SMHD1_MOUSE - dbPTM
SMHD1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMHD1_MOUSE
UniProt AC Q6P5D8
Protein Name Structural maintenance of chromosomes flexible hinge domain-containing protein 1
Gene Name Smchd1
Organism Mus musculus (Mouse).
Sequence Length 2007
Subcellular Localization Chromosome .
Protein Description Required for maintenance of X inactivation in females and hypermethylation of CpG islands associated with inactive X. Involved in a pathway that mediates the methylation of a subset of CpG islands slowly and requires the methyltransferase DNMT3B. [PubMed: 18425126]
Protein Sequence MAAEGASDPAGLSEGSGRDGAVDGCRTVYLFDRRGKDSELGDRALQVSEHADYAGFRASVCQTIGISSEEKFVITTTSRKEITCNNFDHTVKDGVTLYLLQSVDQSLLTATKERIDFLPHYDTLVKSGMYEYYASEGQNPLPFALAELIDNSLSATSRNNGVRRIQIKLLFDETQGKPAVAVVDNGRGMTSKQLNNWAVYRLSKFTRQGDFESDHSGYVRPLPVPRSLNSDISYFGVGGKQAVFFVGQSARMISKPIDSKDVHELVLSKEDFEKKEKNKEAIYSGYIRNRKPADSAHITNDDERFLHNLIEEEKEKDSFTAVVITGVQPEHIQYLKNYLHLWTRQLTHIYHYYIHGPKGNEISTAKAIGPFNNIDIEISLFEKGKTPKIINLREIQDDMQTLYINTASDSFEFKAHVEGDGVVEGVIRYHPFLYDRETFPDDPCFPSKLKDEDDDDDCFISEKAARGKRPIFECFWNGRLIPYTSVGDFDWCAPPKKRGLVPIECFNRISGALFTNDKFQVSTNKLTFMDLELKLKDKNTLFTRILNGQEQRMKIDREFALWLKDCHEKHDKQIKFTLFKGIITRPDLPTKKQGPWATFSAIEWDGKIYKAGQLVKTIKTLPLCYGSIVRFFLHGDHDGEVYATGGEVQIAMEPQALYDEIKTVPIAKLDRTVAEKTIRKYVEDEMARLPDRLSVTWPEGDELLPNEVRPAGTPIGALRIEILNKKGEAMQKLPGTSHGGSKKLLVELKVILHTSSGNKEIISHISQHGGKWPYWFKKMENIQKLGNYTLKLQVVLNESNADTYAGRSLPSKVIKFSVKEGKPEKFSFGLLDSPFRVGVPFNIPLELQDEFGHTTQLLSDIEPVLEASGLSLHYEGITKGPNCVIQGVVAKGPVNSCQGKNFNLKVILPGLKEDSQILKIRLLPGPPHQLKVKPDSEVLVIENGTAFPFQVEVVDESDNITAQPKLIVHCKFLGAPNLPVYTVDCSSSGTSILTGSPIQVQNIKKDQKTLTARIEIPSCKDVSPVEKTIKLLPSSHAACLQIFSVEEQKAIQIKHQDEVTWVAGDVIRNLIFQMYDEGEREINITPSLAEKIKVNWTPEVNKEHLVQGLLPDVQVPTSVKDVRYCHVSFQDDHVCLESAFTVRPLPDDPKHLKCELKGGKTVQMGQELQGEIVVIIADQYGNQISSFSPDSLSTLSITGDGLDSSNLKITLEANSQSVSVQGIRFTPGPPGPKDLCFTWREFSDFLRVQLVSGPPTKLLLMDWPELKESIPVINGRQLENPLIVQLCDQWDNPALVPNVKICLIKASSLRLLPSNQQHKTDDKGRANLGVFTVCAPRGEHTVQVKGVYNKSTIEGPTIKLTILPDPEKPIRLNVKYDQDASFIAGDIFTDFMVSVISESGSVIKNINPTRISMKMWKLSSGMSRPPANAETFSCNKIKGNDKEDGCFYFREKTIPNKVGAYCIQFDFMIDKTNILSSQQVIVDVLPNQPMKLVPDSQPATPAVSNVRSIASRTLVKDLRLSITDNYGNHTGMDLVGTVVATIKGFNEEDTDTPLFIGKVRTLEFPFVKGSAEITTLVLAENSPGRDSTEYFIIFEPRLSTVSGTLESYSLPFMFYNDVKKQQQMAALTKEKDELSKSITMYRSLFDANKQLVDEMKCQAEEAKLKETQLRNELKAYNIDIPATQQTTHIEALLEKKITEQNELKKRPRRLCTLPNYTKRSGDILGKIAHLAQIEDDRAAMVISWHLASDMDCVVTLTTDAARAIYDETQGRQQVLPLDSIYRKTLPDWKRPLPHFRNGKLHFKPFGNPVFARDLLTFPDNIEHCETVFGMLLGDTIILDNLDAANHYRKEVVKITHCPTLLTRDGDRIRSNGKFGGLQNKAPPMDKLRGMVFGAPVPKQCVVLGKQIDLIQQYRTALYRLSSVNEDLDNQLQYLHTPDMKKKKQELDEQEKSLKRIEQKLGMTPVRRCNESLCHSPKIEVTECPIPTKRMRRESTRQNRRPKGDVPN
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
2Acetylation------MAAEGASDP
------CCCCCCCCC		26.06-
7Phosphorylation-MAAEGASDPAGLSE
-CCCCCCCCCCCCCC		55.7928066266
13PhosphorylationASDPAGLSEGSGRDG
CCCCCCCCCCCCCCC		38.7124759943
16PhosphorylationPAGLSEGSGRDGAVD
CCCCCCCCCCCCCCC		26.9724759943
63PhosphorylationFRASVCQTIGISSEE
CEEHHHHHCCCCCCC		18.9529514104
67PhosphorylationVCQTIGISSEEKFVI
HHHHCCCCCCCEEEE		26.8729514104
68PhosphorylationCQTIGISSEEKFVIT
HHHCCCCCCCEEEEE		48.1029514104
403PhosphorylationQDDMQTLYINTASDS
CCCCCEEEEECCCCC		8.7720139300
408PhosphorylationTLYINTASDSFEFKA
EEEEECCCCCEEEEE		31.5820139300
410PhosphorylationYINTASDSFEFKAHV
EEECCCCCEEEEEEE		24.9520139300
483PhosphorylationWNGRLIPYTSVGDFD
ECCEEEECCCCCCCC		12.4926745281
484PhosphorylationNGRLIPYTSVGDFDW
CCEEEECCCCCCCCC		16.1626745281
485PhosphorylationGRLIPYTSVGDFDWC
CEEEECCCCCCCCCC		20.4726745281
527PhosphorylationQVSTNKLTFMDLELK
EEECCCEEEEEEEEE		20.65-
619UbiquitinationGQLVKTIKTLPLCYG
HHHHHHHHHHCCCCC		49.6022790023
754PhosphorylationELKVILHTSSGNKEI
EEEEEEECCCCCHHH		22.5728285833
755PhosphorylationLKVILHTSSGNKEII
EEEEEECCCCCHHHH		26.0425338131
756PhosphorylationKVILHTSSGNKEIIS
EEEEECCCCCHHHHH		47.7627841257
784SumoylationKKMENIQKLGNYTLK
HHCHHHHHHCCEEEE		55.3428289178
833PhosphorylationFSFGLLDSPFRVGVP
EEEEECCCCCEECCC		26.3826643407
981PhosphorylationGAPNLPVYTVDCSSS
CCCCCCEEEEECCCC		10.1026643407
982PhosphorylationAPNLPVYTVDCSSSG
CCCCCEEEEECCCCC		15.3126643407
986PhosphorylationPVYTVDCSSSGTSIL
CEEEEECCCCCCEEC		24.0726643407
987PhosphorylationVYTVDCSSSGTSILT
EEEEECCCCCCEECC		38.8326643407
988PhosphorylationYTVDCSSSGTSILTG
EEEECCCCCCEECCC		29.7826643407
990PhosphorylationVDCSSSGTSILTGSP
EECCCCCCEECCCCC		17.9726643407
991PhosphorylationDCSSSGTSILTGSPI
ECCCCCCEECCCCCE		21.0826643407
994PhosphorylationSSGTSILTGSPIQVQ
CCCCEECCCCCEEEE		33.6626643407
996PhosphorylationGTSILTGSPIQVQNI
CCEECCCCCEEEEEE		17.3726643407
1049AcetylationIFSVEEQKAIQIKHQ
EEECCHHCCEEEECC		51.2222826441
1085PhosphorylationGEREINITPSLAEKI
CCCEEECCHHHHHHC		11.4430482847
1256PhosphorylationQLVSGPPTKLLLMDW
EECCCCCCEEEEECC		37.1424759943
1350AcetylationQVKGVYNKSTIEGPT
EEEEEEECCCEECCE		31.15-
1420PhosphorylationMKMWKLSSGMSRPPA
EEEEECCCCCCCCCC		49.2924719451
1500PhosphorylationVPDSQPATPAVSNVR
CCCCCCCCCCHHHHH		20.6125338131
1521PhosphorylationLVKDLRLSITDNYGN
HHCEEEEEEECCCCC		19.6025777480
1523PhosphorylationKDLRLSITDNYGNHT
CEEEEEEECCCCCCC		18.1525777480
1526PhosphorylationRLSITDNYGNHTGMD
EEEEECCCCCCCCCC		23.3225777480
1530PhosphorylationTDNYGNHTGMDLVGT
ECCCCCCCCCCCCEE		37.9025777480
1537PhosphorylationTGMDLVGTVVATIKG
CCCCCCEEEEEEECC		12.3425777480
1541PhosphorylationLVGTVVATIKGFNEE
CCEEEEEEECCCCCC		16.1825777480
1635PhosphorylationTKEKDELSKSITMYR
HHCHHHHHHHHHHHH		23.4723737553
1637PhosphorylationEKDELSKSITMYRSL
CHHHHHHHHHHHHHH		21.6624719451
1639PhosphorylationDELSKSITMYRSLFD
HHHHHHHHHHHHHHH		18.4224719451
1641PhosphorylationLSKSITMYRSLFDAN
HHHHHHHHHHHHHHC		6.6023737553
1665AcetylationQAEEAKLKETQLRNE
HHHHHHHHHHHHHHH		58.9922902405
1765PhosphorylationTDAARAIYDETQGRQ
HHHHHHHHHCCCCCC		13.52-
1803AcetylationRNGKLHFKPFGNPVF
CCCEEEEEECCCCEE		28.7923806337
1803SuccinylationRNGKLHFKPFGNPVF
CCCEEEEEECCCCEE		28.7923806337
1803SuccinylationRNGKLHFKPFGNPVF
CCCEEEEEECCCCEE		28.79-
1886AcetylationNKAPPMDKLRGMVFG
CCCCCHHHHCCHHHC		33.567617913
1921PhosphorylationRTALYRLSSVNEDLD
HHHHHHHHCCCCCHH		24.2025777480
1922PhosphorylationTALYRLSSVNEDLDN
HHHHHHHCCCCCHHH		33.2926745281
1933PhosphorylationDLDNQLQYLHTPDMK
CHHHHHHHHCCHHHH		14.7225777480
1936PhosphorylationNQLQYLHTPDMKKKK
HHHHHHCCHHHHHHH		20.5625266776
1943UbiquitinationTPDMKKKKQELDEQE
CHHHHHHHHHHHHHH		58.8622790023
1971PhosphorylationPVRRCNESLCHSPKI
CCHHCCHHHCCCCCC		23.4725159016
1975PhosphorylationCNESLCHSPKIEVTE
CCHHHCCCCCCEEEE		27.2222942356
1977SumoylationESLCHSPKIEVTECP
HHHCCCCCCEEEECC		55.2928289178
1981PhosphorylationHSPKIEVTECPIPTK
CCCCCEEEECCCCCH		21.0525159016
1988AcetylationTECPIPTKRMRREST
EECCCCCHHHCHHHH		38.557614305
1994PhosphorylationTKRMRRESTRQNRRP
CHHHCHHHHHCCCCC		27.38-
1995PhosphorylationKRMRRESTRQNRRPK
HHHCHHHHHCCCCCC		31.3628576409
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 SMHD1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMHD1_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 SMHD1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NRDC_HUMANNRD1physical
26496610
MP2K7_HUMANMAP2K7physical
26496610
SET1A_HUMANSETD1Aphysical
26496610
RM19_HUMANMRPL19physical
26496610
SRRM1_HUMANSRRM1physical
26496610
FBX5_HUMANFBXO5physical
26496610
HSPB8_HUMANHSPB8physical
26496610
RM18_HUMANMRPL18physical
26496610
ZN219_HUMANZNF219physical
26496610
MID51_HUMANMIEF1physical
26496610
DDX60_HUMANDDX60physical
26496610
ACSA_HUMANACSS2physical
26496610
ERGI1_HUMANERGIC1physical
26496610
ELMO3_HUMANELMO3physical
26496610
GLYR1_HUMANGLYR1physical
26496610
TYW3_HUMANTYW3physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMHD1_MOUSE

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Related Literatures of Post-Translational Modification

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