DHX40_HUMAN - dbPTM
DHX40_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DHX40_HUMAN
UniProt AC Q8IX18
Protein Name Probable ATP-dependent RNA helicase DHX40
Gene Name DHX40
Organism Homo sapiens (Human).
Sequence Length 779
Subcellular Localization
Protein Description Probable ATP-dependent RNA helicase..
Protein Sequence MSRFPAVAGRAPRRQEEGERSRDLQEERLSAVCIADREEKGCTSQEGGTTPTFPIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKVGYQVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEKSPNRKEHLKVVVMSATMELAKLSAFFGNCPIFDIPGRLYPVREKFCNLIGPRDRENTAYIQAIVKVTMDIHLNEMAGDILVFLTGQFEIEKSCELLFQMAESVDYDYDVQDTTLDGLLILPCYGSMTTDQQRRIFLPPPPGIRKCVISTNISATSLTIDGIRYVVDGGFVKQLNHNPRLGLDILEVVPISKSEALQRSGRAGRTSSGKCFRIYSKDFWNQCMPDHVIPEIKRTSLTSVVLTLKCLAIHDVIRFPYLDPPNERLILEALKQLYQCDAIDRSGHVTRLGLSMVEFPLPPHLTCAVIKAASLDCEDLLLPIAAMLSVENVFIRPVDPEYQKEAEQRHRELAAKAGGFNDFATLAVIFEQCKSSGAPASWCQKHWIHWRCLFSAFRVEAQLRELIRKLKQQSDFPKETFEGPKHEVLRRCLCAGYFKNVARRSVGRTFCTMDGRGSPVHIHPSSALHEQETKLEWIIFHEVLVTTKVYARIVCPIRYEWVRDLLPKLHEFNAHDLSSVARREVREDARRRWTNKENVKQLKDGISKDVLKKMQRRNDDKSISDARARFLERKQQRTQDHSDTRKETG
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
3Methylation-----MSRFPAVAGR
-----CCCCCCCCCC
40.02-
30PhosphorylationDLQEERLSAVCIADR
HHHHHHHHHEEEECC
25.5228555341
40UbiquitinationCIADREEKGCTSQEG
EEECCHHCCCCCCCC
55.31-
50PhosphorylationTSQEGGTTPTFPIQK
CCCCCCCCCCCCCHH
24.4925159151
57UbiquitinationTPTFPIQKQRKKIIQ
CCCCCCHHHHHHHHH
53.44-
61UbiquitinationPIQKQRKKIIQAVRD
CCHHHHHHHHHHHHC
47.43-
70PhosphorylationIQAVRDNSFLIVTGN
HHHHHCCCEEEEECC
26.2220873877
78PhosphorylationFLIVTGNTGSGKTTQ
EEEEECCCCCCCCCC
33.79-
82UbiquitinationTGNTGSGKTTQLPKY
ECCCCCCCCCCCCHH
50.53-
83PhosphorylationGNTGSGKTTQLPKYL
CCCCCCCCCCCCHHH
24.25-
84PhosphorylationNTGSGKTTQLPKYLY
CCCCCCCCCCCHHHH
31.43-
91PhosphorylationTQLPKYLYEAGFSQH
CCCCHHHHHCCCCCC
10.7221403953
91 (in isoform 2)Ubiquitination-10.7221890473
104PhosphorylationQHGMIGVTQPRKVAA
CCCCCCCCCCCHHHH
27.8721406692
108UbiquitinationIGVTQPRKVAAISVA
CCCCCCCHHHHHHHH
42.80-
123UbiquitinationQRVAEEMKCTLGSKV
HHHHHHHCCCCCCCC
27.61-
125PhosphorylationVAEEMKCTLGSKVGY
HHHHHCCCCCCCCEE
28.7428152594
128PhosphorylationEMKCTLGSKVGYQVR
HHCCCCCCCCEEEEE
27.5528152594
129UbiquitinationMKCTLGSKVGYQVRF
HCCCCCCCCEEEEEE
37.57-
142AcetylationRFDDCSSKETAIKYM
EECCCCCCHHHHHHH
42.6726051181
142UbiquitinationRFDDCSSKETAIKYM
EECCCCCCHHHHHHH
42.67-
148PhosphorylationSKETAIKYMTDGCLL
CCHHHHHHHCCCCHH
10.1129496907
156UbiquitinationMTDGCLLKHILGDPN
HCCCCHHHHHHCCCC
18.69-
168PhosphorylationDPNLTKFSVIILDEA
CCCCCEEEEEEECHH
17.60-
190 (in isoform 3)Ubiquitination-53.0921890473
190 (in isoform 1)Ubiquitination-53.0921890473
190UbiquitinationDILFGLLKKLFQEKS
HHHHHHHHHHHHHCC
53.0921906983
197PhosphorylationKKLFQEKSPNRKEHL
HHHHHHCCCCHHHHH
27.0130266825
240AcetylationRLYPVREKFCNLIGP
CEECHHHHHHHCCCC
44.6525953088
240UbiquitinationRLYPVREKFCNLIGP
CEECHHHHHHHCCCC
44.65-
340 (in isoform 2)Ubiquitination-30.8221890473
367UbiquitinationVVDGGFVKQLNHNPR
EEECCHHHCCCCCCC
46.9721890473
367 (in isoform 1)Ubiquitination-46.9721890473
367 (in isoform 3)Ubiquitination-46.9721890473
367UbiquitinationVVDGGFVKQLNHNPR
EEECCHHHCCCCCCC
46.9721890473
387UbiquitinationLEVVPISKSEALQRS
EEEEECCHHHHHHHC
53.702190698
387 (in isoform 1)Ubiquitination-53.7021890473
387 (in isoform 3)Ubiquitination-53.7021890473
394PhosphorylationKSEALQRSGRAGRTS
HHHHHHHCCCCCCCC
21.48-
404UbiquitinationAGRTSSGKCFRIYSK
CCCCCCCCEEEEEEH
31.95-
410PhosphorylationGKCFRIYSKDFWNQC
CCEEEEEEHHHHHHH
24.31-
465UbiquitinationRLILEALKQLYQCDA
HHHHHHHHHHHCCCC
45.35-
468PhosphorylationLEALKQLYQCDAIDR
HHHHHHHHCCCCCCC
12.4724043423
534UbiquitinationPVDPEYQKEAEQRHR
CCCHHHHHHHHHHHH
58.97-
601UbiquitinationRELIRKLKQQSDFPK
HHHHHHHHHCCCCCH
49.69-
608UbiquitinationKQQSDFPKETFEGPK
HHCCCCCHHHCCCHH
70.18-
615UbiquitinationKETFEGPKHEVLRRC
HHHCCCHHHHHHHHH
64.35-
648PhosphorylationCTMDGRGSPVHIHPS
EECCCCCCCEEECCC
23.5325849741
724PhosphorylationEDARRRWTNKENVKQ
HHHHHHHCCHHHHHH
34.3027135362
730AcetylationWTNKENVKQLKDGIS
HCCHHHHHHHHHCCC
62.5925953088
733AcetylationKENVKQLKDGISKDV
HHHHHHHHHCCCHHH
51.9511921431
737PhosphorylationKQLKDGISKDVLKKM
HHHHHCCCHHHHHHH
28.4727135362
743AcetylationISKDVLKKMQRRNDD
CCHHHHHHHHHHCCC
35.7811921443
768PhosphorylationLERKQQRTQDHSDTR
HHHHHHHHCCCHHHH
33.73-
772PhosphorylationQQRTQDHSDTRKETG
HHHHCCCHHHHHCCC
49.30-
774PhosphorylationRTQDHSDTRKETG--
HHCCCHHHHHCCC--
46.81-

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 DHX40_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DHX40_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 DHX40_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IFIT2_HUMANIFIT2physical
22939629
IKKA_HUMANCHUKphysical
22939629
SNAA_HUMANNAPAphysical
22939629
HAUS7_HUMANHAUS7physical
22939629
SPG21_HUMANSPG21physical
22939629
MD2BP_HUMANMAD2L1BPphysical
22939629
PKN3_HUMANPKN3physical
22939629
SPDLY_HUMANSPDL1physical
22939629
PGLT1_HUMANPOGLUT1physical
22939629
MTDC_HUMANMTHFD2physical
22939629

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 DHX40_HUMAN

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Related Literatures of Post-Translational Modification

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