dbPTM

LTN1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LTN1_SCHPO
UniProt AC	O74349
Protein Name	E3 ubiquitin-protein ligase listerin
Gene Name	rkr1 {ECO:0000312\|PomBase:SPBC21D10.09c}
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	1610
Subcellular Localization	Nucleus. Cytoplasm .
Protein Description	E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Ubiquitination leads to cdc48 recruitment for extraction and degradation of the incomplete translation product..
Protein Sequence	MKKKSTDLYGRKNPGMQSMSGSFSSLQIALDESSSNFSTIYEPPDLSGLDAEMIVIVKNLQKRDIVTKCRALQDLIQWNDPSQFDNEQFLNALAVLFPRLSIEVERHVRLKIFVFMSVLSSALQKKLAPWLKFYITPWVMGFFDSDRAVSVSAKDSFKNLLSEEKWPHVWLKFGSTIAPIVTDVFLHEDKESLTDLRFFSNEEAESKVTRVKSSCLLTLSFLFKQTADLENLETDKKIDKQTFKSSLYENLSTLFKSDEFWSLVSSPQDGVTVSLSDLLLIILKYDKPFVTQYKEKYFKRVSRMISRLTSLTCVPMLRLLSNMISNFPNEVHQFANDSKRPLSKLFSNLITKRISLPNSGFYTSLLNLFKSIGAMQLVPSIESVDELCDAFLETANQEQRFLSTEVYDCLLNFLSFVYTDSSDPQIKDHVRDRLRTIFTRYFKGEFVLRCSTSDFDHCLQSVFDKNSDFASLWNEVLFGFFNDESMDIETIPFDSLSRNLSLTVQTVLYLKNRNFQTGNEVMSILGPCLSFLMKLSTHKNERIACLSASQLITVCHIFSDTTLIKPVKELFQKYLVNDLPSSILKLGPQSPAFTLLRDILLLLKDYADLSEPWENVANQFTVSFDELENIRVLNSLPSLFADGKLRGKISLVKTLVEYYDTAVFAIMQNPGNDWDMIRACIGSKEILVPEETIKNILFTTLEYFLTNDWVDNHLIILCASLHSLKAHLPTIFDENKSLYSLLPVILFSKPEDDGHVAAHFESIFSLLKEKALEDSGFSLKLCSEVQEWSLNKVLNGSINEKLAADKCVLVFNSFGKLPSNFFTFPASFWDAKISSCIPFFSNKLFIDQDFILGFLDLVASEPINVDMTDVGTQFVHIFHASLYTLYYVETTGCDGDALFNLTFAYLLIRIYLQNGIQSIIDVPIRDAGIFVESFECYFKGEVVKFMRDKDALTVLNELLIDDIDGKMPVLFKRFKNLSSAENTTSFSIFAAQGLTDFLIVVSNLLEMDEKHVDVVLGKLGLSSSKSPIFVSSILEGLKPLEVDSEIIQRIRFKAVNDLTGKLHSANEVSKSLLILNAATTQQITEKPLLPITRCRLFLENITNWCSESGIKSLELLPVCCFLRFMYYFLPTVFSLSGSYWNSIFDYIKYAMKMSVVDAPIVKSFELFALRLYNALSKNYEMNSDIKDCIVESNESMNYLLLKRFLFTHESTLRNSVTARMCNQYLVKLLENCPGKVVRSFQYQEFFPSLCNSNDLQMESVCMKFLREKLSHELKELTVYYMVESDYEPDVSLCPELLSLAIDFPGDPFVMVSKMEKYEHALRVYLLVWDLIFYHFEETTYNIKLSIINQLHAMDLLRPLLNTLVEILNLSYDRPINVDKYPKIDYNLMDYSSATDRIRCLAIHIYYQCLRHLSSSVRSYWSEVKNRAFTSTVESFTGYNVSPLLISASLDDVERSIESEDFQSVGDVNVKVNRNTREISFIYNVDEHKLEMAIKIPSVYPLQNVQVEGIERVGVNERQWRSWILASQSILSSQNGSITDALLVLKKNISMHFEGVEECAICYSVLSVERTLPNKRCGTCRHKFHASCLYKWFKSSNSSRCPLCRSSFTFV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
245	Phosphorylation	IDKQTFKSSLYENLS CCHHHHHHHHHHHHH	22.76	25720772
246	Phosphorylation	DKQTFKSSLYENLST CHHHHHHHHHHHHHH	35.24	25720772

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of LTN1_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LTN1_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of LTN1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
MEU23_SCHPO	meu23	physical	26771498

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LTN1_SCHPO

Related Literatures of Post-Translational Modification