MBD5_HUMAN - dbPTM
MBD5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MBD5_HUMAN
UniProt AC Q9P267
Protein Name Methyl-CpG-binding domain protein 5
Gene Name MBD5
Organism Homo sapiens (Human).
Sequence Length 1494
Subcellular Localization Isoform 1: Nucleus. Chromosome. Associated with pericentric heterochromatin.
Isoform 2: Nucleus. Not associated with pericentric heterochromatin.
Protein Description Binds to heterochromatin. Does not interact with either methylated or unmethylated DNA (in vitro)..
Protein Sequence MNGGKECDGGDKEGGLPAIQVPVGWQRRVDQNGVLYVSPSGSLLSCLEQVKTYLLTDGTCKCGLECPLILPKVFNFDPGAAVKQRTAEDVKADEDVTKLCIHKRKIIAVATLHKSMEAPHPSLVLTSPGGGTNATPVVPSRAATPRSVRNKSHEGITNSVMPECKNPFKLMIGSSNAMGRLYVQELPGSQQQELHPVYPRQRLGSSEHGQKSPFRGSHGGLPSPASSGSQIYGDGSISPRTDPLGSPDVFTRSNPGFHGAPNSSPIHLNRTPLSPPSVMLHGSPVQSSCAMAGRTNIPLSPTLTTKSPVMKKPMCNFSTNMEIPRAMFHHKPPQGPPPPPPPSCALQKKPLTSEKDPLGILDPIPSKPVNQNPVIINPTSFHSNVHSQVPMMNVSMPPAVVPLPSNLPLPTVKPGHMNHGSHVQRVQHSASTSLSPSPVTSPVHMMGTGIGRIEASPQRSRSSSTSSDHGNFMMPPVGPQATSSGIKVPPRSPRSTIGSPRPSMPSSPSTKSDGHHQYKDIPNPLIAGISNVLNTPSSAAFPTASAGSSSVKSQPGLLGMPLNQILNQHNAASFPASSLLSAAAKAQLANQNKLAGNNSSSSSNSGAVAGSGNTEGHSTLNTMFPPTANMLLPTGEGQSGRAALRDKLMSQQKDALRKRKQPPTTVLSLLRQSQMDSSAVPKPGPDLLRKQGQGSFPISSMSQLLQSMSCQSSHLSSNSTPGCGASNTALPCSANQLHFTDPSMNSSVLQNIPLRGEAVHCHNANTNFVHSNSPVPNHHLAGLINQIQASGNCGMLSQSGMALGNSLHPNPPQSRISTSSTPVIPNSIVSSYNQTSSEAGGSGPSSSIAIAGTNHPAITKTTSVLQDGVIVTTAAGNPLQSQLPIGSDFPFVGQEHALHFPSNSTSNNHLPHPLNPSLLSSLPISLPVNQQHLLNQNLLNILQPSAGEGDMSSINNTLSNHQLTHLQSLLNNNQMFPPNQQQQQLLQGYQNLQAFQGQSTIPCPANNNPMACLFQNFQVRMQEDAALLNKRISTQPGLTALPENPNTTLPPFQDTPCELQPRIDPSLGQQVKDGLVVGGPGDASVDAIYKAVVDAASKGMQVVITTAVNSTTQISPIPALSAMSAFTASIGDPLNLSSAVSAVIHGRNMGGVDHDGRLRNSRGARLPKNLDHGKNVNEGDGFEYFKSASCHTSKKQWDGEQSPRGERNRWKYEEFLDHPGHIHSSPCHERPNNVSTLPFLPGEQHPILLPPRNCPGDKILEENFRYNNYKRTMMSFKERLENTVERCAHINGNRPRQSRGFGELLSTAKQDLVLEEQSPSSSNSLENSLVKDYIHYNGDFNAKSVNGCVPSPSDAKSISSEDDLRNPDSPSSNELIHYRPRTFNVGDLVWGQIKGLTSWPGKLVREDDVHNSCQQSPEEGKVEPEKLKTLTEGLEAYSRVRKRNRKSGKLNNHLEAAIHEAMSELDKMSGTVHQIPQGDRQMRPPKPKRRKISR
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
205PhosphorylationYPRQRLGSSEHGQKS
CCCCCCCCCCCCCCC
36.8327273156
206PhosphorylationPRQRLGSSEHGQKSP
CCCCCCCCCCCCCCC
31.6420873877
212PhosphorylationSSEHGQKSPFRGSHG
CCCCCCCCCCCCCCC
22.7620873877
236PhosphorylationSQIYGDGSISPRTDP
CCCCCCCCCCCCCCC
25.3225850435
238PhosphorylationIYGDGSISPRTDPLG
CCCCCCCCCCCCCCC
15.2725850435
246PhosphorylationPRTDPLGSPDVFTRS
CCCCCCCCCCCCCCC
26.1321815630
251PhosphorylationLGSPDVFTRSNPGFH
CCCCCCCCCCCCCCC
32.7930108239
253PhosphorylationSPDVFTRSNPGFHGA
CCCCCCCCCCCCCCC
44.3023403867
263PhosphorylationGFHGAPNSSPIHLNR
CCCCCCCCCCCCCCC
36.1123403867
264PhosphorylationFHGAPNSSPIHLNRT
CCCCCCCCCCCCCCC
34.2223403867
295PhosphorylationSCAMAGRTNIPLSPT
CCCCCCCCCCCCCCC
36.2622199227
300PhosphorylationGRTNIPLSPTLTTKS
CCCCCCCCCCCCCCC
15.5222199227
302PhosphorylationTNIPLSPTLTTKSPV
CCCCCCCCCCCCCCC
33.1023403867
304PhosphorylationIPLSPTLTTKSPVMK
