dbPTM

HELB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HELB_HUMAN
UniProt AC	Q8NG08
Protein Name	DNA helicase B {ECO:0000305}
Gene Name	HELB {ECO:0000312\|HGNC:HGNC:17196}
Organism	Homo sapiens (Human).
Sequence Length	1087
Subcellular Localization	Nucleus . Cytoplasm . Chromosome . Predominantly nuclear (PubMed:15146062). Phosphorylation at Ser-967 by CDK2 during the G1/S transition results in its nuclear export into the cytoplasm as cells approach and progress through S phase (PubMed:15146062
Protein Description	5'-3' DNA helicase involved in DNA damage response by acting as an inhibitor of DNA end resection. [PubMed: 25617833]
Protein Sequence	MARSSPYLRQLQGPLLPPRDLVEEDDDYLNDDVEEDEESVFIDAEELCSGGVKAGSLPGCLRVSICDENTQETCKVFGRFPITGAWWRVKVQVKPVVGSRSYQYQVQGFPSYFLQSDMSPPNQKHICALFLKECEVSSDDVNKFLTWVKEVSNYKNLNFENLRETLRTFHKETGRKDQKQPTQNGQEELFLDNEMSLPLENTIPFRNVMTALQFPKIMEFLPVLLPRHFKWIIGSGSKEMLKEIEEILGTHPWKLGFSKITYREWKLLRCEASWIAFCQCESLLQLMTDLEKNALIMYSRLKQICREDGHTYVEVNDLTLTLSNHMSFHAASESLKFLKDIGVVTYEKSCVFPYDLYHAERAIAFSICDLMKKPPWHLCVDVEKVLASIHTTKPENSSDDALNESKPDEVRLENPVDVVDTQDNGDHIWTNGENEINAEISEVQLDQDQVEVPLDRDQVAALEMICSNPVTVISGKGGCGKTTIVSRLFKHIEQLEEREVKKACEDFEQDQNASEEWITFTEQSQLEADKAIEVLLTAPTGKAAGLLRQKTGLHAYTLCQVNYSFYSWTQTMMTTNKPWKFSSVRVLVVDEGSLVSVGIFKSVLNLLCEHSKLSKLIILGDIRQLPSIEPGNLLKDLFETLKSRNCAIELKTNHRAESQLIVDNATRISRRQFPKFDAELNISDNPTLPISIQDKTFIFVRLPEEDASSQSSKTNHHSCLYSAVKTLLQENNLQNAKTSQFIAFRRQDCDLINDCCCKHYTGHLTKDHQSRLVFGIGDKICCTRNAYLSDLLPENISGSQQNNDLDASSEDFSGTLPDFAKNKRDFESNVRLCNGEIFFITNDVTDVTFGKRRSLTINNMAGLEVTVDFKKLMKYCRIKHAWARTIHTFQGSEEQTVVYVVGKAGRQHWQHVYTAVTRGRCRVYVIAEESQLRNAIMKNSFPRKTRLKHFLQSKLSSSGAPPADFPSPRKSSGDSGGPSTPSASPLPVVTDHAMTNDVTWSEASSPDERTLTFAERWQLSSPDGVDTDDDLPKSRASKRTCGVNDDESPSKIFMVGESPQVSSRLQNLRLNNLIPRQLFKPTDNQET

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
64	Phosphorylation	LPGCLRVSICDENTQ CCCCEEEEEECCCHH	15.86	23312004
75	Ubiquitination	ENTQETCKVFGRFPI CCHHHHHHEEEEECC	48.28	-
102	Phosphorylation	PVVGSRSYQYQVQGF ECCCCCEEEEEECCC	15.32	22817900
112	Phosphorylation	QVQGFPSYFLQSDMS EECCCCHHHCCCCCC	14.46	22817900
143	Ubiquitination	VSSDDVNKFLTWVKE CCHHHHHHHHHHHHH	41.41	29967540
146	Phosphorylation	DDVNKFLTWVKEVSN HHHHHHHHHHHHHHC	31.20	-
152	Phosphorylation	LTWVKEVSNYKNLNF HHHHHHHHCCCCCCH	35.22	-
155	Ubiquitination	VKEVSNYKNLNFENL HHHHHCCCCCCHHHH	60.24	29967540
235	Phosphorylation	HFKWIIGSGSKEMLK HHEEECCCCCHHHHH	29.50	-
242	Ubiquitination	SGSKEMLKEIEEILG CCCHHHHHHHHHHHC	56.17	25015289
254 (in isoform 2)	Ubiquitination	-	43.09	21890473
254 (in isoform 1)	Ubiquitination	-	43.09	21890473
254	Ubiquitination	ILGTHPWKLGFSKIT HHCCCCCCCCCCCCC	43.09	22817900
259	Ubiquitination	PWKLGFSKITYREWK CCCCCCCCCCHHCCC	36.48	22817900
336	Ubiquitination	HAASESLKFLKDIGV HHHHHHHHHHHHCCC	58.91	-
393	Ubiquitination	LASIHTTKPENSSDD HHHHHCCCCCCCCCH	52.03	29967540
397	Phosphorylation	HTTKPENSSDDALNE HCCCCCCCCCHHHCC	33.22	28555341
405	Phosphorylation	SDDALNESKPDEVRL CCHHHCCCCCCCCCC	48.71	28555341
467	Phosphorylation	AALEMICSNPVTVIS HHHHHHHCCCEEEEE	32.99	-
486	Phosphorylation	CGKTTIVSRLFKHIE CCHHHHHHHHHHHHH	21.29	-
640	Phosphorylation	LLKDLFETLKSRNCA HHHHHHHHHHHCCCE	31.95	-
642	Ubiquitination	KDLFETLKSRNCAIE HHHHHHHHHCCCEEE	55.58	29967540
651	Ubiquitination	RNCAIELKTNHRAES CCCEEEECCCCCCCC	34.19	-
658	Phosphorylation	KTNHRAESQLIVDNA CCCCCCCCEEEECCH	29.33	27282143
666	Phosphorylation	QLIVDNATRISRRQF EEEECCHHHHCCCCC	34.49	22985185
708	Phosphorylation	RLPEEDASSQSSKTN ECCHHHCCCCCCCCC	41.03	25159151
709	Phosphorylation	LPEEDASSQSSKTNH CCHHHCCCCCCCCCH	35.48	17525332
711	Phosphorylation	EEDASSQSSKTNHHS HHHCCCCCCCCCHHH	35.43	25627689
721	Phosphorylation	TNHHSCLYSAVKTLL CCHHHHHHHHHHHHH	10.02	25839225
737	Ubiquitination	ENNLQNAKTSQFIAF HCCCCCCCHHHHEEE	57.15	-
739	Phosphorylation	NLQNAKTSQFIAFRR CCCCCCHHHHEEEHH	23.53	27282143
779	Ubiquitination	LVFGIGDKICCTRNA EEEECCCEEEECCCH	32.22	-
828	Phosphorylation	KNKRDFESNVRLCNG HCHHHHHHCEEECCC	40.39	-
854	Phosphorylation	VTFGKRRSLTINNMA CCCCCCEEEEEECCC	33.62	23532336
856	Phosphorylation	FGKRRSLTINNMAGL CCCCEEEEEECCCCC	23.94	23532336
956	Phosphorylation	HFLQSKLSSSGAPPA HHHHHHHHCCCCCCC	26.62	22210691
958	Phosphorylation	LQSKLSSSGAPPADF HHHHHHCCCCCCCCC	35.28	23186163
967	Phosphorylation	APPADFPSPRKSSGD CCCCCCCCCCCCCCC	37.01	23401153
971	Phosphorylation	DFPSPRKSSGDSGGP CCCCCCCCCCCCCCC	40.61	-
979	Phosphorylation	SGDSGGPSTPSASPL CCCCCCCCCCCCCCC	57.11	21552520
980	Phosphorylation	GDSGGPSTPSASPLP CCCCCCCCCCCCCCC	25.13	21552520
982	Phosphorylation	SGGPSTPSASPLPVV CCCCCCCCCCCCCEE	41.28	-
984	Phosphorylation	GPSTPSASPLPVVTD CCCCCCCCCCCEECC	31.16	21552520
1005	Phosphorylation	VTWSEASSPDERTLT CCHHHCCCCCCCEEE	43.34	22468782
1020	Phosphorylation	FAERWQLSSPDGVDT HHHHHCCCCCCCCCC	25.40	25159151
1021	Phosphorylation	AERWQLSSPDGVDTD HHHHCCCCCCCCCCC	35.29	25159151
1027	Phosphorylation	SSPDGVDTDDDLPKS CCCCCCCCCCCCCCC	38.63	25159151
1034	Phosphorylation	TDDDLPKSRASKRTC CCCCCCCCHHCCCCC	31.01	22468782
1040	Phosphorylation	KSRASKRTCGVNDDE CCHHCCCCCCCCCCC	19.83	28464451
1048	Phosphorylation	CGVNDDESPSKIFMV CCCCCCCCCCCEEEE	41.28	23401153
1050	Phosphorylation	VNDDESPSKIFMVGE CCCCCCCCCEEEEEC	47.89	30266825
1058	Phosphorylation	KIFMVGESPQVSSRL CEEEEECCHHHHHHH	18.07	29255136
1062	Phosphorylation	VGESPQVSSRLQNLR EECCHHHHHHHHHHH	12.42	29978859
1063	Phosphorylation	GESPQVSSRLQNLRL ECCHHHHHHHHHHHH	37.85	29396449

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
967	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
967	S	Phosphorylation		15146062
Phosphorylated at Ser-967 by CDK2 during the G1/S transition, resulting in its nuclear export into the cytoplasm.

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 HELB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
DPOLA_HUMAN	POLA1	physical	12181327
DPOA2_HUMAN	POLA2	physical	12181327

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 HELB_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-967 AND SER-1021, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-709, AND MASSSPECTROMETRY.	17525332 [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-708; SER-967; SER-1021AND SER-1048, AND MASS SPECTROMETRY.	15302935 [Abstract]
"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 THR-1027, AND MASSSPECTROMETRY.	19690332 [Abstract]

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