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

3 structures for Q5XKE0

Entry ID Method Resolution Chain Position Source
1X5Y NMR - A 731-828 PDB
2DLT NMR - A 433-525 PDB
AF-Q5XKE0-F1 Predicted AlphaFoldDB

45 variants for Q5XKE0

Variant ID(s) Position Change Description Diseaes Association Provenance
rs220930961 17 A>T No EVA
rs253452016 21 A>D No EVA
rs3388907011 152 P>S No EVA
rs238767052 161 L>F No EVA
rs3412971963 180 F>I No EVA
rs3388902200 208 E>* No EVA
rs3388888011 209 I>F No EVA
rs3388906515 233 L>H No EVA
rs3388893773 241 K>N No EVA
rs3388864299 251 A>V No EVA
rs3388864246 260 A>P No EVA
rs3388908562 265 R>K No EVA
rs3388887927 302 V>I No EVA
rs3388887928 315 L>P No EVA
rs3388902237 324 A>S No EVA
rs3388907053 351 Q>L No EVA
rs3388893779 359 E>K No EVA
rs3388907063 360 M>I No EVA
rs3388899280 463 T>DG* No EVA
rs3388902212 463 T>R No EVA
rs3388879983 465 K>SVE* No EVA
rs3388864300 492 I>V No EVA
rs3388909807 541 S>P No EVA
rs3412089096 558 R>W No EVA
rs3388904571 563 I>F No EVA
rs3388906549 577 D>N No EVA
rs234252566 582 A>V No EVA
rs37670914 619 V>A No EVA
rs3388864298 638 E>G No EVA
rs3388899212 718 Q>R No EVA
rs3388897018 794 K>R No EVA
rs3388908567 832 Q>* No EVA
rs3388893713 859 F>L No EVA
rs3388902236 873 G>W No EVA
rs3388887930 917 T>I No EVA
rs3388899238 949 Q>E No EVA
rs3388885516 974 W>* No EVA
rs240332828 1001 I>V No EVA
rs3388902240 1003 S>R No EVA
rs3388906566 1021 R>* No EVA
rs3388885444 1036 E>V No EVA
rs3388906886 1045 F>I No EVA
rs3388899303 1070 P>T No EVA
rs3388864266 1080 K>* No EVA
rs3413055744 1119 N>I No EVA

No associated diseases with Q5XKE0

26 regional properties for Q5XKE0

Type Name Position InterPro Accession
domain Immunoglobulin subtype 2 552 - 620 IPR003598-1
domain Immunoglobulin subtype 2 848 - 914 IPR003598-2
domain Immunoglobulin subtype 2 1055 - 1122 IPR003598-3
domain Immunoglobulin subtype 54 - 150 IPR003599-1
domain Immunoglobulin subtype 258 - 337 IPR003599-2
domain Immunoglobulin subtype 347 - 430 IPR003599-3
domain Immunoglobulin subtype 440 - 526 IPR003599-4
domain Immunoglobulin subtype 546 - 631 IPR003599-5
domain Immunoglobulin subtype 842 - 925 IPR003599-6
domain Immunoglobulin subtype 1049 - 1133 IPR003599-7
domain Fibronectin type III 634 - 732 IPR003961-1
domain Fibronectin type III 732 - 829 IPR003961-2
domain Fibronectin type III 928 - 1025 IPR003961-3
domain Immunoglobulin-like domain 340 - 435 IPR007110-1
domain Immunoglobulin-like domain 438 - 504 IPR007110-2
domain Immunoglobulin-like domain 534 - 624 IPR007110-3
domain Immunoglobulin-like domain 833 - 921 IPR007110-4
domain Immunoglobulin-like domain 1043 - 1131 IPR007110-5
domain Immunoglobulin I-set 50 - 148 IPR013098-1
domain Immunoglobulin I-set 253 - 328 IPR013098-2
domain Immunoglobulin I-set 343 - 418 IPR013098-3
domain Immunoglobulin I-set 436 - 506 IPR013098-4
domain Immunoglobulin I-set 547 - 630 IPR013098-5
domain Immunoglobulin I-set 847 - 924 IPR013098-6
domain Immunoglobulin I-set 1043 - 1132 IPR013098-7
domain MyBP-C, tri-helix bundle domain 208 - 241 IPR040849

Functions

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

2 GO annotations of cellular component

Name Definition
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
myosin filament A supramolecular fiber containing myosin heavy chains, plus associated light chains and other proteins, in which the myosin heavy chains are arranged into a filament.

2 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
structural constituent of cytoskeleton The action of a molecule that contributes to the structural integrity of a cytoskeletal structure.

2 GO annotations of biological process

Name Definition
cell adhesion The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules.
muscle contraction A process in which force is generated within muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q14324 MYBPC2 Myosin-binding protein C, fast-type Homo sapiens (Human) PR
10 20 30 40 50 60
MPEAKPAAKK ASKGKDAPKE APAKQTPEEP PKEAPPEDQS PTAEEPTGIF LKKPDSVSVE
70 80 90 100 110 120
TGKDAVILAK VNGKELPGKP TIKWFKGKWQ ELGSKSGARF IFKESHDSTS NVYTVELHIG
130 140 150 160 170 180
KVVLGDRGDY RLEIKAKDVC DSCSFNVDVE APRQDSSGQS LESFKRSGDG KSEDAGELDF
190 200 210 220 230 240
SGLLKKREVV EEEKKKKKDD DDLGIPPEIW ELLKGAKKSE YEKIAFQYGI TDLRGMLKRL
250 260 270 280 290 300
KKAKVEVKKS AAFTKKLDPA YQVDRGNKIK LVVEISDPDL PLKWFKNGQE IKPSSKYVFE
310 320 330 340 350 360
NVGKKRILTI NKCTLADDAA YEVAVQDEKC FTELFVKEPP VLIVTPLEDQ QVFVGDRVEM
370 380 390 400 410 420
SVEVSEEGAQ VMWMKDGVEM TREDSYKARY RFKKDGKRHI LIYSDVAQED GGRYQVITNG
430 440 450 460 470 480
GQCEAELIVE EKQLEVLQDI ADLTVKAAEQ AVFKCEVSDE KVTGKWYKNG VEVRPSKRIT
490 500 510 520 530 540
ISHVGRFHKL VIDDVRPEDE GDYTFVPDGY ALSLSAKLNF LEIKVEYVPK QEPPKIHLDC
550 560 570 580 590 600
SGKTSDNSIV VVAGNKLRLD VAITGEPPPT ATWLRGDEVF TATEGRTHIE QRPDCSSFVI
610 620 630 640 650 660
ESAERSDEGR YTIKVTNPVG EDVASIFLRV VDVPDPPEAV RVTSVGEDWA ILVWEPPKYD
670 680 690 700 710 720
GGQPVTGYLM ERKKKGSQRW MKINFEVFTD TTYESTKMIE GVLYEMRVFA VNAIGVSQPS
730 740 750 760 770 780
MNTKPFMPIA PTSAPQHLTV EDVTDTTTTL KWRPPDRIGA GGIDGYLVEY CLEGSEEWVP
790 800 810 820 830 840
ANKEPVERCG FTVKDLPTGA RILFRVVGVN IAGRSEPATL LQPVTIREIV EQPKIRLPRH
850 860 870 880 890 900
LRQTYIRKVG EALNLVIPFQ GKPRPQVVWT KGGAPLDTSR VNVRTSDFDT VFFVRQAARS
910 920 930 940 950 960
DSGEYELSVQ IENMKDTATI RIRVVEKAGP AENVMVKEVW GTNALVEWQP PKDDGNSEIT
970 980 990 1000 1010 1020
GYFVQKADKK TMEWFNVYEH NRHTSCTVSD LIVGNEYYFR IFSENICGLS DSPGVSKNTA
1030 1040 1050 1060 1070 1080
RILKTGITLK PLEYKEHDFR TAPKFLTPLM DRVVVAGYTA ALNCAVRGHP KPKVVWMKNK
1090 1100 1110 1120 1130
MEIHEDPKFL ITNYQGILTL NIRRPSPFDA GTYSCRAFNE LGEALAECKL DVRVPQ