ID2_HUMAN - dbPTM
ID2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ID2_HUMAN
UniProt AC Q02363
Protein Name DNA-binding protein inhibitor ID-2
Gene Name ID2
Organism Homo sapiens (Human).
Sequence Length 134
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Restricts the CLOCK and ARNTL/BMAL1 localization to the cytoplasm. Plays a role in both the input and output pathways of the circadian clock: in the input component, is involved in modulating the magnitude of photic entrainment and in the output component, contributes to the regulation of a variety of liver clock-controlled genes involved in lipid metabolism..
Protein Sequence MKAFSPVRSVRKNSLSDHSLGISRSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVSKMEILQHVIDYILDLQIALDSHPTIVSLHHQRPGQNQASRTPLTTLNTDISILSLQASEFPSELMSNDSKALCG
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
5Phosphorylation---MKAFSPVRSVRK
---CCCCCCCCHHHC
27.619029153
12UbiquitinationSPVRSVRKNSLSDHS
CCCCHHHCCCCCCCC
49.052097226
14PhosphorylationVRSVRKNSLSDHSLG
CCHHHCCCCCCCCCC
32.0823401153
16PhosphorylationSVRKNSLSDHSLGIS
HHHCCCCCCCCCCCC
32.8523911959
19PhosphorylationKNSLSDHSLGISRSK
CCCCCCCCCCCCCCC
33.0324117733
23PhosphorylationSDHSLGISRSKTPVD
CCCCCCCCCCCCCCC
28.8024117733
25PhosphorylationHSLGISRSKTPVDDP
CCCCCCCCCCCCCCH
33.8127080861
27PhosphorylationLGISRSKTPVDDPMS
CCCCCCCCCCCCHHH
29.7728450419
34PhosphorylationTPVDDPMSLLYNMND
CCCCCHHHHHHHHHH
22.1727080861
43PhosphorylationLYNMNDCYSKLKELV
HHHHHHHHHHHHHHC
16.23-
44PhosphorylationYNMNDCYSKLKELVP
HHHHHHHHHHHHHCC
37.53-

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
5SPhosphorylationKinaseCDK2P24941
PhosphoELM
27TPhosphorylationKinaseDYRK1BQ9Y463
PSP
-KUbiquitinationE3 ubiquitin ligaseASB4Q9Y574
PMID:24586788
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:16810178

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ID2_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 ID2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HTF4_HUMANTCF12physical
9242638
RBM48_HUMANRBM48physical
16169070
LRIF1_HUMANLRIF1physical
16169070
U119A_HUMANUNC119physical
16169070
CASL_HUMANNEDD9physical
10502414
BCAR1_HUMANBCAR1physical
10502414
TFE2_HUMANTCF3physical
9242638
ITF2_HUMANTCF4physical
9242638
MYOD1_HUMANMYOD1physical
9242638
MYF5_HUMANMYF5physical
9242638
GATA4_HUMANGATA4physical
16556596
NKX25_HUMANNKX2-5physical
16556596
UBP1_HUMANUSP1physical
21925315
RB_HUMANRB1physical
11034201
RBL1_HUMANRBL1physical
11034201
RBL2_HUMANRBL2physical
11034201
TFE2_HUMANTCF3physical
19321746
HTF4_HUMANTCF12physical
19321746
ID2_HUMANID2physical
21988832
MK08_HUMANMAPK8physical
21988832
FCL_HUMANTSTA3physical
21988832
KDM1A_HUMANKDM1Aphysical
23455924
ANM6_HUMANPRMT6physical
23455924
SUV91_HUMANSUV39H1physical
23455924
SUV92_HUMANSUV39H2physical
23455924
ASB4_HUMANASB4physical
24586788
DYR1A_HUMANDYRK1Aphysical
26735018
DYR1B_HUMANDYRK1Bphysical
26735018
TFE2_HUMANTCF3physical
26735018
HTF4_HUMANTCF12physical
26735018
R113A_HUMANRNF113Aphysical
26735018
ELOC_HUMANTCEB1physical
26735018
ELP4_HUMANELP4physical
26735018
GRP78_HUMANHSPA5physical
26735018
STK38_HUMANSTK38physical
26735018
HSP7C_HUMANHSPA8physical
26735018
TBB4B_HUMANTUBB4Bphysical
26735018
TBA1B_HUMANTUBA1Bphysical
26735018
EF1A2_HUMANEEF1A2physical
26735018
GRP75_HUMANHSPA9physical
26735018
HS71L_HUMANHSPA1Lphysical
26735018
TBB5_HUMANTUBBphysical
26735018
ANM5_HUMANPRMT5physical
26735018
VHL_HUMANVHLphysical
26735018
TFE2_HUMANTCF3physical
28514442
ITF2_HUMANTCF4physical
28514442
HTF4_HUMANTCF12physical
28514442
ID4_HUMANID4physical
28514442
PHF3_HUMANPHF3physical
28514442
WBP11_HUMANWBP11physical
28514442
CLAP2_HUMANCLASP2physical
28514442
TYY1_HUMANYY1physical
28514442
ZGPAT_HUMANZGPATphysical
28514442
MACF1_HUMANMACF1physical
28514442
DIDO1_HUMANDIDO1physical
28514442
SLTM_HUMANSLTMphysical
28514442
RCBT2_HUMANRCBTB2physical
28514442
RABL6_HUMANRABL6physical
28514442
CA131_HUMANC1orf131physical
28514442
AFAD_HUMANMLLT4physical
28514442
RBM27_HUMANRBM27physical
28514442
HDGR2_HUMANHDGFRP2physical
28514442
UB2E1_HUMANUBE2E1physical
28514442
CFDP1_HUMANCFDP1physical
28514442
KI20B_HUMANKIF20Bphysical
28514442
KLH20_HUMANKLHL20physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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 ID2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP