CYLD_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CYLD_RAT
• UniProt AC: Q66H62
• Protein Name: Ubiquitin carboxyl-terminal hydrolase CYLD
• Gene Name: Cyld
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 953
• Subcellular Localization: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane ; Peripheral membrane protein ; Cytoplasmic side . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Cytoplasm, cytoskel
• Protein Description: Deubiquitinase that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Has endodeubiquitinase activity. Plays an important role in the regulation of pathways leading to NF-kappa-B activation (By similarity). Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation (By similarity). Negative regulator of Wnt signaling (By similarity). Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules (By similarity). Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis (By similarity). Required for normal cell cycle progress and normal cytokinesis (By similarity). Inhibits nuclear translocation of NF-kappa-B (By similarity). Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (By similarity). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells (By similarity). Negatively regulates TNFRSF11A signaling and osteoclastogenesis (By similarity). Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (By similarity). Also able to remove linear ('Met-1'-linked) polyubiquitin chains to regulate innate immunity: recruited to the LUBAC complex and, together with OTULIN, restricts linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (By similarity)..
• Protein Sequence: MSSGLWNQEKVTSPYWEERLFYLLLQECSVTDKQTQKLLRVPKGSIGQYIQDRSVGHSRVPSAKGKKNQIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERLSLFRNRIRLSKGLQVDVGSPVRVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDNGLESDFAGPGDTVQVEPPPLEINSRVSLKVGESTESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFASVESTVLLHINDIIPDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQQQSKSKNPWYIDEVAEDPAKSLTEMSSDFGHSSPPPQPPSMNSLSSENRFHSLPFSLTKMPNTNGSMAHSPLSLSVQSVMGELNSTPVQESPPMPSSSGNAHGLEVGSLAEVKENPPFYGVIRWIGQPPGLSDVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSALDTVLLRPKEKNDVEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHDILRVEPLLKIRSAGQKVQDCNFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCSTQVHLHPRRLNHTYHPVSLPKDLPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSGLWNQE ------CCCCCCCCC	32.87	23984901
3	Phosphorylation	-----MSSGLWNQEK -----CCCCCCCCCC	36.28	23984901
12	Phosphorylation	LWNQEKVTSPYWEER CCCCCCCCCCHHHHH	34.74	22108457
13	Phosphorylation	WNQEKVTSPYWEERL CCCCCCCCCHHHHHH	20.98	22108457
15	Phosphorylation	QEKVTSPYWEERLFY CCCCCCCHHHHHHHH	25.81	-
43	Ubiquitination	QKLLRVPKGSIGQYI HHHHCCCCCCHHHHC	63.53	-
121	Ubiquitination	RNRIRLSKGLQVDVG HHHHHHCCCCCCCCC	69.13	-
181	Phosphorylation	QGFTDGVYQGKQLFQ CCCCCCCCCCCEEEE	19.65	-
339	Phosphorylation	NKPKVTGSTSDPGSR CCCCCCCCCCCCCCC	18.51	25403869
340	Phosphorylation	KPKVTGSTSDPGSRN CCCCCCCCCCCCCCC	38.19	25403869
341	Phosphorylation	PKVTGSTSDPGSRNR CCCCCCCCCCCCCCH	43.43	25403869
384	Phosphorylation	VAEDPAKSLTEMSSD HHCCHHHHHHHHCCC	42.50	-
415	Phosphorylation	SSENRFHSLPFSLTK CCCCCCCCCCCCCEE	34.72	28432305
419	Phosphorylation	RFHSLPFSLTKMPNT CCCCCCCCCEECCCC	32.94	22673903
421	Phosphorylation	HSLPFSLTKMPNTNG CCCCCCCEECCCCCC	24.89	22673903
544	Phosphorylation	RPDSRFASLQPVSNQ CCCCCCCCCCCCCHH	25.48	25575281
549	Phosphorylation	FASLQPVSNQIERCN CCCCCCCCHHHHHHH	29.69	25575281

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

Oops, there are no upstream regulatory protein records of CYLD_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CYLD_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CYLD_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of CYLD_RAT !!

Drug and Disease Associations

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