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

5 structures for Q5EBH1

Entry ID Method Resolution Chain Position Source
1RFH NMR - A 108-166 PDB
2FNF NMR - X 95-166 PDB
2YMY X-ray 169 A A/B 370-413 PDB
3DDC X-ray 180 A B 200-357 PDB
AF-Q5EBH1-F1 Predicted AlphaFoldDB

18 variants for Q5EBH1

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388494541 123 L>Q No EVA
rs3388497918 173 L>P No EVA
rs237284655 175 R>T No EVA
rs3388498834 183 T>I No EVA
rs3388497412 211 D>V No EVA
rs3390645979 223 M>T No EVA
rs3388498188 259 A>V No EVA
rs3388497959 265 P>L No EVA
rs3388498807 280 D>E No EVA
rs3388497776 303 K>M No EVA
rs3388494579 347 T>I No EVA
rs3388498278 365 D>G No EVA
rs3388496547 383 E>Q No EVA
rs3388497759 384 Q>H No EVA
rs3388495650 388 H>R No EVA
rs3388498836 389 Q>* No EVA
rs3388498618 390 L>M No EVA
rs3388497713 393 K>M No EVA

No associated diseases with Q5EBH1

No regional properties for Q5EBH1

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q5EBH1

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cytoplasm, cytoskeleton
  • Isoform 2 is mainly located in the perinuclear region of unstimulated primary T-cells
  • Upon stimulation translocates to the leading edge and colocalizes with ITGAL/LFA-1 in the peripheral zone of the immunological synapse
  • Isoform 2 is localized to growing microtubules in vascular endothelial cells and is dissociated from microtubules by activated RAP1A (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

3 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.
metal ion binding Binding to a metal ion.
small GTPase binding Binding to a small monomeric GTPase.

7 GO annotations of biological process

Name Definition
apoptotic process A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
lymphocyte proliferation The expansion of a lymphocyte population by cell division.
negative regulation of lymphocyte proliferation Any process that stops, prevents or reduces the rate or extent of lymphocyte proliferation.
positive regulation of protein ubiquitination Any process that activates or increases the frequency, rate or extent of the addition of ubiquitin groups to a protein.
regulation of apoptotic process Any process that modulates the occurrence or rate of cell death by apoptotic process.
regulation of protein localization to nucleus Any process that modulates the frequency, rate or extent of protein localization to nucleus.
signal transduction The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q6ZTQ3 RASSF6 Ras association domain-containing protein 6 Homo sapiens (Human) PR
Q9NS23 RASSF1 Ras association domain-containing protein 1 Homo sapiens (Human) PR
Q8WWW0 RASSF5 Ras association domain-containing protein 5 Homo sapiens (Human) PR
Q80UQ2 Rassf6 Ras association domain-containing protein 6 Mus musculus (Mouse) PR
Q99MK9 Rassf1 Ras association domain-containing protein 1 Mus musculus (Mouse) PR
Q4QR82 Rassf6 Ras association domain-containing protein 6 Rattus norvegicus (Rat) PR
O35141 Rassf5 Ras association domain-containing protein 5 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MASPAIGQRP YPLLLDPEPP RYLQSLGGTE PPPPARPRRC IPTALIPAAG ASEDRGGRRS
70 80 90 100 110 120
GRRDPEPTPR DCRHARPVRP GLQPRLRLRP GSHRPRDVRS IFEQPQDPRV LAERGEGHRF
130 140 150 160 170 180
VELALRGGPG WCDLCGREVL RQALRCANCK FTCHSECRSL IQLDCRQKGG PALDRRSPES
190 200 210 220 230 240
TLTPTLNQNV CKAVEETQHP PTIQEIKQKI DSYNSREKHC LGMKLSEDGT YTGFIKVHLK
250 260 270 280 290 300
LRRPVTVPAG IRPQSIYDAI KEVNPAATTD KRTSFYLPLD AIKQLHISST TTVSEVIQGL
310 320 330 340 350 360
LKKFMVVDNP QKFALFKRIH KDGQVLFQKL SIADYPLYLR LLAGPDTDVL SFVLKENETG
370 380 390 400 410
EVEWDAFSIP ELQNFLTILE KEEQDKIHQL QKKYNKFRQK LEEALRESQG KPG