CHD1_HUMAN - dbPTM
CHD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHD1_HUMAN
UniProt AC O14646
Protein Name Chromodomain-helicase-DNA-binding protein 1
Gene Name CHD1
Organism Homo sapiens (Human).
Sequence Length 1710
Subcellular Localization Nucleus . Cytoplasm . Is released into the cytoplasm when cells enter mitosis and is reincorporated into chromatin during telophase-cytokinesis.
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. Is also associated with histone deacetylase (HDAC) activity (By similarity). 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. [PubMed: 18042460]
Protein Sequence MNGHSDEESVRNSSGESSQSDDDSGSASGSGSGSSSGSSSDGSSSQSGSSDSDSGSESGSQSESESDTSRENKVQAKPPKVDGAEFWKSSPSILAVQRSAILKKQQQQQQQQQHQASSNSGSEEDSSSSEDSDDSSSEVKRKKHKDEDWQMSGSGSPSQSGSDSESEEEREKSSCDETESDYEPKNKVKSRKPQNRSKSKNGKKILGQKKRQIDSSEEDDDEEDYDNDKRSSRRQATVNVSYKEDEEMKTDSDDLLEVCGEDVPQPEEEEFETIERFMDCRIGRKGATGATTTIYAVEADGDPNAGFEKNKEPGEIQYLIKWKGWSHIHNTWETEETLKQQNVRGMKKLDNYKKKDQETKRWLKNASPEDVEYYNCQQELTDDLHKQYQIVERIIAHSNQKSAAGYPDYYCKWQGLPYSECSWEDGALISKKFQACIDEYFSRNQSKTTPFKDCKVLKQRPRFVALKKQPSYIGGHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWASQMNAVVYLGDINSRNMIRTHEWTHHQTKRLKFNILLTTYEILLKDKAFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYASLHKELEPFLLRRVKKDVEKSLPAKVEQILRMEMSALQKQYYKWILTRNYKALSKGSKGSTSGFLNIMMELKKCCNHCYLIKPPDNNEFYNKQEALQHLIRSSGKLILLDKLLIRLRERGNRVLIFSQMVRMLDILAEYLKYRQFPFQRLDGSIKGELRKQALDHFNAEGSEDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGSVEEDILERAKKKMVLDHLVIQRMDTTGKTVLHTGSAPSSSTPFNKEELSAILKFGAEELFKEPEGEEQEPQEMDIDEILKRAETHENEPGPLTVGDELLSQFKVANFSNMDEDDIELEPERNSKNWEEIIPEDQRRRLEEEERQKELEEIYMLPRMRNCAKQISFNGSEGRRSRSRRYSGSDSDSISEGKRPKKRGRPRTIPRENIKGFSDAEIRRFIKSYKKFGGPLERLDAIARDAELVDKSETDLRRLGELVHNGCIKALKDSSSGTERTGGRLGKVKGPTFRISGVQVNAKLVISHEEELIPLHKSIPSDPEERKQYTIPCHTKAAHFDIDWGKEDDSNLLIGIYEYGYGSWEMIKMDPDLSLTHKILPDDPDKKPQAKQLQTRADYLIKLLSRDLAKKEALSGAGSSKRRKARAKKNKAMKSIKVKEEIKSDSSPLPSEKSDEDDDKLSESKSDGRERSKKSSVSDAPVHITASGEPVPISEESEELDQKTFSICKERMRPVKAALKQLDRPEKGLSEREQLEHTRQCLIKIGDHITECLKEYTNPEQIKQWRKNLWIFVSKFTEFDARKLHKLYKHAIKKRQESQQNSDQNSNLNPHVIRNPDVERLKENTNHDDSSRDSYSSDRHLTQYHDHHKDRHQGDSYKKSDSRKRPYSSFSNGKDHRDWDHYKQDSRYYSDREKHRKLDDHRSRDHRSNLEGSLKDRSHSDHRSHSDHRLHSDHRSSSEYTHHKSSRDYRYHSDWQMDHRASSSGPRSPLDQRSPYGSRSPFEHSVEHKSTPEHTWSSRKT
