O75674 · TM1L1_HUMAN
- ProteinTOM1-like protein 1
- GeneTOM1L1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids476 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Probable adapter protein involved in signaling pathways. Interacts with the SH2 and SH3 domains of various signaling proteins when it is phosphorylated. May promote FYN activation, possibly by disrupting intramolecular SH3-dependent interactions (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 | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | endosome | |
Cellular Component | endosome membrane | |
Cellular Component | extracellular exosome | |
Cellular Component | Golgi stack | |
Cellular Component | lysosome | |
Cellular Component | membrane | |
Molecular Function | clathrin binding | |
Molecular Function | phosphatidylinositol binding | |
Molecular Function | protein kinase activator activity | |
Molecular Function | protein kinase binding | |
Molecular Function | SH3 domain binding | |
Molecular Function | ubiquitin binding | |
Biological Process | activation of protein kinase activity | |
Biological Process | negative regulation of mitotic nuclear division | |
Biological Process | positive regulation of protein autophosphorylation | |
Biological Process | protein transport | |
Biological Process | signal transduction | |
Biological Process | ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTOM1-like protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO75674
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Peripheral membrane protein
Note: A small proportion is membrane-associated.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_047469 | 108 | in dbSNP:rs16955377 | |||
Sequence: R → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 520 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 (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000072566 | 1-476 | UniProt | TOM1-like protein 1 | |||
Sequence: MAFGKSHRDPYATSVGHLIEKATFAGVQTEDWGQFMHICDIINTTQDGPKDAVKALKKRISKNYNHKEIQLTLSLIDMCVQNCGPSFQSLIVKKEFVKENLVKLLNPRYNLPLDIQNRILNFIKTWSQGFPGGVDVSEVKEVYLDLVKKGVQFPPSEAEAETARQETAQISSNPPTSVPTAPALSSVIAPKNSTVTLVPEQIGKLHSELDMVKMNVRVMSAILMENTPGSENHEDIELLQKLYKTGREMQERIMDLLVVVENEDVTVELIQVNEDLNNAILGYERFTRNQQRILEQNKNQKEATNTTSEPSAPSQDLLDLSPSPRMPRATLGELNTMNNQLSGLNFSLPSSDVTNNLKPSLHPQMNLLALENTEIPPFAQRTSQNLTSSHAYDNFLEHSNSVFLQPVSLQTIAAAPSNQSLPPLPSNHPAMTKSDLQPPNYYEVMEFDPLAPAVTTEAIYEEIDAHQHKGAQNDGD | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 171 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 311 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 314 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 314 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 321 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 321 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 323 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 323 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 460 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 460 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Phosphorylated on tyrosines by FYN and LYN.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with FYN, GRB2 and PIK3R1 when phosphorylated. Interacts with LYN.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O75674 | CLTC Q00610 | 4 | EBI-712991, EBI-354967 | |
BINARY | O75674 | EGFR P00533 | 6 | EBI-712991, EBI-297353 | |
BINARY | O75674 | GRB2 P62993 | 2 | EBI-712991, EBI-401755 | |
BINARY | O75674 | TOLLIP Q9H0E2 | 6 | EBI-712991, EBI-74615 | |
BINARY | O75674 | TOM1 O60784 | 2 | EBI-712991, EBI-74634 | |
