O43815 · STRN_HUMAN
- ProteinStriatin
- GeneSTRN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids780 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Calmodulin-binding scaffolding protein which is the center of the striatin-interacting phosphatase and kinase (STRIPAK) complexes (PubMed:18782753).
STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (Probable)
STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (Probable)
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | bicellular tight junction | |
Cellular Component | cytosol | |
Cellular Component | dendrite | |
Cellular Component | dendritic spine | |
Cellular Component | FAR/SIN/STRIPAK complex | |
Cellular Component | membrane | |
Cellular Component | neuronal cell body | |
Cellular Component | postsynaptic density | |
Cellular Component | postsynaptic membrane | |
Molecular Function | armadillo repeat domain binding | |
Molecular Function | calmodulin binding | |
Molecular Function | nuclear estrogen receptor binding | |
Molecular Function | protein phosphatase 2A binding | |
Molecular Function | protein-containing complex binding | |
Biological Process | bicellular tight junction assembly | |
Biological Process | dendrite development | |
Biological Process | locomotory behavior | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | Wnt signaling pathway |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameStriatin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO43815
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Peripheral membrane protein
Note: CTTNBP2-binding may regulate dendritic spine distribution.
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 870 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000051232 | 1-780 | UniProt | Striatin | |||
Sequence: MDEQAGPGVFFSNNHPGAGGAKGLGPLAEAAAAGDGAAAAGAARAQYSLPGILHFLQHEWARFEVERAQWEVERAELQAQIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAKYHKLKYGTELNQGDMKPPSYDSDEGNETEVQPQQNSQLMWKQGRQLLRQYLQEVGYTDTILDVKSKRVRALLGFSSDVTDREDDKNQDSVVNGTEAEVKETAMIAKSELTDSASVLDNFKFLESAAADFSDEDEDDDVDGREKSVIDTSTIVRKKALPDSGEDRDTKEALKEFDFLVTSEEGDNESRSAGDGTDWEKEDQCLMPEAWNVDQGVITKLKEQYKKERKGKKGVKRPNRSKLQDMLANLRDVDELPSLQPSVGSPSRPSSSRLPEHEINRADEVEALTFPPSSGKSFIMGADEALESELGLGELAGLTVANEADSLTYDIANNKDALRKTWNPKFTLRSHFDGIRALAFHPIEPVLITASEDHTLKMWNLQKTAPAKKSTSLDVEPIYTFRAHKGPVLCVVMSSNGEQCYSGGTDGLIQGWNTTNPNIDPYDSYDPSVLRGPLLGHTDAVWGLAYSAAHQRLLSCSADGTLRLWNTTEVAPALSVFNDTKELGIPASVDLVSSDPSHMVASFSKGYTSIFNMETQQRILTLESNVDTTANSSCQINRVISHPTLPISITAHEDRHIKFYDNNTGKLIHSMVAHLEAVTSLAVDPNGLYLMSGSHDCSIRLWNLESKTCIQEFTAHRKKFEESIHDVAFHPSKCYIASAGADALAKVFV | |||||||
Modified residue | 137 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 137 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 143 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 190 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 204 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 225 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 225 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 227 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 227 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 229 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 229 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 239 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 245 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 245 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 259 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 259 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 265 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 373 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 376 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 378 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 503 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 672 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Part of the core of STRIPAK complexes composed of PP2A catalytic and scaffolding subunits, the striatins (PP2A regulatory subunits), the striatin-associated proteins MOB4, STRIP1 and STRIP2, PDCD10 and members of the STE20 kinases, such as STK24 and STK26 (PubMed:18782753).
Interacts with CTTNBP2; this interaction may regulate dendritic spine distribution of STRN. Activation of glutamate receptors weakens the interaction with CTTNBP2 (By similarity).
