dbPTM

DHX29_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DHX29_HUMAN
UniProt AC	Q7Z478
Protein Name	ATP-dependent RNA helicase DHX29 {ECO:0000255\|HAMAP-Rule:MF_03068}
Gene Name	DHX29 {ECO:0000255\|HAMAP-Rule:MF_03068}
Organism	Homo sapiens (Human).
Sequence Length	1369
Subcellular Localization	Cytoplasm .
Protein Description	ATP-binding RNA helicase involved in translation initiation. Part of the 43S pre-initiation complex that is required for efficient initiation on mRNAs of higher eukaryotes with structured 5'-UTRs by promoting efficient NTPase-dependent 48S complex formation. Specifically binds to the 40S ribosome near the mRNA entrance. Does not possess a processive helicase activity..
Protein Sequence	MGGKNKKHKAPAAAVVRAAVSASRAKSAEAGIAGEAQSKKPVSRPATAAAAAAGSREPRVKQGPKIYSFNSTNDSSGPANLDKSILKVVINNKLEQRIIGVINEHKKQNNDKGMISGRLTAKKLQDLYMALQAFSFKTKDIEDAMTNTLLYGGDLHSALDWLCLNLSDDALPEGFSQEFEEQQPKSRPKFQSPQIQATISPPLQPKTKTYEEDPKSKPKKEEKNMEVNMKEWILRYAEQQNEEEKNENSKSLEEEEKFDPNERYLHLAAKLLDAKEQAATFKLEKNKQGQKEAQEKIRKFQREMETLEDHPVFNPAMKISHQQNERKKPPVATEGESALNFNLFEKSAAATEEEKDKKKEPHDVRNFDYTARSWTGKSPKQFLIDWVRKNLPKSPNPSFEKVPVGRYWKCRVRVIKSEDDVLVVCPTILTEDGMQAQHLGATLALYRLVKGQSVHQLLPPTYRDVWLEWSDAEKKREELNKMETNKPRDLFIAKLLNKLKQQQQQQQQHSENKRENSEDPEESWENLVSDEDFSALSLESANVEDLEPVRNLFRKLQSTPKYQKLLKERQQLPVFKHRDSIVETLKRHRVVVVAGETGSGKSTQVPHFLLEDLLLNEWEASKCNIVCTQPRRISAVSLANRVCDELGCENGPGGRNSLCGYQIRMESRACESTRLLYCTTGVLLRKLQEDGLLSNVSHVIVDEVHERSVQSDFLLIILKEILQKRSDLHLILMSATVDSEKFSTYFTHCPILRISGRSYPVEVFHLEDIIEETGFVLEKDSEYCQKFLEEEEEVTINVTSKAGGIKKYQEYIPVQTGAHADLNPFYQKYSSRTQHAILYMNPHKINLDLILELLAYLDKSPQFRNIEGAVLIFLPGLAHIQQLYDLLSNDRRFYSERYKVIALHSILSTQDQAAAFTLPPPGVRKIVLATNIAETGITIPDVVFVIDTGRTKENKYHESSQMSSLVETFVSKASALQRQGRAGRVRDGFCFRMYTRERFEGFMDYSVPEILRVPLEELCLHIMKCNLGSPEDFLSKALDPPQLQVISNAMNLLRKIGACELNEPKLTPLGQHLAALPVNVKIGKMLIFGAIFGCLDPVATLAAVMTEKSPFTTPIGRKDEADLAKSALAMADSDHLTIYNAYLGWKKARQEGGYRSEITYCRRNFLNRTSLLTLEDVKQELIKLVKAAGFSSSTTSTSWEGNRASQTLSFQEIALLKAVLVAGLYDNVGKIIYTKSVDVTEKLACIVETAQGKAQVHPSSVNRDLQTHGWLLYQEKIRYARVYLRETTLITPFPVLLFGGDIEVQHRERLLSIDGWIYFQAPVKIAVIFKQLRVLIDSVLRKKLENPKMSLENDKILQIITELIKTENN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Ubiquitination	-MGGKNKKHKAPAAA -CCCCCCCCCCCHHH	60.78	24816145
21	Phosphorylation	AVVRAAVSASRAKSA HHHHHHHHHHHHHHH	18.79	29514088
23	Phosphorylation	VRAAVSASRAKSAEA HHHHHHHHHHHHHHC	25.84	29514088
26	Methylation	AVSASRAKSAEAGIA HHHHHHHHHHHCCCC	49.44	-
27	Phosphorylation	VSASRAKSAEAGIAG HHHHHHHHHHCCCCC	30.29	29255136
38	Phosphorylation	GIAGEAQSKKPVSRP CCCCCCCCCCCCCCH	50.09	-
39	Ubiquitination	IAGEAQSKKPVSRPA CCCCCCCCCCCCCHH	49.36	24816145
43	Phosphorylation	AQSKKPVSRPATAAA CCCCCCCCCHHHHHH	40.86	28555341
47	Phosphorylation	KPVSRPATAAAAAAG CCCCCHHHHHHHHHC	21.36	28555341
65	Acetylation	PRVKQGPKIYSFNST CCCCCCCEEEEECCC	62.19	26051181
67	Phosphorylation	VKQGPKIYSFNSTND CCCCCEEEEECCCCC	17.21	25394399
68	Phosphorylation	KQGPKIYSFNSTNDS CCCCEEEEECCCCCC	22.79	28450419
71	Phosphorylation	PKIYSFNSTNDSSGP CEEEEECCCCCCCCC	26.95	28355574
72	Phosphorylation	KIYSFNSTNDSSGPA EEEEECCCCCCCCCC	44.12	25159151
75	Phosphorylation	SFNSTNDSSGPANLD EECCCCCCCCCCCCC	38.98	28450419
76	Phosphorylation	FNSTNDSSGPANLDK ECCCCCCCCCCCCCH	52.22	28450419
83	Acetylation	SGPANLDKSILKVVI CCCCCCCHHHHHHHH	42.43	25953088
83	Ubiquitination	SGPANLDKSILKVVI CCCCCCCHHHHHHHH	42.43	29967540
84	Phosphorylation	GPANLDKSILKVVIN CCCCCCHHHHHHHHC	32.59	24719451
87	Acetylation	NLDKSILKVVINNKL CCCHHHHHHHHCCHH	32.55	90671
93	Acetylation	LKVVINNKLEQRIIG HHHHHCCHHHHHHHH	49.24	26051181
93	Ubiquitination	LKVVINNKLEQRIIG HHHHHCCHHHHHHHH	49.24	32015554
106	2-Hydroxyisobutyrylation	IGVINEHKKQNNDKG HHHHHHHHHHCCCCC	50.29	-
112	Ubiquitination	HKKQNNDKGMISGRL HHHHCCCCCCCCCHH	53.13	24816145
135	Phosphorylation	YMALQAFSFKTKDIE HHHHHHHCCCCCCHH	28.93	24719451
157	Phosphorylation	LYGGDLHSALDWLCL ECCCCHHHHHHHHHC	37.51	-
192	Phosphorylation	KSRPKFQSPQIQATI CCCCCCCCCCCEEEE	23.16	25159151
198	Phosphorylation	QSPQIQATISPPLQP CCCCCEEEECCCCCC	12.95	30266825
200	Phosphorylation	PQIQATISPPLQPKT CCCEEEECCCCCCCC	18.99	29255136
210	Phosphorylation	LQPKTKTYEEDPKSK CCCCCCCCCCCCCCC	20.91	-
230	Ubiquitination	KNMEVNMKEWILRYA HCCCCHHHHHHHHHH	44.70	-
251	Phosphorylation	EKNENSKSLEEEEKF HHCCCCCCHHHHHHC	40.61	23663014
257	Ubiquitination	KSLEEEEKFDPNERY CCHHHHHHCCCCHHH	59.35	29967540
270	Acetylation	RYLHLAAKLLDAKEQ HHHHHHHHHHHHHHH	43.93	25953088
270	Ubiquitination	RYLHLAAKLLDAKEQ HHHHHHHHHHHHHHH	43.93	29967540
275	2-Hydroxyisobutyrylation	AAKLLDAKEQAATFK HHHHHHHHHHHHHHH	50.45	-
275	Malonylation	AAKLLDAKEQAATFK HHHHHHHHHHHHHHH	50.45	26320211
275	Ubiquitination	AAKLLDAKEQAATFK HHHHHHHHHHHHHHH	50.45	32015554
282	Acetylation	KEQAATFKLEKNKQG HHHHHHHHHHHCHHH	51.92	26051181
333	Phosphorylation	RKKPPVATEGESALN CCCCCCCCCCCCHHC	44.77	-
337	Phosphorylation	PVATEGESALNFNLF CCCCCCCCHHCCCCC	49.25	28555341
346	Ubiquitination	LNFNLFEKSAAATEE HCCCCCHHHCCCCHH	37.75	29967540
372	Methylation	RNFDYTARSWTGKSP CCCCEECCCCCCCCH	25.56	-
380	Acetylation	SWTGKSPKQFLIDWV CCCCCCHHHHHHHHH	61.85	26051181
380	Ubiquitination	SWTGKSPKQFLIDWV CCCCCCHHHHHHHHH	61.85	-
389	Ubiquitination	FLIDWVRKNLPKSPN HHHHHHHHHCCCCCC	53.90	24816145
393	Ubiquitination	WVRKNLPKSPNPSFE HHHHHCCCCCCCCCC	80.06	29967540
394	Phosphorylation	VRKNLPKSPNPSFEK HHHHCCCCCCCCCCC	28.15	25159151
401	Malonylation	SPNPSFEKVPVGRYW CCCCCCCCCCCCCEE	50.24	26320211
401	Ubiquitination	SPNPSFEKVPVGRYW CCCCCCCCCCCCCEE	50.24	29967540
445	Ubiquitination	HLGATLALYRLVKGQ HHHHHHHHHHHHCCC	2.62	33845483
474	Ubiquitination	LEWSDAEKKREELNK HHCCHHHHHHHHHHH	59.87	29967540
481	Ubiquitination	KKREELNKMETNKPR HHHHHHHHCCCCCHH	51.22	24816145
494	Acetylation	PRDLFIAKLLNKLKQ HHHHHHHHHHHHHHH	49.00	26051181
494	Ubiquitination	PRDLFIAKLLNKLKQ HHHHHHHHHHHHHHH	49.00	23000965
498	Ubiquitination	FIAKLLNKLKQQQQQ HHHHHHHHHHHHHHH	57.96	23000965
500	Ubiquitination	AKLLNKLKQQQQQQQ HHHHHHHHHHHHHHH	47.90	23000965
517	Phosphorylation	SENKRENSEDPEESW HHHHHHCCCCHHHHH	38.33	29507054
523	Phosphorylation	NSEDPEESWENLVSD CCCCHHHHHHHHCCH	37.72	23898821
529	Phosphorylation	ESWENLVSDEDFSAL HHHHHHCCHHHHCHH	38.15	28102081
534	Phosphorylation	LVSDEDFSALSLESA HCCHHHHCHHCCCCC	40.39	28102081
537	Phosphorylation	DEDFSALSLESANVE HHHHCHHCCCCCCCH	29.79	28102081
540	Phosphorylation	FSALSLESANVEDLE HCHHCCCCCCCHHCH	30.36	28102081
555	Ubiquitination	PVRNLFRKLQSTPKY HHHHHHHHHHCCHHH	43.47	29967540
564	Ubiquitination	QSTPKYQKLLKERQQ HCCHHHHHHHHHHHC	53.34	-
576	Acetylation	RQQLPVFKHRDSIVE HHCCCCCCCCHHHHH	37.65	25953088
576	Ubiquitination	RQQLPVFKHRDSIVE HHCCCCCCCCHHHHH	37.65	29967540
580	Phosphorylation	PVFKHRDSIVETLKR CCCCCCHHHHHHHHH	28.61	20873877
584	Phosphorylation	HRDSIVETLKRHRVV CCHHHHHHHHHCCEE	27.04	23312004
599	Ubiquitination	VVAGETGSGKSTQVP EEEECCCCCCCCCCC	50.93	32142685
634	Phosphorylation	CTQPRRISAVSLANR ECCCCCCCHHHHHHH	22.32	20873877
637	Phosphorylation	PRRISAVSLANRVCD CCCCCHHHHHHHHHH	22.83	20873877
668	Dimethylation	YQIRMESRACESTRL HHHCCCCCCCCCCCH	29.92	-
674	Methylation	SRACESTRLLYCTTG CCCCCCCCHHHCHHH	31.79	-
734	Phosphorylation	DLHLILMSATVDSEK CCEEEEEECCCCHHH	19.83	20068231
736	Phosphorylation	HLILMSATVDSEKFS EEEEEECCCCHHHHH	19.96	24114839
739	Phosphorylation	LMSATVDSEKFSTYF EEECCCCHHHHHHHH	38.05	24114839
756	Ubiquitination	CPILRISGRSYPVEV CCEEEECCCCCEEEE	21.85	29967540
807	Ubiquitination	SKAGGIKKYQEYIPV CCCCCCEEEEEEECC	50.69	29967540
808	Phosphorylation	KAGGIKKYQEYIPVQ CCCCCEEEEEEECCC	11.11	25394399
811	Phosphorylation	GIKKYQEYIPVQTGA CCEEEEEEECCCCCC	8.59	25884760
816	Phosphorylation	QEYIPVQTGAHADLN EEEECCCCCCCCCCC	36.25	29978859
826	Phosphorylation	HADLNPFYQKYSSRT CCCCCHHHHHHHHHC	12.83	29978859
828	Acetylation	DLNPFYQKYSSRTQH CCCHHHHHHHHHCCE	35.40	26051181
828	Ubiquitination	DLNPFYQKYSSRTQH CCCHHHHHHHHHCCE	35.40	-
956	Phosphorylation	GRTKENKYHESSQMS CCCCCCCCCCHHHHH	23.54	23663014
959	Phosphorylation	KENKYHESSQMSSLV CCCCCCCHHHHHHHH	16.74	23663014
960	Phosphorylation	ENKYHESSQMSSLVE CCCCCCHHHHHHHHH	27.24	23663014
963	Phosphorylation	YHESSQMSSLVETFV CCCHHHHHHHHHHHH	16.94	23663014
964	Phosphorylation	HESSQMSSLVETFVS CCHHHHHHHHHHHHH	30.96	23663014
968	Phosphorylation	QMSSLVETFVSKASA HHHHHHHHHHHHHHH	23.12	23663014
971	Phosphorylation	SLVETFVSKASALQR HHHHHHHHHHHHHHH	20.50	23663014
1004	Ubiquitination	ERFEGFMDYSVPEIL HHCCCCCCCCHHHHH	30.23	29967540
1014	Ubiquitination	VPEILRVPLEELCLH HHHHHCCCHHHHHHH	27.85	29967540
1030	Ubiquitination	MKCNLGSPEDFLSKA HHCCCCCHHHHHHHC	43.29	33845483
1047	Phosphorylation	PPQLQVISNAMNLLR HHHHHHHHHHHHHHH	21.49	20068231
1055	Ubiquitination	NAMNLLRKIGACELN HHHHHHHHHCCCCCC	45.52	29967540
1065	Acetylation	ACELNEPKLTPLGQH CCCCCCCCCCCCHHH	59.83	26051181
1065	Ubiquitination	ACELNEPKLTPLGQH CCCCCCCCCCCCHHH	59.83	29967540
1081	Ubiquitination	AALPVNVKIGKMLIF HCCCCCCCCCHHHHH	40.30	33845483
1084	Ubiquitination	PVNVKIGKMLIFGAI CCCCCCCHHHHHHHH	33.72	-
1159	Phosphorylation	GGYRSEITYCRRNFL CCCCCHHHHHCCCCC	16.71	-
1160	Phosphorylation	GYRSEITYCRRNFLN CCCCHHHHHCCCCCC	6.93	-
1178	Acetylation	LLTLEDVKQELIKLV CCCHHHHHHHHHHHH	50.83	26051181
1178	Ubiquitination	LLTLEDVKQELIKLV CCCHHHHHHHHHHHH	50.83	-
1184	Ubiquitination	VKQELIKLVKAAGFS HHHHHHHHHHHCCCC	3.66	32015554
1191	Ubiquitination	LVKAAGFSSSTTSTS HHHHCCCCCCCCCCC	23.59	29967540
1233	Phosphorylation	DNVGKIIYTKSVDVT CCCCCEEEEECCCCH	16.16	27794612
1234	Phosphorylation	NVGKIIYTKSVDVTE CCCCEEEEECCCCHH	13.36	27794612
1235	Acetylation	VGKIIYTKSVDVTEK CCCEEEEECCCCHHH	31.35	26051181
1235	Ubiquitination	VGKIIYTKSVDVTEK CCCEEEEECCCCHHH	31.35	32015554
1236	Phosphorylation	GKIIYTKSVDVTEKL CCEEEEECCCCHHHH	18.75	26437602
1240	Phosphorylation	YTKSVDVTEKLACIV EEECCCCHHHHHHHH	23.96	27794612
1242	Acetylation	KSVDVTEKLACIVET ECCCCHHHHHHHHHC	31.83	26051181
1242	Ubiquitination	KSVDVTEKLACIVET ECCCCHHHHHHHHHC	31.83	29967540
1267	Phosphorylation	SVNRDLQTHGWLLYQ HCCHHHHHCCEEHHH	29.65	25690035
1273	Phosphorylation	QTHGWLLYQEKIRYA HHCCEEHHHHHHHHC	16.68	25690035
1291	Ubiquitination	LRETTLITPFPVLLF CCCCCEECCCCEEEE	23.22	29967540
1342	Ubiquitination	LIDSVLRKKLENPKM HHHHHHHHHCCCCCC	58.51	29967540
1361	Phosphorylation	DKILQIITELIKTEN HHHHHHHHHHHHHCC	26.77	-
1366	Phosphorylation	IITELIKTENN---- HHHHHHHHCCC----	36.63	-

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 DHX29_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DHX29_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 DHX29_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAPOG_HUMAN	PAPOLG	physical	22939629
FOXM1_HUMAN	FOXM1	physical	22939629
RECQ5_HUMAN	RECQL5	physical	22939629
IKKA_HUMAN	CHUK	physical	22939629
IFIT2_HUMAN	IFIT2	physical	22939629
SNAA_HUMAN	NAPA	physical	22939629
HAUS7_HUMAN	HAUS7	physical	22939629
PGLT1_HUMAN	POGLUT1	physical	22939629
MTDC_HUMAN	MTHFD2	physical	22939629
CKAP5_HUMAN	CKAP5	physical	26344197
DJC17_HUMAN	DNAJC17	physical	26344197
EDF1_HUMAN	EDF1	physical	26344197
RECQ5_HUMAN	RECQL5	physical	26344197

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 DHX29_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-200, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-192 AND SER-200, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-200, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.	15302935 [Abstract]