CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
90QGSQSPQKQEEQRQHubiquitination[1]
281AIRAELWKVLDVSDLubiquitination[1]
294DLESVTSKEIRQALEubiquitination[1]
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
 IPR014876; DEK_C.
 IPR000340; Dual-sp_phosphatase_cat-dom.
 IPR020422; Dual-sp_phosphatase_subgr_cat.
 IPR024950; DUSP.
 IPR009057; Homeodomain-like.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS. 
Pfam
 PF08766; DEK_C
 PF00782; DSPc 
SMART
 SM00195; DSPc 
PROSITE
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50054; TYR_PHOSPHATASE_DUAL 
PRINTS