CHD1_MOUSE - dbPTM
CHD1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHD1_MOUSE
UniProt AC P40201
Protein Name Chromodomain-helicase-DNA-binding protein 1
Gene Name Chd1
Organism Mus musculus (Mouse).
Sequence Length 1711
Subcellular Localization Nucleus . Cytoplasm . Is released into the cytoplasm when cells enter mitosis and is reincorporated into chromatin during telophase-cytokinesis (PubMed:7739555).
Protein Description ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3 (By similarity). Required for maintaining open chromatin and pluripotency in embryonic stem cells. [PubMed: 19587682 Is also associated with histone deacetylase (HDAC) activity]
Protein Sequence MNGHSDEESVRNGSGESSQSGDDCGSASGSGSGSSSGSSSDGSSSQSGSSDSDSGSDSGSQSESESDTSRENKVQAKPPKVDGAEFWKSSPSILAVQRSAMLRKQPQQAQQQRPASSNSGSEEDSSSSEDSDDSSSGAKRKKHNDEDWQMSGSGSPSQSGSDSESEEERDKSSCDGTESDYEPKNKVRSRKPQNRSKSKNGKKILGQKKRQIDSSEDEDDEDYDNDKRSSRRQATVNVSYKEDEEMKTDSDDLLEVCGEDVPQPEDEEFETIERVMDCRVGRKGATGATTTIYAVEADGDPNAGFERNKEPGDIQYLIKWKGWSHIHNTWETEETLKQQNVRGMKKLDNYKKKDQETKRWLKNASPEDVEYYNCQQELTDDLHKQYQIVERIIAHSNQKSAAGLPDYYCKWQGLPYSECSWEDGALISKKFQTCIDEYFSRNQSKTTPFKDCKVLKQRPRFVALKKQPSYIGGHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWASQMNAVVYLGDINSRNMIRTHEWMHPQTKRLKFNILLTTYEILLKDKAFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYASLHKELEPFLLRRVKKDVEKSLPAKVEQILRMEMSALQKQYYKWILTRNYKALSKGSKGSTSGFLNIMMELKKCCNHCYLIKPPDNNEFYNKQEALQHLIRSSGKLILLDKLLIRLRERGNRVLIFSQMVRMLDILAEYLKYRQFPFQRLDGSIKGELRKQALDHFNAEGSEDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGSVEEDILERAKKKMVLDHLVIQRMDTTGKTVLHTGSAPSSSTPFNKEELSAILKFGAEELFKEPEGEEQEPQEMDIDEILKRAETHENEPGPLSVGDELLSQFKVANFSNMDEDDIELEPERNSKNWEEIIPEEQRRRLEEEERQKELEEIYMLPRMRNCAKQISFNGSEGRRSRSRRYSGSDSDSISERKRPKKRGRPRTIPRENIKGFSDAEIRRFIKSYKKFGGPLERLDAIARDAELVDKSETDLRRLGELVHNGCVKALKDSSSGTERAGGRLGKVKGPTFRISGVQVNAKLVIAHEDELIPLHKSIPSDPEERKQYTIPCHTKAAHFDIDWGKEDDSNLLIGIYEYGYGSWEMIKMDPDLSLTHKILPDDPDKKPQAKQLQTRADYLIKLLSRDLAKREAQRLCGAGGSKRRKTRAKKSKAMKSIKVKEEIKSDSSPLPSEKSDEDDDKLNDSKPESKDRSKKSVVSDAPVHITASGEPVPIAEESEELDQKTFSICKERMRPVKAALKQLDRPEKGLSEREQLEHTRQCLIKIGDHITECLKEYSNPEQIKQWRKNLWIFVSKFTEFDARKLHKLYKHAIKKRQESQQNSDQNSNVATTHVIRNPDMERLKENTNHDDSSRDSYSSDRHLSQYHDHHKDRHQGDSYKKSDSRKRPYSSFSNGKDHREWDHYRQDSRYYSDREKHRKLDDHRSREHRPSLEGGLKDRCHSDHRSHSDHRMHSDHRSSSEHTHHKSSRDYRYLSDWQLDHRAASSGPRSPLDQRSPYGSRSPFEHSAEHRSTPEHTWSSRKT
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
1Oxidation-------MNGHSDEE
-------CCCCCCHH
52.8017242355
5Phosphorylation---MNGHSDEESVRN
---CCCCCCHHHHCC
48.3823684622
9PhosphorylationNGHSDEESVRNGSGE
CCCCCHHHHCCCCCC
25.0821149613
89PhosphorylationDGAEFWKSSPSILAV
CHHHHHHCCHHHHHH
37.7721082442
90PhosphorylationGAEFWKSSPSILAVQ
HHHHHHCCHHHHHHH
20.9522942356
92PhosphorylationEFWKSSPSILAVQRS
HHHHCCHHHHHHHHH
31.9825619855
173PhosphorylationEEERDKSSCDGTESD
HHHHHHHCCCCCCCC
23.2025195567
214PhosphorylationQKKRQIDSSEDEDDE
HHHHCCCCCCCCCCC
36.9427087446
215PhosphorylationKKRQIDSSEDEDDED
HHHCCCCCCCCCCCC
45.3727087446
235PhosphorylationRSSRRQATVNVSYKE
CCCCCEEEEECCCCC
12.32-
239PhosphorylationRQATVNVSYKEDEEM
CEEEEECCCCCCHHC
25.86-
248PhosphorylationKEDEEMKTDSDDLLE
CCCHHCCCCCHHHHH
39.1521149613
250PhosphorylationDEEMKTDSDDLLEVC
CHHCCCCCHHHHHHH
37.9521149613
469PhosphorylationVALKKQPSYIGGHEG
EEECCCCCCCCCCCC
27.2128285833
915PhosphorylationYRLVTKGSVEEDILE
EEEECCCCHHHHHHH
28.1022705319
944PhosphorylationRMDTTGKTVLHTGSA
EECCCCCEEEECCCC
29.6428576409
1023PhosphorylationQFKVANFSNMDEDDI
HCEECCCCCCCHHHC
30.93-
1038PhosphorylationELEPERNSKNWEEII
CCCCHHCCCCHHHHC
33.3225619855
1066PhosphorylationQKELEEIYMLPRMRN
HHHHHHHHHHHHHHH
8.9022817900
1079PhosphorylationRNCAKQISFNGSEGR
HHHHHHHCCCCCCCC
15.3427600695
1083PhosphorylationKQISFNGSEGRRSRS
HHHCCCCCCCCCCCC
37.6728285833
1088PhosphorylationNGSEGRRSRSRRYSG
CCCCCCCCCCCCCCC
32.9929514104
1093PhosphorylationRRSRSRRYSGSDSDS
CCCCCCCCCCCCCCC
19.1025159016
1094PhosphorylationRSRSRRYSGSDSDSI
CCCCCCCCCCCCCCH
29.9723684622
1096PhosphorylationRSRRYSGSDSDSISE
CCCCCCCCCCCCHHH
28.1823684622
1098PhosphorylationRRYSGSDSDSISERK
CCCCCCCCCCHHHCC
34.6523684622
1100PhosphorylationYSGSDSDSISERKRP
CCCCCCCCHHHCCCC
31.7823429704
1102PhosphorylationGSDSDSISERKRPKK
CCCCCCHHHCCCCCC
34.9925159016
1125PhosphorylationRENIKGFSDAEIRRF
HHHCCCCCHHHHHHH
44.5828066266
1159PhosphorylationDAELVDKSETDLRRL
CHHHCCCCHHHHHHH
41.06-
1181PhosphorylationCVKALKDSSSGTERA
HHHHHHCCCCCCCCC
25.4730635358
1182PhosphorylationVKALKDSSSGTERAG
HHHHHCCCCCCCCCC
42.8130635358
1183PhosphorylationKALKDSSSGTERAGG
HHHHCCCCCCCCCCC
54.4030635358
1185PhosphorylationLKDSSSGTERAGGRL
HHCCCCCCCCCCCCC
25.0130635358
1228PhosphorylationPLHKSIPSDPEERKQ
CCCCCCCCCHHHHHC
65.2226824392
1281PhosphorylationIKMDPDLSLTHKILP
EEECCCCCCCEECCC
38.3020531401
1283PhosphorylationMDPDLSLTHKILPDD
ECCCCCCCEECCCCC
20.1120531401
1353PhosphorylationKVKEEIKSDSSPLPS
HHHHHHCCCCCCCCC
48.6822817900
1355PhosphorylationKEEIKSDSSPLPSEK
HHHHCCCCCCCCCCC
40.7322817900
1356PhosphorylationEEIKSDSSPLPSEKS
HHHCCCCCCCCCCCC
35.1322817900
1360PhosphorylationSDSSPLPSEKSDEDD
CCCCCCCCCCCCCCC
66.4022817900
1363PhosphorylationSPLPSEKSDEDDDKL
CCCCCCCCCCCCCCC
42.0329550500
1373PhosphorylationDDDKLNDSKPESKDR
CCCCCCCCCCCCCCC
49.38-
1396PhosphorylationAPVHITASGEPVPIA
CCEEEEECCCCCCCC
34.7322006019
1541PhosphorylationNTNHDDSSRDSYSSD
HCCCCCCCCCCHHCH
47.2930387612
1544PhosphorylationHDDSSRDSYSSDRHL
CCCCCCCCHHCHHHH
26.2927149854
1545PhosphorylationDDSSRDSYSSDRHLS
CCCCCCCHHCHHHHH
19.2427149854
1546PhosphorylationDSSRDSYSSDRHLSQ
CCCCCCHHCHHHHHH
29.7027149854
1547PhosphorylationSSRDSYSSDRHLSQY
CCCCCHHCHHHHHHH
30.3627149854
1552PhosphorylationYSSDRHLSQYHDHHK
HHCHHHHHHHHHHCC
23.6727149854
1554PhosphorylationSDRHLSQYHDHHKDR
CHHHHHHHHHHCCCC
13.0727149854
1600PhosphorylationRQDSRYYSDREKHRK
HCCCCCCCCHHHHHC
22.66-
1619PhosphorylationRSREHRPSLEGGLKD
CCCCCCCCCCCCCCC
38.7226824392
1648PhosphorylationHSDHRSSSEHTHHKS
CCCCCCCCCCCCCCC
34.3425266776
1661PhosphorylationKSSRDYRYLSDWQLD
CCCCCCHHCCHHHCC
12.3428066266
1663PhosphorylationSRDYRYLSDWQLDHR
CCCCHHCCHHHCCHH
28.0626745281
1673PhosphorylationQLDHRAASSGPRSPL
HCCHHHHCCCCCCCC
34.5427149854
1674PhosphorylationLDHRAASSGPRSPLD
CCHHHHCCCCCCCCC
48.3527149854
1678PhosphorylationAASSGPRSPLDQRSP
HHCCCCCCCCCCCCC
32.7125521595
1684PhosphorylationRSPLDQRSPYGSRSP
CCCCCCCCCCCCCCC
19.4823684622
1686PhosphorylationPLDQRSPYGSRSPFE
CCCCCCCCCCCCCCC
29.0426643407
1688PhosphorylationDQRSPYGSRSPFEHS
CCCCCCCCCCCCCCC
24.6026824392
1690PhosphorylationRSPYGSRSPFEHSAE
CCCCCCCCCCCCCCC
35.3223684622
1695PhosphorylationSRSPFEHSAEHRSTP
CCCCCCCCCCCCCCC
28.3126643407
1700PhosphorylationEHSAEHRSTPEHTWS
CCCCCCCCCCCCCCC
50.6626643407
1701PhosphorylationHSAEHRSTPEHTWSS
CCCCCCCCCCCCCCC
32.4326643407
1705PhosphorylationHRSTPEHTWSSRKT-
CCCCCCCCCCCCCC-
25.9426643407
1707PhosphorylationSTPEHTWSSRKT---
CCCCCCCCCCCC---
22.7826643407
1708PhosphorylationTPEHTWSSRKT----
CCCCCCCCCCC----
29.3826643407

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 CHD1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHD1_MOUSE !!

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 CHD1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SSRP1_HUMANSSRP1physical
10199952

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHD1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND MASSSPECTROMETRY.

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