Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website soon. Please explore and share your feedback. Take me to the new website.

UniProtKB - Q3V6T2 (GRDN_HUMAN)

Entry version 139 (23 Feb 2022)
Sequence version 2 (15 May 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Girdin

Gene

CCDC88A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Bifunctional modulator of guanine nucleotide-binding proteins (G proteins) (PubMed:19211784, PubMed:27621449).

Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits (PubMed:19211784, PubMed:21954290, PubMed:23509302, PubMed:25187647).

Also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS (PubMed:27621449).

Essential for cell migration (PubMed:20462955, PubMed:16139227, PubMed:19211784, PubMed:21954290).

Interacts in complex with G(i) alpha subunits with the EGFR receptor, retaining EGFR at the cell membrane following ligand stimulation and promoting EGFR signaling which triggers cell migration (PubMed:20462955).

Binding to Gi-alpha subunits displaces the beta and gamma subunits from the heterotrimeric G-protein complex which enhances phosphoinositide 3-kinase (PI3K)-dependent phosphorylation and kinase activity of AKT1/PKB (PubMed:19211784).

Phosphorylation of AKT1/PKB induces the phosphorylation of downstream effectors GSK3 and FOXO1/FKHR, and regulates DNA replication and cell proliferation (By similarity).

Binds in its tyrosine-phosphorylated form to the phosphatidylinositol 3-kinase (PI3K) regulatory subunit PIK3R1 which enables recruitment of PIK3R1 to the EGFR receptor, enhancing PI3K activity and cell migration (PubMed:21954290).

Plays a role as a key modulator of the AKT-mTOR signaling pathway, controlling the tempo of the process of newborn neuron integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity).

Inhibition of G(s) subunit alpha GNAS leads to reduced cellular levels of cAMP and suppression of cell proliferation (PubMed:27621449).

Essential for the integrity of the actin cytoskeleton (PubMed:16139227, PubMed:19211784).

Required for formation of actin stress fibers and lamellipodia (PubMed:15882442).

May be involved in membrane sorting in the early endosome (PubMed:15882442).

Plays a role in ciliogenesis and cilium morphology and positioning and this may partly be through regulation of the localization of scaffolding protein CROCC/Rootletin (PubMed:27623382).

By similarity9 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGuanine-nucleotide releasing factor
Biological processCilium biogenesis/degradation, DNA replication, Neurogenesis

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q3V6T2

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-9696264, RND3 GTPase cycle
R-HSA-9696273, RND1 GTPase cycle

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q3V6T2

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q3V6T2

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Girdin
Alternative name(s):
Akt phosphorylation enhancer
Short name:
APE
Coiled-coil domain-containing protein 88A
G alpha-interacting vesicle-associated protein
Short name:
GIV
Girders of actin filament
Hook-related protein 1
Short name:
HkRP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CCDC88A
Synonyms:APEImported, GRDN, KIAA1212Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:25523, CCDC88A

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		609736, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q3V6T2

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000115355

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

PEHO-like syndrome (PEHOL)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive syndrome characterized by microcephaly and moderately severe hypotonia manifesting at birth, seizures that progress into infantile spasms with hypsarrhythmia, brain atrophy with bilateral polymicrogyria and pachygyria, thin corpus callosum, and mild reduction in cerebellar vermis volume. Patients also display optic atrophy, severe cognitive delay, puffiness of the maxillary region of the face, and edema of the dorsum of the hands and feet.
Related information in OMIM

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1417S → A: Phosphorylation-deficient mutant which disrupts actin organization, cell migration and lamellipodia formation but has no effect on tyrosine phosphorylation. 2 Publications1
Mutagenesisi1417S → D: Phosphomimetic mutant which has no effect on tyrosine phosphorylation. 1 Publication1
Mutagenesisi1675S → A: Phosphorylation-deficient mutant which disrupts binding to GNAI3 and GNAS. 1 Publication1
Mutagenesisi1675S → D: Phosphomimetic mutant which results in slight increase in binding to GNAI3 and GNAS. Increased inhibition of GNAS; when associated with D-1690. 1 Publication1
Mutagenesisi1684Q → A: No effect on guanine nucleotide exchange factor activity. 1 Publication1
Mutagenesisi1686F → A: Abolishes interaction with and activation of GNAI3 and also abolishes recruitment of GNAI3 to EGFR. Reduced EGFR autophosphorylation and SH2 adapter recruitment, reduced localization of EGFR at the cell membrane following ligand stimulation with increased endosomal localization, reduced cell migration and increased cell proliferation. Abolishes enhancement of AKT signaling. Abolishes interaction with GNAS. 4 Publications1
Mutagenesisi1689E → A: Abolishes interaction with GNAI3. 1 Publication1
Mutagenesisi1690S → A: Phosphorylation-deficient mutant which retains the ability to bind GNAI3. 1 Publication1
Mutagenesisi1690S → D: Phosphomimetic mutant which abolishes interaction with GNAI3, inhibits guanine nucleotide exchange factor activity, inhibits cell migration and triggers cell proliferation. Retains ability to bind to GNAS. Increased inhibition of GNAS; when associated with D-1675. 2 Publications1
Mutagenesisi1723K → E: Abolishes binding to phosphorylated EGFR. 1 Publication1
Mutagenesisi1725K → E: Does not affect binding to phosphorylated EGFR. 1 Publication1
Mutagenesisi1746R → K or L: Abolishes binding to phosphorylated EGFR. 1 Publication1
Mutagenesisi1750K → E: Abolishes binding to phosphorylated EGFR. 1 Publication1
Mutagenesisi1765Y → F: Abolishes phosphorylation and leads to reduced AKT phosphorylation, impaired formation of actin stress fibers and impaired cell migration abolishes interaction with PIK3R1 and activation of PI3K, reduces phosphorylation of Ser-1417 but does not affect interaction with or activation of GNAI3; when associated with F-1799. 1 Publication1
Mutagenesisi1766F → T: Increases binding to phosphorylated EGFR. 1 Publication1
Mutagenesisi1778Q → E: Abolishes binding to phosphorylated EGFR. 1 Publication1
Mutagenesisi1799Y → F: Abolishes phosphorylation and leads to reduced AKT phosphorylation, impaired formation of actin stress fibers and impaired cell migration, abolishes interaction with PIK3R1 and activation of PI3K activity, reduces phosphorylation of Ser-1417 but does not affect interaction with or activation of GNAI3; when associated with F-1765. 1 Publication1

Keywords - Diseasei

Epilepsy, Mental retardation, Neurodegeneration

Organism-specific databases

DisGeNET

More...DisGeNETi		55704

MalaCards human disease database

More...MalaCardsi		CCDC88A
MIMi617507, phenotype

Open Targets

More...OpenTargetsi		ENSG00000115355

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		99807, PEHO-like syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA162381751

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q3V6T2, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CCDC88A

Domain mapping of disease mutations (DMDM)

More...DMDMi		147644956

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002874291 – 1871GirdinAdd BLAST1871

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei233PhosphoserineCombined sources1
Modified residuei237PhosphoserineBy similarity1
Modified residuei449PhosphoserineCombined sources1
Modified residuei1020PhosphoserineCombined sources1
Modified residuei1387PhosphoserineCombined sources1
Modified residuei1417Phosphoserine; by PKB/AKT1Combined sources1 Publication1
Modified residuei1421PhosphothreonineCombined sources1
Modified residuei1673PhosphothreonineCombined sources1
Modified residuei1675Phosphoserine1 Publication1
Modified residuei1690Phosphoserine; by PKC/PRKCQ2 Publications1
Modified residuei1717PhosphoserineCombined sources1
Modified residuei1765Phosphotyrosine1 Publication1
Modified residuei1799Phosphotyrosine1 Publication1
Modified residuei1820PhosphoserineCombined sources1
Modified residuei1837PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation is induced by epidermal growth factor (EGF) in a phosphoinositide 3-kinase (PI3K)-dependent manner (PubMed:16139227). Phosphorylation by AKT1/PKB is necessary for delocalization from the cell membrane and for cell migration (PubMed:16139227). Phosphorylated on tyrosine residues which promotes binding to phosphatidylinositol 3-kinase (PI3K) regulatory subunit PIK3R1/p85a and enhances PI3K activity (PubMed:21954290). Tyrosine-phosphorylated by both receptor and non-receptor tyrosine kinases in vitro (PubMed:21954290). Tyrosine phosphorylation is required for AKT1-dependent phosphorylation of Ser-1417 (PubMed:21954290). Phosphorylation at Ser-1690 by PRKCQ disrupts interaction with GNAI3 and inhibits guanine nucleotide exchange factor activity (PubMed:23509302).3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q3V6T2

