CDKA2_HUMAN - dbPTM
CDKA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDKA2_HUMAN
UniProt AC O75956
Protein Name Cyclin-dependent kinase 2-associated protein 2
Gene Name CDK2AP2
Organism Homo sapiens (Human).
Sequence Length 126
Subcellular Localization Cytoplasm . Nucleus . Accumulates in immature oocytes in the nucleus. During the first meiotic division, accumulates in the cytoplasm and localizes in dots in the vicinity of the chromosomes in a region enriched in microtubules.
Protein Description Plays a role in regulating the self-renewal of embryonic stem cells (ESCs) and in maintaining cell survival during terminal differentiation of ESCs. Regulates microtubule organization of metaphase II oocytes (By similarity). Inhibits cell cycle G1/S phase transition by repressing CDK2 expression and activation; represses CDK2 activation by inhibiting its interaction with cyclin E and A. [PubMed: 23781148]
Protein Sequence MSYKPIAPAPSSTPGSSTPGPGTPVPTGSVPSPSGSVPGAGAPFRPLFNDFGPPSMGYVQAMKPPGAQGSQSTYTDLLSVIEEMGKEIRPTYAGSKSAMERLKRGIIHARALVRECLAETERNART
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
11PhosphorylationKPIAPAPSSTPGSST
CCCCCCCCCCCCCCC
49.2928111955
12PhosphorylationPIAPAPSSTPGSSTP
CCCCCCCCCCCCCCC
37.2528111955
13PhosphorylationIAPAPSSTPGSSTPG
CCCCCCCCCCCCCCC
35.6928111955
16PhosphorylationAPSSTPGSSTPGPGT
CCCCCCCCCCCCCCC
32.0428111955
17PhosphorylationPSSTPGSSTPGPGTP
CCCCCCCCCCCCCCC
44.5328111955
18PhosphorylationSSTPGSSTPGPGTPV
CCCCCCCCCCCCCCC
33.6828111955
23PhosphorylationSSTPGPGTPVPTGSV
CCCCCCCCCCCCCCC
25.0128111955
27PhosphorylationGPGTPVPTGSVPSPS
CCCCCCCCCCCCCCC
42.1828111955
29PhosphorylationGTPVPTGSVPSPSGS
CCCCCCCCCCCCCCC
33.0828111955
32PhosphorylationVPTGSVPSPSGSVPG
CCCCCCCCCCCCCCC
29.5528111955
34PhosphorylationTGSVPSPSGSVPGAG
CCCCCCCCCCCCCCC
48.3028111955
36PhosphorylationSVPSPSGSVPGAGAP
CCCCCCCCCCCCCCC
29.4928111955
55PhosphorylationFNDFGPPSMGYVQAM
CCCCCCCCCCCCEEE
28.1527050516
91O-linked_GlycosylationMGKEIRPTYAGSKSA
HHHHHCCCCCCCHHH
19.02OGP
91PhosphorylationMGKEIRPTYAGSKSA
HHHHHCCCCCCCHHH
19.0221406692
92PhosphorylationGKEIRPTYAGSKSAM
HHHHCCCCCCCHHHH
16.2021406692
95PhosphorylationIRPTYAGSKSAMERL
HCCCCCCCHHHHHHH
18.4428152594
96UbiquitinationRPTYAGSKSAMERLK
CCCCCCCHHHHHHHH
41.12-
97PhosphorylationPTYAGSKSAMERLKR
CCCCCCHHHHHHHHH
34.2525072903

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

Oops, there are no upstream regulatory protein records of CDKA2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDKA2_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 CDKA2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSF4_HUMANHSF4physical
21900206
YIF1A_HUMANYIF1Aphysical
21900206
DREB_HUMANDBN1physical
21900206
TZAP_HUMANZBTB48physical
21900206
RCC1_HUMANRCC1physical
21900206
TRA2A_HUMANTRA2Aphysical
21900206
A2MG_HUMANA2Mphysical
21900206
RLA1_HUMANRPLP1physical
21900206
IKZF1_HUMANIKZF1physical
21900206
EF1G_HUMANEEF1Gphysical
21900206
EED_HUMANEEDphysical
21900206
MBTP1_HUMANMBTPS1physical
21900206
P5CR1_HUMANPYCR1physical
21900206
A4_HUMANAPPphysical
21832049
CDKA1_HUMANCDK2AP1physical
14985111
MR1L1_HUMANMRFAP1L1physical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDKA2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP