dbPTM

RECQ1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RECQ1_HUMAN
UniProt AC	P46063
Protein Name	ATP-dependent DNA helicase Q1
Gene Name	RECQL
Organism	Homo sapiens (Human).
Sequence Length	649
Subcellular Localization	Nucleus .
Protein Description	DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction..
Protein Sequence	MASVSALTEELDSITSELHAVEIQIQELTERQQELIQKKKVLTKKIKQCLEDSDAGASNEYDSSPAAWNKEDFPWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSNTEDFIEDIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQQKLYEMVSYCQNISKCRRVLMAQHFDEVWNSEACNKMCDNCCKDSAFERKNITEYCRDLIKILKQAEELNEKLTPLKLIDSWMGKGAAKLRVAGVVAPTLPREDLEKIIAHFLIQQYLKEDYSFTAYATISYLKIGPKANLLNNEAHAITMQVTKSTQNSFRAESSQTCHSEQGDKKMEEKNSGNFQKKAANMLQQSGSKNTGAKKRKIDDA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASVSALTE ------CCCHHHHHH	20.74	-
38	Ubiquitination	RQQELIQKKKVLTKK HHHHHHHHHHHHHHH	47.79	21890473
38	2-Hydroxyisobutyrylation	RQQELIQKKKVLTKK HHHHHHHHHHHHHHH	47.79	-
39	Ubiquitination	QQELIQKKKVLTKKI HHHHHHHHHHHHHHH	31.57	-
47	Ubiquitination	KVLTKKIKQCLEDSD HHHHHHHHHHHHCCC	43.78	21890473
53	Phosphorylation	IKQCLEDSDAGASNE HHHHHHCCCCCCCCC	21.71	30108239
58	Phosphorylation	EDSDAGASNEYDSSP HCCCCCCCCCCCCCC	29.31	26657352
61	Phosphorylation	DAGASNEYDSSPAAW CCCCCCCCCCCCCCC	25.94	30108239
63	Phosphorylation	GASNEYDSSPAAWNK CCCCCCCCCCCCCCC	37.00	30576142
64	Phosphorylation	ASNEYDSSPAAWNKE CCCCCCCCCCCCCCC	18.70	25159151
70	Ubiquitination	SSPAAWNKEDFPWSG CCCCCCCCCCCCCCC	48.21	-
78	Ubiquitination	EDFPWSGKVKDILQN CCCCCCCHHHHHHHH	40.36	-
80	Ubiquitination	FPWSGKVKDILQNVF CCCCCHHHHHHHHHH	42.40	-
88	Methylation	DILQNVFKLEKFRPL HHHHHHHHHHHCCCC	51.99	23644510
88	Ubiquitination	DILQNVFKLEKFRPL HHHHHHHHHHHCCCC	51.99	-
88	Sumoylation	DILQNVFKLEKFRPL HHHHHHHHHHHCCCC	51.99	-
88	Acetylation	DILQNVFKLEKFRPL HHHHHHHHHHHCCCC	51.99	26051181
91	Methylation	QNVFKLEKFRPLQLE HHHHHHHHCCCCEEE	58.05	23644510
91	Ubiquitination	QNVFKLEKFRPLQLE HHHHHHHHCCCCEEE	58.05	21890473
91	Acetylation	QNVFKLEKFRPLQLE HHHHHHHHCCCCEEE	58.05	26051181
99	Phosphorylation	FRPLQLETINVTMAG CCCCEEEEEEEEECC	26.83	21406692
103	Phosphorylation	QLETINVTMAGKEVF EEEEEEEEECCEEEE	9.23	21406692
104	Sulfoxidation	LETINVTMAGKEVFL EEEEEEEECCEEEEE	3.94	28183972
113	Sulfoxidation	GKEVFLVMPTGGGKS CEEEEEEEECCCCCC	2.40	21406390
157	Phosphorylation	VLKQLGISATMLNAS HHHHHCCCEEECCCC	18.85	21406692
159	Phosphorylation	KQLGISATMLNASSS HHHCCCEEECCCCCC	18.53	21406692
160	Sulfoxidation	QLGISATMLNASSSK HHCCCEEECCCCCCH	2.44	28183972
164	Phosphorylation	SATMLNASSSKEHVK CEEECCCCCCHHHHH	33.79	21406692
165	Phosphorylation	ATMLNASSSKEHVKW EEECCCCCCHHHHHE	42.91	21406692
166	Phosphorylation	TMLNASSSKEHVKWV EECCCCCCHHHHHEE	39.30	20068231
167	Ubiquitination	MLNASSSKEHVKWVH ECCCCCCHHHHHEEE	54.51	-
167	Malonylation	MLNASSSKEHVKWVH ECCCCCCHHHHHEEE	54.51	26320211
171	Ubiquitination	SSSKEHVKWVHAEMV CCCHHHHHEEEHECC	45.46	-
171	Acetylation	SSSKEHVKWVHAEMV CCCHHHHHEEEHECC	45.46	25953088