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q3V6T2

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q3V6T2

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q3V6T2

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q3V6T2

PeptideAtlas

More...PeptideAtlasi		Q3V6T2

PRoteomics IDEntifications database

More...PRIDEi		Q3V6T2

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		61886 [Q3V6T2-1]
61887 [Q3V6T2-2]
61888 [Q3V6T2-3]
61889 [Q3V6T2-4]
7248

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q3V6T2

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q3V6T2

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed ubiquitously.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000115355, Expressed in testis and 222 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q3V6T2, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q3V6T2, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000115355, Tissue enhanced (brain)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:16139227).

Interacts (via GBA motif) with guanine nucleotide-binding protein G(i) alpha subunits GNAI1, GNAI2 and GNAI3 (PubMed:19211784, PubMed:21954290, PubMed:23509302, PubMed:27621449, PubMed:31363053).

Also interacts (via GNA motif) with guanine nucleotide-binding protein G(s) alpha subunit GNAS (PubMed:27621449). Interaction with G(i) alpha subunits occurs before interaction with GNAS and is regulated by phosphorylation; phosphorylation at Ser-1675 enhances binding to G(i) alpha subunits while phosphorylation at Ser-1690 abolishes G(i) alpha subunit binding, promoting binding to GNAS (PubMed:27621449).

Interacts (via C-terminal SH2-like region) with growth factor receptors EGFR, INSR and KDR/VEGFR2 (via their autophosphorylated cytoplasmic tails) (PubMed:25187647).

Forms a complex with EGFR and GNAI3 which leads to enhanced EGFR signaling and triggering of cell migration; ligand stimulation is required for recruitment of GNAI3 to the complex (PubMed:20462955, PubMed:25187647).

Interacts (tyrosine-phosphorylated form) with phosphatidylinositol 3-kinase (PI3K) regulatory subunit PIK3R1/p85a (via SH2 domains); the interaction enables recruitment of PIK3R1 to the EGFR receptor, enhancing PI3K activity and cell migration (PubMed:21954290).

Interacts with serine/threonine-protein kinase PRKCQ; the interaction leads to phosphorylation of CCDC88A and inhibition of its guanine nucleotide exchange factor activity (PubMed:23509302).

Interacts (via C-terminus) with DISC1; the interaction is direct (By similarity).

Interacts with AKT proteins; the interaction is inhibited in the presence of DISC1 (By similarity).

Interacts with AKT1/PKB (via C-terminus) (PubMed:16139227). The non-phosphorylated form interacts with phosphatidylinositol 4-phosphate [PI4P] and weakly with phosphatidylinositol 3-phosphate [PI3P] (PubMed:16139227).

Interacts with microtubules (By similarity).

Interacts with actin (PubMed:16139227).

By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		120829, 162 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q3V6T2

Database of interacting proteins

More...DIPi		DIP-50784N

Protein interaction database and analysis system

More...IntActi		Q3V6T2, 75 interactors

Molecular INTeraction database

More...MINTi		Q3V6T2

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000338728

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q3V6T2, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11871
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q3V6T2

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini12 – 132Calponin-homology (CH)PROSITE-ProRule annotationAdd BLAST121

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni816 – 842DisorderedSequence analysisAdd BLAST27
Regioni1010 – 1035DisorderedSequence analysisAdd BLAST26
Regioni1390 – 1408Phosphoinositide-binding1 PublicationAdd BLAST19
Regioni1407 – 1459DisorderedSequence analysisAdd BLAST53
Regioni1559 – 1601DisorderedSequence analysisAdd BLAST43
Regioni1713 – 1823SH2-like; required for interaction with growth factor receptors1 PublicationAdd BLAST111
Regioni1736 – 1871DisorderedSequence analysisAdd BLAST136

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili196 – 425Sequence analysisAdd BLAST230
Coiled coili458 – 1385Sequence analysisAdd BLAST928

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1672 – 1702GBA1 PublicationAdd BLAST31

