Q9UQ13 · SHOC2_HUMAN
- ProteinLeucine-rich repeat protein SHOC-2
- GeneSHOC2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids582 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 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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Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLeucine-rich repeat protein SHOC-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UQ13
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Involvement in disease
Noonan syndrome-like disorder with loose anagen hair 1 (NSLH1)
- Note
- DescriptionA 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 alsoMIM:607721
Natural variants in NSLH1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_060199 | 2 | S>G | in NSLH1; creates a N-myristoylation site, resulting in myristoylation of the protein and aberrant targeting to the plasma membrane; dbSNP:rs267607048 | |
VAR_074030 | 173 | M>I | in 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_060199 | 2 | in NSLH1; creates a N-myristoylation site, resulting in myristoylation of the protein and aberrant targeting to the plasma membrane; dbSNP:rs267607048 | |||
Sequence: S → G | ||||||
Natural variant | VAR_074030 | 173 | in 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 | |||
Sequence: M → I |
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.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000097737 | 1-582 | UniProt | Leucine-rich repeat protein SHOC-2 | |||
Sequence: MSSSLGKEKDSKEKDPKVPSAKEREKEAKASGGFGKESKEKEPKTKGKDAKDGKKDSSAAQPGVAFSVDNTIKRPNPAPGTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENSLTSLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCNLITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENNNISTLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTNNQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQIVAGGPSFIIQFLKMQGPYRAMV | |||||||
Modified residue (large scale data) | 71 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Proteomic databases
PTM databases
Expression
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-56 | Basic and acidic residues | ||||
Sequence: MSSSLGKEKDSKEKDPKVPSAKEREKEAKASGGFGKESKEKEPKTKGKDAKDGKKD | ||||||
Region | 1-88 | Disordered | ||||
Sequence: MSSSLGKEKDSKEKDPKVPSAKEREKEAKASGGFGKESKEKEPKTKGKDAKDGKKDSSAAQPGVAFSVDNTIKRPNPAPGTRKKSSNA | ||||||
Repeat | 101-122 | LRR 1 | ||||
Sequence: NSMRLDLSKRSIHILPSSIKEL | ||||||
Repeat | 124-145 | LRR 2 | ||||
Sequence: QLTELYLYSNKLQSLPAEVGCL | ||||||
Repeat | 147-169 | LRR 3 | ||||
Sequence: NLMTLALSENSLTSLPDSLDNLK | ||||||
Repeat | 170-191 | LRR 4 | ||||
Sequence: KLRMLDLRHNKLREIPSVVYRL | ||||||
Repeat | 193-214 | LRR 5 | ||||
Sequence: SLTTLYLRFNRITTVEKDIKNL | ||||||
Repeat | 216-237 | LRR 6 | ||||
Sequence: KLSMLSIRENKIKQLPAEIGEL | ||||||
Repeat | 239-260 | LRR 7 | ||||
Sequence: NLITLDVAHNQLEHLPKEIGNC | ||||||
Repeat | 262-283 | LRR 8 | ||||
Sequence: QITNLDLQHNELLDLPDTIGNL | ||||||
Repeat | 285-307 | LRR 9 | ||||
Sequence: SLSRLGLRYNRLSAIPRSLAKCS | ||||||
Repeat | 308-329 | LRR 10 | ||||
Sequence: ALEELNLENNNISTLPESLLSS | ||||||
Repeat | 332-353 | LRR 11 | ||||
Sequence: KLNSLTLARNCFQLYPVGGPSQ | ||||||
Repeat | 356-377 | LRR 12 | ||||
Sequence: TIYSLNMEHNRINKIPFGIFSR | ||||||
Repeat | 380-400 | LRR 13 | ||||
Sequence: VLSKLNMKDNQLTSLPLDFGT | ||||||
Repeat | 403-424 | LRR 14 | ||||
Sequence: SMVELNLATNQLTKIPEDVSGL | ||||||
Repeat | 426-448 | LRR 15 | ||||
Sequence: SLEVLILSNNLLKKLPHGLGNLR | ||||||
Repeat | 449-470 | LRR 16 | ||||
Sequence: KLRELDLEENKLESLPNEIAYL | ||||||
Repeat | 472-494 | LRR 17 | ||||
Sequence: DLQKLVLTNNQLTTLPRGIGHLT | ||||||
Repeat | 495-516 | LRR 18 | ||||
Sequence: NLTHLGLGENLLTHLPEEIGTL | ||||||
Repeat | 518-540 | LRR 19 | ||||
Sequence: NLEELYLNDNPNLHSLPFELALC | ||||||
Repeat | 542-563 | LRR 20 | ||||
Sequence: KLSIMSIENCPLSHLPPQIVAG |
Sequence similarities
Belongs to the SHOC2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- Length582
- Mass (Da)64,888
- Last updated2001-06-20 v2
- ChecksumF3F828646642A855
Q9UQ13-2
- Name2
- Differences from canonical
- 234-279: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5QJS4 | A0A8I5QJS4_HUMAN | SHOC2 | 479 | ||
X6RI37 | X6RI37_HUMAN | SHOC2 | 221 | ||
A0A8I5KUQ6 | A0A8I5KUQ6_HUMAN | SHOC2 | 290 | ||
A0A8I5KUD9 | A0A8I5KUD9_HUMAN | SHOC2 | 520 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-56 | Basic and acidic residues | ||||
Sequence: MSSSLGKEKDSKEKDPKVPSAKEREKEAKASGGFGKESKEKEPKTKGKDAKDGKKD | ||||||
Alternative sequence | VSP_038188 | 234-279 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 475 | in Ref. 4; BAF85522 | ||||
Sequence: K → E | ||||||
Sequence conflict | 535 | in Ref. 3; BAA74885 | ||||
Sequence: F → L |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |