dbPTM

CDN1B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDN1B_MOUSE
UniProt AC	P46414
Protein Name	Cyclin-dependent kinase inhibitor 1B
Gene Name	Cdkn1b
Organism	Mus musculus (Mouse).
Sequence Length	197
Subcellular Localization	Nucleus. Cytoplasm. Endosome . Nuclear and cytoplasmic in quiescent cells. AKT- or RSK-mediated phosphorylation on Thr-197, binds 14-3-3, translocates to the cytoplasm and promotes cell cycle progression. Mitogen-activated UHMK1 phosphorylation on Se
Protein Description	Important regulator of cell cycle progression. [PubMed: 8033213]
Protein Sequence	MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVNHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGRYEWQEVERGSLPEFYYRPPRPPKSACKVLAQESQDVSGSRQAVPLIGSQANSEDRHLVDQMPDSSDNPAGLAEQCPGMRKRPAAEDSSSQNKRANRTEENVSDGSPNAGTVEQTPKKPGLRRQT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSNVRVSNG ------CCCCCCCCC	43.99	26160508
7	Phosphorylation	-MSNVRVSNGSPSLE -CCCCCCCCCCCCHH	25.55	25521595
10	Phosphorylation	NVRVSNGSPSLERMD CCCCCCCCCCHHHHH	18.63	27087446
12	Phosphorylation	RVSNGSPSLERMDAR CCCCCCCCHHHHHHH	44.55	28973931
42	Phosphorylation	PVNHEELTRDLEKHC CCCHHHHHHHHHHHH	25.97	-
74	Phosphorylation	HKPLEGRYEWQEVER CCCCCCCCEEEEEHH	32.17	-
83	Phosphorylation	WQEVERGSLPEFYYR EEEEHHCCCCCEECC	47.15	22817900
88	Phosphorylation	RGSLPEFYYRPPRPP HCCCCCEECCCCCCC	9.26	21423214
89	Phosphorylation	GSLPEFYYRPPRPPK CCCCCEECCCCCCCH	23.20	-
100	Acetylation	RPPKSACKVLAQESQ CCCHHHHHHHHHHCC	39.74	22826441
106	Phosphorylation	CKVLAQESQDVSGSR HHHHHHHCCCCCCCC	21.43	25521595
110	Phosphorylation	AQESQDVSGSRQAVP HHHCCCCCCCCCCCC	39.06	28066266
112	Phosphorylation	ESQDVSGSRQAVPLI HCCCCCCCCCCCCCC	17.45	28066266
125	Phosphorylation	LIGSQANSEDRHLVD CCCCCCCCCCCCHHH	43.84	28973931
138	Phosphorylation	VDQMPDSSDNPAGLA HHCCCCCCCCCCHHH	48.22	28507225
170	Phosphorylation	QNKRANRTEENVSDG HHHHCCCCCCCCCCC	47.67	25619855
175	Phosphorylation	NRTEENVSDGSPNAG CCCCCCCCCCCCCCC	48.08	25619855
178	Phosphorylation	EENVSDGSPNAGTVE CCCCCCCCCCCCCCC	21.70	23527152
183	Phosphorylation	DGSPNAGTVEQTPKK CCCCCCCCCCCCCCC	20.61	25619855
187	Phosphorylation	NAGTVEQTPKKPGLR CCCCCCCCCCCCCCC	24.46	25168779
197	Phosphorylation	KPGLRRQT------- CCCCCCCC-------	38.47	22139837

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
10	S	Phosphorylation	Kinase	UHMK1	P97343	Uniprot
10	S	Phosphorylation	Kinase	DYR1B	Q9Z188	PhosphoELM
10	S	Phosphorylation	Kinase	CDK5	P49615	PSP
10	S	Phosphorylation	Kinase	AKT1	P31749	PSP
12	S	Phosphorylation	Kinase	IKKA	Q60680	PSP
42	T	Phosphorylation	Kinase	IKKA	Q60680	PSP
74	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
83	S	Phosphorylation	Kinase	PRKAA1	P54645	GPS
88	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
88	Y	Phosphorylation	Kinase	LYN	P25911	Uniprot
88	Y	Phosphorylation	Kinase	JAK2	Q62120	Uniprot
88	Y	Phosphorylation	Kinase	ABL	P00520	Uniprot
170	T	Phosphorylation	Kinase	PRKAA1	P54645	GPS
170	T	Phosphorylation	Kinase	CAMK1	Q91YS8	Uniprot
170	T	Phosphorylation	Kinase	CAMK1	Q14012	GPS
175	S	Phosphorylation	Kinase	IKKA	Q60680	PSP
178	S	Phosphorylation	Kinase	IKKA	Q60680	PSP
183	T	Phosphorylation	Kinase	IKKA	Q60680	PSP
183	T	Phosphorylation	Kinase	CHUK	O15111	GPS
187	T	Phosphorylation	Kinase	CDK5	P49615	PSP
187	T	Phosphorylation	Kinase	CDK2	P97377	Uniprot
187	T	Phosphorylation	Kinase	CDK1	P11440	Uniprot
187	T	Phosphorylation	Kinase	AKT1	P31750	Uniprot
197	T	Phosphorylation	Kinase	AMPKA1	Q13131	PSP
197	T	Phosphorylation	Kinase	CAMK1	Q14012	GPS
197	T	Phosphorylation	Kinase	PRKAA1	P54645	GPS
197	T	Phosphorylation	Kinase	CAMK1	Q91YS8	Uniprot
197	T	Phosphorylation	Kinase	RPS6KA1	P18653	Uniprot
197	T	Phosphorylation	Kinase	RPS6KA3	P18654	Uniprot
197	T	Phosphorylation	Kinase	PIM1	P06803	Uniprot
197	T	Phosphorylation	Kinase	AKT1	P31750	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Rchy1	Q9CR50	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Rnf123	Q5XPI3	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Skp2	Q9Z0Z3	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
10	S	Phosphorylation	9399644
Phosphorylation on Ser-10 is the major site of phosphorylation in resting cells, takes place at the G(0)-G(1) phase and leads to protein stability.
187	T	Phosphorylation	9399644
Dephosphorylated on Thr-187 by PPM1H, leading to CDKN1B stability (By similarity).
187	T	Phosphorylation	9399644
Phosphorylation on Thr-187, by CDK1 and CDK2 leads to protein ubiquitination and proteasomal degradation.
187	T	Phosphorylation	9399644
The latter requires prior phosphorylation on Thr-187.
187	T	ubiquitylation	9399644
Phosphorylation on Thr-187, by CDK1 and CDK2 leads to protein ubiquitination and proteasomal degradation.
197	T	Phosphorylation	23707388
Phosphorylation on Thr-197 is required for interaction with 14-3-3 proteins.

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 CDN1B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NUP50_MOUSE	Nup50	physical	10811608
CCNA2_MOUSE	Ccna2	physical	8822197
CCNE1_MOUSE	Ccne1	physical	8822197
CCND3_RAT	Ccnd3	physical	8822197
CDK4_MOUSE	Cdk4	physical	8822197
CDK2_MOUSE	Cdk2	physical	8822197
CDK6_MOUSE	Cdk6	physical	8822197
CSN5_MOUSE	Cops5	physical	10086358
SKP1_MOUSE	Skp1a	physical	10585767
CSN5_MOUSE	Cops5	physical	11704659
CCND1_MOUSE	Ccnd1	physical	8033213
CCND2_MOUSE	Ccnd2	physical	8033213
CCND3_MOUSE	Ccnd3	physical	8033213
CDK4_MOUSE	Cdk4	physical	8033213
CCNE1_MOUSE	Ccne1	physical	8033213
CDK2_MOUSE	Cdk2	physical	22898779

Drug and Disease Associations

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

Regulatory Network of CDN1B_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Role of serine 10 phosphorylation in p27 stabilization revealed byanalysis of p27 knock-in mice harboring a serine 10 mutation."; Kotake Y., Nakayama K., Ishida N., Nakayama K.I.; J. Biol. Chem. 280:1095-1102(2005). Cited for: PHOSPHORYLATION AT SER-10, FUNCTION, AND MUTAGENESIS OF SER-10.	15528185 [Abstract]
"A growth factor-dependent nuclear kinase phosphorylates p27(Kip1) andregulates cell cycle progression."; Boehm M., Yoshimoto T., Crook M.F., Nallamshetty S., True A.,Nabel G.J., Nabel E.G.; EMBO J. 21:3390-3401(2002). Cited for: INTERACTION WITH UHMK1, FUNCTION, SUBCELLULAR LOCATION, ANDPHOSPHORYLATION AT SER-10.	12093740 [Abstract]
"Cdk2-dependent phosphorylation of p27 facilitates its Myc-inducedrelease from cyclin E/cdk2 complexes."; Mueller D., Bouchard C., Rudolph B., Steiner P., Stuckmann I.,Saffrich R., Ansorge W., Huttner W., Eilers M.; Oncogene 15:2561-2576(1997). Cited for: PHOSPHORYLATION AT THR-187, INTERACTION WITH CCNE1 IN CCNE1/CDK2/CDKN1B COMPLEX, FUNCTION, AND MUTAGENESIS OF SER-10 AND THR-187.	9399644 [Abstract]

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