CIP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CIP1_HUMAN
• UniProt AC: Q9NPC3
• Protein Name: E3 ubiquitin-protein ligase CCNB1IP1
• Gene Name: CCNB1IP1
• Organism: Homo sapiens (Human).
• Sequence Length: 277
• Subcellular Localization: Nucleus. Chromosome. Associates to the synaptonemal complex.
• Protein Description: Ubiquitin E3 ligase that acts as a limiting factor for crossing-over during meiosis: required during zygonema to limit the colocalization of RNF212 with MutS-gamma-associated recombination sites and thereby establish early differentiation of crossover and non-crossover sites. Later, it is directed by MutL-gamma to stably accumulate at designated crossover sites. Probably promotes the dissociation of RNF212 and MutS-gamma to allow the progression of recombination and the implementation of the final steps of crossing over (By similarity). Modulates cyclin-B levels and participates in the regulation of cell cycle progression through the G2 phase. Overexpression causes delayed entry into mitosis.; E3 ubiquitin-protein ligase. Modulates cyclin B levels and participates in the regulation of cell cycle progression through the G2 phase. Overexpression causes delayed entry into mitosis..
• Protein Sequence: MSLCEDMLLCNYRKCRIKLSGYAWVTACSHIFCDQHGSGEFSRSPAICPACNSTLSGKLDIVRTELSPSEEYKAMVLAGLRPEIVLDISSRALAFWTYQVHQERLYQEYNFSKAEGHLKQMEKIYTQQIQSKDVELTSMKGEVTSMKKVLEEYKKKFSDISEKLMERNRQYQKLQGLYDSLRLRNITIANHEGTLEPSMIAQSGVLGFPLGNNSKFPLDNTPVRNRGDGDGDFQFRPFFAGSPTAPEPSNSFFSFVSPSRELEQQQVSSRAFKVKRI

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
125	Phosphorylation	LKQMEKIYTQQIQSK HHHHHHHHHHHHHCC	15.01	22817900
132	Ubiquitination	YTQQIQSKDVELTSM HHHHHHCCCCCHHHC	49.79	2190698
153	Phosphorylation	MKKVLEEYKKKFSDI HHHHHHHHHHHHHHH	20.80	29396449
154	Ubiquitination	KKVLEEYKKKFSDIS HHHHHHHHHHHHHHH	53.41	-
158	Phosphorylation	EEYKKKFSDISEKLM HHHHHHHHHHHHHHH	42.80	23403867
161	Phosphorylation	KKKFSDISEKLMERN HHHHHHHHHHHHHHH	33.40	23403867
178	Phosphorylation	YQKLQGLYDSLRLRN HHHHHHHHHHHHHCC	15.43	17322306
180	Phosphorylation	KLQGLYDSLRLRNIT HHHHHHHHHHHCCCE	11.22	-
221	Phosphorylation	SKFPLDNTPVRNRGD CCCCCCCCCCCCCCC	23.87	23403867
257	Phosphorylation	NSFFSFVSPSRELEQ CCCCCCCCCCHHHHH	18.36	12612082
259	Phosphorylation	FFSFVSPSRELEQQQ CCCCCCCCHHHHHHH	30.77	12612082

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
-	K	Ubiquitination	E3 ubiquitin ligase	CCNB1IP1	Q9NPC3	PMID:12612082

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CIP1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CIP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CIP1_HUMAN	CCNB1IP1	physical	16189514
MERL_HUMAN	NF2	physical	16532029
A4_HUMAN	APP	physical	21832049
CCNB1_HUMAN	CCNB1	physical	12612082
UB2L3_HUMAN	UBE2L3	physical	12612082
CIP1_HUMAN	CCNB1IP1	physical	12612082
CIP1_HUMAN	CCNB1IP1	physical	25416956
H13_HUMAN	HIST1H1D	physical	26186194
EPMIP_HUMAN	EPM2AIP1	physical	21516116
H13_HUMAN	HIST1H1D	physical	28514442

Drug and Disease Associations

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