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1416 – 1459Polar residuesSequence analysisAdd BLAST44
Compositional biasi1743 – 1759Basic and acidic residuesSequence analysisAdd BLAST17
Compositional biasi1767 – 1819Polar residuesSequence analysisAdd BLAST53
Compositional biasi1839 – 1856Polar residuesSequence analysisAdd BLAST18
Compositional biasi1857 – 1871Basic and acidic residuesSequence analysisAdd BLAST15

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The GBA (G-alpha binding and activating) motif mediates binding to the alpha subunits of guanine nucleotide-binding proteins (G proteins).2 Publications
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.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the CCDC88 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4643, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155559

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_001421_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q3V6T2

Identification of Orthologs from Complete Genome Data

More...OMAi		LNNQCEX

Database of Orthologous Groups

More...OrthoDBi		59187at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q3V6T2

TreeFam database of animal gene trees

More...TreeFami		TF320231

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.418.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001715, CH-domain
IPR036872, CH_dom_sf
IPR027717, Girdin
IPR043936, HOOK_N

The PANTHER Classification System

More...PANTHERi		PTHR18947:SF30, PTHR18947:SF30, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF19047, HOOK_N, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50021, CH, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 5 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 5 described isoforms and 33 potential isoforms that are computationally mapped.Show allAlign All

Isoform 11 Publication (identifier: Q3V6T2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MENEIFTPLL EQFMTSPLVT WVKTFGPLAA GNGTNLDEYV ALVDGVFLNQ 
        60         70         80         90        100
VMLQINPKLE SQRVNKKVNN DASLRMHNLS ILVRQIKFYY QETLQQLIMM 
       110        120        130        140        150
SLPNVLIIGK NPFSEQGTEE VKKLLLLLLG CAVQCQKKEE FIERIQGLDF 
       160        170        180        190        200
DTKAAVAAHI QEVTHNQENV FDLQWMEVTD MSQEDIEPLL KNMALHLKRL 
       210        220        230        240        250
IDERDEHSET IIELSEERDG LHFLPHASSS AQSPCGSPGM KRTESRQHLS 
       260        270        280        290        300
VELADAKAKI RRLRQELEEK TEQLLDCKQE LEQMEIELKR LQQENMNLLS 
       310        320        330        340        350
DARSARMYRD ELDALREKAV RVDKLESEVS RYKERLHDIE FYKARVEELK 
       360        370        380        390        400
EDNQVLLETK TMLEDQLEGT RARSDKLHEL EKENLQLKAK LHDMEMERDM 
       410        420        430        440        450
DRKKIEELME ENMTLEMAQK QSMDESLHLG WELEQISRTS ELSEAPQKSL 
       460        470        480        490        500
GHEVNELTSS RLLKLEMENQ SLTKTVEELR TTVDSVEGNA SKILKMEKEN 
       510        520        530        540        550
QRLSKKVEIL ENEIVQEKQS LQNCQNLSKD LMKEKAQLEK TIETLRENSE 
       560        570        580        590        600
