DD19B_HUMAN - dbPTM
DD19B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DD19B_HUMAN
UniProt AC Q9UMR2
Protein Name ATP-dependent RNA helicase DDX19B
Gene Name DDX19B
Organism Homo sapiens (Human).
Sequence Length 479
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, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins..
Protein Sequence MATDSWALAVDEQEAAAESLSNLHLKEEKIKPDTNGAVVKTNANAEKTDEEEKEDRAAQSLLNKLIRSNLVDNTNQVEVLQRDPNSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDGNPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNILNRIQEHFNKKIERLDTDDLDEIEKIAN
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
-----CCCCCCEEEH
29.3028634298
5Phosphorylation---MATDSWALAVDE
---CCCCCCEEEHHH
15.1928634298
19PhosphorylationEQEAAAESLSNLHLK
HHHHHHHHHHCCCCC
32.1627251275
41PhosphorylationTNGAVVKTNANAEKT
CCCCEEECCCCCCCC
28.1423312004
48PhosphorylationTNANAEKTDEEEKED
CCCCCCCCCHHHHHH
39.9028985074
60PhosphorylationKEDRAAQSLLNKLIR
HHHHHHHHHHHHHHH
30.0524275569
64UbiquitinationAAQSLLNKLIRSNLV
HHHHHHHHHHHCCCC
45.3121890473
64 (in isoform 2)Ubiquitination-45.3121890473
64UbiquitinationAAQSLLNKLIRSNLV
HHHHHHHHHHHCCCC
45.3121890473
64 (in isoform 1)Ubiquitination-45.3121890473
69UbiquitinationLNKLIRSNLVDNTNQ
HHHHHHCCCCCCCCC
33.9521890473
74PhosphorylationRSNLVDNTNQVEVLQ
HCCCCCCCCCEEEEC
23.6723186163
78UbiquitinationVDNTNQVEVLQRDPN
CCCCCCEEEECCCCC
27.9621890473
86PhosphorylationVLQRDPNSPLYSVKS
EECCCCCCCCCCCCC
22.9725159151
89PhosphorylationRDPNSPLYSVKSFEE
CCCCCCCCCCCCHHH
18.1428450419
90PhosphorylationDPNSPLYSVKSFEEL
CCCCCCCCCCCHHHH
30.6528450419
92UbiquitinationNSPLYSVKSFEELRL
CCCCCCCCCHHHHCC
43.4121890473
92 (in isoform 1)Ubiquitination-43.4121890473
92 (in isoform 2)Ubiquitination-43.4121890473
92UbiquitinationNSPLYSVKSFEELRL
CCCCCCCCCHHHHCC
43.4121890473
93 (in isoform 2)Phosphorylation-35.4224275569
93PhosphorylationSPLYSVKSFEELRLK
CCCCCCCCHHHHCCC
35.4228857561
97UbiquitinationSVKSFEELRLKPQLL
CCCCHHHHCCCHHHH
6.4721890473
98 (in isoform 4)Phosphorylation-43.9024275569
108PhosphorylationPQLLQGVYAMGFNRP
HHHHHHHHHCCCCCC
9.5528842319
145PhosphorylationSQSGTGKTAAFVLAM
CCCCCCHHHHHHHHH
25.27-
154PhosphorylationAFVLAMLSQVEPANK
HHHHHHHHCCCCCCC
21.0624850871
156 (in isoform 2)Ubiquitination-9.5121890473
161UbiquitinationSQVEPANKYPQCLCL
HCCCCCCCCCCCEEE
61.4921890473
169PhosphorylationYPQCLCLSPTYELAL
CCCCEEECCCHHHHH
17.7528258704
172PhosphorylationCLCLSPTYELALQTG
CEEECCCHHHHHHHC
16.6028258704
187UbiquitinationKVIEQMGKFYPELKL
HHHHHHHHHCHHHHH
36.0621890473
187UbiquitinationKVIEQMGKFYPELKL
HHHHHHHHHCHHHHH
36.0621890473
187 (in isoform 1)Ubiquitination-36.0621890473
193UbiquitinationGKFYPELKLAYAVRG
HHHCHHHHHHHHHHC
29.43-
198AcetylationELKLAYAVRGNKLER
HHHHHHHHHCCCCCC
5.4019608861
199MethylationLKLAYAVRGNKLERG
HHHHHHHHCCCCCCC
34.49-
202AcetylationAYAVRGNKLERGQKI
HHHHHCCCCCCCCCC
55.337670197
203AcetylationYAVRGNKLERGQKIS
HHHHCCCCCCCCCCC
6.6919608861
217PhosphorylationSEQIVIGTPGTVLDW
CCEEECCCCCCHHHH
13.8628348404
220PhosphorylationIVIGTPGTVLDWCSK
EECCCCCCHHHHHHC
21.0628348404
229AcetylationLDWCSKLKFIDPKKI
HHHHHCCCCCCHHHC
43.9719608861
287AcetylationSVWKFAQKVVPDPNV
HHHHHHHHHCCCCCE
41.5924780969
287UbiquitinationSVWKFAQKVVPDPNV
HHHHHHHHHCCCCCE
41.59-
308UbiquitinationEETLDTIKQYYVLCS
HHHHHHHHHHHHHHC
34.05-
345PhosphorylationIFCHTRKTASWLAAE
HHHCCHHHHHHHHHH
23.7220068231
347PhosphorylationCHTRKTASWLAAELS
HCCHHHHHHHHHHHC
28.0520068231
354PhosphorylationSWLAAELSKEGHQVA
HHHHHHHCCCCCCEE
21.8420068231
422PhosphorylationDGNPDNETYLHRIGR
CCCCCCCCCHHHCCC
37.32-
423PhosphorylationGNPDNETYLHRIGRT
CCCCCCCCHHHCCCC
8.37-
445PhosphorylationLAVNMVDSKHSMNIL
EEEEECCCHHHHHHH
22.3620860994
448PhosphorylationNMVDSKHSMNILNRI
EECCCHHHHHHHHHH
19.7722798277
468PhosphorylationKKIERLDTDDLDEIE
HHHHCCCCCCHHHHH
35.6827273156
476UbiquitinationDDLDEIEKIAN----
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
93SPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DD19B_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 DD19B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCK_HUMANDCKphysical
16169070
RACK1_HUMANGNB2L1physical
16169070
XPO7_HUMANXPO7physical
16169070
A4_HUMANAPPphysical
21832049
CTBP2_HUMANCTBP2physical
22863883
MI4GD_HUMANMIF4GDphysical
25416956
TRFE_HUMANTFphysical
26186194
PLEC_HUMANPLECphysical
26186194
EPIPL_HUMANEPPK1physical
26186194
EVPL_HUMANEVPLphysical
26186194
CO3_HUMANC3physical
26186194
ANXA1_HUMANANXA1physical
26186194
AACT_HUMANSERPINA3physical
26186194
TRI29_HUMANTRIM29physical
26186194
CALL5_HUMANCALML5physical
26186194
GELS_HUMANGSNphysical
26186194
FIBB_HUMANFGBphysical
26186194
TGM1_HUMANTGM1physical
26186194
FIBG_HUMANFGGphysical
26186194
PEPL_HUMANPPLphysical
26186194
APOA1_HUMANAPOA1physical
26186194
AK1BA_HUMANAKR1B10physical
26186194
TRI25_HUMANTRIM25physical
26186194
PLSL_HUMANLCP1physical
26186194
DRA_HUMANHLA-DRAphysical
26186194
PSME1_HUMANPSME1physical
26186194
TREX2_HUMANTREX2physical
26186194
IQGA1_HUMANIQGAP1physical
26186194
SPB5_HUMANSERPINB5physical
26186194
CALL3_HUMANCALML3physical
26186194
MVP_HUMANMVPphysical
26186194
SPB4_HUMANSERPINB4physical
26186194
SPB3_HUMANSERPINB3physical
26186194
ST2B1_HUMANSULT2B1physical
26186194
FIBA_HUMANFGAphysical
26186194
RNAS7_HUMANRNASE7physical
26186194
POF1B_HUMANPOF1Bphysical
26186194
CAPG_HUMANCAPGphysical
26186194
NGAL_HUMANLCN2physical
26186194
SYNC_HUMANNARSphysical
26186194
INVO_HUMANIVLphysical
26186194
HMOX1_HUMANHMOX1physical
26186194
SAP3_HUMANGM2Aphysical
26186194
ILEU_HUMANSERPINB1physical
26186194
RAB5A_HUMANRAB5Aphysical
26186194
TYPH_HUMANTYMPphysical
26186194
STAT3_HUMANSTAT3physical
26186194
PPAP_HUMANACPPphysical
26186194
TRFL_HUMANLTFphysical
26186194
ANXA8_HUMANANXA8physical
26186194
S10A7_HUMANS100A7physical
26186194
