DD19A_HUMAN - dbPTM
DD19A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DD19A_HUMAN
UniProt AC Q9NUU7
Protein Name ATP-dependent RNA helicase DDX19A
Gene Name DDX19A
Organism Homo sapiens (Human).
Sequence Length 478
Subcellular Localization Cytoplasm. Nucleus, nuclear pore complex. Nucleus membrane
Peripheral membrane protein
Cytoplasmic side. Nuclear pore complex cytoplasmic fibrils.
Protein Description ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19 functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins (By similarity)..
Protein Sequence MATDSWALAVDEQEAAVKSMTNLQIKEEKVKADTNGIIKTSTTAEKTDEEEKEDRAAQSLLNKLIRSNLVDNTNQVEVLQRDPNSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPMMLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDGNPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNILNRIQEHFNKKIERLDTDDLDEIEKIAN
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
2Acetylation------MATDSWALA
------CCCCCCEEE		21.8022223895
3Phosphorylation-----MATDSWALAV
-----CCCCCCEEEC		29.3027251275
5Phosphorylation---MATDSWALAVDE
---CCCCCCEEECCH		15.1927251275
19PhosphorylationEQEAAVKSMTNLQIK
HHHHHHHHHHCCHHC		25.0025159151
20SulfoxidationQEAAVKSMTNLQIKE
HHHHHHHHHCCHHCC		2.0921406390
21PhosphorylationEAAVKSMTNLQIKEE
HHHHHHHHCCHHCCE		39.6125159151
26SumoylationSMTNLQIKEEKVKAD
HHHCCHHCCEEECCC		47.0325114211
26SumoylationSMTNLQIKEEKVKAD
HHHCCHHCCEEECCC		47.03-
34PhosphorylationEEKVKADTNGIIKTS
CEEECCCCCCCEEEC		39.96-
40PhosphorylationDTNGIIKTSTTAEKT
CCCCCEEECCCCCCC		22.3928111955
41PhosphorylationTNGIIKTSTTAEKTD
CCCCEEECCCCCCCC		20.8228111955
42PhosphorylationNGIIKTSTTAEKTDE
CCCEEECCCCCCCCH		34.9428111955
43PhosphorylationGIIKTSTTAEKTDEE
CCEEECCCCCCCCHH		32.3628111955
46AcetylationKTSTTAEKTDEEEKE
EECCCCCCCCHHHHH		59.8325953088
47PhosphorylationTSTTAEKTDEEEKED
ECCCCCCCCHHHHHH		39.9028111955
59PhosphorylationKEDRAAQSLLNKLIR
HHHHHHHHHHHHHHH		30.0528555341
63UbiquitinationAAQSLLNKLIRSNLV
HHHHHHHHHHHCCCC		45.3121890473
63UbiquitinationAAQSLLNKLIRSNLV
HHHHHHHHHHHCCCC		45.3121890473
63UbiquitinationAAQSLLNKLIRSNLV
HHHHHHHHHHHCCCC		45.3121890473
73PhosphorylationRSNLVDNTNQVEVLQ
HCCCCCCCCCEEEEC		23.6723186163
85PhosphorylationVLQRDPNSPLYSVKS
EECCCCCCCCCCCCC		22.9725159151
88PhosphorylationRDPNSPLYSVKSFEE
CCCCCCCCCCCCHHH		18.1428450419
89PhosphorylationDPNSPLYSVKSFEEL
CCCCCCCCCCCHHHH		30.6528450419
91UbiquitinationNSPLYSVKSFEELRL
CCCCCCCCCHHHHCC		43.4121890473
91UbiquitinationNSPLYSVKSFEELRL
CCCCCCCCCHHHHCC		43.4121890473
91UbiquitinationNSPLYSVKSFEELRL
CCCCCCCCCHHHHCC		43.4121890473
92PhosphorylationSPLYSVKSFEELRLK
CCCCCCCCHHHHCCC		35.4228857561
96UbiquitinationSVKSFEELRLKPQLL
CCCCHHHHCCCHHHH		6.47-
107PhosphorylationPQLLQGVYAMGFNRP
HHHHHHHHHCCCCCC		9.5528842319
144PhosphorylationSQSGTGKTAAFVLAM
CCCCCCHHHHHHHHH		25.2720860994
168PhosphorylationYPQCLCLSPTYELAL
CCCCEEECCCHHHHH		17.7528152594
170PhosphorylationQCLCLSPTYELALQT
CCEEECCCHHHHHHH		26.6728152594