CCCCCCCCCCCCCCC
34.3623403867
305PhosphorylationPLSPTLTTKSPVMKK
CCCCCCCCCCCCCCC
32.4123403867
307PhosphorylationSPTLTTKSPVMKKPM
CCCCCCCCCCCCCCC
22.1922199227
366PhosphorylationGILDPIPSKPVNQNP
CCCCCCCCCCCCCCC
50.7624719451
429PhosphorylationHVQRVQHSASTSLSP
CCEEEECCCCCCCCC
13.56-
431PhosphorylationQRVQHSASTSLSPSP
EEEECCCCCCCCCCC
22.88-
432PhosphorylationRVQHSASTSLSPSPV
EEECCCCCCCCCCCC
33.14-
437PhosphorylationASTSLSPSPVTSPVH
CCCCCCCCCCCCCCE
28.7321712546
440PhosphorylationSLSPSPVTSPVHMMG
CCCCCCCCCCCEECC
30.6021712546
441PhosphorylationLSPSPVTSPVHMMGT
CCCCCCCCCCEECCC
25.7621712546
456PhosphorylationGIGRIEASPQRSRSS
CCCCEECCCCCCCCC
14.5824719451
463PhosphorylationSPQRSRSSSTSSDHG
CCCCCCCCCCCCCCC
36.2024719451
484PhosphorylationVGPQATSSGIKVPPR
CCCCCCCCCCCCCCC
39.9324719451
492PhosphorylationGIKVPPRSPRSTIGS
CCCCCCCCCCCCCCC
30.3624247654
495PhosphorylationVPPRSPRSTIGSPRP
CCCCCCCCCCCCCCC
27.9727732954
496PhosphorylationPPRSPRSTIGSPRPS
CCCCCCCCCCCCCCC
30.5427732954
499PhosphorylationSPRSTIGSPRPSMPS
CCCCCCCCCCCCCCC
17.5627732954
503PhosphorylationTIGSPRPSMPSSPST
CCCCCCCCCCCCCCC
44.6027732954
506PhosphorylationSPRPSMPSSPSTKSD
CCCCCCCCCCCCCCC
46.3627732954
507PhosphorylationPRPSMPSSPSTKSDG
CCCCCCCCCCCCCCC
19.5927732954
509PhosphorylationPSMPSSPSTKSDGHH
CCCCCCCCCCCCCCC
50.8727732954
510PhosphorylationSMPSSPSTKSDGHHQ
CCCCCCCCCCCCCCC
37.6427732954
664PhosphorylationRKRKQPPTTVLSLLR
HHCCCCCHHHHHHHH
35.9024719451
668PhosphorylationQPPTTVLSLLRQSQM
CCCHHHHHHHHHHHC
22.4824719451
673PhosphorylationVLSLLRQSQMDSSAV
HHHHHHHHHCCCCCC
22.4924719451
820PhosphorylationQSRISTSSTPVIPNS
CCCCCCCCCCCCCHH
36.5028857561
832PhosphorylationPNSIVSSYNQTSSEA
CHHHHHCCCCCCCCC
12.0928857561
1272PhosphorylationRYNNYKRTMMSFKER
CCCCHHHHHHHHHHH
17.0522210691
1275PhosphorylationNYKRTMMSFKERLEN
CHHHHHHHHHHHHHH
23.5028348404
1283PhosphorylationFKERLENTVERCAHI
HHHHHHHHHHHHHHH
17.8623312004
1402AcetylationGLTSWPGKLVREDDV
CCCCCCCEEEEHHHC
39.4625953088

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 MBD5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MBD5_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 MBD5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBE2T_HUMANUBE2Tphysical
26186194
IF2B_HUMANEIF2S2physical
26186194
PMVK_HUMANPMVKphysical
26186194
HDGR2_HUMANHDGFRP2physical
26186194
UB2E1_HUMANUBE2E1physical
26186194
NAA15_HUMANNAA15physical
26186194
ERF1_HUMANETF1physical
26186194
SNX3_HUMANSNX3physical
26186194
HMCS1_HUMANHMGCS1physical
26186194
RHOA_HUMANRHOAphysical
26186194
UBA6_HUMANUBA6physical
26186194
HMCS1_HUMANHMGCS1physical
28514442
LZIC_HUMANLZICphysical
28514442
SNX3_HUMANSNX3physical
28514442
UBE2T_HUMANUBE2Tphysical
28514442
HDGR2_HUMANHDGFRP2physical
28514442
UB2E1_HUMANUBE2E1physical
28514442
BID_HUMANBIDphysical
28514442
PMVK_HUMANPMVKphysical
28514442
ERF1_HUMANETF1physical
28514442
NAA50_HUMANNAA50physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MBD5_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP