CDN1C_HUMAN - dbPTM
CDN1C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDN1C_HUMAN
UniProt AC P49918
Protein Name Cyclin-dependent kinase inhibitor 1C
Gene Name CDKN1C
Organism Homo sapiens (Human).
Sequence Length 316
Subcellular Localization Nucleus.
Protein Description Potent tight-binding inhibitor of several G1 cyclin/CDK complexes (cyclin E-CDK2, cyclin D2-CDK4, and cyclin A-CDK2) and, to lesser extent, of the mitotic cyclin B-CDC2. Negative regulator of cell proliferation. May play a role in maintenance of the non-proliferative state throughout life..
Protein Sequence MSDASLRSTSTMERLVARGTFPVLVRTSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFYRETVQVGRCRLLLAPRPVAVAVAVSPPLEPAAESLDGLEEAPEQLPSVPVPAPASTPPPVPVLAPAPAPAPAPVAAPVAAPVAVAVLAPAPAPAPAPAPAPAPVAAPAPAPAPAPAPAPAPAPAPDAAPQESAEQGANQGQRGQEPLADQLHSGISGRPAAGTAAASANGAAIKKLSGPLISDFFAKRKRSAPEKSSGDVPAPCPSPSAAPGVGSVEQTPRKRLR
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 Orthologous
Protein Cluster
27PhosphorylationTFPVLVRTSACRSLF
CCCEEEECHHHHHHH
17.1324719451
43PhosphorylationPVDHEELSRELQARL
CCCHHHHHHHHHHHH
27.3024719451
107MethylationCRLLLAPRPVAVAVA
EEEEECCCCEEEEEE
32.49-
266AcetylationANGAAIKKLSGPLIS
CCCHHHHHHHCCHHH
41.6030591107
268PhosphorylationGAAIKKLSGPLISDF
CHHHHHHHCCHHHHH
47.4418669648
275UbiquitinationSGPLISDFFAKRKRS
HCCHHHHHHHHCCCC
5.2521963094
278AcetylationLISDFFAKRKRSAPE
HHHHHHHHCCCCCCC
53.9824468109
282PhosphorylationFFAKRKRSAPEKSSG
HHHHCCCCCCCCCCC
51.73-
286UbiquitinationRKRSAPEKSSGDVPA
CCCCCCCCCCCCCCC
49.1921963094
286PhosphorylationRKRSAPEKSSGDVPA
CCCCCCCCCCCCCCC
49.1933259812
287PhosphorylationKRSAPEKSSGDVPAP
CCCCCCCCCCCCCCC
37.5827251275
288PhosphorylationRSAPEKSSGDVPAPC
CCCCCCCCCCCCCCC
50.5126552605
297PhosphorylationDVPAPCPSPSAAPGV
CCCCCCCCCCCCCCC
37.9025159151
299PhosphorylationPAPCPSPSAAPGVGS
CCCCCCCCCCCCCCC
41.2127050516
306PhosphorylationSAAPGVGSVEQTPRK
CCCCCCCCCCCCCCH
21.7826552605
310PhosphorylationGVGSVEQTPRKRLR-
CCCCCCCCCCHHCC-
16.1412925736

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
282SPhosphorylationKinaseAKT1P31749
PSP
310TPhosphorylationKinaseAKT1P31749
PSP
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:12925736
-KUbiquitinationE3 ubiquitin ligaseFBXL12Q9NXK8
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDN1C_HUMAN !!

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 CDN1C_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LIMK1_HUMANLIMK1physical
14530263
SKP2_HUMANSKP2physical
12925736
PCNA_HUMANPCNAphysical
9465025
MYOD1_HUMANMYOD1physical
10764802
CCND1_HUMANCCND1physical
10764802
CCNE2_HUMANCCNE2physical
9840943
AKT1_HUMANAKT1physical
23421998
CSN5_HUMANCOPS5physical
26606000
CCND1_HUMANCCND1physical
10713702
CDN1C_HUMANCDKN1Cphysical
10713702
CDK4_HUMANCDK4physical
10713702

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
130650Beckwith-Wiedemann syndrome (BWS)
614732Intrauterine growth retardation, metaphyseal dysplasia, adrenal hypoplasia congenita, and genital anomalies (IMAGE)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDN1C_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASSSPECTROMETRY.

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