Q2M3G4 · SHRM1_HUMAN

  • Protein
    Protein Shroom1
  • Gene
    SHROOM1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

May be involved in the assembly of microtubule arrays during cell elongation.

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 Componentadherens junction
Cellular Componentapical junction complex
Cellular Componentapical plasma membrane
Cellular Componentcortical actin cytoskeleton
Cellular Componentmicrotubule
Molecular Functionactin filament binding
Molecular Functionmyosin II binding
Biological Processactin filament bundle assembly
Biological Processcell morphogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein Shroom1
  • Alternative names
    • Apical protein 2

Gene names

    • Name
      SHROOM1
    • Synonyms
      APXL2, KIAA1960

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q2M3G4
  • Secondary accessions
    • B7WP40
    • B7ZL01
    • Q8TDP0
    • Q8TF41

Proteomes

Organism-specific databases

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_032061180in dbSNP:rs2292030

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,182 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue, chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue1UniProtN-acetylmethionine
ChainPRO_00002860611-852UniProtProtein Shroom1
Modified residue (large scale data)12PRIDEPhosphoserine
Modified residue18UniProtPhosphoserine
Modified residue (large scale data)40PRIDEPhosphoserine
Modified residue (large scale data)49PRIDEPhosphoserine
Modified residue (large scale data)62PRIDEPhosphotyrosine
Modified residue (large scale data)82PRIDEPhosphoserine
Modified residue103UniProtPhosphothreonine
Modified residue (large scale data)103PRIDEPhosphothreonine
Modified residue133UniProtPhosphoserine
Modified residue (large scale data)133PRIDEPhosphoserine
Modified residue137UniProtPhosphoserine
Modified residue166UniProtPhosphoserine
Modified residue (large scale data)166PRIDEPhosphoserine
Modified residue (large scale data)186PRIDEPhosphoserine
Modified residue (large scale data)188PRIDEPhosphoserine
Modified residue190UniProtPhosphoserine
Modified residue224UniProtPhosphoserine
Modified residue (large scale data)224PRIDEPhosphoserine
Modified residue (large scale data)302PRIDEPhosphoserine
Modified residue (large scale data)304PRIDEPhosphoserine
Modified residue (large scale data)363PRIDEPhosphoserine
Modified residue (large scale data)364PRIDEPhosphoserine
Modified residue (large scale data)401PRIDEPhosphoserine
Modified residue (large scale data)408PRIDEPhosphoserine
Modified residue (large scale data)515PRIDEPhosphothreonine
Modified residue (large scale data)735PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with F-actin.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region34-54Disordered
Region81-109Disordered
Region125-218Disordered
Domain145-233ASD1
Region276-320Disordered
Region399-431Disordered
Compositional bias464-495Polar residues
Region464-496Disordered
Domain543-825ASD2
Region823-852Disordered
Compositional bias830-852Pro residues

Domain

The ASD1 domain mediates F-actin binding.

Sequence similarities

Belongs to the shroom family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q2M3G4-1

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.

  • Length
    852
  • Mass (Da)
    90,786
  • Last updated
    2006-02-21 v1
  • Checksum
    43DFAF54E8355877
MEALGPGGDRASPASSTSSLDLWHLSMRADSAYSSFSAASGGPEPRTQSPGTDLLPYLDWDYVRVVWGGPGPAPPDAALCTSPRPRPAVAARSGPQPTEVPGTPGPLNRQATPLLYALAAEAEAAAQAAEPPSPPASRAAYRQRLQGAQRRVLRETSFQRKELRMSLPARLRPTVPARPPATHPRSASLSHPGGEGEPARSRAPAPGTAGRGPLANQQRKWCFSEPGKLDRVGRGGGPARECLGEACSSSGLPGPEPLEFQHPALAKFEDHEVGWLPETQPQGSMNLDSGSLKLGDAFRPASRSRSASGEVLGSWGGSGGTIPIVQAVPQGAETPRPLFQTKLSRFLPQKEAAVMYPAELPQSSPADSEQRVSETCIVPAWLPSLPDEVFLEEAPLVRMRSPPDPHASQGPPASVHASDQPYGTGLGQRTGQVTVPTEYPLHECPGTAGADDCWQGVNGSVGISRPTSHTPTGTANDNIPTIDPTGLTTNPPTAAESDLLKPVPADALGLSGNDTPGPSHNTALARGTGQPGSRPTWPSQCLEELVQELARLDPSLCDPLASQPSPEPPLGLLDGLIPLAEVRAAMRPACGEAGEEAASTFEPGSYQFSFTQLLPAPREETRLENPATHPVLDQPCGQGLPAPNNSIQGKKVELAARLQKMLQDLHTEQERLQGEAQAWARRQAALEAAVRQACAPQELERFSRFMADLERVLGLLLLLGSRLARVRRALARAASDSDPDEQASLLQRLRLLQRQEEDAKELKEHVARRERAVREVLVRALPVEELRVYCALLAGKAAVLAQQRNLDERIRLLQDQLDAIRDDLGHHAPSPSPARPPGTCPPVQPPFPLLLT

Q2M3G4-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9JXU1C9JXU1_HUMANSHROOM1324
A6NN40A6NN40_HUMANSHROOM1783

Sequence caution

The sequence BAB85546.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for sequence conflict, compositional bias, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict129in Ref. 1; AAM15526
Compositional bias464-495Polar residues
Alternative sequenceVSP_024962742-746in isoform 2
Compositional bias830-852Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF314142
EMBL· GenBank· DDBJ
AAM15526.1
EMBL· GenBank· DDBJ
mRNA
AB075840
EMBL· GenBank· DDBJ
BAB85546.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AC004775
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471062
EMBL· GenBank· DDBJ
EAW62311.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471062
EMBL· GenBank· DDBJ
EAW62312.1
EMBL· GenBank· DDBJ
Genomic DNA
BC104914
EMBL· GenBank· DDBJ
AAI04915.1
EMBL· GenBank· DDBJ
mRNA
BC104916
EMBL· GenBank· DDBJ
AAI04917.1
EMBL· GenBank· DDBJ
mRNA
BC143494
EMBL· GenBank· DDBJ
AAI43495.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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