Q3V6T2 (GRDN_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 68.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 1871 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Enhances phosphoinositide 3-kinase (PI3K)-dependent phosphorylation and kinase activity of AKT1/PKB, but does not possess kinase activity itself. Phosphorylation of AKT1/PKB thereby induces the phosphorylation of downstream effectors GSK3 and FOXO1/FKHR, and regulates DNA replication and cell proliferation By similarity. Essential for the integrity of the actin cytoskeleton and for cell migration. Required for formation of actin stress fibers and lamellipodia. May be involved in membrane sorting in the early endosome. Ref.1 Ref.2 |
| Subunit structure | Interacts (via C-terminus) with DISC1; the interaction is direct. Interacts with AKT proteins; the interaction is inhibited in presence of DISC1 By similarity. Homodimer. The non-phosphorylated form interacts with phosphatidylinositol 4-phosphate [PI4P] and weakly with phosphatidylinositol 3-phosphate [PI3P]. Interacts with microtubules. Interacts with actin through its C-terminal domain. Interacts with the C-terminus of AKT1/PKB. Ref.1 |
| Subcellular location | Membrane. Cell membrane. Cytoplasm › cytosol. Cytoplasmic vesicle. Cell projection › lamellipodium. Note: Localizes to the cell membrane through interaction with phosphoinositides. Ref.1 Ref.2 Ref.7 |
| Tissue specificity | Expressed ubiquitously. Ref.1 |
| Post-translational modification | Phosphorylation is induced by epidermal growth factor (EGF) in a phosphoinositide 3-kinase (PI3K)-dependent manner. Phosphorylation by AKT1/PKB is necessary for the delocalization from the cell membrane and for cell migration. Ref.1 |
| Sequence similarities | Belongs to the CCDC88 family. |
| Sequence caution | The sequence AAY14932.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAD97945.1 differs from that shown. Reason: Intron retention at the C-terminus. The sequence CAI46020.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
Ontologies
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 Ref.1 Ref.6 (identifier: Q3V6T2-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 Ref.2 Ref.3 Ref.5 Ref.6 (identifier: Q3V6T2-2) The sequence of this isoform differs from the canonical sequence as follows: 1463-1491: MVALKRLPFLRNRPKDKDKMKACYRRSMS → T | ||||||
| Isoform 3 (identifier: Q3V6T2-3) The sequence of this isoform differs from the canonical sequence as follows: 952-952: Missing. | ||||||
| Isoform 4 (identifier: Q3V6T2-4) The sequence of this isoform differs from the canonical sequence as follows: 952-952: Missing. 1463-1491: MVALKRLPFLRNRPKDKDKMKACYRRSMS → T | ||||||
| Isoform 5 (identifier: Q3V6T2-5) The sequence of this isoform differs from the canonical sequence as follows: 952-952: Missing. 1733-1806: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1871 | 1871 | Girdin | PRO_0000287429 | |||||
Regions | |||||||||
| Region | 1390 – 1408 | 19 | Phosphoinositide-binding Ref.1 | ||||||
| Coiled coil | 196 – 425 | 230 | Potential | ||||||
| Coiled coil | 458 – 1385 | 928 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1387 | 1 | Phosphoserine Ref.9 PubMed 16964243 | ||||||
| Modified residue | 1417 | 1 | Phosphoserine; by PKB/AKT1 Ref.1 | ||||||
| Modified residue | 1559 | 1 | Phosphothreonine By similarity UniProtKB Q5SNZ0 | ||||||
| Modified residue | 1560 | 1 | Phosphothreonine By similarity UniProtKB Q5SNZ0 | ||||||
| Modified residue | 1561 | 1 | Phosphoserine By similarity UniProtKB Q5SNZ0 | ||||||
| Modified residue | 1673 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 1675 | 1 | Phosphoserine By similarity UniProtKB Q5SNZ0 | ||||||
| Modified residue | 1702 | 1 | Phosphoserine By similarity UniProtKB Q5SNZ0 | ||||||
| Modified residue | 1837 | 1 | Phosphoserine Ref.9 | ||||||
Natural variations | |||||||||
| Alternative sequence | 952 | 1 | Missing in isoform 3, isoform 4 and isoform 5. | VSP_040129 | |||||
| Alternative sequence | 1463 – 1491 | 29 | MVALK…RRSMS → T in isoform 2 and isoform 4. Ref.2 Ref.3 Ref.5 Ref.6 | VSP_052409 | |||||
| Alternative sequence | 1733 – 1806 | 74 | Missing in isoform 5. | VSP_044943 | |||||
Experimental info | |||||||||
| Mutagenesis | 1417 | 1 | S → A: Disrupts actin organization, cell migration and lamellipodia formation. Ref.1 | ||||||
| Sequence conflict | 1066 | 1 | K → E in CAI46020. Ref.6 | ||||||