NAGK_HUMANNAGKphysical
26186194
A1AT_HUMANSERPINA1physical
26186194
PAI2_HUMANSERPINB2physical
26186194
LOX15_HUMANALOX15physical
26186194
LEG1_HUMANLGALS1physical
26186194
FCGBP_HUMANFCGBPphysical
26186194
HUTH_HUMANHALphysical
26186194
HPT_HUMANHPphysical
26186194
NDRG2_HUMANNDRG2physical
26186194
A1AG1_HUMANORM1physical
26186194
RABP2_HUMANCRABP2physical
26186194
CFAB_HUMANCFBphysical
26186194
IGLL5_HUMANIGLL5physical
26186194
ACOX1_HUMANACOX1physical
26186194
SPB7_HUMANSERPINB7physical
26186194
EHD4_HUMANEHD4physical
26186194
RIR2_HUMANRRM2physical
26344197
FCGBP_HUMANFCGBPphysical
28514442
FIBB_HUMANFGBphysical
28514442
DRA_HUMANHLA-DRAphysical
28514442
CO3_HUMANC3physical
28514442
PEPL_HUMANPPLphysical
28514442
MVP_HUMANMVPphysical
28514442
ANXA8_HUMANANXA8physical
28514442
FIBG_HUMANFGGphysical
28514442
ST2B1_HUMANSULT2B1physical
28514442
FIBA_HUMANFGAphysical
28514442
TYPH_HUMANTYMPphysical
28514442
LOX15_HUMANALOX15physical
28514442
A1AT_HUMANSERPINA1physical
28514442
A1AG1_HUMANORM1physical
28514442
NDRG2_HUMANNDRG2physical
28514442
EVPL_HUMANEVPLphysical
28514442
APOA1_HUMANAPOA1physical
28514442
TREX2_HUMANTREX2physical
28514442
INVO_HUMANIVLphysical
28514442
SPB4_HUMANSERPINB4physical
28514442
ILEU_HUMANSERPINB1physical
28514442
AACT_HUMANSERPINA3physical
28514442
SPB7_HUMANSERPINB7physical
28514442
TRI29_HUMANTRIM29physical
28514442
SPB5_HUMANSERPINB5physical
28514442
NGAL_HUMANLCN2physical
28514442
TRI25_HUMANTRIM25physical
28514442
STAT3_HUMANSTAT3physical
28514442
AK1BA_HUMANAKR1B10physical
28514442
PLSL_HUMANLCP1physical
28514442
HPT_HUMANHPphysical
28514442
CAPG_HUMANCAPGphysical
28514442
SYNC_HUMANNARSphysical
28514442
HUTH_HUMANHALphysical
28514442
RABP2_HUMANCRABP2physical
28514442
TRFE_HUMANTFphysical
28514442
PAI2_HUMANSERPINB2physical
28514442
CALL5_HUMANCALML5physical
28514442
EPIPL_HUMANEPPK1physical
28514442
POF1B_HUMANPOF1Bphysical
28514442
PSME1_HUMANPSME1physical
28514442
TRFL_HUMANLTFphysical
28514442
SPB3_HUMANSERPINB3physical
28514442
RNAS7_HUMANRNASE7physical
28514442
LEG1_HUMANLGALS1physical
28514442
H15_HUMANHIST1H1Bphysical
28514442
CFAB_HUMANCFBphysical
28514442
S10A9_HUMANS100A9physical
28514442
GSDMA_HUMANGSDMAphysical
28514442
I36RA_HUMANIL36RNphysical
28514442
SAP3_HUMANGM2Aphysical
28514442
IGLL5_HUMANIGLL5physical
28514442
HMOX1_HUMANHMOX1physical
28514442
PLEC_HUMANPLECphysical
28514442
CATL2_HUMANCTSVphysical
28514442
TGM1_HUMANTGM1physical
28514442
ABC3A_HUMANAPOBEC3Aphysical
28514442
LAMP2_HUMANLAMP2physical
28514442
ANXA1_HUMANANXA1physical
28514442
KPYM_HUMANPKMphysical
28514442
CALL3_HUMANCALML3physical
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 DD19B_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-229, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASSSPECTROMETRY.

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