ID1_HUMAN - dbPTM
ID1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ID1_HUMAN
UniProt AC P41134
Protein Name DNA-binding protein inhibitor ID-1
Gene Name ID1
Organism Homo sapiens (Human).
Sequence Length 155
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 (By similarity)..
Protein Sequence MKVASGSTATAAAGPSCALKAGKTASGAGEVVRCLSEQSVAISRCAGGAGARLPALLDEQQVNVLLYDMNGCYSRLKELVPTLPQNRKVSKVEILQHVIDYIRDLQLELNSESEVGTPGGRGLPVRAPLSTLNGEISALTAEAACVPADDRILCR
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
2Methylation------MKVASGSTA
------CCCCCCCCC		46.65115971335
2Ubiquitination------MKVASGSTA
------CCCCCCCCC		46.6521963094
5Phosphorylation---MKVASGSTATAA
---CCCCCCCCCCCC		35.9428555341
20UbiquitinationAGPSCALKAGKTASG
CCCCHHHHCCCCCCC		36.2521906983
20 (in isoform 2)Ubiquitination-36.2521906983
20 (in isoform 1)Ubiquitination-36.2521906983
20AcetylationAGPSCALKAGKTASG
CCCCHHHHCCCCCCC		36.2525953088
23 (in isoform 2)Ubiquitination-45.8621906983
23AcetylationSCALKAGKTASGAGE
CHHHHCCCCCCCCHH		45.8625953088
23 (in isoform 1)Ubiquitination-45.8621906983
23UbiquitinationSCALKAGKTASGAGE
CHHHHCCCCCCCCHH		45.8621906983
36PhosphorylationGEVVRCLSEQSVAIS
HHHHHHHHHCCCHHE		36.9022617229
39PhosphorylationVRCLSEQSVAISRCA
HHHHHHCCCHHEECC		14.9522617229
77UbiquitinationNGCYSRLKELVPTLP
CCHHHHHHHHCCCCC		48.1421906983
77 (in isoform 2)Ubiquitination-48.1421906983
77 (in isoform 1)Ubiquitination-48.1421906983
88UbiquitinationPTLPQNRKVSKVEIL
CCCCCCCCCCHHHHH		59.4121963094
91UbiquitinationPQNRKVSKVEILQHV
CCCCCCCHHHHHHHH		47.0421963094
91 (in isoform 2)Ubiquitination-47.0421906983
91 (in isoform 1)Ubiquitination-47.0421906983
111PhosphorylationDLQLELNSESEVGTP
HHHHHCCCCCCCCCC		55.9422817900
117PhosphorylationNSESEVGTPGGRGLP
CCCCCCCCCCCCCCC		24.7621712546
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
36SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
-KUbiquitinationE3 ubiquitin ligaseSMURF2Q9HAU4
PMID:21933340
-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 ID1_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 ID1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSKP_HUMANCASKphysical
15694377
MYOD1_HUMANMYOD1physical
15029197
ITF2_HUMANTCF4physical
9242638
HTF4_HUMANTCF12physical
9242638
MYF5_HUMANMYF5physical
9242638
TFE2_HUMANTCF3physical
9242638
MYOD1_HUMANMYOD1physical
9242638
MYOD1_HUMANMYOD1physical
8380166
MYOD1_HUMANMYOD1physical
9528857
MYOD1_HUMANMYOD1physical
12145280
GATA4_HUMANGATA4physical
16556596
NKX25_HUMANNKX2-5physical
16556596
NEMO_HUMANIKBKGphysical
20211142
PSMD4_HUMANPSMD4physical
17891176
PSMD4_HUMANPSMD4physical
9235903
CDC20_HUMANCDC20physical
18372912
FZR1_HUMANFZR1physical
18372912
CAV1_HUMANCAV1physical
17855368
PP2AA_HUMANPPP2CAphysical
17855368
ITF2_HUMANTCF4physical
21988832
SUV91_HUMANSUV39H1physical
23455924
COCA1_HUMANCOL12A1physical
26496610
EM55_HUMANMPP1physical
26496610
PSMD5_HUMANPSMD5physical
26496610
REQU_HUMANDPF2physical
26496610
STXB1_HUMANSTXBP1physical
26496610
TFE2_HUMANTCF3physical
26496610
HTF4_HUMANTCF12physical
26496610
PIAS1_HUMANPIAS1physical
26496610
MKNK1_HUMANMKNK1physical
26496610
BUD31_HUMANBUD31physical
26496610
CHD1L_HUMANCHD1Lphysical
26496610
UBP15_HUMANUSP15physical
26496610
TXN4A_HUMANTXNL4Aphysical
26496610
B4GT7_HUMANB4GALT7physical
26496610
ERP44_HUMANERP44physical
26496610
ZC3HD_HUMANZC3H13physical
26496610
POTE1_HUMANPOT1physical
26496610
CCDC9_HUMANCCDC9physical
26496610
THOC6_HUMANTHOC6physical
26496610
ELOC_HUMANTCEB1physical
26735018
VHL_HUMANVHLphysical
26735018
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 ID1_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-111, AND MASSSPECTROMETRY.

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