268 - 279 IPR019821

Functions

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

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

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
MSAGQDESSV RVAVRIRPQL AKEKIEGCHI CTSVTPGEPQ VFLGKDKAFT FDYVFNIDSQ
70 80 90 100 110 120
QEEIYIQCIE KLIEGCFEGY NATVFAYGQT GAGKTYTMGT GFDVNITEEE QGIISRAVKH
130 140 150 160 170 180
LFRCIEEKKQ AAIKQGLPPP DFKVNAQFLE LYNEEILDLF DTTRDIDAKN KKSNIKIHED
190 200 210 220 230 240
SAGGIYTVGV TTRTVNGESE MMQCLKLGAL SRTTASTQMN VQSSRSHAIF TIHLCQTRVC
250 260 270 280 290 300
PAFNTDNATD NRIISESSEM NEFETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG
310 320 330 340 350 360
LLALGNVISA LGDKSKKATH VPYRDSKLTR LLQDSLGGNS QTLMIACVSP SDRDFMETLN
370 380 390 400 410 420
TLKYANRARN IKNKVMVNQD RASQQINALR NEITRLQMEL MEYKTGKRII DEEGVESIND
430 440 450 460 470 480
MFHENAMLQT ENNNLRVRIK AMQETIDALR ARVTQLVSDQ ANQVLARAGE GNEEISNMIH
490 500 510 520 530 540
NYIKEIEDLR AKLLESEAVN ENLRRNLSRA STRSTYFGGP SAFSMLSSEK ETLEILDIAK
550 560 570 580 590 600
KDLEKLKKKE RKKKKSVKDD NTDNEQEKRD EKGTSERANN ELEAEEIQEA SDHEDEEEED
610 620 630 640 650 660
DEDEDDMEVV ESSDESDSDS DEKENYQADL ANITCEIAIK QKLIDELENS QRRLQTLKKQ
670 680 690 700 710 720
YEEKLMMLQH KIRDTQLERD QVLQNLGSVE TYSEEKAKKI KSEYEKKLQA MNKELQRLQT
730 740 750 760 770 780
AQKEHARLLK NQSQYEKQLK KLQQEVTEMK KTKVRLMKQM KEEQEKARMT ESRRNREIAQ
790 800 810 820 830 840
LKKEQRKREH QLKLLEAQKR NQEVILRRKT EEVTALRRQV RPLSDKVAGK VSRKLSLPEH
850 860 870 880 890 900
PIQEPSSSSS VEHDGSRTAA QQKMRIPVAR VQALSVTATN GTGKKYQRKA VTSRVYSSRA
910 920 930 940 950 960
ARMKWQLLER RVTDIIMQRM TISNMEADMN RLLTQREELT RRREKLSKKR EKLIKDGGGS
970 980 990 1000 1010 1020
EADRNVQNIN EEMESLTANI DYINDSISDC QANIMQMEEA KEEGETLDVT AVINACTLTE
1030 1040 1050 1060 1070 1080
ARYLLDHFLT MGINKGLQAA QKEAQIKVLE GRLKQTEITS ATQNQLLFHM LKEKAELNPE
1090 1100 1110 1120 1130 1140
LDALLGHALQ EHLEDSTDED APLHSPGTEG SALSSDLLKL CGEVKPKSKA RRRTTTQMEL
1150 1160 1170 1180 1190 1200
LYADSSDLVS DVSAAESTLP GLPESAAETQ ESGMTADTND TSARDREFIP PPTGLPSKIG
1210 1220 1230 1240 1250 1260
SISRQPSLSE KKIPEPSPLA KRKTYEKTME KTKAKDQKLS DSGIPEASLS PPTSPPSRPR
1270 1280 1290 1300 1310 1320
NEMNVFSRLT VSQGNTSVQQ DKSDESDSSL SEVHRGIINP FPASKCIRTS PLQCIYTAEG
1330 1340 1350 1360 1370 1380
HAKPVLCVDA TDDLLFTGSK DRTCKVWNLV TGQEIMSLGG HPNNVVSIKY CNYTSLVFTV
1390 1400 1410 1420 1430 1440
STSYIKVWDI RDSAKCVRTL TSSGQAMPGD VCSGSTNRTV TIPAGENQIN QIALNPTGTF
1450 1460 1470 1480 1490 1500
LYAAAGNSVR MWDLKRFQST GKLTGHLGPV MCLTVDRISN GQDLIVTGSK DHYIKMFDVT
1510 1520 1530 1540 1550 1560
EGALGSVSPT HNFEPPHYDG IEALAIMGDN LFSGSRDNGI KKWDLAQKDL LQQVPNAHKD
1570 1580 1590 1600 1610 1620
WVCALGLVPG APVLLSGCRG GALKLWNVDT FAPIGEMKGH DSPINAICTN SSQIFTASDD
1630 1640
RTVRIWKARN VIDGQISDAG DASEDLASN