dbPTM

DHX30_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DHX30_HUMAN
UniProt AC	Q7L2E3
Protein Name	Putative ATP-dependent RNA helicase DHX30
Gene Name	DHX30
Organism	Homo sapiens (Human).
Sequence Length	1194
Subcellular Localization	Isoform 2: Cytoplasm. Isoform 1: Cytoplasm. Mitochondrion. Cytoplasm . Mitochondrion matrix, mitochondrion nucleoid . Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids.
Protein Description	Plays an important role in the assembly of the mitochondrial large ribosomal subunit. [PubMed: 25683715 Required for optimal function of the zinc-finger antiviral protein ZC3HAV1 (By similarity Associates with mitochondrial DNA]
Protein Sequence	MFSLDSFRKDRAQHRQRQCKLPPPRLPPMCVNPTPGGTISRASRDLLKEFPQPKNLLNSVIGRALGISHAKDKLVYVHTNGPKKKKVTLHIKWPKSVEVEGYGSKKIDAERQAAAAACQLFKGWGLLGPRNELFDAAKYRVLADRFGSPADSWWRPEPTMPPTSWRQLNPESIRPGGPGGLSRSLGREEEEDEEEELEEGTIDVTDFLSMTQQDSHAPLRDSRGSSFEMTDDDSAIRALTQFPLPKNLLAKVIQIATSSSTAKNLMQFHTVGTKTKLSTLTLLWPCPMTFVAKGRRKAEAENKAAALACKKLKSLGLVDRNNEPLTHAMYNLASLRELGETQRRPCTIQVPEPILRKIETFLNHYPVESSWIAPELRLQSDDILPLGKDSGPLSDPITGKPYVPLLEAEEVRLSQSLLELWRRRGPVWQEAPQLPVDPHRDTILNAIEQHPVVVISGDTGCGKTTRIPQLLLERYVTEGRGARCNVIITQPRRISAVSVAQRVSHELGPSLRRNVGFQVRLESKPPSRGGALLFCTVGILLRKLQSNPSLEGVSHVIVDEVHERDVNTDFLLILLKGLQRLNPALRLVLMSATGDNERFSRYFGGCPVIKVPGFMYPVKEHYLEDILAKLGKHQYLHRHRHHESEDECALDLDLVTDLVLHIDARGEPGGILCFLPGWQEIKGVQQRLQEALGMHESKYLILPVHSNIPMMDQKAIFQQPPVGVRKIVLATNIAETSITINDIVHVVDSGLHKEERYDLKTKVSCLETVWVSRANVIQRRGRAGRCQSGFAYHLFPRSRLEKMVPFQVPEILRTPLENLVLQAKIHMPEKTAVEFLSKAVDSPNIKAVDEAVILLQEIGVLDQREYLTTLGQRLAHISTDPRLAKAIVLAAIFRCLHPLLVVVSCLTRDPFSSSLQNRAEVDKVKALLSHDSGSDHLAFVRAVAGWEEVLRWQDRSSRENYLEENLLYAPSLRFIHGLIKQFSENIYEAFLVGKPSDCTLASAQCNEYSEEEELVKGVLMAGLYPNLIQVRQGKVTRQGKFKPNSVTYRTKSGNILLHKSTINREATRLRSRWLTYFMAVKSNGSVFVRDSSQVHPLAVLLLTDGDVHIRDDGRRATISLSDSDLLRLEGDSRTVRLLKELRRALGRMVERSLRSELAALPPSVQEEHGQLLALLAELLRGPCGSFDVRKTADD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MFSLDSFRKD -----CCCHHHHHHH	43.03	23186163
6	Phosphorylation	--MFSLDSFRKDRAQ --CCCHHHHHHHHHH	32.04	23186163
9 (in isoform 3)	Ubiquitination	-	49.94	21890473
15 (in isoform 2)	Phosphorylation	-	22.69	21815630
34	Phosphorylation	PPMCVNPTPGGTISR CCCCCCCCCCCHHCH	29.39	20068231
36 (in isoform 2)	Phosphorylation	-	48.64	28387310
38	Phosphorylation	VNPTPGGTISRASRD CCCCCCCHHCHHHHH	22.99	30177828
40	Phosphorylation	PTPGGTISRASRDLL CCCCCHHCHHHHHHH	22.95	30177828
48	Acetylation	RASRDLLKEFPQPKN HHHHHHHHHCCCCHH	65.68	26051181
48	Ubiquitination	RASRDLLKEFPQPKN HHHHHHHHHCCCCHH	65.68	2189047
48 (in isoform 1)	Ubiquitination	-	65.68	21890473
59	Phosphorylation	QPKNLLNSVIGRALG CCHHHHHHHHHHHHC	18.32	20860994
71	Ubiquitination	ALGISHAKDKLVYVH HHCCCCCCCCEEEEE	50.39	-
73	Acetylation	GISHAKDKLVYVHTN CCCCCCCCEEEEECC	38.86	25953088
76	Phosphorylation	HAKDKLVYVHTNGPK CCCCCEEEEECCCCC	9.28	24719451
76 (in isoform 2)	Ubiquitination	-	9.28	21890473
79	Phosphorylation	DKLVYVHTNGPKKKK CCEEEEECCCCCCCE	31.65	24719451
92	Acetylation	KKVTLHIKWPKSVEV CEEEEEEECCCCEEE	46.85	26051181
95	Ubiquitination	TLHIKWPKSVEVEGY EEEEECCCCEEEEEC	67.05	-
96	Phosphorylation	LHIKWPKSVEVEGYG EEEECCCCEEEEECC	21.30	19060867
102	Phosphorylation	KSVEVEGYGSKKIDA CCEEEEECCCCCCCH	12.53	28152594
104	Phosphorylation	VEVEGYGSKKIDAER EEEEECCCCCCCHHH	23.45	28152594
105	Ubiquitination	EVEGYGSKKIDAERQ EEEECCCCCCCHHHH	49.76	-
122	Acetylation	AAACQLFKGWGLLGP HHHHHHHCCCCCCCC	63.45	26051181
138	Ubiquitination	NELFDAAKYRVLADR HHHHHHHHHHHHHHH	35.00	-
145	Methylation	KYRVLADRFGSPADS HHHHHHHHHCCCCHH	32.02	-
148	Phosphorylation	VLADRFGSPADSWWR HHHHHHCCCCHHCCC	17.76	27174698
152	Phosphorylation	RFGSPADSWWRPEPT HHCCCCHHCCCCCCC	30.55	27174698
166 (in isoform 2)	Ubiquitination	-	30.76	-
172	Phosphorylation	WRQLNPESIRPGGPG HHHCCHHHCCCCCCC	25.75	28555341
182	Phosphorylation	PGGPGGLSRSLGREE CCCCCCHHHCCCCCC	24.09	28555341
205	Phosphorylation	EEGTIDVTDFLSMTQ HHCCEEHHHHHHHHC	19.79	26471730
209	Phosphorylation	IDVTDFLSMTQQDSH EEHHHHHHHHCCCCC	21.56	26471730
211	Phosphorylation	VTDFLSMTQQDSHAP HHHHHHHHCCCCCCC	21.50	26471730
215	Phosphorylation	LSMTQQDSHAPLRDS HHHHCCCCCCCCCCC	19.74	26471730
222	Phosphorylation	SHAPLRDSRGSSFEM CCCCCCCCCCCCCCC	31.91	28857561
225	Phosphorylation	PLRDSRGSSFEMTDD CCCCCCCCCCCCCCC	30.64	23401153
226	Phosphorylation	LRDSRGSSFEMTDDD CCCCCCCCCCCCCCH	28.22	23927012
229	Sulfoxidation	SRGSSFEMTDDDSAI CCCCCCCCCCCHHHH	4.73	21406390
230	Phosphorylation	RGSSFEMTDDDSAIR CCCCCCCCCCHHHHH	29.13	23927012
234	Phosphorylation	FEMTDDDSAIRALTQ CCCCCCHHHHHHHHC	32.37	23927012
240	Phosphorylation	DSAIRALTQFPLPKN HHHHHHHHCCCCCHH	27.46	-
257	Phosphorylation	AKVIQIATSSSTAKN HHHHHHHCCCCHHHH	30.67	20860994
258	Phosphorylation	KVIQIATSSSTAKNL HHHHHHCCCCHHHHH	17.17	22210691
261	Phosphorylation	QIATSSSTAKNLMQF HHHCCCCHHHHHHCC	43.53	22210691
263	Ubiquitination	ATSSSTAKNLMQFHT HCCCCHHHHHHCCCC	51.18	-
274	Ubiquitination	QFHTVGTKTKLSTLT CCCCCCCCCCCCHHE	37.42	-
