Protein detail

GRDN

Girdin (Akt phosphorylation enhancer) (APE) (Coiled-coil domain-containing protein 88A) (G alpha-interacting vesicle-associated protein) (GIV) (Girders of actin filament) (Hook-related protein 1) (HkRP1)

Entry name
GRDN
UniProt ID
EVMP confidence score
0.38
Supporting publications (n)
3
Transmembrane count
Protein classification
Disease related genesHuman disease related genesPredicted intracellular proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information11
Protein Names
Girdin (Akt phosphorylation enhancer) (APE) (Coiled-coil domain-containing protein 88A) (G alpha-interacting vesicle-associated protein) (GIV) (Girders of actin filament) (Hook-related protein 1) (HkRP1)
Protein Class (3)
Disease related genesHuman disease related genesPredicted intracellular proteins
Protein Function (3)
  • Human disease related genes:Nervous system diseases:Neurodegenerative diseases
  • Disease related genes
  • Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym (6)
APEFLJ10392GIVGRDNHkRP1KIAA1212
Gene Description
Coiled-coil domain containing 88A
Chromosome
2
Position
55287842-55419895
Supporting publications (n)
3
EVMP confidence score
0.38
Fluorescence & Localization4
Tissue Specificbone marrowBrain Regional Specificchoroid plexusCell SpecificChoroid plexus epithelial cellsSingle-Nuclei Brain Specificcentral nervous system macrophage
Function & Pathway6
Relations & Evidence26

Enzyme-Mediated Modification (14)

14 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
CCDC88AAKT1P31749S1,417phosphorylationSIGNORProtMapperHPRDdbPTMKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperdbPTM:16139227HPRD:16139227HPRD:20068231KEA:16139227SIGNOR:16139227ProtMapper:16139227
CCDC88AAKT1P31749S1,416phosphorylationMIMPHPRD_MIMPPhosphoSite_MIMP
CCDC88APRKCQQ04759S1,690phosphorylationREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapperProtMapper:26378251
CCDC88ASRCP12931Y1,799phosphorylationSparser_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapperProtMapper:25707853
CCDC88ASRCP12931Y1,765phosphorylationPhosphoSiteSparser_ProtMapperProtMapperProtMapper:25707853
CCDC88AMAPK1P28482S233phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
CCDC88AMAPK1P28482S237phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
CCDC88ACDK5Q00535S1,675phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
CCDC88AEGFRP00533Y1,799phosphorylationPhosphoSiteSparser_ProtMapperProtMapperProtMapper:25707853
CCDC88AEGFRP00533Y1,765phosphorylationPhosphoSiteSparser_ProtMapperProtMapperProtMapper:25707853
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Ligand-Receptor Signaling (7)

7 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo
plasma_membraneplasma_membraneUniProt_locationNoNoNoNoNo
plasma_membraneplasma_membraneOmniPathNoNoNoNoNo

Regulatory Interaction Network (4)

4 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
AKT1P31749GRDNQ3V6T2YesNoNoPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointSIGNORProtMapperHPRDHINTPhosphoSiteKEAdbPTMHPRD_KEAInnateDBSIGNOR_ProtMapperLit-BM-17HPRD-phosPhosphoSite_ProtMapperLit-BM-17:16139227PhosphoSite:25707853PhosphoSite:24662825ProtMapper:16139227InnateDB:16139227HPRD-phos:16139227dbPTM:16139227HINT:15753085HPRD-phos:20068231PhosphoSite:25732845PhosphoSite:30935690HINT:16139227KEA:16139227SIGNOR:16139227PhosphoSite:16139227HPRD:16139227Lit-BM-17:15753085ProtMapper:20068231PhosphoSite:21954290
KPCTQ04759GRDNQ3V6T2YesNoNoiPTMnetProtMapperREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapperPhosphoSite:27621449ProtMapper:26378251PhosphoSite:23509302PhosphoSite:31363053
EGFRP00533GRDNQ3V6T2YesNoNoSparser_ProtMapperProtMapperBioGRIDREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapperBioGRID:15882442PhosphoSite:32307399ProtMapper:25707853
CDK5Q00535GRDNQ3V6T2YesNoNoiPTMnetPhosphoSitePhosphoSite_ProtMapperProtMapperPhosphoSite:27864364PhosphoSite:26286990

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationUltrafiltration / Tangential Flow FiltrationData-Dependent Acquisition LC-MS/MS132795414
Sequence, Structure & Domains16

Sequences

Length
1,871
Mass
216,042
Sequence
MENEIFTPLLEQFMTSPLVTWVKTFGPLAAGNGTNLDEYVALVDGVFLNQVMLQINPKLESQRVNKKVNNDASLRMHNLSILVRQIKFYYQETLQQLIMMSLPNVLIIGKNPFSEQGTEEVKKLLLLLLGCAVQCQKKEEFIERIQGLDFDTKAAVAAHIQEVTHNQENVFDLQWMEVTDMSQEDIEPLLKNMALHLKRLIDERDEHSETIIELSEERDGLHFLPHASSSAQSPCGSPGMKRTESRQHLSVELADAKAKIRRLRQELEEKTEQLLDCKQELEQMEIELKRLQQENMNLLSDARSARMYRDELDALREKAVRVDKLESEVSRYKERLHDIEFYKARVEELKEDNQVLLETKTMLEDQLEGTRARSDKLHELEKENLQLKAKLHDMEMERDMDRKKIEELMEENMTLEMAQKQSMDESLHLGWELEQISRTSELSEAPQKSLGHEVNELTSSRLLKLEMENQSLTKTVEELRTTVDSVEGNASKILKMEKENQRLSKKVEILENEIVQEKQSLQNCQNLSKDLMKEKAQLEKTIETLRENSERQIKILEQENEHLNQTVSSLRQRSQISAEARVKDIEKENKILHESIKETSSKLSKIEFEKRQIKKELEHYKEKGERAEELENELHHLEKENELLQKKITNLKITCEKIEALEQENSELERENRKLKKTLDSFKNLTFQLESLEKENSQLDEENLELRRNVESLKCASMKMAQLQLENKELESEKEQLKKGLELLKASFKKTERLEVSYQGLDIENQRLQKTLENSNKKIQQLESELQDLEMENQTLQKNLEELKISSKRLEQLEKENKSLEQETSQLEKDKKQLEKENKRLRQQAEIKDTTLEENNVKIGNLEKENKTLSKEIGIYKESCVRLKELEKENKELVKRATIDIKTLVTLREDLVSEKLKTQQMNNDLEKLTHELEKIGLNKERLLHDEQSTDDSRYKLLESKLESTLKKSLEIKEEKIAALEARLEESTNYNQQLRQELKTVKKNYEALKQRQDEERMVQSSPPISGEDNKWERESQETTRELLKVKDRLIEVERNNATLQAEKQALKTQLKQLETQNNNLQAQILALQRQTVSLQEQNTTLQTQNAKLQVENSTLNSQSTSLMNQNAQLLIQQSSLENENESVIKEREDLKSLYDSLIKDHEKLELLHERQASEYESLISKHGTLKSAHKNLEVEHRDLEDRYNQLLKQKGQLEDLEKMLKVEQEKMLLENKNHETVAAEYKKLCGENDRLNHTYSQLLKETEVLQTDHKNLKSLLNNSKLEQTRLEAEFSKLKEQYQQLDITSTKLNNQCELLSQLKGNLEEENRHLLDQIQTLMLQNRTLLEQNMESKDLFHVEQRQYIDKLNELRRQKEKLEEKIMDQYKFYDPSPPRRRGNWITLKMRKLIKSKKDINRERQKSLTLTPTRSDSSEGFLQLPHQDSQDSSSVGSNSLEDGQTLGTKKSSMVALKRLPFLRNRPKDKDKMKACYRRSMSMNDLVQSMVLAGQWTGSTENLEVPDDISTGKRRKELGAMAFSTTAINFSTVNSSAGFRSKQLVNNKDTTSFEDISPQGVSDDSSTGSRVHASRPASLDSGRTSTSNSNNNASLHEVKAGAVNNQSRPQSHSSGEFSLLHDHEAWSSSGSSPIQYLKRQTRSSPVLQHKISETLESRHHKIKTGSPGSEVVTLQQFLEESNKLTSVQIKSSSQENLLDEVMKSLSVSSDFLGKDKPVSCGLARSVSGKTPGDFYDRRTTKPEFLRPGPRKTEDTYFISSAGKPTPGTQGKIKLVKESSLSRQSKDSNPYATLPRASSVISTAEGTTRRTSIHDFLTKDSRLPISVDSPPAAADSNTTAASNVDKVQESRNSKSRSREQQSS
Alternative Products
Event=Alternative splicing; Named isoforms=5; Name=1; IsoId=Q3V6T2-1; Sequence=Displayed; Name=2; IsoId=Q3V6T2-2; Sequence=VSP_052409; Name=3; IsoId=Q3V6T2-3; Sequence=VSP_040129; Name=4; IsoId=Q3V6T2-4; Sequence=VSP_040129, VSP_052409; Name=5; IsoId=Q3V6T2-5; Sequence=VSP_040129, VSP_044943
Alternative Sequence
952; Missing (in isoform 3, isoform 4 and isoform 5); 1463..1491; MVALKRLPFLRNRPKDKDKMKACYRRSMS -> T (in isoform 2 and isoform 4); 1733..1806; Missing (in isoform 5)

3D Structural Models

Helix
1683..1690
Beta Strand
1679..1682
3D Structure
X-ray crystallography (1)

Domain & Motif Annotations

Compositional Bias
1026..1035; Basic and acidic residues; 1407..1416; Basic and acidic residues; 1417..1430; Polar residues; 1445..1459; Polar residues; 1559..1578; Polar residues; 1743..1763; Basic and acidic residues; 1787..1799; Polar residues; 1807..1818; Polar residues; 1820..1830; Basic and acidic residues; 1838..1851; Low complexity; 1854..1871; Basic and acidic residues
Motif
1672..1702; GBA
Coiled Coil
196..425; 458..1385
Domain (CC)
The GBA (G-alpha binding and activating) motif mediates binding to the alpha subunits of guanine nucleotide-binding proteins (G proteins).; DOMAIN: In the presence of tyrosine-autophosphorylated growth factor receptors, the C-terminus folds into an SH2-like region which promotes the stable recruitment of CCDC88A to the growth factor receptors. The SH2-like region is phosphorylated by the growth factor receptors prior to completion of folding.
Domain (FT)
12..132; Calponin-homology (CH)
Region
816..842; Disordered; 1010..1035; Disordered; 1390..1408; Phosphoinositide-binding; 1407..1459; Disordered; 1559..1601; Disordered; 1713..1823; SH2-like; required for interaction with growth factor receptors; 1736..1871; Disordered
Protein Families
CCDC88 family
Sequence Similarities
Belongs to the CCDC88 family.
Clinical Relevance2
Disease Involvement (3)
EpilepsyIntellectual disabilityNeurodegeneration
Supporting Publications3
PMIDTitleAbstract
32111925Rigorous characterization of urinary extracellular vesicles (uEVs) in the low centrifugation pellet - a neglected source for uEVs.No abstract available
32795414Extracellular Vesicle and Particle Biomarkers Define Multiple Human Cancers.Among traditional exosome markers, CD9, HSPA8, ALIX, and HSP90AB1 represent pan-EVP markers, while ACTB, MSN, and RAP1B are novel pan-EVP markers.
41216884Extracellular Vesicles From Multiple Sclerosis White Matter Exhibit Synaptic, Mitochondrial, Complement and Ageing-Related Pathway Dysregulation.No abstract available