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
5Phosphorylation---MNGHSDEESVRN
---CCCCCCHHHHCC
48.3823663014
9PhosphorylationNGHSDEESVRNSSGE
CCCCCHHHHCCCCCC
25.0827486199
77AcetylationRENKVQAKPPKVDGA
CCCCCCCCCCCCCHH
44.7725953088
88UbiquitinationVDGAEFWKSSPSILA
CCHHHHHHCCHHHHH
46.51-
89PhosphorylationDGAEFWKSSPSILAV
CHHHHHHCCHHHHHH
37.7723401153
90PhosphorylationGAEFWKSSPSILAVQ
HHHHHHCCHHHHHHH
20.9525159151
92PhosphorylationEFWKSSPSILAVQRS
HHHHCCHHHHHHHHH
31.9822115753
152PhosphorylationKDEDWQMSGSGSPSQ
CCCCCCCCCCCCCCC
18.0822210691
154PhosphorylationEDWQMSGSGSPSQSG
CCCCCCCCCCCCCCC
28.8822210691
162PhosphorylationGSPSQSGSDSESEEE
CCCCCCCCCCCCHHH
43.1222210691
164PhosphorylationPSQSGSDSESEEERE
CCCCCCCCCCHHHHH
44.7330576142
173PhosphorylationSEEEREKSSCDETES
CHHHHHHHCCCCCCC
31.2923663014
174PhosphorylationEEEREKSSCDETESD
HHHHHHHCCCCCCCC
36.3323663014
178PhosphorylationEKSSCDETESDYEPK
HHHCCCCCCCCCCCC
27.7723663014
180PhosphorylationSSCDETESDYEPKNK
HCCCCCCCCCCCCHH
53.5725850435
182PhosphorylationCDETESDYEPKNKVK
CCCCCCCCCCCHHHC
43.3327732954
215PhosphorylationQKKRQIDSSEEDDDE
CCHHCCCCCCCCCCC
41.0822167270
216PhosphorylationKKRQIDSSEEDDDEE
CHHCCCCCCCCCCCC
41.0622167270
225PhosphorylationEDDDEEDYDNDKRSS
CCCCCCCCCCCCCCC
21.6720363803
232PhosphorylationYDNDKRSSRRQATVN
CCCCCCCCCCEEEEE
35.20-
237PhosphorylationRSSRRQATVNVSYKE
CCCCCEEEEECCCCC
12.3218669648
241PhosphorylationRQATVNVSYKEDEEM
CEEEEECCCCCCHHC
25.8621082442
250PhosphorylationKEDEEMKTDSDDLLE
CCCHHCCCCCHHHHH
39.1517192257
252PhosphorylationDEEMKTDSDDLLEVC
CHHCCCCCHHHHHHH
37.9517192257
285UbiquitinationMDCRIGRKGATGATT
HHCCCCCCCCCCCEE
47.92-
311UbiquitinationNAGFEKNKEPGEIQY
CCCCCCCCCCCCEEE
76.10-
339UbiquitinationWETEETLKQQNVRGM
CCCHHHHHHHCCCCH
58.20-
348AcetylationQNVRGMKKLDNYKKK
HCCCCHHHHHHCHHH
52.7819817877
352PhosphorylationGMKKLDNYKKKDQET
CHHHHHHCHHHHHHH
24.6928152594
364UbiquitinationQETKRWLKNASPEDV
HHHHHHHHHCCHHHH
43.43-
367PhosphorylationKRWLKNASPEDVEYY
HHHHHHCCHHHHHHH
37.9128985074
386UbiquitinationELTDDLHKQYQIVER
HHCHHHHHHHHHHHH
58.98-
388PhosphorylationTDDLHKQYQIVERII
CHHHHHHHHHHHHHH
12.6628152594
398PhosphorylationVERIIAHSNQKSAAG
HHHHHHHCCCCCCCC
31.7522817900
401AcetylationIIAHSNQKSAAGYPD
HHHHCCCCCCCCCCC
46.4426051181
401UbiquitinationIIAHSNQKSAAGYPD
HHHHCCCCCCCCCCC
