CYLD_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CYLD_MOUSE
• UniProt AC: Q80TQ2
• Protein Name: Ubiquitin carboxyl-terminal hydrolase CYLD
• Gene Name: Cyld
• Organism: Mus musculus (Mouse).
• Sequence Length: 952
• 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. Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation. Negative regulator of Wnt signaling. Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules. Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis. Required for normal cell cycle progress and normal cytokinesis. 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. Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells. Negatively regulates TNFRSF11A signaling and osteoclastogenesis. 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. [PubMed: 25134987 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: MSSGLWSQEKVTSPYWEERIFYLLLQECSVTDKQTQKLLKVPKGSIGQYIQDRSVGHSRVPSTKGKKNQIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERLSLFRNRLRLSKGLQVDVGSPVKVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDNGLESDFAGPGDTMQVEPPPLEINSRVSLKVGESTESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFASVESTILLHINDIIPDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQQSKSKNPWYIDEVAEDPAKSLTEMSSDFGHSSPPPQPPSMNSLSSENRFHSLPFSLTKMPNTNGSMAHSPLSLSVQSVMGELNSTPVQESPPLPISSGNAHGLEVGSLAEVKENPPFYGVIRWIGQPPGLSDVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSALDTVLLRPKEKNDIEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHDILRVEPLLKIRSAGQKVQDCNFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCSTQVHLHPRRLNHSYHPVSLPKDLPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK

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	------MSSGLWSQE ------CCCCCCCCC	32.87	28066266
3	Phosphorylation	-----MSSGLWSQEK -----CCCCCCCCCC	36.28	28066266
7	Phosphorylation	-MSSGLWSQEKVTSP -CCCCCCCCCCCCCC	33.24	25338131
12	Phosphorylation	LWSQEKVTSPYWEER CCCCCCCCCCHHHHH	34.74	28066266
13	Phosphorylation	WSQEKVTSPYWEERI CCCCCCCCCHHHHHH	20.98	25266776
15	Phosphorylation	QEKVTSPYWEERIFY CCCCCCCHHHHHHHH	25.81	18515860
129	Phosphorylation	GLQVDVGSPVKVQLR CCCCCCCCCEEEEEC	26.77	28066266
328	Phosphorylation	RGVGDKGSSSHNKPK CCCCCCCCCCCCCCC	34.11	21183079
337	O-linked_Glycosylation	SHNKPKVTGSTSDPG CCCCCCCCCCCCCCC	31.38	30016717
339	Phosphorylation	NKPKVTGSTSDPGSR CCCCCCCCCCCCCCC	18.51	29899451
340	Phosphorylation	KPKVTGSTSDPGSRN CCCCCCCCCCCCCCC	38.19	30482847
341	Phosphorylation	PKVTGSTSDPGSRNR CCCCCCCCCCCCCCH	43.43	25521595
345	O-linked_Glycosylation	GSTSDPGSRNRSELF CCCCCCCCCCHHHEE	31.60	30016717
349	Phosphorylation	DPGSRNRSELFYTLN CCCCCCHHHEEEEEC	42.05	29899451
358	Phosphorylation	LFYTLNGSSVDSQQS EEEEECCCCCCCCCC	26.56	29550500
359	Phosphorylation	FYTLNGSSVDSQQSK EEEECCCCCCCCCCC	31.20	28973931
383	Phosphorylation	VAEDPAKSLTEMSSD HHCCHHHHHHHHCCC	42.50	26643407
385	Phosphorylation	EDPAKSLTEMSSDFG CCHHHHHHHHCCCCC	36.41	26643407
388	Phosphorylation	AKSLTEMSSDFGHSS HHHHHHHCCCCCCCC	22.11	26643407
389	Phosphorylation	KSLTEMSSDFGHSSP HHHHHHCCCCCCCCC	35.33	26643407
394	Phosphorylation	MSSDFGHSSPPPQPP HCCCCCCCCCCCCCC	44.94	25266776
395	Phosphorylation	SSDFGHSSPPPQPPS CCCCCCCCCCCCCCC	35.43	25266776
402	Phosphorylation	SPPPQPPSMNSLSSE CCCCCCCCCCCCCCC	36.96	29472430
414	Phosphorylation	SSENRFHSLPFSLTK CCCCCCCCCCCCCEE	34.72	26824392
418	Phosphorylation	RFHSLPFSLTKMPNT CCCCCCCCCEECCCC	32.94	21082442
420	Phosphorylation	HSLPFSLTKMPNTNG CCCCCCCEECCCCCC	24.89	21082442
543	Phosphorylation	RPDSRFASLQPVSNQ CCCCCCCCCCCCCHH	25.48	30352176
548	Phosphorylation	FASLQPVSNQIERCN CCCCCCCCHHHHHHH	29.69	30352176
556	Phosphorylation	NQIERCNSLAFGGYL HHHHHHHHHCCCCHH	25.38	29899451
623	Ubiquitination	VLLRPKEKNDIEYYS HHCCCCCCCCCCCHH	67.08	22790023
623 (in isoform 2)	Ubiquitination	-	67.08	22790023
626 (in isoform 2)	Ubiquitination	-	5.25	-
717	Ubiquitination	FYQIFMEKNEKVGVP CCHHHHHCCCCCCCC	59.63	22790023
717 (in isoform 2)	Ubiquitination	-	59.63	22790023
720 (in isoform 2)	Ubiquitination	-	54.40	-
915	Phosphorylation	VGEYLKMSLEDLHSL HHHHHHCCHHHHHHC	27.33	26370283

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
414	S	Phosphorylation	Kinase	IKBKE	Q14164	GPS

Functions of PTM Sites

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

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SQSTM_MOUSE	Sqstm1	physical	18382763
SQSTM_MOUSE	Sqstm1	physical	18174161
RIPK1_MOUSE	Ripk1	physical	17981138
ITCH_MOUSE	Itch	physical	22057290
FOS_MOUSE	Fos	physical	21478324
JUN_MOUSE	Jun	physical	21478324
NEMO_MOUSE	Ikbkg	physical	22037414
ITCH_MOUSE	Itch	physical	23782702
NEMO_MOUSE	Ikbkg	physical	23825957
UBC_HUMAN	UBC	physical	18174161
RIPK2_MOUSE	Ripk2	physical	26834734

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND MASSSPECTROMETRY.
PubMed: 19367708