Ssh1
entrez
231637
canonical
uniprot
Q76I79
canonical
ensembl
ENSMUSG00000042121
resolver
ensp
ENSMUSP00000076873
resolver
ensp
ENSMUSP00000107917
resolver
ensp
ENSMUSP00000124312
resolver
enst
ENSMUST00000077689
resolver
genesymbol
Ssh1
resolver
genesymbol_syn
Kiaa1298
resolver
genesymbol_syn
Ssh1l
resolver
uniprot
F8WHT2
resolver
uniprot
Q3TDG3
resolver
uniprot
Q69ZM4
resolver
uniprot
Q811E5
resolver
uniprot_entry
F8WHT2_MOUSE
resolver
uniprot_entry
SSH1_MOUSE
resolver
uniprot_sec
Q3TDG3
resolver
uniprot_sec
Q69ZM4
resolver
uniprot_sec
Q811E5
resolver
amino_acid_sequence
MALVTLQRSPTPSAASSSASNSELEAGSDEERKLNLSLSESFFMVKGAALFLQQGNSPQGQRSLQHPHKHAGDLPQHLQVMINLLRCEDRIKLAVRLESVWTDRVRYMVVVYTSGRQDTEENILLGVDFSSKESKSCTIGMVLRLWSDTKIHLDGDGGFSVSTAGRMHIFKPVSVQAMWSALQVLHKACEVARRHNYFPGGVALIWATYYESCISSEQSCINEWNAMQDLESTRPDSPALFVDKPTEGERTERLIKAKLRSIMMSQDLENVTSKEIRNELEKQMNCNLKEFKEFIDNEMLLILGQMDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGILDASKQRHNKLWRQQPTDDTIAEPSEFLPETLDGALDAQLPCLDDTTHPGLPRSLAPGGPALPCCFRRLSDPLLLPHHDETGGLVHLEDLEKDALLEEEESQPVEVHKLVQHPQEGARLCEKDVKRKLEFGNSKPRSDSLPQVEELEKDGSPRTGRWRRASTQLDRSLLDQENLNNNNSKRSCPDDLERDAMFGILSKVKPPYTSCADCMYPTAGGTPEAYMERHEDPSSSAICTQPTFLPHVTSSPMAHASSRSRAPERPASGPANTSPFLLPAGSRKPDVSGSGAGAAPEPPASLLEPSRETSKALPKSLQLKNPHCDKNAANMEVSAKEEPSPKKDPKPAKDLRLLFSNEAEKPTTNSYLMQHQESIIQLQKAGLVRKHTKELERLKSLPSDSPAACRDSATCRLEASIPEEGSQEPAHPALCSQAGSEEQPVGGTLQKSPTSTLPRLDHTSNFSKDFLKTVCYTPTSSSISSNLTRSSSSDSIHSVRGKPGLVKQRAQEIETRLRLAGLTVSSPLKRSHSLAKLGSLNFSTEDLSSEADTSTIADSQDAKCGLSSSFLPEPQSAPRDPAATSKSSGKSAPEHLKSPSRVNKS
uniprot
proteins
ec_number
3.1.3.16
uniprot
proteins
ec_number
3.1.3.48
uniprot
proteins
function
FUNCTION: Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein. {ECO:0000269|PubMed:14531860}.
uniprot
proteins
mass_dalton
115297
uniprot
proteins
mutagenesis
MUTAGEN 393; /note="C->S: Abrogates phosphatase activity."; /evidence="ECO:0000269|PubMed:14531860
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Inhibitory phosphorylation by PAK4 promotes binding to YWHAZ. Phosphorylation at Ser-970 is decreased by stimuli which promote actin reorganization and lamellipodia formation. Can be dephosphorylated and activated by PPP3CA/calcineurin A. Phosphorylation decreases immediately prior to telophase (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
Protein-tyrosine phosphatase family
uniprot
proteins
pubmed
14531860
uniprot
proteins
pubmed
15368895
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15660133
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
1042
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14531860}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Note=Localized to the cleavage furrow and the midbody during cytokinesis (By similarity). Also colocalizes with F-actin in the cytoplasm and the cell periphery, which may allow local control of actin dynamics at sites of cell locomotion. {ECO:0000250}.
uniprot
proteins