CCND3_HUMAN - dbPTM
CCND3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCND3_HUMAN
UniProt AC P30281
Protein Name G1/S-specific cyclin-D3
Gene Name CCND3
Organism Homo sapiens (Human).
Sequence Length 292
Subcellular Localization Nucleus . Cytoplasm . Membrane . Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated to the nucleus through interaction with KIP/CIP family members..
Protein Description Regulatory component of the cyclin D3-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D3/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex..
Protein Sequence MELLCCEGTRHAPRAGPDPRLLGDQRVLQSLLRLEERYVPRASYFQCVQREIKPHMRKMLAYWMLEVCEEQRCEEEVFPLAMNYLDRYLSCVPTRKAQLQLLGAVCMLLASKLRETTPLTIEKLCIYTDHAVSPRQLRDWEVLVLGKLKWDLAAVIAHDFLAFILHRLSLPRDRQALVKKHAQTFLALCATDYTFAMYPPSMIATGSIGAAVQGLGACSMSGDELTELLAGITGTEVDCLRACQEQIEAALRESLREASQTSSSPAPKAPRGSSSQGPSQTSTPTDVTAIHL
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
9PhosphorylationELLCCEGTRHAPRAG
CEEECCCCCCCCCCC		9.29-
30PhosphorylationGDQRVLQSLLRLEER
CCHHHHHHHHHHHHH		25.8024719451
38PhosphorylationLLRLEERYVPRASYF
HHHHHHHHCCCHHHH		20.3426657352
43PhosphorylationERYVPRASYFQCVQR
HHHCCCHHHHHHHHH		27.9726657352
123UbiquitinationTTPLTIEKLCIYTDH
CCCCEEHHHHHHCCC		44.82-
133PhosphorylationIYTDHAVSPRQLRDW
HHCCCCCCHHHCCCC		18.3624719451
169PhosphorylationAFILHRLSLPRDRQA
HHHHHHCCCCHHHHH		35.9624719451
259PhosphorylationRESLREASQTSSSPA
HHHHHHHHHCCCCCC		29.2828450419
261PhosphorylationSLREASQTSSSPAPK
HHHHHHHCCCCCCCC		28.2528450419
262PhosphorylationLREASQTSSSPAPKA
HHHHHHCCCCCCCCC		22.6029255136
263PhosphorylationREASQTSSSPAPKAP
HHHHHCCCCCCCCCC		43.6729255136
264PhosphorylationEASQTSSSPAPKAPR
HHHHCCCCCCCCCCC		25.5029255136
273PhosphorylationAPKAPRGSSSQGPSQ
CCCCCCCCCCCCCCC		28.2628851738
274PhosphorylationPKAPRGSSSQGPSQT
CCCCCCCCCCCCCCC		29.5122617229
275PhosphorylationKAPRGSSSQGPSQTS
CCCCCCCCCCCCCCC		40.6328851738
279PhosphorylationGSSSQGPSQTSTPTD
CCCCCCCCCCCCCCC		53.5722617229
281PhosphorylationSSQGPSQTSTPTDVT
CCCCCCCCCCCCCCE		38.6228450419
282PhosphorylationSQGPSQTSTPTDVTA
CCCCCCCCCCCCCEE		25.4222617229
283PhosphorylationQGPSQTSTPTDVTAI
CCCCCCCCCCCCEEE		33.3325159151
285PhosphorylationPSQTSTPTDVTAIHL
CCCCCCCCCCEEECC		43.0928450419
288PhosphorylationTSTPTDVTAIHL---
CCCCCCCEEECC---		23.7828450419
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
283TPhosphorylationKinaseGSK3BP49841
PSP
283TPhosphorylationKinaseMAPK11Q15759
GPS
283TPhosphorylationKinaseMAPK12P53778
GPS
283TPhosphorylationKinaseMAPK13O15264
GPS
-KUbiquitinationE3 ubiquitin ligaseFBXL2Q9UKC9
PMID:22024926
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCND3_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 CCND3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3K_HUMANEIF3Kphysical
15327989
DTBP1_HUMANDTNBP1physical
16189514
FBLN4_HUMANEFEMP2physical
16189514
MAF1_HUMANMAF1physical
16189514
CDN1B_HUMANCDKN1Bphysical
16189514
CDN1A_HUMANCDKN1Aphysical
16189514
CDK4_HUMANCDK4physical
16189514
MCM10_HUMANMCM10physical
16189514
AKAP8_HUMANAKAP8physical
14641107
CDK4_HUMANCDK4physical
14641107
TSC2_HUMANTSC2physical
16357142
PCNA_HUMANPCNAphysical
7908906
RABP2_HUMANCRABP2physical
12482873
RARA_HUMANRARAphysical
12482873
CDN1B_HUMANCDKN1Bphysical
10597239
CDK2_HUMANCDK2physical
9716181
CDK6_HUMANCDK6physical
9716181
CDK4_HUMANCDK4physical
9716181
CDN1A_HUMANCDKN1Aphysical
9716181
CDN1B_HUMANCDKN1Bphysical
9716181
CDN1B_HUMANCDKN1Bphysical
8978686
RB_HUMANRB1physical
16782892
CDK4_HUMANCDK4physical
16782892
CDK6_HUMANCDK6physical
16782892
CDK2_HUMANCDK2physical
16782892
CDN1B_HUMANCDKN1Bphysical
16782892
A4_HUMANAPPphysical
21832049
DPOD1_HUMANPOLD1physical
9545286
CDN1A_HUMANCDKN1Aphysical
8756624
MCM10_HUMANMCM10physical
15232106
CDN1A_HUMANCDKN1Aphysical
15232106
CDK4_HUMANCDK4physical
15232106
CDK6_HUMANCDK6physical
15232106
CDN1B_HUMANCDKN1Bphysical
23718855
SIL1_HUMANSIL1physical
21988832
TNR6_HUMANFASphysical
21988832
MYB_HUMANMYBphysical
21988832
EIF3K_HUMANEIF3Kphysical
21988832
CD11B_HUMANCDK11Bphysical
21988832
CDK4_HUMANCDK4physical
21988832
CDN1A_HUMANCDKN1Aphysical
21988832
ETV1_HUMANETV1physical
21988832
VTDB_HUMANGCphysical
21988832
NDKA_HUMANNME1physical
21988832
MK06_HUMANMAPK6physical
21988832
VDR_HUMANVDRphysical
21988832
CDK4_HUMANCDK4physical
23880157
CDN1A_HUMANCDKN1Aphysical
23880157
CDK4_HUMANCDK4physical
25416956
CDK6_HUMANCDK6physical
25416956
CDN1A_HUMANCDKN1Aphysical
25416956
TFP11_HUMANTFIP11physical
25416956
RPC7L_HUMANPOLR3GLphysical
25416956
CDK2_HUMANCDK2physical
26186194
CDK1_HUMANCDK1physical
26186194
ZNF2_HUMANZNF2physical
26186194
CDK4_HUMANCDK4physical
26186194
RBL2_HUMANRBL2physical
26186194
CDK6_HUMANCDK6physical
26186194
CLUS_HUMANCLUphysical
26186194
CDN1B_HUMANCDKN1Bphysical
26186194
CDK5_HUMANCDK5physical
26186194
CDN1C_HUMANCDKN1Cphysical
26186194
CDN2C_HUMANCDKN2Cphysical
26186194
CDN1A_HUMANCDKN1Aphysical
26186194
KLK5_HUMANKLK5physical
26186194
CBP_HUMANCREBBPphysical
26186194
CDN1A_HUMANCDKN1Aphysical
25241761
AREG_HUMANAREGphysical
25241761
DTBP1_HUMANDTNBP1physical
27130439
CDK6_HUMANCDK6physical
28514442
CDN1B_HUMANCDKN1Bphysical
28514442
CDK4_HUMANCDK4physical
28514442
CDN1C_HUMANCDKN1Cphysical
28514442
CDN1A_HUMANCDKN1Aphysical
28514442
RBL2_HUMANRBL2physical
28514442
CDN2C_HUMANCDKN2Cphysical
28514442
KLK5_HUMANKLK5physical
28514442
CDK2_HUMANCDK2physical
28514442
CDK5_HUMANCDK5physical
28514442
CBP_HUMANCREBBPphysical
28514442
STAP1_HUMANSTAP1physical
28514442
CDK1_HUMANCDK1physical
28514442
Drug and Disease Associations
Kegg Disease
H00010 Multiple myeloma
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.
Regulatory Network of CCND3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASSSPECTROMETRY.

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