DHX33_HUMAN - dbPTM
DHX33_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DHX33_HUMAN
UniProt AC Q9H6R0
Protein Name ATP-dependent RNA helicase DHX33 {ECO:0000305}
Gene Name DHX33 {ECO:0000312|HGNC:HGNC:16718}
Organism Homo sapiens (Human).
Sequence Length 707
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm . Cytoplasm . Nucleus . Inflammasome . Predominantly in the nucleolus. During mitosis, localizes with the nucleolar organizing regions (PubMed:21930779). Upon dsRNA-binding, localizes in the inflammasome (Pub
Protein Description Implicated in nucleolar organization, ribosome biogenesis, protein synthesis and cytoplasmic dsRNA sensing (By similarity). [PubMed: 21930779]
Protein Sequence MPEEAGFPPAKRFRPGSGPPSRAGSFPPGRQVVMLLTAGSGGRGGGGGRRQQPPLAQPSASPYPEAVELQRRSLPIFQARGQLLAQLRNLDNAVLIGETGSGKTTQIPQYLYEGGISRQGIIAVTQPRRVAAISLATRVSDEKRTELGKLVGYTVRFDDVTSEDTRIKFLTDGMLLREAISDSLLRKYSCVILDEAHERTIHTDVLFGVVKAAQKRRKELGKLPLKVIVMSATMDVDLFSQYFNGAPVLYLEGRQHPIQVFYTKQPQNDYLHAALVSVFQIHQEAPSSQDILVFLTGQEEIEAMSKTCRDIAKHLPDGCPAMLVLPLYASLPYAQQLRVFQGAPKGYRKVIISTNIAETSITITGIKYVVDTGMVKAKKYNPDSGLEVLAVQRVSKTQAWQRTGRAGREDSGICYRLYTEDEFEKFDKMTVPEIQRCNLASVMLQLLAMKVPNVLTFDFMSKPSPDHIQAAIAQLDLLGALEHKDDQLTLTPMGRKMAAFPLEPKFAKTILMSPKFHCTEEILTIVSLLSVDSVLHNPPSRREEVQGVRKKFISSEGDHMTLLNIYRTFKNLGGNKDWCKENFVNSKNMTLVAEVRAQLRDICLKMSMPIASSRGDVESVRRCLAHSLFMSTAELQPDGTYATTDTHQPVAIHPSSVLFHCKPACVVYTELLYTNKCYMRDLCVIDAQWLYEAAPEYFRRKLRTARN
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
17PhosphorylationAKRFRPGSGPPSRAG
HHCCCCCCCCCCCCC		51.3020873877
21PhosphorylationRPGSGPPSRAGSFPP
CCCCCCCCCCCCCCC		37.5930387612
40PhosphorylationVMLLTAGSGGRGGGG
EEEEECCCCCCCCCC		35.2929214152
43MethylationLTAGSGGRGGGGGRR
EECCCCCCCCCCCCC		44.07-
49MethylationGRGGGGGRRQQPPLA
CCCCCCCCCCCCCCC		36.19-
59PhosphorylationQPPLAQPSASPYPEA
CCCCCCCCCCCCCHH		29.3328555341
61PhosphorylationPLAQPSASPYPEAVE
CCCCCCCCCCCHHHH		29.3328555341
63PhosphorylationAQPSASPYPEAVELQ
CCCCCCCCCHHHHHH		15.94-
103UbiquitinationIGETGSGKTTQIPQY
EECCCCCCCCCCCHH		50.5321906983
104PhosphorylationGETGSGKTTQIPQYL
ECCCCCCCCCCCHHH		27.7120860994
125PhosphorylationRQGIIAVTQPRRVAA
CCCEEEECCCCEEEE		24.6721406692
162 (in isoform 1)Ubiquitination-33.0721906983
168UbiquitinationTSEDTRIKFLTDGML
CCCCCEEEEECCCHH		30.91-
171PhosphorylationDTRIKFLTDGMLLRE
CCEEEEECCCHHHHH		33.37-
181PhosphorylationMLLREAISDSLLRKY
HHHHHHHCHHHHHHC		28.3525072903
183PhosphorylationLREAISDSLLRKYSC
HHHHHCHHHHHHCCE		23.6325072903
187AcetylationISDSLLRKYSCVILD
HCHHHHHHCCEEEEE		41.2926051181
187UbiquitinationISDSLLRKYSCVILD
HCHHHHHHCCEEEEE		41.29-
203 (in isoform 2)Ubiquitination-24.7721906983
222UbiquitinationKRRKELGKLPLKVIV
HHHHHHCCCCCEEEE		60.60-
222AcetylationKRRKELGKLPLKVIV
HHHHHHCCCCCEEEE		60.6025953088
252 (in isoform 2)Ubiquitination-38.4821906983
313UbiquitinationKTCRDIAKHLPDGCP
HHHHHHHHHCCCCCC		46.11-
313AcetylationKTCRDIAKHLPDGCP
HHHHHHHHHCCCCCC		46.1126051181
328PhosphorylationAMLVLPLYASLPYAQ
EEEEEHHHHCCCHHH		7.6929496907
333PhosphorylationPLYASLPYAQQLRVF
HHHHCCCHHHHHHHH		23.4929496907
345UbiquitinationRVFQGAPKGYRKVII
HHHCCCCCCCEEEEE		68.95-
345AcetylationRVFQGAPKGYRKVII
HHHCCCCCCCEEEEE		68.9526051181