BINARY | O75674 | TSG101 Q99816 | 2 | EBI-712991, EBI-346882 | |
BINARY | O75674 | VAV2 P52735 | 2 | EBI-712991, EBI-297549 | |
BINARY | O75674-2 | DNAJB13 P59910 | 3 | EBI-12011552, EBI-11514233 | |
BINARY | O75674-2 | TOLLIP Q9H0E2 | 5 | EBI-12011552, EBI-74615 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-154 | VHS | ||||
Sequence: ATFAGVQTEDWGQFMHICDIINTTQDGPKDAVKALKKRISKNYNHKEIQLTLSLIDMCVQNCGPSFQSLIVKKEFVKENLVKLLNPRYNLPLDIQNRILNFIKTWSQGFPGGVDVSEVKEVYLDLVKKGVQFP | ||||||
Region | 155-179 | Disordered | ||||
Sequence: PSEAEAETARQETAQISSNPPTSVP | ||||||
Compositional bias | 162-179 | Polar residues | ||||
Sequence: TARQETAQISSNPPTSVP | ||||||
Domain | 200-288 | GAT | ||||
Sequence: EQIGKLHSELDMVKMNVRVMSAILMENTPGSENHEDIELLQKLYKTGREMQERIMDLLVVVENEDVTVELIQVNEDLNNAILGYERFTR | ||||||
Compositional bias | 298-318 | Polar residues | ||||
Sequence: KNQKEATNTTSEPSAPSQDLL | ||||||
Region | 298-327 | Disordered | ||||
Sequence: KNQKEATNTTSEPSAPSQDLLDLSPSPRMP | ||||||
Region | 392-395 | Interaction with GRB2 | ||||
Sequence: YDNF | ||||||
Motif | 421-425 | SH3-binding | ||||
Sequence: LPPLP | ||||||
Region | 442-445 | Interaction with PIK3R1 | ||||
Sequence: YEVM | ||||||
Motif | 460-463 | SH2-binding | ||||
Sequence: YEEI |
Sequence similarities
Belongs to the TOM1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O75674-1
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
- Length476
- Mass (Da)52,989
- Last updated2008-11-25 v2
- Checksum47ED5FA1F40144C0
O75674-2
- Name2
O75674-3
- Name3
- Differences from canonical
- 1-77: Missing
Computationally mapped potential isoform sequences
There are 13 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3KQU4 | J3KQU4_HUMAN | TOM1L1 | 465 | ||
I3NI44 | I3NI44_HUMAN | TOM1L1 | 326 | ||
K7EP47 | K7EP47_HUMAN | TOM1L1 | 125 | ||
I3L4N3 | I3L4N3_HUMAN | TOM1L1 | 122 | ||
I3L4G0 | I3L4G0_HUMAN | TOM1L1 | 199 | ||
I3L4I4 | I3L4I4_HUMAN | TOM1L1 | 469 | ||
I3L3T4 | I3L3T4_HUMAN | TOM1L1 | 225 | ||
I3L3M3 | I3L3M3_HUMAN | TOM1L1 | 92 | ||
I3L367 | I3L367_HUMAN | TOM1L1 | 229 | ||
I3L1T2 | I3L1T2_HUMAN | TOM1L1 | 38 | ||
I3L1Q1 | I3L1Q1_HUMAN | TOM1L1 | 106 | ||
I3L1G1 | I3L1G1_HUMAN | TOM1L1 | 252 | ||
I3L0N2 | I3L0N2_HUMAN | TOM1L1 | 63 |
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_057424 | 1-77 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 48 | in Ref. 1; CAA08993 | ||||
Sequence: G → A | ||||||
Compositional bias | 162-179 | Polar residues | ||||
Sequence: TARQETAQISSNPPTSVP | ||||||
Compositional bias | 298-318 | Polar residues | ||||
Sequence: KNQKEATNTTSEPSAPSQDLL | ||||||
Alternative sequence | VSP_056852 | 345-346 | in isoform 2 | |||
Sequence: NF → SK | ||||||
Alternative sequence | VSP_056853 | 347-476 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ010071 EMBL· GenBank· DDBJ | CAA08993.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315039 EMBL· GenBank· DDBJ | BAG37522.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315907 EMBL· GenBank· DDBJ | BAH14278.1 EMBL· GenBank· DDBJ | mRNA | ||
AK223125 EMBL· GenBank· DDBJ | BAD96845.1 EMBL· GenBank· DDBJ | mRNA | ||
AC007485 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC090824 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KC877665 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471109 EMBL· GenBank· DDBJ | EAW94551.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471109 EMBL· GenBank· DDBJ | EAW94553.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC029396 EMBL· GenBank· DDBJ | AAH29396.1 EMBL· GenBank· DDBJ | mRNA |