46.44-
412UbiquitinationGYPDYYCKWQGLPYS
CCCCCCCEECCCCHH
26.82-
431UbiquitinationEDGALISKKFQACID
CCCCHHHHHHHHHHH
51.09-
447UbiquitinationYFSRNQSKTTPFKDC
HHHCCCCCCCCCCCC
46.80-
449PhosphorylationSRNQSKTTPFKDCKV
HCCCCCCCCCCCCHH
30.39-
455UbiquitinationTTPFKDCKVLKQRPR
CCCCCCCHHHHCCCC
61.81-
468UbiquitinationPRFVALKKQPSYIGG
CCEEEECCCCCCCCC
69.19-
471PhosphorylationVALKKQPSYIGGHEG
EEECCCCCCCCCCCC
27.2125159151
472PhosphorylationALKKQPSYIGGHEGL
EECCCCCCCCCCCCC
15.4028450419
508SulfoxidationSCILADEMGLGKTIQ
CCEEECCCCCCCHHH
5.7421406390
620UbiquitinationVDEAHRLKNDDSLLY
CCHHHHHCCCCCHHH
59.28-
624PhosphorylationHRLKNDDSLLYKTLI
HHHCCCCCHHHHHHH
24.1228555341
628UbiquitinationNDDSLLYKTLIDFKS
CCCCHHHHHHHCCCC
36.50-
634AcetylationYKTLIDFKSNHRLLI
HHHHHCCCCCCCEEE
46.7525953088
634UbiquitinationYKTLIDFKSNHRLLI
HHHHHCCCCCCCEEE
46.75-
667PhosphorylationIMPEKFSSWEDFEEE
HCCHHCCCHHHHHHH
37.30-
677UbiquitinationDFEEEHGKGREYGYA
HHHHHHCCCCCCCCC
57.62-
681PhosphorylationEHGKGREYGYASLHK
HHCCCCCCCCCHHHH
17.67-
705PhosphorylationVKKDVEKSLPAKVEQ
HHHHHHHCCCHHHHH
26.53-
719PhosphorylationQILRMEMSALQKQYY
HHHHHHHHHHHHHHH
16.72-
725PhosphorylationMSALQKQYYKWILTR
HHHHHHHHHHHHHHH
17.66-
726PhosphorylationSALQKQYYKWILTRN
HHHHHHHHHHHHHHC
9.4326657352
731PhosphorylationQYYKWILTRNYKALS
HHHHHHHHHCHHHHH
14.0326657352
738PhosphorylationTRNYKALSKGSKGST
HHCHHHHHCCCCCCH
39.57-
745PhosphorylationSKGSKGSTSGFLNIM
HCCCCCCHHHHHHHH
41.35-
746PhosphorylationKGSKGSTSGFLNIMM
CCCCCCHHHHHHHHH
29.2824114839
786PhosphorylationALQHLIRSSGKLILL
HHHHHHHHCCCEEHH
36.1325690035
813SulfoxidationRVLIFSQMVRMLDIL
EEEEEHHHHHHHHHH
1.6831801345
823PhosphorylationMLDILAEYLKYRQFP
HHHHHHHHHHHCCCC
11.6821406692
910PhosphorylationQKKQVNIYRLVTKGS
CCCCEEEEEEECCCC
7.8427732954
914PhosphorylationVNIYRLVTKGSVEED
EEEEEEECCCCHHHH
33.9927732954
915UbiquitinationNIYRLVTKGSVEEDI
EEEEEECCCCHHHHH
41.53-
942PhosphorylationLVIQRMDTTGKTVLH
HHHEEECCCCCEEEE
28.2722210691
943PhosphorylationVIQRMDTTGKTVLHT
HHEEECCCCCEEEEC
32.2027282143
945AcetylationQRMDTTGKTVLHTGS
EEECCCCCEEEECCC
33.1126051181
945UbiquitinationQRMDTTGKTVLHTGS
EEECCCCCEEEECCC
33.11-
950PhosphorylationTGKTVLHTGSAPSSS
CCCEEEECCCCCCCC
28.7722210691
952PhosphorylationKTVLHTGSAPSSSTP
CEEEECCCCCCCCCC
37.8622210691
957PhosphorylationTGSAPSSSTPFNKEE
CCCCCCCCCCCCHHH
44.4222210691
958PhosphorylationGSAPSSSTPFNKEEL
CCCCCCCCCCCHHHH
33.5725159151
962AcetylationSSSTPFNKEELSAIL
CCCCCCCHHHHHHHH
53.6026051181
962UbiquitinationSSSTPFNKEELSAIL
CCCCCCCHHHHHHHH
53.60-
966PhosphorylationPFNKEELSAILKFGA
CCCHHHHHHHHHHCH
19.2821815630
997UbiquitinationMDIDEILKRAETHEN
CCHHHHHHHHHCCCC
56.05-
1010PhosphorylationENEPGPLTVGDELLS
CCCCCCCCCCHHHHH
26.1024114839
1025PhosphorylationQFKVANFSNMDEDDI
HCEECCCCCCCHHHC
30.9330576142
1040PhosphorylationELEPERNSKNWEEII
CCCCHHCCCCHHHHC
33.3225159151
1041AcetylationLEPERNSKNWEEIIP
CCCHHCCCCHHHHCC
70.4125953088
1041UbiquitinationLEPERNSKNWEEIIP
CCCHHCCCCHHHHCC
70.41-
1062UbiquitinationLEEEERQKELEEIYM
HHHHHHHHHHHHHHH
71.18-
1068PhosphorylationQKELEEIYMLPRMRN
HHHHHHHHHHHHHHH
8.9021945579
1078AcetylationPRMRNCAKQISFNGS
HHHHHHHHHHCCCCC
50.8225953088
1081PhosphorylationRNCAKQISFNGSEGR
HHHHHHHCCCCCCCC
15.3425159151
1085PhosphorylationKQISFNGSEGRRSRS
HHHCCCCCCCCCCCC
37.6725159151
1090PhosphorylationNGSEGRRSRSRRYSG
CCCCCCCCCCCCCCC
32.9925159151
1092PhosphorylationSEGRRSRSRRYSGSD
CCCCCCCCCCCCCCC
23.5029523821
1095PhosphorylationRRSRSRRYSGSDSDS
CCCCCCCCCCCCCCC
19.1023927012
1096PhosphorylationRSRSRRYSGSDSDSI
CCCCCCCCCCCCCCC
29.9729255136
1098PhosphorylationRSRRYSGSDSDSISE
CCCCCCCCCCCCCCC
28.1829255136
1100PhosphorylationRRYSGSDSDSISEGK
CCCCCCCCCCCCCCC
34.6529255136
1102PhosphorylationYSGSDSDSISEGKRP
CCCCCCCCCCCCCCC
31.7825159151
1104PhosphorylationGSDSDSISEGKRPKK
CCCCCCCCCCCCCCC
44.2223927012
1124MethylationTIPRENIKGFSDAEI
CCCHHHCCCCCHHHH
66.54-
1124UbiquitinationTIPRENIKGFSDAEI
CCCHHHCCCCCHHHH
66.54-
1127PhosphorylationRENIKGFSDAEIRRF
HHHCCCCCHHHHHHH
44.5823898821
1160AcetylationRDAELVDKSETDLRR
HCHHHCCCCHHHHHH
42.5926051181
1160UbiquitinationRDAELVDKSETDLRR
HCHHHCCCCHHHHHH
42.59-
1161PhosphorylationDAELVDKSETDLRRL
CHHHCCCCHHHHHHH
41.0625849741
1163PhosphorylationELVDKSETDLRRLGE
HHCCCCHHHHHHHHH
47.6423186163
1178AcetylationLVHNGCIKALKDSSS
HHHHCHHHHHHCCCC
52.3126051181
1183PhosphorylationCIKALKDSSSGTERT
HHHHHHCCCCCCEEC
25.4723312004
1184PhosphorylationIKALKDSSSGTERTG
HHHHHCCCCCCEECC
42.8128985074
1185PhosphorylationKALKDSSSGTERTGG
HHHHCCCCCCEECCC
54.4023312004
1187PhosphorylationLKDSSSGTERTGGRL
HHCCCCCCEECCCCC
25.0023312004
1190PhosphorylationSSSGTERTGGRLGKV
CCCCCEECCCCCCCC
37.44-
1226UbiquitinationEELIPLHKSIPSDPE