180	Ubiquitination	VHAEMVNKNSELKLI EEHECCCCCCCEEEE	50.90	-
180	Acetylation	VHAEMVNKNSELKLI EEHECCCCCCCEEEE	50.90	23236377
185	Ubiquitination	VNKNSELKLIYVTPE CCCCCCEEEEEECHH	28.87	-
185	Acetylation	VNKNSELKLIYVTPE CCCCCCEEEEEECHH	28.87	26051181
188	Phosphorylation	NSELKLIYVTPEKIA CCCEEEEEECHHHHH	14.54	23312004
190	Phosphorylation	ELKLIYVTPEKIAKS CEEEEEECHHHHHHC	14.57	21815630
193	Acetylation	LIYVTPEKIAKSKMF EEEECHHHHHHCHHH	49.52	23954790
193	Ubiquitination	LIYVTPEKIAKSKMF EEEECHHHHHHCHHH	49.52	19608861
193	2-Hydroxyisobutyrylation	LIYVTPEKIAKSKMF EEEECHHHHHHCHHH	49.52	-
193	Malonylation	LIYVTPEKIAKSKMF EEEECHHHHHHCHHH	49.52	32601280
198	Ubiquitination	PEKIAKSKMFMSRLE HHHHHHCHHHHHHHH	35.14	-
206	Acetylation	MFMSRLEKAYEARRF HHHHHHHHHHHHHHH	61.94	19608861
206	Ubiquitination	MFMSRLEKAYEARRF HHHHHHHHHHHHHHH	61.94	-
206	Malonylation	MFMSRLEKAYEARRF HHHHHHHHHHHHHHH	61.94	26320211
208	Phosphorylation	MSRLEKAYEARRFTR HHHHHHHHHHHHHCE	22.61	20068231
235	Phosphorylation	GHDFRPDYKALGILK CCCCCCCHHHHHHHH	10.80	-
236	Ubiquitination	HDFRPDYKALGILKR CCCCCCHHHHHHHHH	44.51	-
236	Acetylation	HDFRPDYKALGILKR CCCCCCHHHHHHHHH	44.51	26051181
242	Acetylation	YKALGILKRQFPNAS HHHHHHHHHHCCCCE	42.08	25953088
249	Phosphorylation	KRQFPNASLIGLTAT HHHCCCCEEEECEEC	27.45	27080861
254	Phosphorylation	NASLIGLTATATNHV CCEEEECEECCCHHC	19.42	27080861
256	Phosphorylation	SLIGLTATATNHVLT EEEECEECCCHHCCC	28.87	27080861
293	Ubiquitination	LYYEVRQKPSNTEDF EEEEEECCCCCCHHH	39.59	-
306	Ubiquitination	DFIEDIVKLINGRYK HHHHHHHHHHCCCCC	43.94	-
313	Acetylation	KLINGRYKGQSGIIY HHHCCCCCCCCEEEE	49.46	26051181
380	Acetylation	AFGMGIDKPDVRFVI HHCCCCCCCCEEEEE	40.99	19666911
390	Phosphorylation	VRFVIHHSMSKSMEN EEEEEEECCCHHHHH	15.58	27080861
391	Sulfoxidation	RFVIHHSMSKSMENY EEEEEECCCHHHHHH	5.20	28183972
392	Phosphorylation	FVIHHSMSKSMENYY EEEEECCCHHHHHHH	25.29	27080861
395	Sulfoxidation	HHSMSKSMENYYQES EECCCHHHHHHHHHH	4.44	30846556
399	Phosphorylation	SKSMENYYQESGRAG CHHHHHHHHHHCCCC	19.86	27642862
417	Phosphorylation	MKADCILYYGFGDIF HHCCEEEEECCCCHH	5.01	20860994
441	Phosphorylation	NVGQQKLYEMVSYCQ CCCCHHHHHHHHHHH	14.71	27642862
452	Ubiquitination	SYCQNISKCRRVLMA HHHHHHHHHHHHHHH	28.15	-
452	Acetylation	SYCQNISKCRRVLMA HHHHHHHHHHHHHHH	28.15	26051181
473	Acetylation	WNSEACNKMCDNCCK HCHHHHHHHCCCCCC	40.57	26051181
480	Ubiquitination	KMCDNCCKDSAFERK HHCCCCCCCHHHHHC	57.84	-
480	Acetylation	KMCDNCCKDSAFERK HHCCCCCCCHHHHHC	57.84	26051181
487	Methylation	KDSAFERKNITEYCR CCHHHHHCCHHHHHH	45.57	23644510
487	Ubiquitination	KDSAFERKNITEYCR CCHHHHHCCHHHHHH	45.57	-
487	Malonylation	KDSAFERKNITEYCR CCHHHHHCCHHHHHH	45.57	26320211
498	Acetylation	EYCRDLIKILKQAEE HHHHHHHHHHHHHHH	49.65	26051181
501	Ubiquitination	RDLIKILKQAEELNE HHHHHHHHHHHHHHH	51.43	-
501	2-Hydroxyisobutyrylation	RDLIKILKQAEELNE HHHHHHHHHHHHHHH	51.43	-
501	Malonylation	RDLIKILKQAEELNE HHHHHHHHHHHHHHH	51.43	26320211
501	Acetylation	RDLIKILKQAEELNE HHHHHHHHHHHHHHH	51.43	25953088
509	Acetylation	QAEELNEKLTPLKLI HHHHHHHCCCCHHHH	57.50	23954790
509	Ubiquitination	QAEELNEKLTPLKLI HHHHHHHCCCCHHHH	57.50	-
509	2-Hydroxyisobutyrylation	QAEELNEKLTPLKLI HHHHHHHCCCCHHHH	57.50	-
509	Malonylation	QAEELNEKLTPLKLI HHHHHHHCCCCHHHH	57.50	26320211
511	Phosphorylation	EELNEKLTPLKLIDS HHHHHCCCCHHHHHH	37.33	27067055
514	Acetylation	NEKLTPLKLIDSWMG HHCCCCHHHHHHHCC	44.60	19608861
514	Ubiquitination	NEKLTPLKLIDSWMG HHCCCCHHHHHHHCC	44.60	-
514	Malonylation	NEKLTPLKLIDSWMG HHCCCCHHHHHHHCC	44.60	26320211
522	Acetylation	LIDSWMGKGAAKLRV HHHHHCCCCHHHHEE	29.30	19608861
522	Ubiquitination	LIDSWMGKGAAKLRV HHHHHCCCCHHHHEE	29.30	19608861
522	2-Hydroxyisobutyrylation	LIDSWMGKGAAKLRV HHHHHCCCCHHHHEE	29.30	-
522	Malonylation	LIDSWMGKGAAKLRV HHHHHCCCCHHHHEE	29.30	26320211
554	Phosphorylation	AHFLIQQYLKEDYSF HHHHHHHHHCCCCCE	11.90	-
559	Phosphorylation	QQYLKEDYSFTAYAT HHHHCCCCCEEEEEE	13.53	-
575	Ubiquitination	SYLKIGPKANLLNNE EEEEECCCCCCCCCC	44.70	-
592	Acetylation	AITMQVTKSTQNSFR EEEEEEEHHHCCCCC	53.28	26051181
593	Phosphorylation	ITMQVTKSTQNSFRA EEEEEEHHHCCCCCC	26.34	28450419
594	Phosphorylation	TMQVTKSTQNSFRAE EEEEEHHHCCCCCCC	33.07	28450419
597	Phosphorylation	VTKSTQNSFRAESSQ EEHHHCCCCCCCCCC	13.29	23401153
602	Phosphorylation	QNSFRAESSQTCHSE CCCCCCCCCCCCCCH	27.11	30576142
603	Phosphorylation	NSFRAESSQTCHSEQ CCCCCCCCCCCCCHH	22.48	25849741
605	Phosphorylation	FRAESSQTCHSEQGD CCCCCCCCCCCHHCC	17.71	28450419
608	Phosphorylation	ESSQTCHSEQGDKKM CCCCCCCCHHCCHHH	33.49	28450419
613	Acetylation	CHSEQGDKKMEEKNS CCCHHCCHHHHHHCC	61.93	25953088
614	Acetylation	HSEQGDKKMEEKNSG CCHHCCHHHHHHCCC	57.17	30591839
625	2-Hydroxyisobutyrylation	KNSGNFQKKAANMLQ HCCCHHHHHHHHHHH	40.00	-
625	Acetylation	KNSGNFQKKAANMLQ HCCCHHHHHHHHHHH	40.00	26051181
626	Ubiquitination	NSGNFQKKAANMLQQ CCCHHHHHHHHHHHH	41.78	-
630	Sulfoxidation	FQKKAANMLQQSGSK HHHHHHHHHHHHCCC	2.83	30846556
634	Phosphorylation	AANMLQQSGSKNTGA HHHHHHHHCCCCCCC	31.88	30266825
634	O-linked_Glycosylation	AANMLQQSGSKNTGA HHHHHHHHCCCCCCC	31.88	30379171
636	Phosphorylation	NMLQQSGSKNTGAKK HHHHHHCCCCCCCCC	28.16	30266825
637	Ubiquitination	MLQQSGSKNTGAKKR HHHHHCCCCCCCCCC	63.15	-
637	Acetylation	MLQQSGSKNTGAKKR HHHHHCCCCCCCCCC	63.15	26210075
639	Phosphorylation	QQSGSKNTGAKKRKI HHHCCCCCCCCCCCC	42.10	28857561
642	Acetylation	GSKNTGAKKRKIDDA CCCCCCCCCCCCCCC	55.23	30591843
643	Acetylation	SKNTGAKKRKIDDA- CCCCCCCCCCCCCC-	59.39	30591849

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 RECQ1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RECQ1_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 RECQ1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IMA3_HUMAN	KPNA4	physical	9168958
IMA1_HUMAN	KPNA2	physical	9168958
DDB1_HUMAN	DDB1	physical	22705827
MAP7_HUMAN	MAP7	physical	22863883
FEN1_HUMAN	FEN1	physical	26344197
MSH2_HUMAN	MSH2	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 RECQ1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-193; LYS-206; LYS-514 ANDLYS-522, AND MASS SPECTROMETRY.	19608861 [Abstract]