362PhosphorylationNIAETSITITGIKYV
CCCCEEEEEECEEEE		16.56-
368PhosphorylationITITGIKYVVDTGMV
EEEECEEEEEECCCE		12.0922461510
372PhosphorylationGIKYVVDTGMVKAKK
CEEEEEECCCEECEE		18.6322461510
376UbiquitinationVVDTGMVKAKKYNPD
EEECCCEECEECCCC		45.6721906983
376AcetylationVVDTGMVKAKKYNPD
EEECCCEECEECCCC		45.6726051181
378UbiquitinationDTGMVKAKKYNPDSG
ECCCEECEECCCCCC		50.50-
379UbiquitinationTGMVKAKKYNPDSGL
CCCEECEECCCCCCC		55.94-
380PhosphorylationGMVKAKKYNPDSGLE
CCEECEECCCCCCCE		31.0820068231
384PhosphorylationAKKYNPDSGLEVLAV
CEECCCCCCCEEEEE		46.6820068231
396UbiquitinationLAVQRVSKTQAWQRT
EEEEEECCHHHHHHH		41.62-
396MethylationLAVQRVSKTQAWQRT
EEEEEECCHHHHHHH		41.62-
414 (in isoform 2)Ubiquitination-1.5221906983
418PhosphorylationSGICYRLYTEDEFEK
CCCEEEEEEHHHHHH		10.09-
419PhosphorylationGICYRLYTEDEFEKF
CCEEEEEEHHHHHHC		41.36-
425AcetylationYTEDEFEKFDKMTVP
EEHHHHHHCCCCCHH		65.2726051181
425UbiquitinationYTEDEFEKFDKMTVP
EEHHHHHHCCCCCHH		65.2721906983
428AcetylationDEFEKFDKMTVPEIQ
HHHHHCCCCCHHHHH		39.3326051181
428UbiquitinationDEFEKFDKMTVPEIQ
HHHHHCCCCCHHHHH		39.33-
435 (in isoform 1)Ubiquitination-42.0621906983
441PhosphorylationIQRCNLASVMLQLLA
HHHCCHHHHHHHHHH		15.9520068231
456PhosphorylationMKVPNVLTFDFMSKP
CCCCCEEEEECCCCC		19.5120860994
461PhosphorylationVLTFDFMSKPSPDHI
EEEEECCCCCCHHHH		41.2120860994
484 (in isoform 1)Ubiquitination-54.3321906983
484UbiquitinationLLGALEHKDDQLTLT
HHHHHHCCCCCEEEC		54.33-
508UbiquitinationPLEPKFAKTILMSPK
CCCHHHHHHHHCCCC		38.95-
519PhosphorylationMSPKFHCTEEILTIV
CCCCCCCHHHHHHHH		28.2524043423
524PhosphorylationHCTEEILTIVSLLSV
CCHHHHHHHHHHHCC		25.6224043423
527PhosphorylationEEILTIVSLLSVDSV
HHHHHHHHHHCCHHH		21.5324043423
530PhosphorylationLTIVSLLSVDSVLHN
HHHHHHHCCHHHHCC		29.2224043423
533PhosphorylationVSLLSVDSVLHNPPS
HHHHCCHHHHCCCCC		25.1524043423
540PhosphorylationSVLHNPPSRREEVQG
HHHCCCCCHHHHHHH		45.2724043423
550AcetylationEEVQGVRKKFISSEG
HHHHHHHHHHHCCCC		50.027675637
570UbiquitinationLNIYRTFKNLGGNKD
HHHHHHHHHCCCCHH		51.12-
576UbiquitinationFKNLGGNKDWCKENF
HHHCCCCHHHHHHHC		56.75-
580UbiquitinationGGNKDWCKENFVNSK
CCCHHHHHHHCCCCC		51.98-
580AcetylationGGNKDWCKENFVNSK
CCCHHHHHHHCCCCC		51.9826051181
587UbiquitinationKENFVNSKNMTLVAE
HHHCCCCCCCEEHHH		45.602190698
596DimethylationMTLVAEVRAQLRDIC
CEEHHHHHHHHHHHH		14.23-
600DimethylationAEVRAQLRDICLKMS
HHHHHHHHHHHHHHC		21.11-
607PhosphorylationRDICLKMSMPIASSR
HHHHHHHCCCCCCCC		21.5920860994
612PhosphorylationKMSMPIASSRGDVES
HHCCCCCCCCCCHHH		22.6820860994
613PhosphorylationMSMPIASSRGDVESV
HCCCCCCCCCCHHHH		31.1220860994
646 (in isoform 1)Ubiquitination-21.9621906983
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 ligaseTRIM33Q9UPN9
PMID:25172487
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DHX33_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 DHX33_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI33_HUMANTRIM33physical
25172487
NLRP3_HUMANNLRP3physical
25172487
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 DHX33_HUMAN

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Related Literatures of Post-Translational Modification

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