HHHCCCCCCCCCCHH
58.73-
1227PhosphorylationELIPLHKSIPSDPEE
HHCCCCCCCCCCHHH
29.0528985074
1230PhosphorylationPLHKSIPSDPEERKQ
CCCCCCCCCHHHHHC
65.2221815630
1236UbiquitinationPSDPEERKQYTIPCH
CCCHHHHHCCCCCCC
51.43-
1283PhosphorylationIKMDPDLSLTHKILP
EEECCCCCCCEECCC
38.30-
1285PhosphorylationMDPDLSLTHKILPDD
ECCCCCCCEECCCCC
20.11-
1320UbiquitinationLSRDLAKKEALSGAG
HHHHHHHHHHHCCCC
42.48-
1324PhosphorylationLAKKEALSGAGSSKR
HHHHHHHCCCCCHHH
33.3829396449
1328PhosphorylationEALSGAGSSKRRKAR
HHHCCCCCHHHHHHH
31.9517192257
1329PhosphorylationALSGAGSSKRRKARA
HHCCCCCHHHHHHHH
29.3028985074
13302-HydroxyisobutyrylationLSGAGSSKRRKARAK
HCCCCCHHHHHHHHH
58.90-
1330AcetylationLSGAGSSKRRKARAK
HCCCCCHHHHHHHHH
58.9025953088
1338AcetylationRRKARAKKNKAMKSI
HHHHHHHHHHHHHHH
63.80129547
1340AcetylationKARAKKNKAMKSIKV
HHHHHHHHHHHHHHH
59.757661725
1343AcetylationAKKNKAMKSIKVKEE
HHHHHHHHHHHHHHH
54.627661737
1346AcetylationNKAMKSIKVKEEIKS
HHHHHHHHHHHHHCC
55.11129551
1353PhosphorylationKVKEEIKSDSSPLPS
HHHHHHCCCCCCCCC
48.6820044836
1355PhosphorylationKEEIKSDSSPLPSEK
HHHHCCCCCCCCCCC
40.7320044836
1356PhosphorylationEEIKSDSSPLPSEKS
HHHCCCCCCCCCCCC
35.1325159151
1360PhosphorylationSDSSPLPSEKSDEDD
CCCCCCCCCCCCCCC
66.4023401153
1363PhosphorylationSPLPSEKSDEDDDKL
CCCCCCCCCCCCHHH
42.0325159151
1371PhosphorylationDEDDDKLSESKSDGR
CCCCHHHCCCCCCCC
45.6321815630
1373PhosphorylationDDDKLSESKSDGRER
CCHHHCCCCCCCCHH
33.8021815630
1381PhosphorylationKSDGRERSKKSSVSD
CCCCCHHCCCCCCCC
39.4226074081
1384PhosphorylationGRERSKKSSVSDAPV
CCHHCCCCCCCCCCC
39.4425159151
1385PhosphorylationRERSKKSSVSDAPVH
CHHCCCCCCCCCCCE
34.2225159151
1387PhosphorylationRSKKSSVSDAPVHIT
HCCCCCCCCCCCEEE
29.9725159151
1394PhosphorylationSDAPVHITASGEPVP
CCCCCEEEECCCCCC
10.4128122231
1396PhosphorylationAPVHITASGEPVPIS
CCCEEEECCCCCCCC
34.7325159151
1403PhosphorylationSGEPVPISEESEELD
CCCCCCCCCCHHHHC
29.2821082442
1406PhosphorylationPVPISEESEELDQKT
CCCCCCCHHHHCHHH
32.1121082442
1436AcetylationKQLDRPEKGLSEREQ
HHCCCCCCCCCHHHH
68.7625953088
1436UbiquitinationKQLDRPEKGLSEREQ
HHCCCCCCCCCHHHH
68.76-
1453AcetylationHTRQCLIKIGDHITE
HHHHHHHHHHHHHHH
27.9125953088
1463AcetylationDHITECLKEYTNPEQ
HHHHHHHHHCCCHHH
61.4026051181
1483PhosphorylationKNLWIFVSKFTEFDA
HHHHHHHHCCCHHHH
16.0025101063
1491MethylationKFTEFDARKLHKLYK
CCCHHHHHHHHHHHH
43.86-
1507PhosphorylationAIKKRQESQQNSDQN
HHHHHHHHHHCCCCC
28.8228555341
1511PhosphorylationRQESQQNSDQNSNLN
HHHHHHCCCCCCCCC
35.9125159151
1515PhosphorylationQQNSDQNSNLNPHVI
HHCCCCCCCCCHHHH
36.7427050516
1534PhosphorylationVERLKENTNHDDSSR
HHHHHHHCCCCCCCC
34.7120873877
1539PhosphorylationENTNHDDSSRDSYSS
HHCCCCCCCCCCCCC
33.0730576142
1540PhosphorylationNTNHDDSSRDSYSSD
HCCCCCCCCCCCCCH
47.2925849741
1543PhosphorylationHDDSSRDSYSSDRHL
CCCCCCCCCCCHHCH
26.2930576142
1544PhosphorylationDDSSRDSYSSDRHLT
CCCCCCCCCCHHCHH
19.2430576142
1545PhosphorylationDSSRDSYSSDRHLTQ
CCCCCCCCCHHCHHC
29.7028985074
1546PhosphorylationSSRDSYSSDRHLTQY
CCCCCCCCHHCHHCC
30.3629496963
1576PhosphorylationSDSRKRPYSSFSNGK
CCCCCCCCCCCCCCC
22.4528555341
1577PhosphorylationDSRKRPYSSFSNGKD
CCCCCCCCCCCCCCC
27.8228555341
1578PhosphorylationSRKRPYSSFSNGKDH
CCCCCCCCCCCCCCC
27.1825159151
1580PhosphorylationKRPYSSFSNGKDHRD
CCCCCCCCCCCCCCC
46.7725159151
1591PhosphorylationDHRDWDHYKQDSRYY
CCCCCCHHHCCCCCC
14.10-
1595PhosphorylationWDHYKQDSRYYSDRE
CCHHHCCCCCCCCHH
21.4925159151
1599PhosphorylationKQDSRYYSDREKHRK
HCCCCCCCCHHHHHC
22.6630576142
1622PhosphorylationHRSNLEGSLKDRSHS
HHHHCCHHHCCCCCC
23.9125159151
1641PhosphorylationHSDHRLHSDHRSSSE
CCCCCCCCCCCCCCC
39.4429449344
1645PhosphorylationRLHSDHRSSSEYTHH
CCCCCCCCCCCCCCC
34.4929449344
1646PhosphorylationLHSDHRSSSEYTHHK
CCCCCCCCCCCCCCC
27.4427134283
1647PhosphorylationHSDHRSSSEYTHHKS
CCCCCCCCCCCCCCC
35.5527251275
1649PhosphorylationDHRSSSEYTHHKSSR
CCCCCCCCCCCCCCC
17.2029449344
1650PhosphorylationHRSSSEYTHHKSSRD
CCCCCCCCCCCCCCC
17.2929449344
1662PhosphorylationSRDYRYHSDWQMDHR
CCCCCCCCCHHCCCC
31.4528555341
1671PhosphorylationWQMDHRASSSGPRSP
HHCCCCCCCCCCCCC
25.6223401153
1671 (in isoform 2)Phosphorylation-25.6225159151
1672PhosphorylationQMDHRASSSGPRSPL
HCCCCCCCCCCCCCC
38.0330266825
1672 (in isoform 2)Phosphorylation-38.0327762562
1673PhosphorylationMDHRASSSGPRSPLD
CCCCCCCCCCCCCCC
50.7730266825
1673 (in isoform 2)Phosphorylation-50.7727762562
1677PhosphorylationASSSGPRSPLDQRSP
CCCCCCCCCCCCCCC
32.7122167270
1677 (in isoform 2)Phosphorylation-32.7129743597
1683PhosphorylationRSPLDQRSPYGSRSP
CCCCCCCCCCCCCCC
19.4825159151
1683 (in isoform 2)Phosphorylation-19.4828152594
1684 (in isoform 2)Phosphorylation-39.4328152594