276	Ubiquitination	HTVGTKTKLSTLTLL CCCCCCCCCCHHEEE	41.83	-
303	Ubiquitination	RKAEAENKAAALACK HHHHHHHHHHHHHHH	30.79	-
310	Acetylation	KAAALACKKLKSLGL HHHHHHHHHHHHCCC	56.38	25953088
320	Methylation	KSLGLVDRNNEPLTH HHCCCCCCCCCCHHH	40.15	-
334	Phosphorylation	HAMYNLASLRELGET HHHHHHHHHHHHHCC	31.00	24719451
346	Glutathionylation	GETQRRPCTIQVPEP HCCCCCCCEEECCHH	5.06	22555962
357	Ubiquitination	VPEPILRKIETFLNH CCHHHHHHHHHHHHC	41.26	-
377	Methylation	SWIAPELRLQSDDIL CCCCHHHHCCCCCEE	29.08	-
380	Phosphorylation	APELRLQSDDILPLG CHHHHCCCCCEECCC	41.67	30266825
388	Ubiquitination	DDILPLGKDSGPLSD CCEECCCCCCCCCCC	57.30	-
390	Phosphorylation	ILPLGKDSGPLSDPI EECCCCCCCCCCCCC	45.88	28450419
394	Phosphorylation	GKDSGPLSDPITGKP CCCCCCCCCCCCCCC	44.46	22617229
400	Acetylation	LSDPITGKPYVPLLE CCCCCCCCCCCCCEE	25.24	26051181
400	Ubiquitination	LSDPITGKPYVPLLE CCCCCCCCCCCCCEE	25.24	-
402	Phosphorylation	DPITGKPYVPLLEAE CCCCCCCCCCCEEHH	20.41	29496907
495	O-linked_Glycosylation	ITQPRRISAVSVAQR EECCCCCCEEHHHHH	22.32	30379171
495	Phosphorylation	ITQPRRISAVSVAQR EECCCCCCEEHHHHH	22.32	24719451
498	O-linked_Glycosylation	PRRISAVSVAQRVSH CCCCCEEHHHHHHHH	16.08	30379171
498	Phosphorylation	PRRISAVSVAQRVSH CCCCCEEHHHHHHHH	16.08	21406692
504	Phosphorylation	VSVAQRVSHELGPSL EHHHHHHHHHHCHHH	17.27	24532841
590	Sulfoxidation	PALRLVLMSATGDNE HHHHHHHHHCCCCCH	1.68	28183972
610	Acetylation	FGGCPVIKVPGFMYP CCCCCEEECCCCCCC	42.48	26051181
619	Acetylation	PGFMYPVKEHYLEDI CCCCCCCCHHHHHHH	33.98	26051181
619	Ubiquitination	PGFMYPVKEHYLEDI CCCCCCCCHHHHHHH	33.98	-
622	Phosphorylation	MYPVKEHYLEDILAK CCCCCHHHHHHHHHH	16.93	30576142
629	Acetylation	YLEDILAKLGKHQYL HHHHHHHHHCCCHHH	55.09	23236377
629	Ubiquitination	YLEDILAKLGKHQYL HHHHHHHHHCCCHHH	55.09	-
632	Ubiquitination	DILAKLGKHQYLHRH HHHHHHCCCHHHHCC	37.66	-
635	Phosphorylation	AKLGKHQYLHRHRHH HHHCCCHHHHCCCCC	12.28	30576142
673	Glutathionylation	GEPGGILCFLPGWQE CCCCCEEEECCCHHH	2.88	22555962
682	Ubiquitination	LPGWQEIKGVQQRLQ CCCHHHHHHHHHHHH	52.88	-
694	Sulfoxidation	RLQEALGMHESKYLI HHHHHHCCCCCCEEE	3.09	21406390
714	Acetylation	NIPMMDQKAIFQQPP CCCCCCCHHHHCCCC	38.90	26051181
714	Ubiquitination	NIPMMDQKAIFQQPP CCCCCCCHHHHCCCC	38.90	-
753	Ubiquitination	VVDSGLHKEERYDLK HHHCCCCHHHHCCHH	67.33	-
762	Ubiquitination	ERYDLKTKVSCLETV HHCCHHHHHHHHHHH	30.48	-
802	Acetylation	FPRSRLEKMVPFQVP CCHHHHHHHCCCCCC	50.19	26051181
802	Ubiquitination	FPRSRLEKMVPFQVP CCHHHHHHHCCCCCC	50.19	-
824	Ubiquitination	ENLVLQAKIHMPEKT HHHHHHEECCCCHHH	21.86	-
830	Ubiquitination	AKIHMPEKTAVEFLS EECCCCHHHHHHHHH	35.59	-
838	Acetylation	TAVEFLSKAVDSPNI HHHHHHHHHCCCCCC	55.35	25953088
838	Ubiquitination	TAVEFLSKAVDSPNI HHHHHHHHHCCCCCC	55.35	-
925	Ubiquitination	RAEVDKVKALLSHDS HHHHHHHHHHHHCCC	38.77	-
956	Phosphorylation	VLRWQDRSSRENYLE HHHCCCCCHHHCHHH	41.87	24260401
961	Phosphorylation	DRSSRENYLEENLLY CCCHHHCHHHHHHCH	15.67	-
968	Phosphorylation	YLEENLLYAPSLRFI HHHHHHCHHHHHHHH	21.45	-
1040	Acetylation	GKVTRQGKFKPNSVT CCCCCCCCCCCCCEE	41.71	25953088
1040	Ubiquitination	GKVTRQGKFKPNSVT CCCCCCCCCCCCCEE	41.71	-
1042	Acetylation	VTRQGKFKPNSVTYR CCCCCCCCCCCEEEE	46.93	26051181
1042	Ubiquitination	VTRQGKFKPNSVTYR CCCCCCCCCCCEEEE	46.93	-
1045	Phosphorylation	QGKFKPNSVTYRTKS CCCCCCCCEEEEECC	25.10	28857561
1051	Ubiquitination	NSVTYRTKSGNILLH CCEEEEECCCCEEEE	47.57	-
1059	Ubiquitination	SGNILLHKSTINREA CCCEEEEEHHCCHHH	49.62	-
1082	Phosphorylation	TYFMAVKSNGSVFVR HHEEEEECCCCEEEE	39.56	-
1085	Phosphorylation	MAVKSNGSVFVRDSS EEEECCCCEEEECCC	19.34	27251275
1092	Phosphorylation	SVFVRDSSQVHPLAV CEEEECCCCCCCEEE	40.28	-
1103	Phosphorylation	PLAVLLLTDGDVHIR CEEEEEEECCCEEEC	37.59	-
1119	Phosphorylation	DGRRATISLSDSDLL CCCEEEEECCHHHHH	19.91	20860994
1121	Phosphorylation	RRATISLSDSDLLRL CEEEEECCHHHHHHH	28.42	29449344
1123	Phosphorylation	ATISLSDSDLLRLEG EEEECCHHHHHHHCC	27.12	20860994
1139	Ubiquitination	SRTVRLLKELRRALG HHHHHHHHHHHHHHH	60.33	-
1152	Phosphorylation	LGRMVERSLRSELAA HHHHHHHHHHHHHHC	18.03	-
1155	Phosphorylation	MVERSLRSELAALPP HHHHHHHHHHHCCCH	42.11	-
1163	Phosphorylation	ELAALPPSVQEEHGQ HHHCCCHHHHHHHHH	34.20	-

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 DHX30_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
15	S	Phosphorylation		18220336
[Isoform 2]: Phosphorylated on Ser-15.

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 DHX30_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ILF3_HUMAN	ILF3	physical	22939629
GNAI2_HUMAN	GNAI2	physical	22939629
RAB31_HUMAN	RAB31	physical	22939629
NDUA2_HUMAN	NDUFA2	physical	22939629
MCMBP_HUMAN	MCMBP	physical	28514442
TRFL_HUMAN	LTF	physical	28514442
CHIP_HUMAN	STUB1	physical	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 DHX30_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-96 AND SER-104, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-226, ANDMASS SPECTROMETRY.	19007248 [Abstract]

show