171PhosphorylationCLCLSPTYELALQTG
CEEECCCHHHHHHHC		16.6028258704
186AcetylationKVIEQMGKFYPELKL
HHHHHHHHHCHHHHH		36.0625953088
186UbiquitinationKVIEQMGKFYPELKL
HHHHHHHHHCHHHHH		36.0621890473
186UbiquitinationKVIEQMGKFYPELKL
HHHHHHHHHCHHHHH		36.0621890473
186UbiquitinationKVIEQMGKFYPELKL
HHHHHHHHHCHHHHH		36.0621890473
192UbiquitinationGKFYPELKLAYAVRG
HHHCHHHHHHHHHHC		29.43-
196AcetylationPELKLAYAVRGNKLE
HHHHHHHHHHCCCCC		4.48-
198MethylationLKLAYAVRGNKLERG
HHHHHHHHCCCCCCC		34.49-
201AcetylationAYAVRGNKLERGQKI
HHHHHCCCCCCCCCC		55.337670159
216PhosphorylationSEQIVIGTPGTVLDW
CCEEECCCCCCHHHH		13.8628348404
219PhosphorylationIVIGTPGTVLDWCSK
EECCCCCCHHHHHHC		21.0628348404
228AcetylationLDWCSKLKFIDPKKI
HHHHHCCCCCCHHHC		43.9726051181
286UbiquitinationSVWKFAQKVVPDPNV
HHHHHHHHHCCCCCE		41.59-
286AcetylationSVWKFAQKVVPDPNV
HHHHHHHHHCCCCCE		41.5923236377
307UbiquitinationEETLDTIKQYYVLCS
HHHHHHHHHHHHHHC		34.05-
3432-HydroxyisobutyrylationMIFCHTRKTASWLAA
HHHHCCHHHHHHHHH		49.99-
343MalonylationMIFCHTRKTASWLAA
HHHHCCHHHHHHHHH		49.9926320211
344PhosphorylationIFCHTRKTASWLAAE
HHHCCHHHHHHHHHH		23.7220068231
346PhosphorylationCHTRKTASWLAAELS
HCCHHHHHHHHHHHC		28.0520068231
353PhosphorylationSWLAAELSKEGHQVA
HHHHHHHCCCCCCEE		21.8420068231
355AcetylationLAAELSKEGHQVALL
HHHHHCCCCCCEEEE		59.54-
421PhosphorylationDGNPDNETYLHRIGR
CCCCCCCCCHHHCCC		37.32-
422PhosphorylationGNPDNETYLHRIGRT
CCCCCCCCHHHCCCC		8.37-
441SulfoxidationKRGLAVNMVDSKHSM
CCCEEEEECCCHHHH		2.5930846556
444PhosphorylationLAVNMVDSKHSMNIL
EEEEECCCHHHHHHH		22.3620860994
445AcetylationAVNMVDSKHSMNILN
EEEECCCHHHHHHHH		34.9221466224
447PhosphorylationNMVDSKHSMNILNRI
EECCCHHHHHHHHHH		19.7722798277
4602-HydroxyisobutyrylationRIQEHFNKKIERLDT
HHHHHHHHHHHCCCC		54.93-
467PhosphorylationKKIERLDTDDLDEIE
HHHHCCCCCCHHHHH		35.6827273156
475UbiquitinationDDLDEIEKIAN----
CCHHHHHHHHC----		53.43-
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
92SPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DD19A_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 DD19A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MI4GD_HUMANMIF4GDphysical
16189514
SPTB2_HUMANSPTBN1physical
22939629
XPO1_HUMANXPO1physical
22939629
NXF1_HUMANNXF1physical
22939629
SPTN1_HUMANSPTAN1physical
22939629
MI4GD_HUMANMIF4GDphysical
25416956
DDX25_HUMANDDX25physical
26186194
DD19B_HUMANDDX19Bphysical
26186194
NU214_HUMANNUP214physical
26186194
NUP88_HUMANNUP88physical
26186194
NUP62_HUMANNUP62physical
26186194
CTIF_HUMANCTIFphysical
26186194
NIF3L_HUMANNIF3L1physical
26344197
DD19B_HUMANDDX19Bphysical
28514442
CTIF_HUMANCTIFphysical
28514442
DDX25_HUMANDDX25physical
28514442
NU214_HUMANNUP214physical
28514442
NUP88_HUMANNUP88physical
28514442
MI4GD_HUMANMIF4GDphysical
28514442
NUP62_HUMANNUP62physical
28514442
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 DD19A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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