CHD1L_HUMAN - dbPTM
CHD1L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHD1L_HUMAN
UniProt AC Q86WJ1
Protein Name Chromodomain-helicase-DNA-binding protein 1-like
Gene Name CHD1L
Organism Homo sapiens (Human).
Sequence Length 897
Subcellular Localization Nucleus . Localizes at sites of DNA damage. Probably recruited to DNA damage sites by PARylated PARP1.
Protein Description DNA helicase which plays a role in chromatin-remodeling following DNA damage. Targeted to sites of DNA damage through interaction with poly(ADP-ribose) and functions to regulate chromatin during DNA repair. Able to catalyze nucleosome sliding in an ATP-dependent manner. Helicase activity is strongly stimulated upon poly(ADP-ribose)-binding..
Protein Sequence MERAGATSRGGQAPGFLLRLHTEGRAEAARVQEQDLRQWGLTGIHLRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSALQKKYYKAILMKDLDAFENETAKKVKLQNILSQLRKCVDHPYLFDGVEPEPFEVGDHLTEASGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFTLGAQKPAADADLQLSEILKFGLDKLLASEGSTMDEIDLESILGETKDGQWVSDALPAAEGGSRDQEEGKNHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRNKGSVLIPGLVEGSTKRKRVLSPEELEDRQKKRQEAAAKRRRLIEEKKRQKEEAEHKKKMAWWESNNYQSFCLPSEESEPEDLENGEESSAELDYQDPDATSLKYVSGDVTHPQAGAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKGQDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAARGIPTYIYYFPRSKSAVLHAQSSSSSSRQLVP
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
7Phosphorylation-MERAGATSRGGQAP
-CCCCCCCCCCCCCC		20.3123403867
8PhosphorylationMERAGATSRGGQAPG
CCCCCCCCCCCCCCC		28.5223403867
9MethylationERAGATSRGGQAPGF
CCCCCCCCCCCCCCE		49.2424129315
10UbiquitinationRAGATSRGGQAPGFL
CCCCCCCCCCCCCEE		32.12-
15UbiquitinationSRGGQAPGFLLRLHT
CCCCCCCCEEEEEEC		28.93-
27UbiquitinationLHTEGRAEAARVQEQ
EECCCCHHHHHHHHH		41.31-
78O-linked_GlycosylationDEMGLGKTCQTIALF
CCCCCCHHHHHHHHH		14.1930379171
122PhosphorylationQRFAPGLSCVTYAGD
HHHCCCCEEEEECCC		16.68-
130AcetylationCVTYAGDKEERACLQ
EEEECCCHHHHHHHH		61.6325953088
130UbiquitinationCVTYAGDKEERACLQ
EEEECCCHHHHHHHH		61.63-
141UbiquitinationACLQQDLKQESRFHV
HHHHHHHHHHHHHHH		61.38-
161PhosphorylationEICLKDASFLKSFPW
HHHHHCHHHHHHCCC		41.0424719451
165PhosphorylationKDASFLKSFPWSVLV
HCHHHHHHCCCEEEE		38.3927461979
169PhosphorylationFLKSFPWSVLVVDEA
HHHHCCCEEEEECHH		13.0527461979
180UbiquitinationVDEAHRLKNQSSLLH
ECHHHHHCCCHHHHH		53.55-
226PhosphorylationFVEPDLFSKEEVGDF
HHCCCCCCHHHHHHH		46.5924719451
242UbiquitinationQRYQDIEKESESASE
HHHHHHHHHCCCHHH		67.86-
252UbiquitinationESASELHKLLQPFLL
CCHHHHHHHHHHHHH		64.61-
263UbiquitinationPFLLRRVKAEVATEL
HHHHHHHHHHHHHCC		36.70-
263SumoylationPFLLRRVKAEVATEL
HHHHHHHHHHHHHCC		36.70-
263SumoylationPFLLRRVKAEVATEL
HHHHHHHHHHHHHCC		36.70-
279PhosphorylationKKTEVVIYHGMSALQ
CCCEEEEECCCHHHH		4.8224719451
283PhosphorylationVVIYHGMSALQKKYY
EEEECCCHHHHHHHH		30.3524719451
289PhosphorylationMSALQKKYYKAILMK
CHHHHHHHHHHHHHH		19.75-
290PhosphorylationSALQKKYYKAILMKD
HHHHHHHHHHHHHHC		11.65-
291UbiquitinationALQKKYYKAILMKDL
HHHHHHHHHHHHHCH		26.34-
296UbiquitinationYYKAILMKDLDAFEN
HHHHHHHHCHHHHCC		52.25-
305PhosphorylationLDAFENETAKKVKLQ
HHHHCCHHHHHHHHH		56.1929083192
