HELLS_HUMAN - dbPTM
HELLS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HELLS_HUMAN
UniProt AC Q9NRZ9
Protein Name Lymphoid-specific helicase
Gene Name HELLS {ECO:0000312|HGNC:HGNC:4861}
Organism Homo sapiens (Human).
Sequence Length 838
Subcellular Localization Nucleus. Closely associated with pericentric heterochromatin..
Protein Description Plays an essential role in normal development and survival. Involved in regulation of the expansion or survival of lymphoid cells. Required for de novo or maintenance DNA methylation. May control silencing of the imprinted CDKN1C gene through DNA methylation. May play a role in formation and organization of heterochromatin, implying a functional role in the regulation of transcription and mitosis (By similarity)..
Protein Sequence MPAERPAGSGGSEAPAMVEQLDTAVITPAMLEEEEQLEAAGLERERKMLEKARMSWDRESTEIRYRRLQHLLEKSNIYSKFLLTKMEQQQLEEQKKKEKLERKKESLKVKKGKNSIDASEEKPVMRKKRGREDESYNISEVMSKEEILSVAKKNKKENEDENSSSTNLCVEDLQKNKDSNSIIKDRLSETVRQNTKFFFDPVRKCNGQPVPFQQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHGTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKEREQNVLHMLHQILTPFLLRRLKSDVALEVPPKREVVVYAPLSKKQEIFYTAIVNRTIANMFGSSEKETIELSPTGRPKRRTRKSINYSKIDDFPNELEKLISQIQPEVDRERAVVEVNIPVESEVNLKLQNIMMLLRKCCNHPYLIEYPIDPVTQEFKIDEELVTNSGKFLILDRMLPELKKRGHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFKGGQSGLNLSKNFLDPKELMELLKSRDYEREIKGSREKVISDKDLELLLDRSDLIDQMNASGPIKEKMGIFKILENSEDSSPECLF
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
55PhosphorylationMLEKARMSWDRESTE
HHHHHHHHCCHHHHH		21.9224719451
58 (in isoform 2)Ubiquitination-33.2421890473
60PhosphorylationRMSWDRESTEIRYRR
HHHCCHHHHHHHHHH		32.0329449344
61PhosphorylationMSWDRESTEIRYRRL
HHCCHHHHHHHHHHH		30.5829449344
64 (in isoform 2)Ubiquitination-16.8121890473
65PhosphorylationRESTEIRYRRLQHLL
HHHHHHHHHHHHHHH		13.0224719451
74UbiquitinationRLQHLLEKSNIYSKF
HHHHHHHHCCHHHHH		49.0921890473
74AcetylationRLQHLLEKSNIYSKF
HHHHHHHHCCHHHHH		49.0925953088
74 (in isoform 1)Ubiquitination-49.0921890473
74 (in isoform 3)Ubiquitination-49.0921890473
74 (in isoform 4)Ubiquitination-49.0921890473
74 (in isoform 5)Ubiquitination-49.0921890473
74 (in isoform 6)Ubiquitination-49.0921890473
74 (in isoform 7)Ubiquitination-49.0921890473
74 (in isoform 8)Ubiquitination-49.0921890473
74 (in isoform 9)Ubiquitination-49.0921890473
80UbiquitinationEKSNIYSKFLLTKME
HHCCHHHHHHHHHHH		24.0621890473
80 (in isoform 1)Ubiquitination-24.0621890473
80 (in isoform 3)Ubiquitination-24.0621890473
80 (in isoform 4)Ubiquitination-24.0621890473
80 (in isoform 5)Ubiquitination-24.0621890473
80 (in isoform 6)Ubiquitination-24.0621890473
80 (in isoform 7)Ubiquitination-24.0621890473
80 (in isoform 8)Ubiquitination-24.0621890473
80 (in isoform 9)Ubiquitination-24.0621890473
85UbiquitinationYSKFLLTKMEQQQLE
HHHHHHHHHHHHHHH		40.17-
99AcetylationEEQKKKEKLERKKES
HHHHHHHHHHHHHHH		65.617666429
103AcetylationKKEKLERKKESLKVK
HHHHHHHHHHHHHCC		52.067666441
104AcetylationKEKLERKKESLKVKK
HHHHHHHHHHHHCCC		59.777666453
106PhosphorylationKLERKKESLKVKKGK
HHHHHHHHHHCCCCC		42.2326074081
115PhosphorylationKVKKGKNSIDASEEK
HCCCCCCCCCCCCCC		25.9025159151
119PhosphorylationGKNSIDASEEKPVMR
CCCCCCCCCCCCCCC		42.4125159151
122AcetylationSIDASEEKPVMRKKR
CCCCCCCCCCCCCCC		38.5723749302
122SumoylationSIDASEEKPVMRKKR
CCCCCCCCCCCCCCC		38.57-
122UbiquitinationSIDASEEKPVMRKKR
CCCCCCCCCCCCCCC		38.57-
122SumoylationSIDASEEKPVMRKKR
CCCCCCCCCCCCCCC		38.57-
125SulfoxidationASEEKPVMRKKRGRE
CCCCCCCCCCCCCCC		7.6321406390
135PhosphorylationKRGREDESYNISEVM
CCCCCCCCCCHHHHC		35.4828555341
136PhosphorylationRGREDESYNISEVMS
CCCCCCCCCHHHHCC		17.9228555341
144UbiquitinationNISEVMSKEEILSVA
CHHHHCCHHHHHHHH		41.07-
149PhosphorylationMSKEEILSVAKKNKK
CCHHHHHHHHHHCCC		26.2024719451
152UbiquitinationEEILSVAKKNKKENE
HHHHHHHHHCCCCCC		55.51-
152AcetylationEEILSVAKKNKKENE
HHHHHHHHHCCCCCC		55.5125953088
155UbiquitinationLSVAKKNKKENEDEN
HHHHHHCCCCCCCCC		71.05-
155AcetylationLSVAKKNKKENEDEN
HHHHHHCCCCCCCCC		71.0526051181
163PhosphorylationKENEDENSSSTNLCV
CCCCCCCCCCCCHHH		24.5029978859
164PhosphorylationENEDENSSSTNLCVE
CCCCCCCCCCCHHHH		53.4129978859
165PhosphorylationNEDENSSSTNLCVED
CCCCCCCCCCHHHHH		22.5730576142
166PhosphorylationEDENSSSTNLCVEDL
CCCCCCCCCHHHHHH		33.8729978859
175UbiquitinationLCVEDLQKNKDSNSI
HHHHHHHHCCCCCCH		73.58-
177UbiquitinationVEDLQKNKDSNSIIK
HHHHHHCCCCCCHHH		70.35-
181PhosphorylationQKNKDSNSIIKDRLS
HHCCCCCCHHHHHHH		29.6424719451
184UbiquitinationKDSNSIIKDRLSETV
CCCCCHHHHHHHHHH		34.82-
188PhosphorylationSIIKDRLSETVRQNT
CHHHHHHHHHHHHHC		31.9220068231
190PhosphorylationIKDRLSETVRQNTKF
HHHHHHHHHHHHCCC		20.0120068231
196UbiquitinationETVRQNTKFFFDPVR
HHHHHHCCCCCCCCC		47.96-
204SumoylationFFFDPVRKCNGQPVP
CCCCCCCCCCCCCCC		32.08-
204UbiquitinationFFFDPVRKCNGQPVP
CCCCCCCCCCCCCCC		32.08-
204SumoylationFFFDPVRKCNGQPVP
CCCCCCCCCCCCCCC		32.08-
216UbiquitinationPVPFQQPKHFTGGVM
CCCCCCCCCCCCCCE		47.19-
331PhosphorylationQIHPVVITSFEIAMR
EEECEEEEEEEHHHC		18.7623401153
332PhosphorylationIHPVVITSFEIAMRD
EECEEEEEEEHHHCC		15.1223401153
390 (in isoform 6)Ubiquitination-5.7321890473
409SumoylationPDVFDDLKSFESWFD
HHHHHHHHHCHHHCC		61.16-
422 (in isoform 5)Ubiquitination-58.2821890473
469PhosphorylationPKREVVVYAPLSKKQ
CCCEEEEEEECCCCC		7.2921406692
473PhosphorylationVVVYAPLSKKQEIFY
EEEEEECCCCCHHHH		36.4321406692
474UbiquitinationVVYAPLSKKQEIFYT
EEEEECCCCCHHHHH		67.18-
475SumoylationVYAPLSKKQEIFYTA
EEEECCCCCHHHHHH		50.19-
475UbiquitinationVYAPLSKKQEIFYTA
EEEECCCCCHHHHHH		50.19-
475SumoylationVYAPLSKKQEIFYTA
EEEECCCCCHHHHHH		50.19-
481PhosphorylationKKQEIFYTAIVNRTI
CCCHHHHHHHHCHHH		10.12-
487PhosphorylationYTAIVNRTIANMFGS
HHHHHCHHHHHHHCC		21.1621406692
488 (in isoform 3)Ubiquitination-2.0521890473
494PhosphorylationTIANMFGSSEKETIE
HHHHHHCCCCCCEEE		24.8621406692
495PhosphorylationIANMFGSSEKETIEL
HHHHHCCCCCCEEEC		53.7324114839
499PhosphorylationFGSSEKETIELSPTG
HCCCCCCEEECCCCC		30.7128122231
503PhosphorylationEKETIELSPTGRPKR
CCCEEECCCCCCCCC		13.9723401153
504 (in isoform 2)Ubiquitination-52.0421890473
505PhosphorylationETIELSPTGRPKRRT
CEEECCCCCCCCCCC		42.3129255136
514UbiquitinationRPKRRTRKSINYSKI
CCCCCCCCCCCHHHC		55.89-
515PhosphorylationPKRRTRKSINYSKID
CCCCCCCCCCHHHCC		16.8721712546
518PhosphorylationRTRKSINYSKIDDFP
CCCCCCCHHHCCCCC		15.0729978859
519PhosphorylationTRKSINYSKIDDFPN
CCCCCCHHHCCCCCH		20.7429978859
520UbiquitinationRKSINYSKIDDFPNE
CCCCCHHHCCCCCHH		39.5321906983
520 (in isoform 1)Ubiquitination-39.5321890473
520 (in isoform 4)Ubiquitination-39.5321890473
530UbiquitinationDFPNELEKLISQIQP
CCCHHHHHHHHHHCC		64.84-
554PhosphorylationEVNIPVESEVNLKLQ
EEECCCCCHHHHHHH		47.2622468782
569MethylationNIMMLLRKCCNHPYL
HHHHHHHHHCCCCCE		43.0123644510
596PhosphorylationKIDEELVTNSGKFLI
ECCHHHHCCCCCEEE		35.9720068231
598PhosphorylationDEELVTNSGKFLILD
CHHHHCCCCCEEEEC		33.7120068231
600UbiquitinationELVTNSGKFLILDRM
HHHCCCCCEEEECCC		36.50-
612UbiquitinationDRMLPELKKRGHKVL
CCCHHHHHHCCCCHH		38.47-
613UbiquitinationRMLPELKKRGHKVLL
CCHHHHHHCCCCHHH		76.00-
633 (in isoform 6)Ubiquitination-39.1921890473
648PhosphorylationNFSRLDGSMSYSERE
CCHHCCCCCCHHHHH		12.2929978859
650PhosphorylationSRLDGSMSYSEREKN
HHCCCCCCHHHHHHC		27.4921815630
651PhosphorylationRLDGSMSYSEREKNM
HCCCCCCHHHHHHCH		13.10-
652PhosphorylationLDGSMSYSEREKNMH
CCCCCCHHHHHHCHH		23.9129978859
665 (in isoform 5)Ubiquitination-37.3021890473
665 (in isoform 6)Ubiquitination-37.3021890473
697 (in isoform 5)Ubiquitination-29.7121890473
714PhosphorylationRCHRIGQTKPVVVYR
HHHHCCCCCCEEEEE		31.9121406692
715UbiquitinationCHRIGQTKPVVVYRL
HHHCCCCCCEEEEEE		28.11-
715AcetylationCHRIGQTKPVVVYRL
HHHCCCCCCEEEEEE		28.1126051181
720PhosphorylationQTKPVVVYRLVTANT
CCCCEEEEEEEECCC		6.1421406692
724PhosphorylationVVVYRLVTANTIDQK
EEEEEEEECCCCCHH		20.8425278378
727PhosphorylationYRLVTANTIDQKIVE
EEEEECCCCCHHHHH		24.3825278378
731UbiquitinationTANTIDQKIVERAAA
ECCCCCHHHHHHHHH		45.00-
731 (in isoform 3)Ubiquitination-45.0021890473
741UbiquitinationERAAAKRKLEKLIIH
HHHHHHHHHHHHHEE		61.36-
744UbiquitinationAAKRKLEKLIIHKNH
HHHHHHHHHHEECCC		56.26-
747 (in isoform 2)Ubiquitination-5.6921890473
749UbiquitinationLEKLIIHKNHFKGGQ
HHHHHEECCCCCCCC		41.53-
753MethylationIIHKNHFKGGQSGLN
HEECCCCCCCCCCCC		55.3682976311
753UbiquitinationIIHKNHFKGGQSGLN
HEECCCCCCCCCCCC		55.36-
757PhosphorylationNHFKGGQSGLNLSKN
CCCCCCCCCCCCCCC		48.8221406692
762PhosphorylationGQSGLNLSKNFLDPK
CCCCCCCCCCCCCHH		25.2021406692
763UbiquitinationQSGLNLSKNFLDPKE
CCCCCCCCCCCCHHH		55.6821906983
763 (in isoform 1)Ubiquitination-55.6821890473
763 (in isoform 3)Ubiquitination-55.6821890473
763 (in isoform 4)Ubiquitination-55.6821890473
769UbiquitinationSKNFLDPKELMELLK
CCCCCCHHHHHHHHH		64.25-
776UbiquitinationKELMELLKSRDYERE
HHHHHHHHCCCHHHH		56.95-
779 (in isoform 2)Ubiquitination-57.6521890473
785UbiquitinationRDYEREIKGSREKVI
CCHHHHHCCCHHHCC		46.19-
790UbiquitinationEIKGSREKVISDKDL
HHCCCHHHCCCHHHH		43.70-
795UbiquitinationREKVISDKDLELLLD
HHHCCCHHHHHHHHC		58.3821906983
795 (in isoform 1)Ubiquitination-58.3821890473
803MethylationDLELLLDRSDLIDQM
HHHHHHCHHHHHHHH		31.85115478433
804PhosphorylationLELLLDRSDLIDQMN
HHHHHCHHHHHHHHC		36.1121406692
810SulfoxidationRSDLIDQMNASGPIK
HHHHHHHHCCCCCHH		3.9221406390
813PhosphorylationLIDQMNASGPIKEKM
HHHHHCCCCCHHHHH		39.8521815630
817UbiquitinationMNASGPIKEKMGIFK
HCCCCCHHHHHCCCH		55.18-
819UbiquitinationASGPIKEKMGIFKIL
CCCCHHHHHCCCHHH		37.11-
829PhosphorylationIFKILENSEDSSPEC
CCHHHCCCCCCCCCC		33.1525159151
832PhosphorylationILENSEDSSPECLF-
HHCCCCCCCCCCCC-		43.6826503892
833PhosphorylationLENSEDSSPECLF--
HCCCCCCCCCCCC--		36.7226503892
836GlutathionylationSEDSSPECLF-----
CCCCCCCCCC-----		5.5222555962
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 HELLS_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HELLS_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 HELLS_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC1_HUMANHDAC1physical
19561196
HDAC2_HUMANHDAC2physical
19561196
DNMT1_HUMANDNMT1physical
17967891
DNM3B_HUMANDNMT3Bphysical
17967891
A4_HUMANAPPphysical
21832049
WDR5_HUMANWDR5physical
26344197
RCBT2_HUMANRCBTB2physical
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 HELLS_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-832, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-505, AND MASSSPECTROMETRY.

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