RQIKILEQEN EHLNQTVSSL RQRSQISAEA RVKDIEKENK ILHESIKETS 
       610        620        630        640        650
SKLSKIEFEK RQIKKELEHY KEKGERAEEL ENELHHLEKE NELLQKKITN 
       660        670        680        690        700
LKITCEKIEA LEQENSELER ENRKLKKTLD SFKNLTFQLE SLEKENSQLD 
       710        720        730        740        750
EENLELRRNV ESLKCASMKM AQLQLENKEL ESEKEQLKKG LELLKASFKK 
       760        770        780        790        800
TERLEVSYQG LDIENQRLQK TLENSNKKIQ QLESELQDLE MENQTLQKNL 
       810        820        830        840        850
EELKISSKRL EQLEKENKSL EQETSQLEKD KKQLEKENKR LRQQAEIKDT 
       860        870        880        890        900
TLEENNVKIG NLEKENKTLS KEIGIYKESC VRLKELEKEN KELVKRATID 
       910        920        930        940        950
IKTLVTLRED LVSEKLKTQQ MNNDLEKLTH ELEKIGLNKE RLLHDEQSTD 
       960        970        980        990       1000
DSRYKLLESK LESTLKKSLE IKEEKIAALE ARLEESTNYN QQLRQELKTV 
      1010       1020       1030       1040       1050
KKNYEALKQR QDEERMVQSS PPISGEDNKW ERESQETTRE LLKVKDRLIE 
      1060       1070       1080       1090       1100
VERNNATLQA EKQALKTQLK QLETQNNNLQ AQILALQRQT VSLQEQNTTL 
      1110       1120       1130       1140       1150
QTQNAKLQVE NSTLNSQSTS LMNQNAQLLI QQSSLENENE SVIKEREDLK 
      1160       1170       1180       1190       1200
SLYDSLIKDH EKLELLHERQ ASEYESLISK HGTLKSAHKN LEVEHRDLED 
      1210       1220       1230       1240       1250
RYNQLLKQKG QLEDLEKMLK VEQEKMLLEN KNHETVAAEY KKLCGENDRL 
      1260       1270       1280       1290       1300
NHTYSQLLKE TEVLQTDHKN LKSLLNNSKL EQTRLEAEFS KLKEQYQQLD 
      1310       1320       1330       1340       1350
ITSTKLNNQC ELLSQLKGNL EEENRHLLDQ IQTLMLQNRT LLEQNMESKD 
      1360       1370       1380       1390       1400
LFHVEQRQYI DKLNELRRQK EKLEEKIMDQ YKFYDPSPPR RRGNWITLKM 
      1410       1420       1430       1440       1450
RKLIKSKKDI NRERQKSLTL TPTRSDSSEG FLQLPHQDSQ DSSSVGSNSL 
      1460       1470       1480       1490       1500
EDGQTLGTKK SSMVALKRLP FLRNRPKDKD KMKACYRRSM SMNDLVQSMV 
      1510       1520       1530       1540       1550
LAGQWTGSTE NLEVPDDIST GKRRKELGAM AFSTTAINFS TVNSSAGFRS 
      1560       1570       1580       1590       1600
KQLVNNKDTT SFEDISPQGV SDDSSTGSRV HASRPASLDS GRTSTSNSNN 
      1610       1620       1630       1640       1650
NASLHEVKAG AVNNQSRPQS HSSGEFSLLH DHEAWSSSGS SPIQYLKRQT 
      1660       1670       1680       1690       1700
RSSPVLQHKI SETLESRHHK IKTGSPGSEV VTLQQFLEES NKLTSVQIKS 
      1710       1720       1730       1740       1750
SSQENLLDEV MKSLSVSSDF LGKDKPVSCG LARSVSGKTP GDFYDRRTTK 
      1760       1770       1780       1790       1800
PEFLRPGPRK TEDTYFISSA GKPTPGTQGK IKLVKESSLS RQSKDSNPYA 
      1810       1820       1830       1840       1850
TLPRASSVIS TAEGTTRRTS IHDFLTKDSR LPISVDSPPA AADSNTTAAS 
      1860       1870 
NVDKVQESRN SKSRSREQQS S
Length:1,871
Mass (Da):216,042
Last modified:May 15, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9DD2E06F2A235AA5
GO
Isoform 22 Publications (identifier: Q3V6T2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1463-1491: MVALKRLPFLRNRPKDKDKMKACYRRSMS → T

