SSH1
entrez
54434
canonical
uniprot
Q8WYL5
canonical
ensembl
ENSG00000084112
resolver
ensp
ENSP00000315713
resolver
ensp
ENSP00000326107
resolver
ensp
ENSP00000448824
resolver
genesymbol
SSH1
resolver
genesymbol_syn
KIAA1298
resolver
genesymbol_syn
SSH1L
resolver
hgnc
HGNC:30579
resolver
uniprot
Q6P6C0
resolver
uniprot
Q8N9A7
resolver
uniprot
Q8WYL3
resolver
uniprot
Q8WYL4
resolver
uniprot
Q9P2P8
resolver
uniprot_entry
SSH1_HUMAN
resolver
uniprot_sec
Q6P6C0
resolver
uniprot_sec
Q8N9A7
resolver
uniprot_sec
Q8WYL3
resolver
uniprot_sec
Q8WYL4
resolver
uniprot_sec
Q9P2P8
resolver
amino_acid_sequence
MALVTLQRSPTPSAASSSASNSELEAGSEEDRKLNLSLSESFFMVKGAALFLQQGSSPQGQRSLQHPHKHAGDLPQHLQVMINLLRCEDRIKLAVRLESAWADRVRYMVVVYSSGRQDTEENILLGVDFSSKESKSCTIGMVLRLWSDTKIHLDGDGGFSVSTAGRMHIFKPVSVQAMWSALQVLHKACEVARRHNYFPGGVALIWATYYESCISSEQSCINEWNAMQDLESTRPDSPALFVDKPTEGERTERLIKAKLRSIMMSQDLENVTSKEIRNELEKQMNCNLKELKEFIDNEMLLILGQMDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGILDASKQRHNKLWRQQTDSSLQQPVDDPAGPGDFLPETPDGTPESQLPFLDDAAQPGLGPPLPCCFRRLSDPLLPSPEDETGSLVHLEDPEREALLEEAAPPAEVHRPARQPQQGSGLCEKDVKKKLEFGSPKGRSGSLLQVEETEREEGLGAGRWGQLPTQLDQNLLNSENLNNNSKRSCPNGMEDDAIFGILNKVKPSYKSCADCMYPTASGAPEASRERCEDPNAPAICTQPAFLPHITSSPVAHLASRSRVPEKPASGPTEPPPFLPPAGSRRADTSGPGAGAALEPPASLLEPSRETPKVLPKSLLLKNSHCDKNPPSTEVVIKEESSPKKDMKPAKDLRLLFSNESEKPTTNSYLMQHQESIIQLQKAGLVRKHTKELERLKSVPADPAPPSRDGPASRLEASIPEESQDPAALHELGPLVMPSQAGSDEKSEAAPASLEGGSLKSPPPFFYRLDHTSSFSKDFLKTICYTPTSSSMSSNLTRSSSSDSIHSVRGKPGLVKQRTQEIETRLRLAGLTVSSPLKRSHSLAKLGSLTFSTEDLSSEADPSTVADSQDTTLSESSFLHEPQGTPRDPAATSKPSGKPAPENLKSPSWMSKS
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:11832213, ECO:0000269|PubMed:12684437, ECO:0000269|PubMed:12807904, ECO:0000269|PubMed:14531860, ECO:0000269|PubMed:14645219, ECO:0000269|PubMed:15056216, ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:16230460}.
uniprot
proteins
mass_dalton
115511
uniprot
proteins
mutagenesis
MUTAGEN 393; /note="C->S: Abrogates phosphatase activity."; /evidence="ECO:0000269|PubMed:11832213, ECO:0000269|PubMed:12684437, ECO:0000269|PubMed:12807904, ECO:0000269|PubMed:15056216, ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:16230460"; MUTAGEN 458; /note="W->A: Impairs stimulation of phosphatase activity by actin but does not affect basal activity."; /evidence="ECO:0000269|PubMed:16230460"; MUTAGEN 937; /note="S->A: Reduces binding to YWHAB, YWHAG, YWHAQ and YWHAZ. Abolishes binding to YWHAB, YWHAG, YWHAQ and YWHAZ and increases association with F-actin; when associated with A-978."; /evidence="ECO:0000269|PubMed:15159416"; MUTAGEN 978; /note="S->A: Reduces binding to YWHAB, YWHAG, YWHAQ and YWHAZ. Abolishes binding to YWHAB, YWHAG, YWHAQ and YWHAZ and increases association with F-actin; when associated with A-937."; /evidence="ECO:0000269|PubMed:15159416
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Inhibitory phosphorylation by PAK4 promotes binding to YWHAZ. Phosphorylation at Ser-978 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. {ECO:0000269|PubMed:12807904, ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:15671020}.
uniprot
proteins
protein_family
Protein-tyrosine phosphatase family
uniprot
proteins
pubmed
10718198
uniprot
proteins
pubmed
11832213
uniprot
proteins
pubmed
12684437
uniprot
proteins
pubmed
12807904
uniprot
proteins
pubmed
14531860
uniprot
proteins
pubmed
14645219
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15056216
uniprot
proteins
pubmed
15159416
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15660133
uniprot
proteins
pubmed
15671020
uniprot
proteins
pubmed
16230460
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
sequence_length
1049
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cleavage furrow. Midbody. Note=Also recruited to actin rich membrane protrusions such as lamellipodia, which may allow local control of actin dynamics at sites of cell locomotion. Also localized to the cleavage furrow and the midbody during cytokinesis.
uniprot
proteins