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 Q8R001

Entry ID Method Resolution Chain Position Source
AF-Q8R001-F1 Predicted AlphaFoldDB

17 variants for Q8R001

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389401130 58 S>C No EVA
rs3389483085 73 N>I No EVA
rs3389486098 127 M>I No EVA
rs3389490422 134 P>R No EVA
rs3389505911 145 D>E No EVA
rs3389438440 147 L>M No EVA
rs3389401082 159 A>D No EVA
rs3389487360 185 E>G No EVA
rs3389498182 193 K>N No EVA
rs3389448773 198 N>H No EVA
rs3389493740 208 S>N No EVA
rs3389487298 226 A>V No EVA
rs3389401104 254 K>* No EVA
rs3389469624 273 E>A No EVA
rs3389401109 291 R>* No EVA
rs249788518 301 E>D No EVA
rs3389502325 318 Q>L No EVA

No associated diseases with Q8R001

2 regional properties for Q8R001

Type Name Position InterPro Accession
domain Calponin homology domain 56 - 158 IPR001715
domain EB1, C-terminal 235 - 305 IPR004953

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cytoplasm, cytoskeleton
  • Associated with the microtubule network
  • Accumulates at the plus end of microtubules (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
cytoplasmic microtubule Any microtubule in the cytoplasm of a cell.
focal adhesion A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ).
microtubule cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins.
microtubule organizing center An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides.
microtubule plus-end The growing (plus) end of a microtubule. In vitro, microtubules polymerize more quickly at the plus end than at the minus end. In vivo, microtubule growth occurs only at the plus end, and the plus end switches between periods of growth and shortening, a behavior known as dynamic instability.
spindle midzone The area in the center of the spindle where the spindle microtubules from opposite poles overlap.

4 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.
microtubule binding Binding to a microtubule, a filament composed of tubulin monomers.
microtubule plus-end binding Binding to the plus end of a microtubule.
protein kinase binding Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.

8 GO annotations of biological process

Name Definition
cell division The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
positive regulation of ARF protein signal transduction Any process that activates or increases the frequency, rate or extent of ARF protein signal transduction.
positive regulation of focal adhesion disassembly Any process that activates or increases the frequency, rate or extent of disaggregation of a focal adhesion into its constituent components.
positive regulation of GTPase activity Any process that activates or increases the activity of a GTPase.
positive regulation of keratinocyte migration Any process that activates or increases the frequency, rate or extent of keratinocyte migration.
protein localization to microtubule plus-end A process in which a protein is transported to, or maintained in, a location at a microtubule plus-end.
regulation of microtubule polymerization or depolymerization Any process that modulates the frequency, rate or extent of microtubule polymerization or depolymerization by the addition or removal of tubulin heterodimers from a microtubule.
spindle assembly The aggregation, arrangement and bonding together of a set of components to form the spindle, the array of microtubules and associated molecules that serves to move duplicated chromosomes apart.

12 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3ZBD9 MAPRE1 Microtubule-associated protein RP/EB family member 1 Bos taurus (Bovine) SS
Q5ZLC7 MAPRE1 Microtubule-associated protein RP/EB family member 1 Gallus gallus (Chicken) SS
Q15691 MAPRE1 Microtubule-associated protein RP/EB family member 1 Homo sapiens (Human) EV
Q9UPY8 MAPRE3 Microtubule-associated protein RP/EB family member 3 Homo sapiens (Human) SS
Q15555 MAPRE2 Microtubule-associated protein RP/EB family member 2 Homo sapiens (Human) PR
Q61166 Mapre1 Microtubule-associated protein RP/EB family member 1 Mus musculus (Mouse) SS
Q6PER3 Mapre3 Microtubule-associated protein RP/EB family member 3 Mus musculus (Mouse) SS
Q5XIT1 Mapre3 Microtubule-associated protein RP/EB family member 3 Rattus norvegicus (Rat) SS
Q66HR2 Mapre1 Microtubule-associated protein RP/EB family member 1 Rattus norvegicus (Rat) SS
Q9FJJ5 EB1B Microtubule-associated protein RP/EB family member 1B Arabidopsis thaliana (Mouse-ear cress) EV
Q7XJ60 EB1A Microtubule-associated protein RP/EB family member 1A Arabidopsis thaliana (Mouse-ear cress) SS
Q6P848 mapre1 Microtubule-associated protein RP/EB family member 1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) SS
10 20 30 40 50 60
MPGPTQTLSP NGENNNDIIQ DNGTIIPFRK HTVRGERSYS WGMAVNVYST SITQETMSRH
70 80 90 100 110 120
DIIAWVNDIV SLNYTKVEQL CSGAAYCQFM DMLFPGCISL KKVKFQAKLE HEYIHNFKLL
130 140 150 160 170 180
QASFKRMNVD KVIPVEKLVK GRFQDNLDFI QWFKKFYDAN YDGKEYDPVE ARQGQDAIPP
190 200 210 220 230 240
PDPGEQIFNL PKKSHHANSP TAGAAKSSPA SKPGSTPSRP SSAKRASSSG SASRSDKDLE
250 260 270 280 290 300
TQVIQLNEQV HSLKLALEGV EKERDFYFGK LREIELLCQE HGQENDDLVQ RLMEVLYASD
310 320
EQEGQTEEPE AEEQAHDQQP QQQEEY