P31948 · STIP1_HUMAN
- ProteinStress-induced-phosphoprotein 1
- GeneSTIP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids543 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a co-chaperone for HSP90AA1 (PubMed:27353360).
Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity).
Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity).
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 | cytosol | |
Cellular Component | dynein axonemal particle | |
Cellular Component | Golgi apparatus | |
Cellular Component | nucleus | |
Cellular Component | protein folding chaperone complex | |
Cellular Component | protein-containing complex | |
Molecular Function | Hsp90 protein binding | |
Molecular Function | RNA binding | |
Biological Process | cellular response to interleukin-7 |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameStress-induced-phosphoprotein 1
- Short namesSTI1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP31948
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 590 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000106372 | 1-543 | UniProt | Stress-induced-phosphoprotein 1 | |||
Sequence: MEQVNELKEKGNKALSVGNIDDALQCYSEAIKLDPHNHVLYSNRSAAYAKKGDYQKAYEDGCKTVDLKPDWGKGYSRKAAALEFLNRFEEAKRTYEEGLKHEANNPQLKEGLQNMEARLAERKFMNPFNMPNLYQKLESDPRTRTLLSDPTYRELIEQLRNKPSDLGTKLQDPRIMTTLSVLLGVDLGSMDEEEEIATPPPPPPPKKETKPEPMEEDLPENKKQALKEKELGNDAYKKKDFDTALKHYDKAKELDPTNMTYITNQAAVYFEKGDYNKCRELCEKAIEVGRENREDYRQIAKAYARIGNSYFKEEKYKDAIHFYNKSLAEHRTPDVLKKCQQAEKILKEQERLAYINPDLALEEKNKGNECFQKGDYPQAMKHYTEAIKRNPKDAKLYSNRAACYTKLLEFQLALKDCEECIQLEPTFIKGYTRKAAALEAMKDYTKAMDVYQKALDLDSSCKEAADGYQRCMMAQYNRHDSPEDVKRRAMADPEVQQIMSDPAMRLILEQMQKDPQALSEHLKNPVIAQKIQKLMDVGLIAIR | |||||||
Modified residue | 8 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 16 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 16 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 41 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 42 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 123 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 123 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 198 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 198 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 210 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 210 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 301 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 312 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 325 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 332 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 332 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 344 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 354 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 354 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 446 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 460 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 481 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 481 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155).
Forms a complex with HSPA8/HSC70, HSPCA/HSP-86 and HSPCB/HSP-84 (By similarity).
Interacts with PACRG (PubMed:14532270).
Interacts with EEF1AKMT3 (PubMed:23349634).
Interacts with HSP90/HSP90AA1; the interaction dissociates the PPP5C:HSP90AA1 interaction (PubMed:27353360, PubMed:9195923).
Interacts with FLCN, FNIP1 and FNIP2 (PubMed:27353360).
Interacts with HSPA8/HSC70 (By similarity).
Interacts with HSP90AB1; upon SMYD2-dependent HSP90AB1 methylation (PubMed:24880080).
Forms a complex with HSPA8/HSC70, HSPCA/HSP-86 and HSPCB/HSP-84 (By similarity).
Interacts with PACRG (PubMed:14532270).
Interacts with EEF1AKMT3 (PubMed:23349634).
Interacts with HSP90/HSP90AA1; the interaction dissociates the PPP5C:HSP90AA1 interaction (PubMed:27353360, PubMed:9195923).
Interacts with FLCN, FNIP1 and FNIP2 (PubMed:27353360).
Interacts with HSPA8/HSC70 (By similarity).