Interacts with CTTNBP2; this interaction may regulate dendritic spine distribution of STRN. Activation of glutamate receptors weakens the interaction with CTTNBP2 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O43815 | CTTNBP2NL Q9P2B4 | 8 | EBI-1046642, EBI-1774273 | |
BINARY | O43815 | MOB4 Q9Y3A3 | 7 | EBI-1046642, EBI-713935 | |
BINARY | O43815 | PDCD10 Q9BUL8 | 7 | EBI-1046642, EBI-740195 | |
BINARY | O43815 | PPP2CA P67775 | 7 | EBI-1046642, EBI-712311 | |
BINARY | O43815 | PPP2R1A P30153 | 10 | EBI-1046642, EBI-302388 | |
BINARY | O43815 | RINT1 Q6NUQ1 | 3 | EBI-1046642, EBI-726876 | |
BINARY | O43815 | STK24 Q9Y6E0 | 6 | EBI-1046642, EBI-740175 | |
BINARY | O43815 | STK25 O00506 | 7 | EBI-1046642, EBI-618295 | |
BINARY | O43815 | STRN3 Q13033 | 12 | EBI-1046642, EBI-1053857 | |
BINARY | O43815 | TFIP11 Q9UBB9 | 3 | EBI-1046642, EBI-1105213 | |
BINARY | O43815 | TNKS2 Q9H2K2 | 2 | EBI-1046642, EBI-4398527 | |
BINARY | O43815 | TRAF3IP3 Q9Y228 | 4 | EBI-1046642, EBI-765817 | |
BINARY | O43815-2 | PDCD10 Q9BUL8 | 3 | EBI-1266294, EBI-740195 | |
BINARY | O43815-2 | PPP2R1A P30153 | 3 | EBI-1266294, EBI-302388 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for coiled coil, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 53-120 | |||||
Sequence: LHFLQHEWARFEVERAQWEVERAELQAQIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAKYHKLK | ||||||
Region | 55-63 | Caveolin-binding | ||||
Sequence: FLQHEWARF | ||||||
Region | 124-150 | Disordered | ||||
Sequence: ELNQGDMKPPSYDSDEGNETEVQPQQN | ||||||
Region | 149-166 | Calmodulin-binding | ||||
Sequence: QNSQLMWKQGRQLLRQYL | ||||||
Region | 289-310 | Disordered | ||||
Sequence: DFLVTSEEGDNESRSAGDGTDW | ||||||
Region | 365-387 | Disordered | ||||
Sequence: DELPSLQPSVGSPSRPSSSRLPE | ||||||
Repeat | 461-500 | WD 1 | ||||
Sequence: SHFDGIRALAFHPIEPVLITASEDHTLKMWNLQKTAPAKK | ||||||
Repeat | 514-553 | WD 2 | ||||
Sequence: AHKGPVLCVVMSSNGEQCYSGGTDGLIQGWNTTNPNIDPY | ||||||
Repeat | 567-606 | WD 3 | ||||
Sequence: GHTDAVWGLAYSAAHQRLLSCSADGTLRLWNTTEVAPALS | ||||||
Repeat | 662-701 | WD 4 | ||||
Sequence: NSSCQINRVISHPTLPISITAHEDRHIKFYDNNTGKLIHS | ||||||
Repeat | 704-743 | WD 5 | ||||
Sequence: AHLEAVTSLAVDPNGLYLMSGSHDCSIRLWNLESKTCIQE | ||||||
Repeat | 750-780 | WD 6 | ||||
Sequence: KFEESIHDVAFHPSKCYIASAGADALAKVFV |
Sequence similarities
Belongs to the WD repeat striatin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O43815-1
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.
- Name1
- Length780
- Mass (Da)86,132
- Last updated2007-03-06 v4
- ChecksumDDB18A11102BEA35
O43815-2
- Name2
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_023495 | 29-40 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 191 | in Ref. 1; CAA11560 | ||||
Sequence: S → I | ||||||
Alternative sequence | VSP_023496 | 311-348 | in isoform 2 | |||
Sequence: EKEDQCLMPEAWNVDQGVITKLKEQYKKERKGKKGVKR → G | ||||||
Sequence conflict | 423 | in Ref. 1; CAA11560 | ||||
Sequence: L → P | ||||||
Sequence conflict | 611 | in Ref. 1; CAA11560 | ||||
Sequence: T → I | ||||||
Sequence conflict | 677 | in Ref. 1; CAA11560 | ||||
Sequence: P → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ223814 EMBL· GenBank· DDBJ | CAA11560.1 EMBL· GenBank· DDBJ | mRNA | ||
AC007404 EMBL· GenBank· DDBJ | AAY24273.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC007382 EMBL· GenBank· DDBJ | AAF66162.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC106879 EMBL· GenBank· DDBJ | AAI06880.1 EMBL· GenBank· DDBJ | mRNA |