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 Q8K298

Entry ID Method Resolution Chain Position Source
AF-Q8K298-F1 Predicted AlphaFoldDB

69 variants for Q8K298

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389027890 6 E>K No EVA
rs225193183 55 P>S No EVA
rs3389030427 71 R>L No EVA
rs37932230 96 S>F No EVA
rs37157079 138 T>A No EVA
rs3389023494 187 S>T No EVA
rs38027729 271 P>R No EVA
rs265252769 297 A>S No EVA
rs37272738 299 T>P No EVA
rs258759247 303 E>K No EVA
rs242487726 307 A>V No EVA
rs223794682 317 A>V No EVA
rs260590324 325 R>G No EVA
rs237471318 325 R>L No EVA
rs3389032877 337 A>P No EVA
rs220725387 337 A>V No EVA
rs3399552323 350 Q>L* No EVA
rs3389019302 363 R>* No EVA
rs3389009706 380 S>I No EVA
rs243645917 388 A>E No EVA
rs3399883416 402 I>F No EVA
rs38133168 445 A>T No EVA
rs3389035768 453 S>G No EVA
rs3389029371 462 V>L No EVA
rs3389009657 477 S>R No EVA
rs37859091 478 T>A No EVA
rs3389004392 504 S>F No EVA
rs3389031740 513 S>N No EVA
rs3389027932 521 L>V No EVA
rs3388997792 543 R>S No EVA
rs3389027869 560 I>N No EVA
rs3389032911 571 G>R No EVA
rs3389027909 577 K>R No EVA
rs3389004389 599 I>N No EVA
rs3389035821 602 M>L No EVA
rs213152048 621 I>S No EVA
rs243729029 625 P>L No EVA
rs226708982 632 N>S No EVA
rs3389032935 637 S>R No EVA
rs3389035804 638 P>A No EVA
rs3389024084 648 V>L No EVA
rs3389027928 662 R>L No EVA
rs218585683 702 K>N No EVA
rs3389036956 733 S>I No EVA
rs3389027880 770 D>Y No EVA
rs3389036981 791 Q>H No EVA
rs219271054 795 A>V No EVA
rs36930798 844 P>S No EVA
rs3389032902 861 T>S No EVA
rs37518540 868 V>D No EVA
rs37770781 873 E>D No EVA
rs3389027844 883 Q>* No EVA
rs3389004356 890 P>S No EVA
rs3388997759 928 L>F No EVA
rs3389028049 932 R>C No EVA
rs3389035858 939 V>L No EVA
rs37547815 955 A>G No EVA
rs3389024054 959 V>I No EVA
rs37513608 966 E>A No EVA
rs3388997824 973 I>K No EVA
rs38554154 994 S>G No EVA
rs3389028077 996 F>L No EVA
rs3389024062 1012 S>P No EVA
rs3389036919 1013 Y>* No EVA
rs37952958 1013 Y>S No EVA
rs3388978823 1033 N>T No EVA
rs3389029388 1039 I>K No EVA
rs3389009667 1046 F>L No EVA
rs3389019264 1081 K>* No EVA

No associated diseases with Q8K298

5 regional properties for Q8K298

Type Name Position InterPro Accession
domain Pleckstrin homology domain 980 - 1106 IPR001849
domain Anillin homology domain 797 - 950 IPR012966
domain Anillin, N-terminal domain 141 - 227 IPR031970-1
domain Anillin, N-terminal domain 424 - 480 IPR031970-2
domain Anillin, PH domain 981 - 1107 IPR037840

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
  • Cytoplasm, cytoskeleton
  • Cytoplasm, cell cortex
  • Cell projection, bleb
  • Mainly found in the nucleus during interphase
  • Colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis and subsequently concentrates in the area of the prospective contractile ring in anaphase
  • This pattern persists until telophase, when the protein becomes concentrated in the midbody
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
actin cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
actomyosin contractile ring A cytoskeletal structure composed of actin filaments and myosin that forms beneath the plasma membrane of many cells, including animal cells and yeast cells, in a plane perpendicular to the axis of the spindle, i.e. the cell division plane. In animal cells, the contractile ring is located at the cleavage furrow. In budding fungal cells, e.g. mitotic S. cerevisiae cells, the contractile ring forms at the mother-bud neck before mitosis.
bleb A cell extension caused by localized decoupling of the cytoskeleton from the plasma membrane and characterized by rapid formation, rounded shape, and scarcity of organelles within the protrusion. Blebs are formed during apoptosis and other cellular processes, including cell locomotion, cell division, and as a result of physical or chemical stresses. [GOC:mtg_apoptosis, PMID:12083798, PMID:16624291, Wikipedia:Bleb_(cell_biology)]
cell cortex The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.
midbody A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.

