DHX36_HUMAN - dbPTM
DHX36_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DHX36_HUMAN
UniProt AC Q9H2U1
Protein Name ATP-dependent RNA helicase DHX36
Gene Name DHX36
Organism Homo sapiens (Human).
Sequence Length 1008
Subcellular Localization Nucleus. Cytoplasm. Chromosome, telomere . Isoform 1 preferentially localized to the nucleus and isoform 2 localized to the cytoplasm. However, partitioning of cellular localization between the nucleus and cytoplasm is not exclusive, as isoform 1 was
Protein Description Proposed to have a global role in regulating mRNA expression including transcriptional regulation and mRNA stability. Binds with high affinity to and resolves tetramolecular RNA and DNA quadruplex structures. Unwinds intramolecular quadruplexes derived from the ZIC1 and the MYC promoters. Binds to quadruplex structures in the promoters of YY1 and ALPL genes and regulates their expression. Binds to telomerase RNA template component (TERC) 5'-end (nucleotides 1-43) and unwinds an internal quadruplex formation in TERC 5'-end to promote P1 helix formation; the P1 helix acts as a template boundary ensuring accurate reverse transcription and is disrupted by quadruplex formation. May be involved in regulation of telomere length. Plays a role in degradation and deadenylation of mRNAs containing in their 3'-UTR the consensus ARE sequence element. May function in sex development and spermatogenesis. May play a role in ossification..
Protein Sequence MSYDYHQNWGRDGGPRSSGGGYGGGPAGGHGGNRGSGGGGGGGGGGRGGRGRHPGHLKGREIGMWYAKKQGQKNKEAERQERAVVHMDERREEQIVQLLNSVQAKNDKESEAQISWFAPEDHGYGTEVSTKNTPCSENKLDIQEKKLINQEKKMFRIRNRSYIDRDSEYLLQENEPDGTLDQKLLEDLQKKKNDLRYIEMQHFREKLPSYGMQKELVNLIDNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACRIVCTQPRRISAISVAERVAAERAESCGSGNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDPYLSSVSHIVLDEIHERNLQSDVLMTVVKDLLNFRSDLKVILMSATLNAEKFSEYFGNCPMIHIPGFTFPVVEYLLEDVIEKIRYVPEQKEHRSQFKRGFMQGHVNRQEKEEKEAIYKERWPDYVRELRRRYSASTVDVIEMMEDDKVDLNLIVALIRYIVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKSDKFLIIPLHSLMPTVNQTQVFKRTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYHLYNGLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAYFLSRLMDPPSNEAVLLSIRHLMELNALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKEKIADARRKELAKDTRSDHLTVVNAFEGWEEARRRGFRYEKDYCWEYFLSSNTLQMLHNMKGQFAEHLLGAGFVSSRNPKDPESNINSDNEKIIKAVICAGLYPKVAKIRLNLGKKRKMVKVYTKTDGLVAVHPKSVNVEQTDFHYNWLIYHLKMRTSSIYLYDCTEVSPYCLLFFGGDISIQKDNDQETIAVDEWIVFQSPARIAHLVKELRKELDILLQEKIESPHPVDWNDTKSRDCAVLSAIIDLIKTQEKATPRNFPPRFQDGYYS
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
2Phosphorylation------MSYDYHQNW
------CCCCCCCCC		37.7123401153
3Phosphorylation-----MSYDYHQNWG
-----CCCCCCCCCC		32.1723663014
5Phosphorylation---MSYDYHQNWGRD
---CCCCCCCCCCCC		9.3225394399
11MethylationDYHQNWGRDGGPRSS
CCCCCCCCCCCCCCC		30.89-
17PhosphorylationGRDGGPRSSGGGYGG
CCCCCCCCCCCCCCC		36.1529396449
18PhosphorylationRDGGPRSSGGGYGGG
CCCCCCCCCCCCCCC		42.6129396449
22PhosphorylationPRSSGGGYGGGPAGG
CCCCCCCCCCCCCCC		18.8429396449
34MethylationAGGHGGNRGSGGGGG
CCCCCCCCCCCCCCC		43.88-
36PhosphorylationGHGGNRGSGGGGGGG
CCCCCCCCCCCCCCC		30.90-
47MethylationGGGGGGGRGGRGRHP
CCCCCCCCCCCCCCC		47.90-
50MethylationGGGGRGGRGRHPGHL
CCCCCCCCCCCCCCC		41.62-
52MethylationGGRGGRGRHPGHLKG
CCCCCCCCCCCCCCH		31.31-
66PhosphorylationGREIGMWYAKKQGQK
HHHHHHHHHHHCCCC		10.3127642862
90MethylationAVVHMDERREEQIVQ
HEECCCHHHHHHHHH		47.23-
101PhosphorylationQIVQLLNSVQAKNDK
HHHHHHHHHHCCCCC		18.6428555341
105UbiquitinationLLNSVQAKNDKESEA
HHHHHHCCCCCCCCC		48.8929967540
108UbiquitinationSVQAKNDKESEAQIS
HHHCCCCCCCCCEEE		72.9629967540
126PhosphorylationPEDHGYGTEVSTKNT
CCCCCCCCEEECCCC		25.40-
131UbiquitinationYGTEVSTKNTPCSEN
CCCEEECCCCCCCCC		51.8529967540
133PhosphorylationTEVSTKNTPCSENKL
CEEECCCCCCCCCCC		27.5120873877
136PhosphorylationSTKNTPCSENKLDIQ
ECCCCCCCCCCCCHH		45.4620873877
139AcetylationNTPCSENKLDIQEKK
CCCCCCCCCCHHHHH		43.4123749302
139UbiquitinationNTPCSENKLDIQEKK
CCCCCCCCCCHHHHH		43.4133845483
145UbiquitinationNKLDIQEKKLINQEK
CCCCHHHHHHHCHHH		36.1829967540
146UbiquitinationKLDIQEKKLINQEKK
CCCHHHHHHHCHHHH		54.5729967540
1522-HydroxyisobutyrylationKKLINQEKKMFRIRN
HHHHCHHHHHHHCCC		39.51-
152AcetylationKKLINQEKKMFRIRN
HHHHCHHHHHHHCCC		39.5125953088
152UbiquitinationKKLINQEKKMFRIRN
HHHHCHHHHHHHCCC		39.5122817900
152 (in isoform 1)Ubiquitination-39.5121890473
152 (in isoform 2)Ubiquitination-39.5121890473
152 (in isoform 3)Ubiquitination-39.5121890473
153UbiquitinationKLINQEKKMFRIRNR
HHHCHHHHHHHCCCC		42.3821890473
153 (in isoform 1)Ubiquitination-42.3821890473
153 (in isoform 2)Ubiquitination-42.3821890473
153 (in isoform 3)Ubiquitination-42.3821890473
161PhosphorylationMFRIRNRSYIDRDSE
HHHCCCCHHCCCCHH		29.9523401153
162PhosphorylationFRIRNRSYIDRDSEY
HHCCCCHHCCCCHHH		12.0122115753
167PhosphorylationRSYIDRDSEYLLQEN
CHHCCCCHHHHCCCC		29.0922115753
169PhosphorylationYIDRDSEYLLQENEP
HCCCCHHHHCCCCCC		19.3622617229
179PhosphorylationQENEPDGTLDQKLLE
CCCCCCCCCCHHHHH		34.2421406692
183UbiquitinationPDGTLDQKLLEDLQK
CCCCCCHHHHHHHHH		55.4929967540
190UbiquitinationKLLEDLQKKKNDLRY
HHHHHHHHHHHCHHH		73.3729967540
191UbiquitinationLLEDLQKKKNDLRYI
HHHHHHHHHHCHHHH		43.79-
206AcetylationEMQHFREKLPSYGMQ
HHHHHHHHCCCCCCC		62.5325953088
206UbiquitinationEMQHFREKLPSYGMQ
HHHHHHHHCCCCCCC		62.5329967540
209PhosphorylationHFREKLPSYGMQKEL
HHHHHCCCCCCCHHH		44.7629496907
214UbiquitinationLPSYGMQKELVNLID
CCCCCCCHHHHHHHH		44.0929967540
248PhosphorylationTQFILDNYIERGKGS
HHHHHHHHHHCCCCC		12.11-
268PhosphorylationCTQPRRISAISVAER
ECCCCCEEEEHHHHH		20.1028450419
271PhosphorylationPRRISAISVAERVAA
CCCEEEEHHHHHHHH		18.2628450419
283PhosphorylationVAAERAESCGSGNST
HHHHHHHHCCCCCCC		23.8528450419
286PhosphorylationERAESCGSGNSTGYQ
HHHHHCCCCCCCCCE		38.8428450419
412UbiquitinationIRYVPEQKEHRSQFK
HCCCCCHHHHHHHHH		54.5529967540
423SulfoxidationSQFKRGFMQGHVNRQ
HHHHHHHHHHCCCHH		5.3430846556
432UbiquitinationGHVNRQEKEEKEAIY
HCCCHHHHHHHHHHH		63.9429967540
440UbiquitinationEEKEAIYKERWPDYV
HHHHHHHHHHCHHHH		34.3924816145
534PhosphorylationLMPTVNQTQVFKRTP
HCCCCCHHHHHCCCC		22.84-
559UbiquitinationNIAETSITIDDVVYV
CCCCCEEEECCEEEE		20.3729967540
573AcetylationVIDGGKIKETHFDTQ
EEECCEEEEEECCCC		61.1126051181
573MalonylationVIDGGKIKETHFDTQ
EEECCEEEEEECCCC		61.1126320211
573UbiquitinationVIDGGKIKETHFDTQ
EEECCEEEEEECCCC		61.1129967540
579UbiquitinationIKETHFDTQNNISTM
EEEEECCCCCCHHHH		32.0529967540
593UbiquitinationMSAEWVSKANAKQRK
