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 Q8BT60

Entry ID Method Resolution Chain Position Source
AF-Q8BT60-F1 Predicted AlphaFoldDB

19 variants for Q8BT60

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388670282 63 F>S No EVA
rs3393743624 65 I>T No EVA
rs3388674684 121 K>I No EVA
rs3388675783 128 I>F No EVA
rs3388655202 165 F>L No EVA
rs3388669150 181 E>K No EVA
rs3393964424 188 N>Y No EVA
rs215787527 190 M>I No EVA
rs27697673 242 S>N No EVA
rs3388678007 258 K>R No EVA
rs3388673365 260 S>G No EVA
rs3388668751 363 M>K No EVA
rs244456010 367 P>S No EVA
rs3388655145 442 V>F No EVA
rs13469673 451 I>V No EVA
rs3388678593 481 V>M No EVA
rs3388674690 487 V>F No EVA
rs254246182 523 K>R No EVA
rs234676041 532 V>A No EVA

No associated diseases with Q8BT60

5 regional properties for Q8BT60

Type Name Position InterPro Accession
domain C2 domain 1 - 115 IPR000008-1
domain C2 domain 124 - 247 IPR000008-2
domain von Willebrand factor, type A 289 - 495 IPR002035
domain Copine, C-terminal 263 - 524 IPR010734
domain Copine, C2B domain 139 - 251 IPR037768

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
  • Cytoplasm
  • Cell membrane
  • Cell junction
  • Cell junction, focal adhesion
  • Associates to the membrane in a calcium-dependent manner
  • Translocates to the cell membrane and the nucleus in a calcium- or growth factor heregulin-dependent manner
  • Colocalizes with the tyrosine phosphorylated ERBB2 form at cell membrane and focal adhesions in a calcium- or growth factor heregulin-dependent manner
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

9 GO annotations of cellular component

Name Definition
cell junction A cellular component that forms a specialized region of connection between two or more cells, or between a cell and the extracellular matrix, or between two membrane-bound components of a cell, such as flagella.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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).
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
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.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

5 GO annotations of molecular function

Name Definition
calcium-dependent phospholipid binding Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester, in the presence of calcium.
calcium-dependent protein binding Binding to a protein or protein complex in the presence of calcium.
metal ion binding Binding to a metal ion.
protein serine/threonine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
receptor tyrosine kinase binding Binding to a receptor that possesses protein tyrosine kinase activity.

4 GO annotations of biological process

Name Definition
cellular response to calcium ion Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a calcium ion stimulus.
cellular response to growth factor stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a growth factor stimulus.
ERBB2 signaling pathway The series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor ERBB2 on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription. ERBB2 receptors are themselves unable to bind to ligands, but act as a signal-amplifying tyrosine kinase within a heterodimeric pair.
positive regulation of cell migration Any process that activates or increases the frequency, rate or extent of cell migration.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q08DB4 CPNE1 Copine-1 Bos taurus (Bovine) PR
Q99829 CPNE1 Copine-1 Homo sapiens (Human) PR
O75131 CPNE3 Copine-3 Homo sapiens (Human) PR
Q8C166 Cpne1 Copine-1 Mus musculus (Mouse) PR
D4A1R8 Cpne1 Copine-1 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MAAQCVTKVE LNVSCNNLLD ADVTSKSDPL CVLFLNTSGH QWYEVERTER IKNSLNPKFS
70 80 90 100 110 120
KTFVIDYYFE VVQKLKFGIY DIDNKTIELS DDDFLGECEV TLGQIVSSKK LTRPLVLKNG
130 140 150 160 170 180
KPAGKGSITI SAEEIKDNRV VLFEMEARKL DNKDLFGKSD PYLEFHKQTS DGHWLMVHRT
190 200 210 220 230 240
EVIKNNLNPM WKPFKISLNS LCYGDMDKTI KVECYDYDND GSHDLIGTFQ TTMTKLKEAS
250 260 270 280 290 300
RSSPVEYECI NEKKRQKKKS YKNSGVISVK HCEITVECTF LDYIMGGCQL NFTVGVDFTG
310 320 330 340 350 360
SNGDPSSPDS LHYISPNGVN EYLTAIWSVG LVIQDYDADK MFPAFGFGAQ VPPQWQVSHE
370 380 390 400 410 420
FPMNFNPSNP YCNGIQGIVE AYRTCLPQIR LYGPTNFSPI INHVARFAAA ATQQQTASQY
430 440 450 460 470 480
FVLLIITDGV ITDLDETRQA IVNAAKLPMS IIIVGVGGAD FSAMEFLDGD GGSLRAPSGE
490 500 510 520 530
VAIRDIVQFV PFRQFQNAPK EALAQCVLAE IPQQVVGYFN TYKLLPPKNP AVK