307UbiquitinationAFENETAKKVKLQNI
HHCCHHHHHHHHHHH		66.57-
307AcetylationAFENETAKKVKLQNI
HHCCHHHHHHHHHHH		66.5725953088
308UbiquitinationFENETAKKVKLQNIL
HCCHHHHHHHHHHHH		41.98-
309UbiquitinationENETAKKVKLQNILS
CCHHHHHHHHHHHHH		8.03-
310UbiquitinationNETAKKVKLQNILSQ
CHHHHHHHHHHHHHH		53.92-
316PhosphorylationVKLQNILSQLRKCVD
HHHHHHHHHHHHHCC		24.3029978859
319UbiquitinationQNILSQLRKCVDHPY
HHHHHHHHHHCCCCC		23.77-
320UbiquitinationNILSQLRKCVDHPYL
HHHHHHHHHCCCCCC		47.40-
324UbiquitinationQLRKCVDHPYLFDGV
HHHHHCCCCCCCCCC		7.78-
348UbiquitinationHLTEASGKLHLLDKL
HHHHCCCHHHHHHHH		30.18-
349UbiquitinationLTEASGKLHLLDKLL
HHHCCCHHHHHHHHH		3.82-
370PhosphorylationGHRVLLFSQMTQMLD
HHHHHHHHHHHHHHH		21.0024043423
373PhosphorylationVLLFSQMTQMLDILQ
HHHHHHHHHHHHHHH		11.8224043423
382PhosphorylationMLDILQDYMDYRGYS
HHHHHHHHHHHCCCC		4.4824043423
385PhosphorylationILQDYMDYRGYSYER
HHHHHHHHCCCCEEE		6.8724043423
401 (in isoform 3)Ubiquitination-48.5021890473
492 (in isoform 4)Ubiquitination-2.4821890473
511 (in isoform 2)Ubiquitination-35.1821890473
512UbiquitinationKPAADADLQLSEILK
CCCCCCCCCHHHHHH		6.22-
524UbiquitinationILKFGLDKLLASEGS
HHHHCHHHHHHCCCC		50.90-
540PhosphorylationMDEIDLESILGETKD
CCEECHHHHHCCCCC		30.3427732954
545PhosphorylationLESILGETKDGQWVS
HHHHHCCCCCCCCHH		32.4127732954
546SumoylationESILGETKDGQWVSD
HHHHCCCCCCCCHHH		56.40-
552PhosphorylationTKDGQWVSDALPAAE
CCCCCCHHHCCCCCC		17.7628450419
562PhosphorylationLPAAEGGSRDQEEGK
CCCCCCCCCCCCCCC		43.4728450419
569UbiquitinationSRDQEEGKNHMYLFE
CCCCCCCCCCEEEEC		47.13-
580PhosphorylationYLFEGKDYSKEPSKE
EEECCCCCCCCCCHH		25.7329759185
589UbiquitinationKEPSKEDRKSFEQLV
CCCCHHHHHHHHHHH		37.2921890473
589 (in isoform 3)Ubiquitination-37.2921890473
590SumoylationEPSKEDRKSFEQLVN
CCCHHHHHHHHHHHH		72.34-
590SumoylationEPSKEDRKSFEQLVN
CCCHHHHHHHHHHHH		72.34-
590UbiquitinationEPSKEDRKSFEQLVN
CCCHHHHHHHHHHHH		72.34-
591PhosphorylationPSKEDRKSFEQLVNL
CCHHHHHHHHHHHHH		34.6022199227
600UbiquitinationEQLVNLQKTLLEKAS
HHHHHHHHHHHHHHH		44.28-
605 (in isoform 1)Ubiquitination-53.9921890473
605UbiquitinationLQKTLLEKASQEGRS
HHHHHHHHHHHHCHH		53.9921906983
607PhosphorylationKTLLEKASQEGRSLR
HHHHHHHHHHCHHHH		39.5722817901
612PhosphorylationKASQEGRSLRNKGSV
HHHHHCHHHHCCCCE		42.40-
616UbiquitinationEGRSLRNKGSVLIPG
HCHHHHCCCCEECCC		46.24-
618PhosphorylationRSLRNKGSVLIPGLV
HHHHCCCCEECCCCC		18.5023917254
628PhosphorylationIPGLVEGSTKRKRVL
CCCCCCCCCCCCCCC		19.7623401153
629PhosphorylationPGLVEGSTKRKRVLS
CCCCCCCCCCCCCCC		45.8023401153
630UbiquitinationGLVEGSTKRKRVLSP
CCCCCCCCCCCCCCH		58.58-
630AcetylationGLVEGSTKRKRVLSP
CCCCCCCCCCCCCCH		58.5825953088
636PhosphorylationTKRKRVLSPEELEDR
CCCCCCCCHHHHHHH		27.6629255136
680 (in isoform 4)Ubiquitination-39.4521890473
684PhosphorylationWESNNYQSFCLPSEE
HHCCCCCCCCCCCCC		13.9428348404
689PhosphorylationYQSFCLPSEESEPED
CCCCCCCCCCCCHHH		40.8428348404
692PhosphorylationFCLPSEESEPEDLEN
CCCCCCCCCHHHHCC		55.1726657352
699 (in isoform 2)Ubiquitination-71.1621890473
703PhosphorylationDLENGEESSAELDYQ
HHCCCCCCCCCCCCC		30.4628348404
704PhosphorylationLENGEESSAELDYQD
HCCCCCCCCCCCCCC		29.1028348404
709PhosphorylationESSAELDYQDPDATS
CCCCCCCCCCCCCCC		27.6922817900
753PhosphorylationWGRGGLFTALEKRSA
CCCCHHHHHHHHCCC		35.0624719451
757UbiquitinationGLFTALEKRSAEPRK
HHHHHHHHCCCCCHH		53.13-
764UbiquitinationKRSAEPRKIYELAGK
HCCCCCHHHHHHHHH		61.43-
771UbiquitinationKIYELAGKMKDLSLG
HHHHHHHHCCCCCCC		36.85-
776PhosphorylationAGKMKDLSLGGVLLF
HHHCCCCCCCCEEEE		34.79-
788UbiquitinationLLFPVDDKESRNKGQ
EEEECCCHHHHCCCH		53.80-
793UbiquitinationDDKESRNKGQDLLAL
CCHHHHCCCHHHHHH		57.7621890473
793 (in isoform 1)Ubiquitination-57.7621890473
809PhosphorylationVAQHRDRSNVLSGIK
HHHCCCCCCCCCHHH		35.2621406692
813PhosphorylationRDRSNVLSGIKMAAL
CCCCCCCCHHHHHHH		33.9021406692
816AcetylationSNVLSGIKMAALEEG
CCCCCHHHHHHHHHH		26.4725953088
847PhosphorylationLPRIGHATKGFNWYG
CCCCCCCCCCCCCCC		26.4829083192
853PhosphorylationATKGFNWYGTERLIR
CCCCCCCCCHHHHHH		18.4429083192
855PhosphorylationKGFNWYGTERLIRKH
CCCCCCCHHHHHHHH		11.3929083192
871PhosphorylationAARGIPTYIYYFPRS
HHCCCCEEEEEECCC		4.99-
873PhosphorylationRGIPTYIYYFPRSKS
CCCCEEEEEECCCCC		6.66-
891PhosphorylationHAQSSSSSSRQLVP-
EECCCCCCCCCCCC-		31.3318669648
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 CHD1L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHD1L_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 CHD1L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC6_HUMANXRCC6physical
19666485
PARP1_HUMANPARP1physical
19666485
H2A3_HUMANHIST3H2Aphysical
19666485
XRCC5_HUMANXRCC5physical
19666485
H2AX_HUMANH2AFXphysical
19666485
RFA3_HUMANRPA3physical
19666485
SP16H_HUMANSUPT16Hphysical
19666485
H2AZ_HUMANH2AFZphysical
19666485
RFA2_HUMANRPA2physical
19666485
PRKDC_HUMANPRKDCphysical
19666485
PARP2_HUMANPARP2physical
19666485
H2B1K_HUMANHIST1H2BKphysical
19666485
H2B1B_HUMANHIST1H2BBphysical
19666485
PRKDC_HUMANPRKDCphysical
19661379
PARP1_HUMANPARP1physical
19661379
XRCC5_HUMANXRCC5physical
19661379
XRCC6_HUMANXRCC6physical
19661379
RFA1_HUMANRPA1physical
19661379
API5_HUMANAPI5physical
19661379
IF4A1_HUMANEIF4A1physical
19661379
RFC2_HUMANRFC2physical
19661379
RFA2_HUMANRPA2physical
19661379
CBX1_HUMANCBX1physical
19661379
CBX3_HUMANCBX3physical
19661379
CBX5_HUMANCBX5physical
19661379
XRCC1_HUMANXRCC1physical
19661379
APLF_HUMANAPLFphysical
19661379
PARP1_HUMANPARP1physical
22146311
SCYL1_HUMANSCYL1physical
21988832
NR4A1_HUMANNR4A1physical
21988832
PARP1_HUMANPARP1physical
23926104
APLF_HUMANAPLFphysical
23926104
H2B2E_HUMANHIST2H2BEphysical
23926104
XRCC6_HUMANXRCC6physical
23926104
TRI33_HUMANTRIM33physical
23926104
PARP2_HUMANPARP2physical
28514442
XPC_HUMANXPCphysical
28514442
SP16H_HUMANSUPT16Hphysical
28514442
XRCC1_HUMANXRCC1physical
28514442
TNKS2_HUMANTNKS2physical
28514442
HLTF_HUMANHLTFphysical
28514442
PARP1_HUMANPARP1physical
28514442
HSP7C_HUMANHSPA8physical
28514442
TNKS1_HUMANTNKSphysical
28514442
XRCC6_HUMANXRCC6physical
28514442
SSRP1_HUMANSSRP1physical
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 CHD1L_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-636 AND SER-891, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636, AND MASSSPECTROMETRY.

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