1 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.

6 GO annotations of biological process

Name Definition
actomyosin contractile ring assembly The process of assembly of a ring composed of actin, myosin, and associated proteins that will function in cytokinesis.
hematopoietic progenitor cell differentiation The process in which precursor cell type acquires the specialized features of a hematopoietic progenitor cell, a class of cell types including myeloid progenitor cells and lymphoid progenitor cells.
mitotic cytokinesis A cell cycle process that results in the division of the cytoplasm of a cell after mitosis, resulting in the separation of the original cell into two daughter cells.
podocyte cell migration The orderly movement of a podocyte from one site to another, often during the development of a multicellular organism or multicellular structure. A podocyte is a specialized kidney epithelial cell.
positive regulation of bleb assembly Any process that activates or increases the frequency, rate or extent of bleb assembly.
septin ring organization Control of the formation, spatial distribution, and breakdown of the septin ring.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDPFTEKLLE RTRARRENLQ RKMAERPTAV ARSAPHAKRG REPLSEASNQ QQPLPGGEEK
70 80 90 100 110 120
SCTKPSPSKK RCSDKIEVGA PDLENTEPID VAKPCSPMPA PRQAKPPAPA AISESVAAPA
130 140 150 160 170 180
ALLSADRGLN SGSEASATSS VKTRMQRLAE QRRHWDSDLT DDVSESSYFA PVPTEDKAAS
190 200 210 220 230 240
PSKPPISNAS ATPVGRRGRL ANLAATICSW EDDVSHSSAK QNSVQEQPGT ACLSKSSSAS
250 260 270 280 290 300
GASASINSSS VQQEATCCSP RDGNASVRKD PSSNAAHGPL LSASVSSSVK ASSPVTAATF
310 320 330 340 350 360
ITENREAQNP ELLHKTASPL KTEARKPCEK PTLSQGAQPK EEANREVCLQ SQSKDKLATP
370 380 390 400 410 420
GGRGIKPFLE RFGERCQEHS KESPSYRASH KTPNITPNTK AIQERLFKQN TCSSTTHLAQ
430 440 450 460 470 480
QLKQEREKEL ACLRGRLDKG NLWSAEKNEK SRSKHLETKQ EVHCQNTPLK KHQTVASTPL
490 500 510 520 530 540
TSVTDKVAEN EPAVKLSSTE PAGSTESEMT KSSPLKITLF LEEEKSLKVA SDLEVEQNTE
550 560 570 580 590 600
AVREVEMSVD DEDINSSRVI NDIFSDVLEE GELDVEKSQE EMDQVGAENS EEQEDALNIS
610 620 630 640 650 660
SMSLLAPLAQ TVGVVSLENV ISSPPSELRD SNLSAASPKP GKFQRTRVPR AESADSLGSE
670 680 690 700 710 720
DRDLLYSIDA YRSQRFKETE RPSIKQVIVR KEDVTSKLGE KKNVFSGQVN IKQKMQELNN
730 740 750 760 770 780
DINLQQTVIY QASQALNCCV DEEHGKGSLE EAEAERLLLI ATEKRALLID ELNKLKSEGP
790 800 810 820 830 840
QRRNKTSVIS QSEFAPSKGS VTLSEICLPL KADFVCSTAQ KTDASNYYYL IMLKAGAEQM
850 860 870 880 890 900
VATPLASTAN SLSGDALTFP TTFTLHDVSN DFEINIEVYS LVQKKDSLGP DKKKKASKSK
910 920 930 940 950 960
AITPKRLLTS ITSKSSLHSS VMASPGGLGA VRTSNFTLVG SHTLSLSSVG DTKFALDKVP
970 980 990 1000 1010 1020
FLSPLEGHIC LKISCQVNSA VEEKGFLTIF EDVSGFGAWH RRWCVLSGNC ISYWTYPDDE
1030 1040 1050 1060 1070 1080
RRKNPIGRIN LANCISHQIE PANREFCARR NTLELITVRP QREDDRETLV SQCRDTLCVT
1090 1100 1110 1120
KNWLSADTKE ERDLWMQKLN QVIVDIRLWQ PDACYKPVGK P