I3L1I8 · I3L1I8_HUMAN

  • Protein
    Serine/arginine repetitive matrix 2
  • Gene
    SRRM2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    1/5

Function

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnuclear speck

Names & Taxonomy

Subcellular Location

Disease & Variants

Variants

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The viewer provides 411 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue (large scale data)15PRIDEPhosphothreonine
Modified residue (large scale data)46PRIDEPhosphoserine
Modified residue (large scale data)48PRIDEPhosphoserine
Modified residue (large scale data)49PRIDEPhosphotyrosine
Modified residue (large scale data)54PRIDEPhosphoserine
Modified residue (large scale data)81PRIDEPhosphoserine
Modified residue (large scale data)86PRIDEPhosphoserine
Modified residue (large scale data)152PRIDEPhosphoserine
Modified residue (large scale data)155PRIDEPhosphothreonine
Modified residue (large scale data)190PRIDEPhosphothreonine
Modified residue (large scale data)192PRIDEPhosphothreonine
Modified residue (large scale data)193PRIDEPhosphothreonine
Modified residue (large scale data)199PRIDEPhosphoserine
Modified residue (large scale data)201PRIDEPhosphoserine
Modified residue (large scale data)204PRIDEPhosphoserine
Modified residue (large scale data)215PRIDEPhosphoserine
Modified residue (large scale data)219PRIDEPhosphothreonine
Modified residue (large scale data)220PRIDEPhosphothreonine
Modified residue (large scale data)221PRIDEPhosphoserine
Modified residue (large scale data)222PRIDEPhosphothreonine
Modified residue (large scale data)226PRIDEPhosphoserine
Modified residue (large scale data)227PRIDEPhosphoserine
Modified residue (large scale data)230PRIDEPhosphothreonine
Modified residue (large scale data)232PRIDEPhosphothreonine
Modified residue (large scale data)236PRIDEPhosphoserine
Modified residue (large scale data)237PRIDEPhosphoserine
Modified residue (large scale data)250PRIDEPhosphoserine
Modified residue (large scale data)252PRIDEPhosphothreonine
Modified residue (large scale data)255PRIDEPhosphoserine
Modified residue (large scale data)257PRIDEPhosphoserine
Modified residue (large scale data)261PRIDEPhosphoserine
Modified residue (large scale data)262PRIDEPhosphoserine
Modified residue (large scale data)263PRIDEPhosphothreonine
Modified residue (large scale data)271PRIDEPhosphothreonine

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-25Disordered
Region45-297Disordered
Compositional bias113-160Basic residues
Compositional bias168-199Polar residues
Compositional bias215-235Polar residues
Compositional bias236-254Basic and acidic residues

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    297
  • Mass (Da)
    32,590
  • Last updated
    2012-07-11 v1
  • Checksum
    3056F1C21201F3CF
MLLEKDVNPGGKEETPGQRPAVTETHQLAELNEKKNERLRAAFGISDSYVDGSSFDPQRRAREAKQPAPEPPKPYSLVRESSSSRSPTPKQKKKKKKKDRGRRSESSSPRRERKKSSKKKKHRSESESKKRKHRSPTPKSKRKSKDKKRKRSRSTTPAPKSRRAHRSTSADSASSSDTSRSRSRSAAAKTHTTALAGRSPSPASGRRGEGDAPFSEPGTTSTQRPSSPETATKQPSSPYEDKDKDKKEKSATRPSPSPERSSTGPEPPAPTPLLAERHGGSPQPLATTPLSQEPVNP

Computationally mapped potential isoform sequences

There are 8 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q9UQ35SRRM2_HUMANSRRM22752
I3L4U6I3L4U6_HUMANSRRM278
I3L4D8I3L4D8_HUMANSRRM21018
I3L3Q8I3L3Q8_HUMANSRRM21187
A0A087X1W1A0A087X1W1_HUMANSRRM2251
I3L182I3L182_HUMANSRRM2895
I3L0N7I3L0N7_HUMANSRRM2115
A0A994J493A0A994J493_HUMANSRRM2176

Features

Showing features for compositional bias, non-terminal residue.

TypeIDPosition(s)Description
Compositional bias113-160Basic residues
Compositional bias168-199Polar residues
Compositional bias215-235Polar residues
Compositional bias236-254Basic and acidic residues
Non-terminal residue297

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC092117
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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