I3L1I8 · I3L1I8_HUMAN
- ProteinSerine/arginine repetitive matrix 2
- GeneSRRM2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids297 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score1/5
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 | nuclear speck |
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Taxonomic lineagecellular organisms > Eukaryota (eucaryotes) > Opisthokonta > Metazoa (metazoans) > Eumetazoa > Bilateria > Deuterostomia > Chordata (chordates) > Craniata > Vertebrata (vertebrates) > Gnathostomata (jawed vertebrates) > Teleostomi > Euteleostomi (bony vertebrates) > Sarcopterygii > Dipnotetrapodomorpha > Tetrapoda (tetrapods) > Amniota (amniotes) > Mammalia (mammals) > Theria > Eutheria (placentals) > Boreoeutheria > Euarchontoglires > Primates > Haplorrhini > Simiiformes > Catarrhini > Hominoidea (apes) > Hominidae (great apes) > Homininae > Homo
Accessions
- Primary accessionI3L1I8
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 411 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) | 15 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 48 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 49 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 54 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 81 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 86 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 152 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 155 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 190 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 192 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 193 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 199 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 201 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 204 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 215 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 219 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 220 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 221 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 222 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 226 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 227 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 230 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 232 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 236 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 237 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 250 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 252 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 257 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 261 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 262 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 263 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 271 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-25 | Disordered | ||||
Sequence: MLLEKDVNPGGKEETPGQRPAVTET | ||||||
Region | 45-297 | Disordered | ||||
Sequence: ISDSYVDGSSFDPQRRAREAKQPAPEPPKPYSLVRESSSSRSPTPKQKKKKKKKDRGRRSESSSPRRERKKSSKKKKHRSESESKKRKHRSPTPKSKRKSKDKKRKRSRSTTPAPKSRRAHRSTSADSASSSDTSRSRSRSAAAKTHTTALAGRSPSPASGRRGEGDAPFSEPGTTSTQRPSSPETATKQPSSPYEDKDKDKKEKSATRPSPSPERSSTGPEPPAPTPLLAERHGGSPQPLATTPLSQEPVNP | ||||||
Compositional bias | 113-160 | Basic residues | ||||
Sequence: RKKSSKKKKHRSESESKKRKHRSPTPKSKRKSKDKKRKRSRSTTPAPK | ||||||
Compositional bias | 168-199 | Polar residues | ||||
Sequence: TSADSASSSDTSRSRSRSAAAKTHTTALAGRS | ||||||
Compositional bias | 215-235 | Polar residues | ||||
Sequence: SEPGTTSTQRPSSPETATKQP | ||||||
Compositional bias | 236-254 | Basic and acidic residues | ||||
Sequence: SSPYEDKDKDKKEKSATRP |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length297
- Mass (Da)32,590
- Last updated2012-07-11 v1
- Checksum3056F1C21201F3CF
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q9UQ35 | SRRM2_HUMAN | SRRM2 | 2752 | ||
I3L4U6 | I3L4U6_HUMAN | SRRM2 | 78 | ||
I3L4D8 | I3L4D8_HUMAN | SRRM2 | 1018 | ||
I3L3Q8 | I3L3Q8_HUMAN | SRRM2 | 1187 | ||
A0A087X1W1 | A0A087X1W1_HUMAN | SRRM2 | 251 | ||
I3L182 | I3L182_HUMAN | SRRM2 | 895 | ||
I3L0N7 | I3L0N7_HUMAN | SRRM2 | 115 | ||
A0A994J493 | A0A994J493_HUMAN | SRRM2 | 176 |
Features
Showing features for compositional bias, non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 113-160 | Basic residues | ||||
Sequence: RKKSSKKKKHRSESESKKRKHRSPTPKSKRKSKDKKRKRSRSTTPAPK | ||||||
Compositional bias | 168-199 | Polar residues | ||||
Sequence: TSADSASSSDTSRSRSRSAAAKTHTTALAGRS | ||||||
Compositional bias | 215-235 | Polar residues | ||||
Sequence: SEPGTTSTQRPSSPETATKQP | ||||||
Compositional bias | 236-254 | Basic and acidic residues | ||||
Sequence: SSPYEDKDKDKKEKSATRP | ||||||
Non-terminal residue | 297 | |||||
Sequence: P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC092117 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |