C9JUT4 · C9JUT4_HUMAN
- ProteinLIM domain containing preferred translocation partner in lipoma
- GeneLPP
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids428 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
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 | focal adhesion | |
Molecular Function | metal ion binding |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionC9JUT4
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 695 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 12 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 135 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 149 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 151 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 156 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 244 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 273 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 275 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 296 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 297 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 300 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 301 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 307 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 313 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 316 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 317 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 325 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 333 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 346 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 354 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-118 | Disordered | ||||
Sequence: MSHPSWLPPKSTGEPLGHVPARMETTHSFGNPSISVSTQQPPKKFAPVVAPKPKYNPYKQPGGEGDFLPPPPPPLDDSSALPSISGNFPPPPPLDEEAFKVQGNPGGKTLEERRSSLD | ||||||
Compositional bias | 26-42 | Polar residues | ||||
Sequence: THSFGNPSISVSTQQPP | ||||||
Compositional bias | 64-78 | Pro residues | ||||
Sequence: EGDFLPPPPPPLDDS | ||||||
Region | 132-266 | Disordered | ||||
Sequence: ECSSPYKPRPPQSSTGSTASPPVSTPVTGHKRMVIPNQPPLTATKKSTLKPQPAPQAGPIPVAPIGTLKPQPQPVPASYTTASTSSRPTFNVQVKSAQPSPHYMAAPSSGQIYGSGPQGYNTQPVPVSGQCPPPS | ||||||
Compositional bias | 138-156 | Polar residues | ||||
Sequence: KPRPPQSSTGSTASPPVST | ||||||
Compositional bias | 185-202 | Pro residues | ||||
Sequence: APQAGPIPVAPIGTLKPQ | ||||||
Compositional bias | 204-257 | Polar residues | ||||
Sequence: QPVPASYTTASTSSRPTFNVQVKSAQPSPHYMAAPSSGQIYGSGPQGYNTQPVP | ||||||
Region | 307-390 | Disordered | ||||
Sequence: YGGRNDSDPTYGQQGHPNTWKREPGYTPPGAGNQNPPGMYPVTGPKKTYITDPVSAPCAPPLQPKGGHSGQLGPSSVAPSFRPE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length428
- Mass (Da)45,346
- Last updated2009-11-03 v1
- ChecksumC91D546862FDA7B9
Computationally mapped potential isoform sequences
There are 12 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q93052 | LPP_HUMAN | LPP | 612 | ||
C9J5C8 | C9J5C8_HUMAN | LPP | 111 | ||
C9J2R5 | C9J2R5_HUMAN | LPP | 52 | ||
C9J1K7 | C9J1K7_HUMAN | LPP | 93 | ||
C9J4E3 | C9J4E3_HUMAN | LPP | 151 | ||
C9J3U9 | C9J3U9_HUMAN | LPP | 66 | ||
C9JXK9 | C9JXK9_HUMAN | LPP | 252 | ||
C9JT42 | C9JT42_HUMAN | LPP | 65 | ||
C9JIY7 | C9JIY7_HUMAN | LPP | 57 | ||
C9JE51 | C9JE51_HUMAN | LPP | 46 | ||
A0AA34QW10 | A0AA34QW10_HUMAN | LPP | 212 | ||
A0A087WZF1 | A0A087WZF1_HUMAN | LPP | 590 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 26-42 | Polar residues | ||||
Sequence: THSFGNPSISVSTQQPP | ||||||
Compositional bias | 64-78 | Pro residues | ||||
Sequence: EGDFLPPPPPPLDDS | ||||||
Compositional bias | 138-156 | Polar residues | ||||
Sequence: KPRPPQSSTGSTASPPVST | ||||||
Compositional bias | 185-202 | Pro residues | ||||
Sequence: APQAGPIPVAPIGTLKPQ | ||||||
Compositional bias | 204-257 | Polar residues | ||||
Sequence: QPVPASYTTASTSSRPTFNVQVKSAQPSPHYMAAPSSGQIYGSGPQGYNTQPVP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC009319 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC022498 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC055711 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC063932 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC069226 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC069430 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC117507 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF457718 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF510228 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471052 EMBL· GenBank· DDBJ | EAW78132.1 EMBL· GenBank· DDBJ | Genomic DNA |