Reviewed,
UniProtKB/Swiss-Prot Q8CHC4 (SYNJ1_MOUSE)
Last modified
November 3, 2009.
Version 67.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Synaptojanin-1 EC=3.1.3.36 Alternative name(s): Synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1 | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 1574 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Inositol 5-phosphatase which has a role in clathrin-mediated endocytosis By similarity. |
| Catalytic activity | 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate. |
| Subunit structure | Binds AMPH, SH3GL1, SH3GL2 and SH3GL3 By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Domain | Binds to EPS15 (a clathrin coat-associated protein) via a C-terminal domain containing three Asn-Pro-Phe (NPF) repeats By similarity. The C-terminal proline-rich region mediates binding to a variety of SH3 domain-containing proteins including AMPH, SH3GL1, SH3GL2, SH3GL3 and GRB2. |
| Sequence similarities | Belongs to the synaptojanin family. In the central section; belongs to the inositol-1,4,5-trisphosphate 5-phosphatase family. Contains 1 RRM (RNA recognition motif) domain. Contains 1 SAC domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Endocytosis |
| Cellular component | Cytoplasm |
| Domain | Repeat |
| Ligand | RNA-binding |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | learning Inferred from mutant phenotype. Source: MGI phosphoinositide dephosphorylationInferred from mutant phenotype. Source: MGI phosphoinositide-mediated signalingTraceable author statement. Source: MGI synaptic vesicle primingInferred from mutant phenotype. Source: MGI synaptic vesicle uncoatingInferred from mutant phenotype. Source: MGI |
| Cellular component | clathrin coat Traceable author statement. Source: MGI |
| Molecular function | RNA binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol-4,5-bisphosphate 5-phosphatase activityInferred from mutant phenotype. Source: MGI polyphosphoinositide phosphatase activityInferred from mutant phenotype. Source: MGI protein bindingInferred from physical interaction. Source: MGI |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1574 | 1574 | Synaptojanin-1 | PRO_0000209731 | |||||
Regions | |||||||||
| Domain | 119 – 442 | 324 | SAC | ||||||
| Domain | 894 – 971 | 78 | RRM | ||||||
| Compositional bias | 1042 – 1286 | 245 | Pro-rich | ||||||
| Compositional bias | 1533 – 1566 | 34 | Pro-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 784 | 1 | Phosphotyrosine Ref.3 | ||||||
| Modified residue | 786 | 1 | Phosphotyrosine Ref.3 | ||||||
| Modified residue | 830 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1048 | 1 | Phosphothreonine Ref.5 | ||||||
| Modified residue | 1053 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 1084 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 1147 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 1217 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1350 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 1354 | 1 | Phosphothreonine Ref.5 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H. DNA Res. 9:179-188(2002) [PubMed: 12465718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [2] | Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| [3] | "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-784 AND TYR-786, MASS SPECTROMETRY. Tissue: Brain. |
| [4] | "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1053; SER-1084 AND SER-1147, MASS SPECTROMETRY. Tissue: Brain cortex. |
| [5] | "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1048; SER-1350 AND THR-1354, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AB093272 Transcribed RNA. Translation: BAC41456.2. Different initiation. | |
| IPI | IPI00881540. |
| UniGene | Mm.187079 |
3D structure databases | |
| SMR | Q8CHC4. Positions 895-971. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q8CHC4. |
PTM databases | |
| PhosphoSite | Q8CHC4. |
Proteomic databases | |
| PRIDE | Q8CHC4. |
Genome annotation databases | |
| Ensembl | ENSMUST00000023696; ENSMUSP00000023696; ENSMUSG00000022973; Mus musculus. [Genome view] ENSMUST00000118390; ENSMUSP00000113518; ENSMUSG00000022973; Mus musculus. [Genome view] |
| UCSC | uc007zww.1. mouse. |
Organism-specific databases | |
| MGI | MGI:1354961. Synj1. |
| Rouge | Search... |
Phylogenomic databases | |
| HOGENOM | Q8CHC4. |
| HOVERGEN | Q8CHC4. |
| OMA | DYGFFYF. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.36. 244. |
Gene expression databases | |
| Bgee | Q8CHC4. |
| CleanEx | MM_SYNJ1. |
| Genevestigator | Q8CHC4. |
| GermOnline | ENSMUSG00000022973. Mus musculus. |
Family and domain databases | |
| InterPro | IPR015047. DUF1866. IPR005135. Endo/exonuclease/phosphatase. IPR000300. IPPc. IPR000504. RRM_RNP1. IPR002013. Syja_N. [Graphical view] |
| Pfam | PF08952. DUF1866. 1 hit. PF03372. Exo_endo_phos. 1 hit. PF02383. Syja_N. 1 hit. [Graphical view] |
| SMART | SM00128. IPPc. 1 hit. [Graphical view] |
| PROSITE | PS50102. RRM. 1 hit. PS50275. SAC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| SOURCE | Search... |
Entry information
| Entry name | SYNJ1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q8CHC4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |
