IMPCT_HUMAN - dbPTM
IMPCT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IMPCT_HUMAN
UniProt AC Q9P2X3
Protein Name Protein IMPACT
Gene Name IMPACT
Organism Homo sapiens (Human).
Sequence Length 320
Subcellular Localization Cytoplasm .
Protein Description Translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation. Plays a role as a negative regulator of the EIF2AK4/GCN2 kinase activity; impairs GCN1-mediated EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation and subsequent down-regulation of protein synthesis. May be required to regulate translation in specific neuronal cells under amino acid starvation conditions by preventing GCN2 activation and therefore ATF4 synthesis. Through its inhibitory action on EIF2AK4/GCN2, plays a role in differentiation of neuronal cells by stimulating neurite outgrowth..
Protein Sequence MAEGDAGSDQRQNEEIEAMAAIYGEEWCVIDDCAKIFCIRISDDIDDPKWTLCLQVMLPNEYPGTAPPIYQLNAPWLKGQERADLSNSLEEIYIQNIGESILYLWVEKIRDVLIQKSQMTEPGPDVKKKTEEEDVECEDDLILACQPESSLKALDFDISETRTEVEVEELPPIDHGIPITDRRSTFQAHLAPVVCPKQVKMVLSKLYENKKIASATHNIYAYRIYCEDKQTFLQDCEDDGETAAGGRLLHLMEILNVKNVMVVVSRWYGGILLGPDRFKHINNCARNILVEKNYTNSPEESSKALGKNKKVRKDKKRNEH
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
51PhosphorylationDIDDPKWTLCLQVML
CCCCCCEEEEEEEEC
17.4524043423
62PhosphorylationQVMLPNEYPGTAPPI
EEECCCCCCCCCCCE
17.3824043423
65PhosphorylationLPNEYPGTAPPIYQL
CCCCCCCCCCCEEEC
31.3324043423
70PhosphorylationPGTAPPIYQLNAPWL
CCCCCCEEECCCHHH
16.8424043423
127UbiquitinationTEPGPDVKKKTEEED
CCCCCCCCCCCCCCC
56.80-
127 (in isoform 1)Ubiquitination-56.8021906983
150PhosphorylationLACQPESSLKALDFD
EEECCHHHHHHCCCC
32.0227251275
159PhosphorylationKALDFDISETRTEVE
HHCCCCCCCCCEEEE
34.4621815630
161PhosphorylationLDFDISETRTEVEVE
CCCCCCCCCEEEEEE
35.7821815630
200UbiquitinationVVCPKQVKMVLSKLY
CCCHHHHHHHHHHHH
22.31-
207PhosphorylationKMVLSKLYENKKIAS
HHHHHHHHCCCCHHH
22.61-
211UbiquitinationSKLYENKKIASATHN
HHHHCCCCHHHCCCC
55.90-
229UbiquitinationYRIYCEDKQTFLQDC
EEEEECCHHEEECCC
29.01-
229MalonylationYRIYCEDKQTFLQDC
EEEEECCHHEEECCC
29.0126320211
229AcetylationYRIYCEDKQTFLQDC
EEEEECCHHEEECCC
29.0126822725
292UbiquitinationARNILVEKNYTNSPE
HHHHHEECCCCCCHH
48.01-
295PhosphorylationILVEKNYTNSPEESS
HHEECCCCCCHHHHH
38.3229396449
297PhosphorylationVEKNYTNSPEESSKA
EECCCCCCHHHHHHH
26.3723663014
301PhosphorylationYTNSPEESSKALGKN
CCCCHHHHHHHHCCC
35.1623663014
302PhosphorylationTNSPEESSKALGKNK
CCCHHHHHHHHCCCC
25.8129396449

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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IMPCT_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 IMPCT_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCN1_YEASTGCN1physical
22404850
ACT_YEASTACT1physical
22404850
RL39_YEASTRPL39physical
22404850
RS22A_YEASTRPS22Aphysical
22404850
RS22B_YEASTRPS22Bphysical
22404850
CRHBP_HUMANCRHBPphysical
28514442

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

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Related Literatures of Post-Translational Modification

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