1685PhosphorylationPLDQRSPYGSRSPFE
CCCCCCCCCCCCCCC
29.0428176443
1686 (in isoform 2)Phosphorylation-21.7023403867
1687PhosphorylationDQRSPYGSRSPFEHS
CCCCCCCCCCCCCCC
24.6025159151
1688 (in isoform 2)Phosphorylation-43.9425159151
1689PhosphorylationRSPYGSRSPFEHSVE
CCCCCCCCCCCCCCC
35.3229255136
1693 (in isoform 2)Phosphorylation-37.2128152594
1694PhosphorylationSRSPFEHSVEHKSTP
CCCCCCCCCCCCCCC
23.2330266825
1698 (in isoform 2)Phosphorylation-42.3829116813
1699PhosphorylationEHSVEHKSTPEHTWS
CCCCCCCCCCCCCCC
51.6130266825
1700PhosphorylationHSVEHKSTPEHTWSS
CCCCCCCCCCCCCCC
37.1830266825
1704PhosphorylationHKSTPEHTWSSRKT-
CCCCCCCCCCCCCC-
25.9422167270
1706PhosphorylationSTPEHTWSSRKT---
CCCCCCCCCCCC---
22.7825159151
1707PhosphorylationTPEHTWSSRKT----
CCCCCCCCCCC----
29.3822167270

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHD1_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 CHD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCLF1_HUMANBCLAF1physical
12890497
SRSF3_HUMANSRSF3physical
12890497
NCOR1_HUMANNCOR1physical
12890497
SAFB1_HUMANSAFBphysical
12890497
SSRP1_HUMANSSRP1physical
10199952
H31_HUMANHIST1H3Aphysical
16372014
PAF1_HUMANPAF1physical
22046413
FBW1A_HUMANBTRCphysical
28166537

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
DB00445Epirubicin
Regulatory Network of CHD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-92; SER-215; SER-216;SER-1403 AND SER-1406, AND MASS SPECTROMETRY.
"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 THR-237; SER-241; SER-1040;SER-1096; SER-1098; SER-1100 AND SER-1677, AND MASS SPECTROMETRY.
"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 SER-241; THR-250; SER-252;SER-1040; SER-1081; SER-1096; SER-1098; SER-1100; SER-1102; SER-1328;SER-1353; SER-1355; SER-1356; SER-1360; SER-1387; SER-1396; SER-1622;SER-1677; SER-1689 AND THR-1700, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-92; SER-241 ANDSER-1622, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1353; SER-1355; SER-1356AND SER-1360, AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND SER-216, ANDMASS SPECTROMETRY.
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry.";
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1068, AND MASSSPECTROMETRY.

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