Interacts with HSP90AB1; upon SMYD2-dependent HSP90AB1 methylation (PubMed:24880080).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 4-37 | TPR 1 | ||||
Sequence: VNELKEKGNKALSVGNIDDALQCYSEAIKLDPHN | ||||||
Repeat | 38-71 | TPR 2 | ||||
Sequence: HVLYSNRSAAYAKKGDYQKAYEDGCKTVDLKPDW | ||||||
Repeat | 72-105 | TPR 3 | ||||
Sequence: GKGYSRKAAALEFLNRFEEAKRTYEEGLKHEANN | ||||||
Domain | 130-169 | STI1 1 | ||||
Sequence: MPNLYQKLESDPRTRTLLSDPTYRELIEQLRNKPSDLGTK | ||||||
Region | 192-233 | Disordered | ||||
Sequence: EEEEIATPPPPPPPKKETKPEPMEEDLPENKKQALKEKELGN | ||||||
Compositional bias | 208-233 | Basic and acidic residues | ||||
Sequence: ETKPEPMEEDLPENKKQALKEKELGN | ||||||
Motif | 222-239 | Bipartite nuclear localization signal | ||||
Sequence: KKQALKEKELGNDAYKKK | ||||||
Repeat | 225-258 | TPR 4 | ||||
Sequence: ALKEKELGNDAYKKKDFDTALKHYDKAKELDPTN | ||||||
Repeat | 259-292 | TPR 5 | ||||
Sequence: MTYITNQAAVYFEKGDYNKCRELCEKAIEVGREN | ||||||
Repeat | 300-333 | TPR 6 | ||||
Sequence: AKAYARIGNSYFKEEKYKDAIHFYNKSLAEHRTP | ||||||
Repeat | 360-393 | TPR 7 | ||||
Sequence: ALEEKNKGNECFQKGDYPQAMKHYTEAIKRNPKD | ||||||
Repeat | 394-427 | TPR 8 | ||||
Sequence: AKLYSNRAACYTKLLEFQLALKDCEECIQLEPTF | ||||||
Repeat | 428-461 | TPR 9 | ||||
Sequence: IKGYTRKAAALEAMKDYTKAMDVYQKALDLDSSC | ||||||
Domain | 492-531 | STI1 2 | ||||
Sequence: DPEVQQIMSDPAMRLILEQMQKDPQALSEHLKNPVIAQKI |
Domain
The TPR 1 repeat interacts with the C-terminal of HSC70. The TPR 4, 5 and 6 repeats (also called TPR2A domain) and TPR 7, 8 and 9 repeats (also called TPR2B domain) interact with HSP90.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P31948-1
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
- Length543
- Mass (Da)62,639
- Last updated1993-07-01 v1
- Checksum8E58ECA13825CB0E
P31948-2
- Name2
- Differences from canonical
- 1-3: MEQ → MESGSPMGEVEISRTIRTNGRGQRGYDWQCKRPIRVAEVRSSLHSWSLRW
P31948-3
- Name3
- Differences from canonical
- 74-97: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_055034 | 1-3 | in isoform 2 | |||
Sequence: MEQ → MESGSPMGEVEISRTIRTNGRGQRGYDWQCKRPIRVAEVRSSLHSWSLRW | ||||||
Alternative sequence | VSP_055035 | 74-97 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 84 | in Ref. 7; AAH39299 | ||||
Sequence: F → L | ||||||
Compositional bias | 208-233 | Basic and acidic residues | ||||
Sequence: ETKPEPMEEDLPENKKQALKEKELGN | ||||||
Sequence conflict | 364 | in Ref. 4; BAG59782 | ||||
Sequence: K → E | ||||||
Sequence conflict | 533 | in Ref. 4; BAG59782 | ||||
Sequence: K → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M86752 EMBL· GenBank· DDBJ | AAA58682.1 EMBL· GenBank· DDBJ | mRNA | ||
BT020010 EMBL· GenBank· DDBJ | AAV38813.1 EMBL· GenBank· DDBJ | mRNA | ||
BT020011 EMBL· GenBank· DDBJ | AAV38814.1 EMBL· GenBank· DDBJ | mRNA | ||
CR536512 EMBL· GenBank· DDBJ | CAG38750.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297319 EMBL· GenBank· DDBJ | BAG59782.1 EMBL· GenBank· DDBJ | mRNA | ||
AP005668 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471076 EMBL· GenBank· DDBJ | EAW74196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471076 EMBL· GenBank· DDBJ | EAW74197.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002987 EMBL· GenBank· DDBJ | AAH02987.1 EMBL· GenBank· DDBJ | mRNA | ||
BC039299 EMBL· GenBank· DDBJ | AAH39299.1 EMBL· GenBank· DDBJ | mRNA |