Tag | Content |
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CPLM ID | CPLM-018055 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein phosphatase Slingshot homolog 3 |
Protein Synonyms/Alias | SSH-like protein 3; SSH-3L; hSSH-3L |
Gene Name | SSH3 |
Gene Synonyms/Alias | SSH3L |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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90 | QGSQSPQKQEEQRQH | ubiquitination | [1] | 281 | AIRAELWKVLDVSDL | ubiquitination | [1] | 294 | DLESVTSKEIRQALE | ubiquitination | [1] |
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Reference | [1] Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP. Mol Cell. 2011 Oct 21;44(2):325-40. [ PMID: 21906983] |
Functional Description | Protein phosphatase which may play a role in the regulation of actin filament dynamics. Can dephosphorylate and activate the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly (By similarity). |
Sequence Annotation | DOMAIN 328 468 Tyrosine-protein phosphatase. ACT_SITE 413 413 Phosphocysteine intermediate (By MOD_RES 7 7 Phosphoserine (By similarity). MOD_RES 9 9 Phosphoserine (By similarity). MOD_RES 37 37 Phosphoserine (By similarity). MOD_RES 85 85 Phosphoserine. MOD_RES 87 87 Phosphoserine. MOD_RES 649 649 Phosphoserine (By similarity). |
Keyword | Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Hydrolase; Nucleus; Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 659 AA |
Protein Sequence | MALVTVSRSP PGSGASTPVG PWDQAVQRRS RLQRRQSFAV LRGAVLGLQD GGDNDDAAEA 60 SSEPTEKAPS EEELHGDQTD FGQGSQSPQK QEEQRQHLHL MVQLLRPQDD IRLAAQLEAP 120 RPPRLRYLLV VSTREGEGLS QDETVLLGVD FPDSSSPSCT LGLVLPLWSD TQVYLDGDGG 180 FSVTSGGQSR IFKPISIQTM WATLQVLHQA CEAALGSGLV PGGSALTWAS HYQERLNSEQ 240 SCLNEWTAMA DLESLRPPSA EPGGSSEQEQ MEQAIRAELW KVLDVSDLES VTSKEIRQAL 300 ELRLGLPLQQ YRDFIDNQML LLVAQRDRAS RIFPHLYLGS EWNAANLEEL QRNRVTHILN 360 MAREIDNFYP ERFTYHNVRL WDEESAQLLP HWKETHRFIE AARAQGTHVL VHCKMGVSRS 420 AATVLAYAMK QYECSLEQAL RHVQELRPIA RPNPGFLRQL QIYQGILTAS RQSHVWEQKV 480 GGVSPEEHPA PEVSTPFPPL PPEPEGGGEE KVVGMEESQA APKEEPGPRP RINLRGVMRS 540 ISLLEPSLEL ESTSETSDMP EVFSSHESSH EEPLQPFPQL ARTKGGQQVD RGPQPALKSR 600 QSVVTLQGSA VVANRTQAFQ EQEQGQGQGQ GEPCISSTPR FRKVVRQASV HDSGEEGEA 659 |
Gene Ontology | GO:0005737; C:cytoplasm; IBA:RefGenome. GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0003779; F:actin binding; IBA:RefGenome. GO:0003677; F:DNA binding; IEA:InterPro. GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC. GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IBA:RefGenome. GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC. GO:0008064; P:regulation of actin polymerization or depolymerization; IBA:RefGenome. GO:0050770; P:regulation of axonogenesis; IBA:RefGenome. GO:0010591; P:regulation of lamellipodium assembly; IBA:RefGenome. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |