CCND2_HUMAN - dbPTM
CCND2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCND2_HUMAN
UniProt AC P30279
Protein Name G1/S-specific cyclin-D2
Gene Name CCND2
Organism Homo sapiens (Human).
Sequence Length 289
Subcellular Localization Nucleus . Cytoplasm . Membrane . Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members..
Isoform 2: Cytoplasm .
Protein Description Regulatory component of the cyclin D2-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 D2/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity)..
Protein Sequence MELLCHEVDPVRRAVRDRNLLRDDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLAMNYLDRFLAGVPTPKSHLQLLGAVCMFLASKLKETSPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFIEHILRKLPQQREKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDEEVSSLTCDALTELLAKITNTDVDCLKACQEQIEAVLLNSLQQYRQDQRDGSKSEDELDQASTPTDVRDIDL
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
45UbiquitinationLPQCSYFKCVQKDIQ
CCCCCHHHHHHHHCH
25.8423000965
49UbiquitinationSYFKCVQKDIQPYMR
CHHHHHHHHCHHHHH
36.0823000965
111UbiquitinationVCMFLASKLKETSPL
HHHHHHHHCCCCCCC
58.9522817900
113UbiquitinationMFLASKLKETSPLTA
HHHHHHCCCCCCCCH
63.7822817900
148UbiquitinationLVVLGKLKWNLAAVT
EHHHHHCCCCEEECC
37.21-
173UbiquitinationKLPQQREKLSLIRKH
HCHHHHHHHHHHHHH
45.63-
175PhosphorylationPQQREKLSLIRKHAQ
HHHHHHHHHHHHHHH
32.5824719451
244UbiquitinationNTDVDCLKACQEQIE
CCCHHHHHHHHHHHH
54.1422817900
269PhosphorylationRQDQRDGSKSEDELD
HHHCCCCCCCHHHHH
36.9830266825
270UbiquitinationQDQRDGSKSEDELDQ
HHCCCCCCCHHHHHH
64.49-
271PhosphorylationDQRDGSKSEDELDQA
HCCCCCCCHHHHHHC
52.5623401153
279PhosphorylationEDELDQASTPTDVRD
HHHHHHCCCCCCHHH
29.3230108239
280PhosphorylationDELDQASTPTDVRDI
HHHHHCCCCCCHHHC
32.9723927012
282PhosphorylationLDQASTPTDVRDIDL
HHHCCCCCCHHHCCC
47.4130108239

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
280TPhosphorylationKinaseGSK3BP49841
PSP
280TPhosphorylationKinaseMAPK14Q16539
GPS
-KUbiquitinationE3 ubiquitin ligaseFBXL2Q9UKC9
PMID:22323446
-KUbiquitinationE3 ubiquitin ligaseFBXO31Q5XUX0
PMID:21537837

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCND2_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 CCND2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDN1A_HUMANCDKN1Aphysical
16189514
CDN1B_HUMANCDKN1Bphysical
16189514
TSC2_HUMANTSC2physical
16357142
CDK4_HUMANCDK4physical
15169570
RB_HUMANRB1physical
10049762
CDK2_HUMANCDK2physical
9178893
CDK4_HUMANCDK4physical
9178893
CDK6_HUMANCDK6physical
9178893
RB_HUMANRB1physical
9178893
H11_HUMANHIST1H1Aphysical
9178893
PCGF2_HUMANPCGF2physical
16182291
RB_HUMANRB1physical
9885575
H11_HUMANHIST1H1Aphysical
9885575
CDN1A_HUMANCDKN1Aphysical
8756624
CDK5_HUMANCDK5physical
25416956
CDN1A_HUMANCDKN1Aphysical
25416956
CDK2_HUMANCDK2physical
26186194
CDK4_HUMANCDK4physical
26186194
RBL2_HUMANRBL2physical
26186194
CDN1B_HUMANCDKN1Bphysical
26186194
CDK5_HUMANCDK5physical
26186194
CDN1C_HUMANCDKN1Cphysical
26186194
CDN1A_HUMANCDKN1Aphysical
26186194
CDN1A_HUMANCDKN1Aphysical
25241761
DTBP1_HUMANDTNBP1physical
27130439
CDN1A_HUMANCDKN1Aphysical
28514442
CDN1B_HUMANCDKN1Bphysical
28514442
CDN1C_HUMANCDKN1Cphysical
28514442
CDK4_HUMANCDK4physical
28514442
RBL2_HUMANRBL2physical
28514442
CDK2_HUMANCDK2physical
28514442
CDK5_HUMANCDK5physical
28514442
PRS4_HUMANPSMC1physical
27371349
PRS8_HUMANPSMC5physical
27371349
ATPB_HUMANATP5Bphysical
27371349
CBX3_HUMANCBX3physical
27371349
IF5A1_HUMANEIF5Aphysical
27371349
XPO2_HUMANCSE1Lphysical
27371349
UBA3_HUMANUBA3physical
27371349
PFD5_HUMANPFDN5physical
27371349
PLOD3_HUMANPLOD3physical
27371349
PSA3_HUMANPSMA3physical
27371349
FLII_HUMANFLIIphysical
27371349
RFA3_HUMANRPA3physical
27371349
SGTA_HUMANSGTAphysical
27371349
TLN2_HUMANTLN2physical
27371349
TBB4B_HUMANTUBB4Bphysical
27371349
LSM5_HUMANLSM5physical
27371349
UBA1_HUMANUBA1physical
27371349
RSSA_HUMANRPSAphysical
27371349
ACTB_HUMANACTBphysical
27371349
API5_HUMANAPI5physical
27371349
ACTBL_HUMANACTBL2physical
27371349
EIF3B_HUMANEIF3Bphysical
27371349
EIF3F_HUMANEIF3Fphysical
27371349
EIF3I_HUMANEIF3Iphysical
27371349
IF6_HUMANEIF6physical
27371349
H2AV_HUMANH2AFVphysical
27371349
NUDC1_HUMANNUDCD1physical
27371349
RFA1_HUMANRPA1physical
27371349
STRAP_HUMANSTRAPphysical
27371349
PP2AA_HUMANPPP2CAphysical
27371349
TMOD3_HUMANTMOD3physical
27371349
ZPR1_HUMANZPR1physical
27371349
PRS6A_HUMANPSMC3physical
27371349
PRS7_HUMANPSMC2physical
27371349
PSD12_HUMANPSMD12physical
27371349
PSMD3_HUMANPSMD3physical
27371349
ASNA_HUMANASNA1physical
27371349
COPE_HUMANCOPEphysical
27371349
DCTN2_HUMANDCTN2physical
27371349
DYLT1_HUMANDYNLT1physical
27371349
ERF1_HUMANETF1physical
27371349
GELS_HUMANGSNphysical
27371349
HS71L_HUMANHSPA1Lphysical
27371349
HSPB1_HUMANHSPB1physical
27371349
F10A1_HUMANST13physical
27371349
MYL9_HUMANMYL9physical
27371349
PFD2_HUMANPFDN2physical
27371349
PSME2_HUMANPSME2physical
27371349
PSB6_HUMANPSMB6physical
27371349
S10A6_HUMANS100A6physical
27371349
SEPT7_HUMANSEPT7physical
27371349
TIF1B_HUMANTRIM28physical
27371349
TBB6_HUMANTUBB6physical
27371349
PSA_HUMANNPEPPSphysical
27371349
SMD3_HUMANSNRPD3physical
27371349
PRS6B_HUMANPSMC4physical
27371349
PSMD5_HUMANPSMD5physical
27371349
DNJA1_HUMANDNAJA1physical
27371349
TBA1B_HUMANTUBA1Bphysical
27371349
CLIC1_HUMANCLIC1physical
27371349
PLEC_HUMANPLECphysical
27371349

Drug and Disease Associations
Kegg Disease
H00023 Testicular cancer
OMIM Disease
615938Megalencephaly-polymicrogyria-polydactyly-hydrocephalus syndrome 3 (MPPH3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CCND2_HUMAN

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Related Literatures of Post-Translational Modification

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