| Sequence conflict | 1081 | 1 | A → T in CAD97945. Ref.6 | ||||||
| Sequence conflict | 1661 | 1 | S → P in CAD97945. Ref.6 | ||||||
| Sequence conflict | 1710 | 1 | V → I in CAI46020. Ref.6 | ||||||
| Sequence conflict | 1799 | 1 | Y → H in CAD98038. Ref.6 | ||||||
| Sequence conflict | 1836 | 1 | D → G in CAI46020. Ref.6 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Akt/PKB regulates actin organization and cell motility via Girdin/APE." Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M. Dev. Cell 9:389-402(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AKT1, INTERACTION WITH PHOSPHOINOSITIDES, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1417 BY AKT1, MUTAGENESIS OF SER-1417. Tissue: Fetal brain. |
| [2] | "A novel hook-related protein family and the characterization of hook-related protein 1." Simpson F., Martin S., Evans T.M., Kerr M., James D.E., Parton R.G., Teasdale R.D., Wicking C. Traffic 6:442-458(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING. Tissue: Fetal brain. |
| [3] | Anai M. Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). |
| [4] | "Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. Wilson R.K.Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5). |
| [6] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 811-1871 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 826-1850 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 851-1871 (ISOFORM 4). Tissue: Amygdala and Testis. |
| [7] | "Identification and characterization of GIV, a novel Galpha i/s-interacting protein found on COPI, endoplasmic reticulum-Golgi transport vesicles." Le-Niculescu H., Niesman I., Fischer T., DeVries L., Farquhar M.G. J. Biol. Chem. 280:22012-22020(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION, SUBCELLULAR LOCATION. |
| [8] | "Girdin, a novel actin-binding protein, and its family of proteins possess versatile functions in the Akt and Wnt signaling pathways." Enomoto A., Ping J., Takahashi M. Ann. N. Y. Acad. Sci. 1086:169-184(2006) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW. |
| [9] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1387; THR-1673 AND SER-1837, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [10] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell. |
| [11] | "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma. |
| [12] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [13] | "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | 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. |
| IPI | IPI00171134. IPI00654603. IPI00892916. IPI00893288. IPI00943263. |
| RefSeq | NP_001129069.1. NM_001135597.1. NP_001241872.1. NM_001254943.1. NP_060554.3. NM_018084.4. |
| UniGene | Hs.292925. |
3D structure databases | |
| ProteinModelPortal | Q3V6T2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q3V6T2. 7 interactions. |
| STRING | 9606.ENSP00000338728. |
PTM databases | |
| PhosphoSite | Q3V6T2. |
Polymorphism databases | |
| DMDM | 147644956. |
Proteomic databases | |
| PaxDb | Q3V6T2. |
| PRIDE | Q3V6T2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000263630; ENSP00000263630; ENSG00000115355. ENST00000336838; ENSP00000338728; ENSG00000115355. ENST00000413716; ENSP00000404431; ENSG00000115355. ENST00000436346; ENSP00000410608; ENSG00000115355. |
| GeneID | 55704. |
| KEGG | hsa:55704. |
| UCSC | uc002ryu.2. human. uc002ryv.2. human. uc002ryw.3. human. uc010yoz.1. human. uc010ypa.1. human. |
Organism-specific databases | |
| CTD | 55704. |
| GeneCards | GC02M055514. |
| HGNC | HGNC:25523. CCDC88A. |
| HPA | HPA038101. |
| MIM | 609736. gene. |
| neXtProt | NX_Q3V6T2. |
| PharmGKB | PA162381751. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| HOVERGEN | HBG057867. |
| InParanoid | Q3V6T2. |
| OMA | TGFRSKQ. |
Gene expression databases | |
| ArrayExpress | Q3V6T2. |
| Bgee | Q3V6T2. |
| CleanEx | HS_CCDC88A. |
| Genevestigator | Q3V6T2. |
Family and domain databases | |
| InterPro | IPR008636. HOOK/CCDC88. [Graphical view] |
| Pfam | PF05622. HOOK. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | CCDC88A. human. |
| GenomeRNAi | 55704. |
| NextBio | 60553. |
| SOURCE | Search... |
Entry information
| Entry name | GRDN_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q3V6T2 Secondary accession number(s): A1IGE7 Q7Z3C5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 2 Human chromosome 2: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
