dbPTM

CUL2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CUL2_MOUSE
UniProt AC	Q9D4H8
Protein Name	Cullin-2
Gene Name	Cul2
Organism	Mus musculus (Mouse).
Sequence Length	745
Subcellular Localization
Protein Description	Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. ECS complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins (By similarity). May serve as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the ECS complex depends on the substrate recognition component. ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF) (By similarity)..
Protein Sequence	MSLKPRVVDFDETWNKLLTTIKAVVMLEYVERATWNDRFSDIYALCVAYPEPLGERLYAETKIFLESHVRHLYKRVLESEEQVLVMYHRYWEEYSKGADYMDCLYRYLNTQYIKKNKLTEADIQYGYGGVDMNEPLMEIGELALDMWRKLMVEPLQNILIRMLLREIKNDRGGEDPNQKVIHGVINSFVHVEQYKKKFPLKFYQGIFVSPFLTETGEYYKQEASNLLQESNCSQYMEKVLGRLKDEEIRCRKYLHPSSYTKVIHECQQRMVADHLQFLHSECHSIIQQERKNDMANMYVLLRAVSSGLPHMIEELQKHIHDEGLRATSNLTQEHMPTLFVESVLEVHGKFVQLINTVLNGDQHFMSALDKALTSVVNYREPKSVCKAPELLAKYCDNLLKKSAKGMTENEVEDKLTSFITVFKYIDDKDVFQKFYARMLAKRLIHGLSMSMDSEEAMINKLKQACGYEFTSKLHRMYTDMSVSADLNNKFNNFIRNQDTVIDLGISFQIYVLQAGAWPLTQAPSSTFAIPQELEKSVQMFELFYSQHFSGRKLTWLHYLCTGEVKMNYLGKPYVAMVTTYQMAVLLAFNNSETVSYKELQDSTQMNEKELTKTIKSLLDVKMINHDSEKEDIDAESSFSLNMSFSSKRTKFKITTSMQKDTPQELEQTRSAVDEDRKMYLQAAIVRIMKARKVLRHNALIQEVISQSRARFNPSISMIKKCIEVLIDKQYIERSQASADEYSYVA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Ubiquitination	DFDETWNKLLTTIKA CCHHHHHHHHHHHHH	36.11	-
107	Phosphorylation	YMDCLYRYLNTQYIK HHHHHHHHHCHHHHH	7.25	28576409
110	Phosphorylation	CLYRYLNTQYIKKNK HHHHHHCHHHHHHCC	21.83	28576409
112	Phosphorylation	YRYLNTQYIKKNKLT HHHHCHHHHHHCCCC	16.81	28576409
114	Ubiquitination	YLNTQYIKKNKLTEA HHCHHHHHHCCCCHH	45.41	-
238	Ubiquitination	NCSQYMEKVLGRLKD CHHHHHHHHHHHHCH	26.65	-
270	Oxidation	IHECQQRMVADHLQF HHHHHHHHHHHHHHH	2.24	17203969
284	Phosphorylation	FLHSECHSIIQQERK HHHHHHHHHHHHHHH	32.80	17203969
291	Ubiquitination	SIIQQERKNDMANMY HHHHHHHHHHHHHHH	57.45	-
382	Acetylation	VVNYREPKSVCKAPE HCCCCCCHHHCCCHH	51.25	19849299
382	Ubiquitination	VVNYREPKSVCKAPE HCCCCCCHHHCCCHH	51.25	-
393	Ubiquitination	KAPELLAKYCDNLLK CCHHHHHHHHHHHHH	46.51	-
393	Acetylation	KAPELLAKYCDNLLK CCHHHHHHHHHHHHH	46.51	23806337
394	Phosphorylation	APELLAKYCDNLLKK CHHHHHHHHHHHHHH	10.22	17203969
404	Ubiquitination	NLLKKSAKGMTENEV HHHHHHHCCCCHHHH	57.20	27667366
428	Ubiquitination	VFKYIDDKDVFQKFY HHHHCCCHHHHHHHH	52.63	-
433	Ubiquitination	DDKDVFQKFYARMLA CCHHHHHHHHHHHHH	28.95	-
602	Phosphorylation	SYKELQDSTQMNEKE CHHHHHCCCCCCHHH	13.95	25338131
603	Phosphorylation	YKELQDSTQMNEKEL HHHHHCCCCCCHHHH	39.88	25338131
608	Ubiquitination	DSTQMNEKELTKTIK CCCCCCHHHHHHHHH	53.68	-
611	Phosphorylation	QMNEKELTKTIKSLL CCCHHHHHHHHHHHH	27.51	25338131
613	Phosphorylation	NEKELTKTIKSLLDV CHHHHHHHHHHHHCH	28.53	25338131
616	Phosphorylation	ELTKTIKSLLDVKMI HHHHHHHHHHCHHCC	30.25	22006019
661	Phosphorylation	TTSMQKDTPQELEQT EECCCCCCHHHHHHH	33.63	-

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 CUL2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CUL2_MOUSE !!

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 CUL2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CUL2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of CUL2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284 AND TYR-394, ANDMASS SPECTROMETRY.	17203969 [Abstract]