Show »
Length:1,843
Mass (Da):212,620
Checksum:i32BCF709F5ADEDC0
GO
Isoform 3 (identifier: Q3V6T2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     952-952: Missing.

Show »
Length:1,870
Mass (Da):215,954
Checksum:i259F771ECE3DDCFD
GO
Isoform 4 (identifier: Q3V6T2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     952-952: Missing.
     1463-1491: MVALKRLPFLRNRPKDKDKMKACYRRSMS → T

Show »
Length:1,842
Mass (Da):212,533
Checksum:i48C4D509CC7EEE68
GO
Isoform 5 (identifier: Q3V6T2-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     952-952: Missing.
     1733-1806: Missing.

Show »
Length:1,796
Mass (Da):207,797
Checksum:iDE7B152EACCC2422
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 33 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2U3TZV9A0A2U3TZV9_HUMAN
Girdin
CCDC88A
1,797Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y4W8A0A2R8Y4W8_HUMAN
Girdin
CCDC88A
1,493Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8YG73A0A2R8YG73_HUMAN
Girdin
CCDC88A
1,494Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y846A0A2R8Y846_HUMAN
Girdin
CCDC88A
268Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y4X4A0A2R8Y4X4_HUMAN
Girdin
CCDC88A
1,406Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0Y470H0Y470_HUMAN
Girdin
CCDC88A
888Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C2C6H7C2C6_HUMAN
Girdin
CCDC88A
1,202Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0Y7U8H0Y7U8_HUMAN
Girdin
CCDC88A
736Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y7B1A0A2R8Y7B1_HUMAN
Girdin
CCDC88A
1,604Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y7D4A0A2R8Y7D4_HUMAN
Girdin
CCDC88A
939Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
There are more potential isoformsShow all

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAY14932 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence CAD97945 differs from that shown. Intron retention at the C-terminus.Curated
The sequence CAI46020 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti1066K → E in CAI46020 (PubMed:17974005).Curated1
Sequence conflicti1081A → T in CAD97945 (PubMed:17974005).Curated1
Sequence conflicti1661S → P in CAD97945 (PubMed:17974005).Curated1
Sequence conflicti1710V → I in CAI46020 (PubMed:17974005).Curated1
Sequence conflicti1799Y → H in CAD98038 (PubMed:17974005).Curated1
Sequence conflicti1836D → G in CAI46020 (PubMed:17974005).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_040129952Missing in isoform 3, isoform 4 and isoform 5. 3 Publications1
Alternative sequenceiVSP_0524091463 – 1491MVALK…RRSMS → T in isoform 2 and isoform 4. 4 PublicationsAdd BLAST29
Alternative sequenceiVSP_0449431733 – 1806Missing in isoform 5. 1 PublicationAdd BLAST74

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AB201172 mRNA Translation: BAE44387.1
AB125644 mRNA Translation: BAF44475.1
AC019198 Genomic DNA Translation: AAY14932.1 Different initiation.
AC092176 Genomic DNA Translation: AAX82029.1
AC012358 Genomic DNA No translation available.
BC132736 mRNA Translation: AAI32737.1
BC144320 mRNA Translation: AAI44321.1
BX537985 mRNA Translation: CAD97945.1 Sequence problems.
BX538154 mRNA Translation: CAD98038.1
BX648138 mRNA Translation: CAI46020.1 Different initiation.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS33203.1 [Q3V6T2-2]
CCDS46288.1 [Q3V6T2-3]
CCDS58710.1 [Q3V6T2-5]

NCBI Reference Sequences

More...RefSeqi		NP_001129069.1, NM_001135597.1 [Q3V6T2-3]
NP_001241872.1, NM_001254943.1 [Q3V6T2-5]
NP_060554.3, NM_018084.4 [Q3V6T2-2]
XP_011531267.1, XM_011532965.2
XP_011531268.1, XM_011532966.2 [Q3V6T2-1]
XP_011531269.1, XM_011532967.2 [Q3V6T2-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000263630; ENSP00000263630; ENSG00000115355 [Q3V6T2-2]
ENST00000336838; ENSP00000338728; ENSG00000115355 [Q3V6T2-3]
ENST00000436346; ENSP00000410608; ENSG00000115355
ENST00000642200; ENSP00000495919; ENSG00000115355
ENST00000643413; ENSP00000494811; ENSG00000115355 [Q3V6T2-4]
ENST00000646796; ENSP00000493703; ENSG00000115355 [Q3V6T2-5]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		55704

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:55704

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000436346.7; ENSP00000410608.1; NM_001365480.1; NP_001352409.1

UCSC genome browser

More...UCSCi		uc002ryv.3, human [Q3V6T2-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB201172 mRNA Translation: BAE44387.1
AB125644 mRNA Translation: BAF44475.1
AC019198 Genomic DNA Translation: AAY14932.1 Different initiation.
AC092176 Genomic DNA Translation: AAX82029.1
AC012358 Genomic DNA No translation available.
BC132736 mRNA Translation: AAI32737.1
BC144320 mRNA Translation: AAI44321.1
BX537985 mRNA Translation: CAD97945.1 Sequence problems.
BX538154 mRNA Translation: CAD98038.1
BX648138 mRNA Translation: CAI46020.1 Different initiation.
CCDSiCCDS33203.1 [Q3V6T2-2]
CCDS46288.1 [Q3V6T2-3]
CCDS58710.1 [Q3V6T2-5]
RefSeqiNP_001129069.1, NM_001135597.1 [Q3V6T2-3]
NP_001241872.1, NM_001254943.1 [Q3V6T2-5]
NP_060554.3, NM_018084.4 [Q3V6T2-2]
XP_011531267.1, XM_011532965.2
XP_011531268.1, XM_011532966.2 [Q3V6T2-1]
XP_011531269.1, XM_011532967.2 [Q3V6T2-2]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6MHFX-ray2.00C1672-1702[»]
SMRiQ3V6T2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi120829, 162 interactors
CORUMiQ3V6T2
DIPiDIP-50784N
IntActiQ3V6T2, 75 interactors
MINTiQ3V6T2
STRINGi9606.ENSP00000338728