HCHHHHHHHCHHHHC		35.7229967540
621PhosphorylationLYNGLRASLLDDYQL
HCCCHHHHHCCCCCC		24.0320068231
626PhosphorylationRASLLDDYQLPEILR
HHHHCCCCCCHHHHC		16.18-
656PhosphorylationGGIAYFLSRLMDPPS
CHHHHHHHHHCCCCC		17.30-
682UbiquitinationMELNALDKQEELTPL
HHHCCCCCCCCCCCC		61.53-
726PhosphorylationLTIAASLSFKDPFVI
HHHHHHCCCCCCEEE		27.9624719451
803UbiquitinationNMKGQFAEHLLGAGF
HCCHHHHHHHHCCCC		36.0421963094
815UbiquitinationAGFVSSRNPKDPESN
CCCCCCCCCCCCCCC		50.3429967540
817AcetylationFVSSRNPKDPESNIN
CCCCCCCCCCCCCCC		84.8826051181
817UbiquitinationFVSSRNPKDPESNIN
CCCCCCCCCCCCCCC		84.8821963094
829AcetylationNINSDNEKIIKAVIC
CCCCCHHHHHHHHHH		56.8623236377
829UbiquitinationNINSDNEKIIKAVIC
CCCCCHHHHHHHHHH		56.8629967540
838UbiquitinationIKAVICAGLYPKVAK
HHHHHHCCCCHHHHH		22.7224816145
844UbiquitinationAGLYPKVAKIRLNLG
CCCCHHHHHEEECCC		14.0029967540
845AcetylationGLYPKVAKIRLNLGK
CCCHHHHHEEECCCC		31.2071003
845UbiquitinationGLYPKVAKIRLNLGK
CCCHHHHHEEECCCC		31.20-
848UbiquitinationPKVAKIRLNLGKKRK
HHHHHEEECCCCCCC		7.6529967540
852UbiquitinationKIRLNLGKKRKMVKV
HEEECCCCCCCEEEE		53.2024816145
853AcetylationIRLNLGKKRKMVKVY
EEECCCCCCCEEEEE		56.2971007
858MalonylationGKKRKMVKVYTKTDG
CCCCCEEEEEECCCC		26.4826320211
858UbiquitinationGKKRKMVKVYTKTDG
CCCCCEEEEEECCCC		26.4829967540
860PhosphorylationKRKMVKVYTKTDGLV
CCCEEEEEECCCCEE		9.22-
862UbiquitinationKMVKVYTKTDGLVAV
CEEEEEECCCCEEEE		27.2529967540
933AcetylationETIAVDEWIVFQSPA
CEEEEEEEEEECCHH		6.3819608861
933UbiquitinationETIAVDEWIVFQSPA
CEEEEEEEEEECCHH		6.3829967540
937UbiquitinationVDEWIVFQSPARIAH
EEEEEEECCHHHHHH		37.3029967540
944 (in isoform 3)Ubiquitination-28.8721890473
946UbiquitinationPARIAHLVKELRKEL
HHHHHHHHHHHHHHH		3.0429967540
947AcetylationARIAHLVKELRKELD
HHHHHHHHHHHHHHH		58.3419608861
947UbiquitinationARIAHLVKELRKELD
HHHHHHHHHHHHHHH		58.3419608861
951UbiquitinationHLVKELRKELDILLQ
HHHHHHHHHHHHHHH		75.2229967540
959UbiquitinationELDILLQEKIESPHP
HHHHHHHHCCCCCCC		56.8433845483
959 (in isoform 2)Ubiquitination-56.8421890473
960UbiquitinationLDILLQEKIESPHPV
HHHHHHHCCCCCCCC		38.5229967540
963PhosphorylationLLQEKIESPHPVDWN
HHHHCCCCCCCCCCC		31.7918279852
973AcetylationPVDWNDTKSRDCAVL
CCCCCCCCHHHHHHH		46.4825953088
973UbiquitinationPVDWNDTKSRDCAVL
CCCCCCCCHHHHHHH		46.4822817900
973 (in isoform 1)Ubiquitination-46.4821890473
1006PhosphorylationPPRFQDGYYS-----
CCCCCCCCCC-----		14.6128796482
1007PhosphorylationPRFQDGYYS------
CCCCCCCCC------		17.2728796482
1008PhosphorylationRFQDGYYS-------
CCCCCCCC-------		25.8427794612
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 DHX36_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DHX36_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 DHX36_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HINT1_HUMANHINT1physical
22939629
FUBP1_HUMANFUBP1physical
22939629
S10A6_HUMANS100A6physical
22939629
TAGL2_HUMANTAGLN2physical
22939629
TEBP_HUMANPTGES3physical
22939629
SEPT7_HUMANSEPT7physical
22939629
HEBP1_HUMANHEBP1physical
22939629
IL7RA_HUMANIL7Rphysical
23151878
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 DHX36_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-947, AND MASS SPECTROMETRY.

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