Q9UQ13 · SHOC2_HUMAN

  • Protein
    Leucine-rich repeat protein SHOC-2
  • Gene
    SHOC2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Regulatory subunit of protein phosphatase 1 (PP1c) that acts as a M-Ras/MRAS effector and participates in MAPK pathway activation. Upon M-Ras/MRAS activation, targets PP1c to specifically dephosphorylate the 'Ser-259' inhibitory site of RAF1 kinase and stimulate RAF1 activity at specialized signaling complexes.

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 Componentcytoplasm
Cellular Componentcytosol
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentprotein phosphatase type 1 complex
Molecular Functionprotein phosphatase 1 binding
Molecular Functionprotein phosphatase binding
Molecular Functionprotein phosphatase regulator activity
Biological Processcellular response to growth hormone stimulus
Biological Processcyclic-GMP-AMP transmembrane import across plasma membrane
Biological Processfibroblast growth factor receptor signaling pathway
Biological Processnegative regulation of neural precursor cell proliferation
Biological Processnegative regulation of neuron differentiation
Biological Processnerve growth factor signaling pathway
Biological Processpositive regulation of neuron differentiation
Biological Processpositive regulation of neuron projection development
Biological Processpositive regulation of Ras protein signal transduction
Biological ProcessRas protein signal transduction
Biological Processsignal transduction

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Leucine-rich repeat protein SHOC-2
  • Alternative names
    • Protein soc-2 homolog
    • Protein sur-8 homolog

Gene names

    • Name
      SHOC2
    • Synonyms
      KIAA0862

Organism names

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

Accessions

  • Primary accession
    Q9UQ13
  • Secondary accessions
    • A8K9W8
    • B3KR23
    • O76063
    • Q5VZS8
    • Q5VZS9

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
Note: Translocates from cytoplasm to nucleus upon growth factor stimulation.

Keywords

Disease & Variants

Involvement in disease

Noonan syndrome-like disorder with loose anagen hair 1 (NSLH1)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A syndrome characterized by Noonan dysmorphic features such as macrocephaly, high forehead, hypertelorism, palpebral ptosis, low-set and posteriorly rotated ears, short and webbed neck, pectus anomalies, in association with pluckable, sparse, thin and slow-growing hair.
  • See also
    MIM:607721
Natural variants in NSLH1
Variant IDPosition(s)ChangeDescription
VAR_0601992S>Gin NSLH1; creates a N-myristoylation site, resulting in myristoylation of the protein and aberrant targeting to the plasma membrane; dbSNP:rs267607048
VAR_074030173M>Iin NSLH1; significantly decreases ERK1/2 activity; does not affect cytoplasm and nucleus localization; does not affect SHOC2-MRAS-RAF1 complex assembly; impairs interaction with phosphatase 1c; dbSNP:rs730881020

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_0601992in NSLH1; creates a N-myristoylation site, resulting in myristoylation of the protein and aberrant targeting to the plasma membrane; dbSNP:rs267607048
Natural variantVAR_074030173in NSLH1; significantly decreases ERK1/2 activity; does not affect cytoplasm and nucleus localization; does not affect SHOC2-MRAS-RAF1 complex assembly; impairs interaction with phosphatase 1c; dbSNP:rs730881020

Variants

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

The viewer provides 450 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

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

TypeIDPosition(s)SourceDescription
ChainPRO_00000977371-582UniProtLeucine-rich repeat protein SHOC-2
Modified residue (large scale data)71PRIDEPhosphothreonine

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with M-Ras/MRAS, and RAF1 (PubMed:16630891, PubMed:25137548).
Forms a multiprotein complex with Ras (M-Ras/MRAS), Raf (RAF1) and protein phosphatase 1 (PPP1CA, PPP1CB and PPP1CC) (PubMed:16630891, PubMed:25137548).
Interacts with ERBIN; disrupts the interaction with RAF1 and Ras, leading to prevent activation of the Ras signaling pathway (PubMed:16301319).
Specifically binds K-Ras/KRAS, M-Ras/MRAS and N-Ras/NRAS but not H-Ras/HRAS (PubMed:9674433).
Interacts with LZTR1 (PubMed:30368668).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for compositional bias, region, repeat.

TypeIDPosition(s)Description
Compositional bias1-56Basic and acidic residues
Region1-88Disordered
Repeat101-122LRR 1
Repeat124-145LRR 2
Repeat147-169LRR 3
Repeat170-191LRR 4
Repeat193-214LRR 5
Repeat216-237LRR 6
Repeat239-260LRR 7
Repeat262-283LRR 8
Repeat285-307LRR 9
Repeat308-329LRR 10
Repeat332-353LRR 11
Repeat356-377LRR 12
Repeat380-400LRR 13
Repeat403-424LRR 14
Repeat426-448LRR 15
Repeat449-470LRR 16
Repeat472-494LRR 17
Repeat495-516LRR 18
Repeat518-540LRR 19
Repeat542-563LRR 20

Sequence similarities

Belongs to the SHOC2 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9UQ13-1

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
    582
  • Mass (Da)
    64,888
  • Last updated
    2001-06-20 v2
  • Checksum
    F3F828646642A855
MSSSLGKEKDSKEKDPKVPSAKEREKEAKASGGFGKESKEKEPKTKGKDAKDGKKDSSAAQPGVAFSVDNTIKRPNPAPGTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENSLTSLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCNLITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENNNISTLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTNNQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQIVAGGPSFIIQFLKMQGPYRAMV

Q9UQ13-2

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

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I5QJS4A0A8I5QJS4_HUMANSHOC2479
X6RI37X6RI37_HUMANSHOC2221
A0A8I5KUQ6A0A8I5KUQ6_HUMANSHOC2290
A0A8I5KUD9A0A8I5KUD9_HUMANSHOC2520

Sequence caution

The sequence BAA74885.2 differs from that shown. Reason: Erroneous initiation Extended N-terminus.
The sequence BAG52235.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

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

TypeIDPosition(s)Description
Compositional bias1-56Basic and acidic residues
Alternative sequenceVSP_038188234-279in isoform 2
Sequence conflict475in Ref. 4; BAF85522
Sequence conflict535in Ref. 3; BAA74885

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF068920
EMBL· GenBank· DDBJ
AAC39856.1
EMBL· GenBank· DDBJ
mRNA
AF054828
EMBL· GenBank· DDBJ
AAC25698.1
EMBL· GenBank· DDBJ
mRNA
AB020669
EMBL· GenBank· DDBJ
BAA74885.2
EMBL· GenBank· DDBJ
mRNA Different initiation
AK090820
EMBL· GenBank· DDBJ
BAG52235.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK292833
EMBL· GenBank· DDBJ
BAF85522.1
EMBL· GenBank· DDBJ
mRNA
AL158163
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471066
EMBL· GenBank· DDBJ
EAW49548.1
EMBL· GenBank· DDBJ
Genomic DNA
BC050445
EMBL· GenBank· DDBJ
AAH50445.1
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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