PTM databases

iPTMnetiQ3V6T2
PhosphoSitePlusiQ3V6T2

Genetic variation databases

BioMutaiCCDC88A
DMDMi147644956

Proteomic databases

EPDiQ3V6T2
jPOSTiQ3V6T2
MassIVEiQ3V6T2
MaxQBiQ3V6T2
PaxDbiQ3V6T2
PeptideAtlasiQ3V6T2
PRIDEiQ3V6T2
ProteomicsDBi61886 [Q3V6T2-1]
61887 [Q3V6T2-2]
61888 [Q3V6T2-3]
61889 [Q3V6T2-4]
7248

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		47423, 247 antibodies from 33 providers

The DNASU plasmid repository

More...DNASUi		55704

Genome annotation databases

EnsembliENST00000263630; ENSP00000263630; ENSG00000115355 [Q3V6T2-2]
ENST00000336838; ENSP00000338728; ENSG00000115355 [Q3V6T2-3]
ENST00000436346; ENSP00000410608; ENSG00000115355
ENST00000642200; ENSP00000495919; ENSG00000115355
ENST00000643413; ENSP00000494811; ENSG00000115355 [Q3V6T2-4]
ENST00000646796; ENSP00000493703; ENSG00000115355 [Q3V6T2-5]
GeneIDi55704
KEGGihsa:55704
MANE-SelectiENST00000436346.7; ENSP00000410608.1; NM_001365480.1; NP_001352409.1
UCSCiuc002ryv.3, human [Q3V6T2-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		55704
DisGeNETi55704

GeneCards: human genes, protein and diseases

More...GeneCardsi		CCDC88A
HGNCiHGNC:25523, CCDC88A
HPAiENSG00000115355, Tissue enhanced (brain)
MalaCardsiCCDC88A
MIMi609736, gene
617507, phenotype
neXtProtiNX_Q3V6T2
OpenTargetsiENSG00000115355
Orphaneti99807, PEHO-like syndrome
PharmGKBiPA162381751
VEuPathDBiHostDB:ENSG00000115355

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG4643, Eukaryota
GeneTreeiENSGT00940000155559
HOGENOMiCLU_001421_1_0_1
InParanoidiQ3V6T2
OMAiLNNQCEX
OrthoDBi59187at2759
PhylomeDBiQ3V6T2
TreeFamiTF320231

Enzyme and pathway databases

PathwayCommonsiQ3V6T2
ReactomeiR-HSA-9696264, RND3 GTPase cycle
R-HSA-9696273, RND1 GTPase cycle
SignaLinkiQ3V6T2
SIGNORiQ3V6T2

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		55704, 10 hits in 1051 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		CCDC88A, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CCDC88A

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		55704
PharosiQ3V6T2, Tbio

Protein Ontology

More...PROi		PR:Q3V6T2
RNActiQ3V6T2, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000115355, Expressed in testis and 222 other tissues
ExpressionAtlasiQ3V6T2, baseline and differential
GenevisibleiQ3V6T2, HS

Family and domain databases

Gene3Di1.10.418.10, 1 hit
InterProiView protein in InterPro
IPR001715, CH-domain
IPR036872, CH_dom_sf
IPR027717, Girdin
IPR043936, HOOK_N
PANTHERiPTHR18947:SF30, PTHR18947:SF30, 1 hit
PfamiView protein in Pfam
PF19047, HOOK_N, 1 hit
PROSITEiView protein in PROSITE
PS50021, CH, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGRDN_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q3V6T2
Secondary accession number(s): A1IGE7
, B7ZM78, C9JG83, Q53SF1, Q581G3, Q5HYD0, Q7Z339, Q7Z3C5
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: February 23, 2022
This is version 139 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again