SAMH1_MOUSE - dbPTM
SAMH1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAMH1_MOUSE
UniProt AC Q60710
Protein Name Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
Gene Name Samhd1
Organism Mus musculus (Mouse).
Sequence Length 627
Subcellular Localization Nucleus .
Protein Description Host restriction nuclease involved in defense response to virus. Has dNTPase activity and reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur. Blocks early-stage virus replication in dendritic and other myeloid cells. Likewise, suppresses LINE-1 retrotransposon activity. May play a role in mediating proinflammatory responses to TNF-alpha signaling. Has ribonuclease activity, acting on single-stranded RNA..
Protein Sequence MQSAPLEQPAKRPRCDGSPRTPPSTPPATANLSADDDFQNTDLRTWEPEDVCSFLENRGFREKKVLDIFRDNKIAGSFLPFLDEDRLEDLGVSSLEERKKMIECIQQLSQSRIDLMKVFNDPIHGHIEFHPLLIRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVRALAEKQPELQISERDILCVQIAGLCHDLGHGPFSHMFDGRFIPRARPEKKWKHEQGSIEMFEHLVNSNELKLVMKNYGLVPEEDITFIKEQIMGPPITPVKDSLWPYKGRPATKSFLYEIVSNKRNGIDVDKWDYFARDCHHLGIQNNFDYKRFIKFARICEVEYKVKEDKTYIRKVKHICSREKEVGNLYDMFHTRNCLHRRAYQHKISNLIDIMITDAFLKADPYVEITGTAGKKFRISTAIDDMEAFTKLTDNIFLEVLHSTDPQLSEAQSILRNIECRNLYKYLGETQPKREKIRKEEYERLPQEVAKAKPEKAPDVELKAEDFIVDVINVDYGMEDKNPIDRVHFYCKSNSKQAVRINKEQVSQLLPEKFAEQLIRVYCKKKDGKSLDAAGKHFVQWCALRDFTKPQDGDIIAPLITPLKWNNKTSSCLQEVSKVKTCLKF
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
1Acetylation-------MQSAPLEQ
-------CCCCCCCC		6.83-
3Phosphorylation-----MQSAPLEQPA
-----CCCCCCCCCC		30.4729472430
11UbiquitinationAPLEQPAKRPRCDGS
CCCCCCCCCCCCCCC		70.40-
18PhosphorylationKRPRCDGSPRTPPST
CCCCCCCCCCCCCCC		9.6525521595
21PhosphorylationRCDGSPRTPPSTPPA
CCCCCCCCCCCCCCC		42.8227087446
24PhosphorylationGSPRTPPSTPPATAN
CCCCCCCCCCCCCCC		55.5427087446
25PhosphorylationSPRTPPSTPPATANL
CCCCCCCCCCCCCCC		38.7827087446
29PhosphorylationPPSTPPATANLSADD
CCCCCCCCCCCCCCC		23.1127742792
33PhosphorylationPPATANLSADDDFQN
CCCCCCCCCCCCCCC		29.4727742792
41PhosphorylationADDDFQNTDLRTWEP
CCCCCCCCCCCCCCH		26.1525619855
42UbiquitinationDDDFQNTDLRTWEPE
CCCCCCCCCCCCCHH		41.5222790023
49PhosphorylationDLRTWEPEDVCSFLE
CCCCCCHHHHHHHHH		52.1124719451
52PhosphorylationTWEPEDVCSFLENRG
CCCHHHHHHHHHHCC		3.5424719451
55PhosphorylationPEDVCSFLENRGFRE
HHHHHHHHHHCCCCC		3.0724719451
56PhosphorylationEDVCSFLENRGFREK
HHHHHHHHHCCCCCH		42.7624719451
64PhosphorylationNRGFREKKVLDIFRD
HCCCCCHHHHHHHCC		43.19-
64UbiquitinationNRGFREKKVLDIFRD
HCCCCCHHHHHHHCC		43.19-
94PhosphorylationLEDLGVSSLEERKKM
HHHCCCCCHHHHHHH		37.08-
95UbiquitinationEDLGVSSLEERKKMI
HHCCCCCHHHHHHHH		6.5422790023
104S-palmitoylationERKKMIECIQQLSQS
HHHHHHHHHHHHHHH		2.0528526873
125PhosphorylationVFNDPIHGHIEFHPL
HHCCCCCCCCCCCCE		24.96-
256AcetylationNELKLVMKNYGLVPE
HHHHHHHHHCCCCCH		39.276566001
270UbiquitinationEEDITFIKEQIMGPP
HHHCHHHHHHHCCCC		39.10-
274OxidationTFIKEQIMGPPITPV
HHHHHHHCCCCCCCC		7.0517242355
279PhosphorylationQIMGPPITPVKDSLW
HHCCCCCCCCCCCCC		28.0125521595
282UbiquitinationGPPITPVKDSLWPYK
CCCCCCCCCCCCCCC		42.68-
284PhosphorylationPITPVKDSLWPYKGR
CCCCCCCCCCCCCCC		26.9826239621
288PhosphorylationVKDSLWPYKGRPATK
CCCCCCCCCCCCCCH		17.9428833060
305UbiquitinationLYEIVSNKRNGIDVD
HHHHHCCCCCCCCHH		39.47-
310PhosphorylationSNKRNGIDVDKWDYF
CCCCCCCCHHHHHHH		43.9224719451
313UbiquitinationRNGIDVDKWDYFARD
CCCCCHHHHHHHHHH		41.6422790023
313UbiquitinationRNGIDVDKWDYFARD
CCCCCHHHHHHHHHH		41.6427667366
316PhosphorylationIDVDKWDYFARDCHH
CCHHHHHHHHHHHHH		9.68-
333AcetylationIQNNFDYKRFIKFAR
CCCCCCHHHHHHHHE		42.5591205
336UbiquitinationNFDYKRFIKFARICE
CCCHHHHHHHHEEEE		4.1022790023
347MalonylationRICEVEYKVKEDKTY
EEEEEEEEECCCHHH		33.0726320211
347UbiquitinationRICEVEYKVKEDKTY
EEEEEEEEECCCHHH		33.07-
352MalonylationEYKVKEDKTYIRKVK
EEEECCCHHHHHHHH		44.3026320211
352UbiquitinationEYKVKEDKTYIRKVK
EEEECCCHHHHHHHH		44.30-
372PhosphorylationEKEVGNLYDMFHTRN
CCCHHCHHHHHHHHC		14.90-
378UbiquitinationLYDMFHTRNCLHRRA
HHHHHHHHCCHHHHH		24.2422790023
408PhosphorylationAFLKADPYVEITGTA
HHHHCCCCEEEEECC		15.9730635358
412PhosphorylationADPYVEITGTAGKKF
CCCCEEEEECCCCCE		18.2530635358
467AcetylationIECRNLYKYLGETQP
HHHHHHHHHHCCCCC		36.8523954790
467UbiquitinationIECRNLYKYLGETQP
HHHHHHHHHHCCCCC		36.85-
495UbiquitinationPQEVAKAKPEKAPDV
HHHHHHCCCCCCCCC		53.67-
498UbiquitinationVAKAKPEKAPDVELK
HHHCCCCCCCCCEEC		73.9822790023
526UbiquitinationGMEDKNPIDRVHFYC
CCCCCCCCCEEEEEE		8.0522790023
549PhosphorylationRINKEQVSQLLPEKF
ECCHHHHHHHCCHHH		18.1427180971
555AcetylationVSQLLPEKFAEQLIR
HHHHCCHHHHHHHHH		48.1923954790
590PhosphorylationWCALRDFTKPQDGDI
HHHHCCCCCCCCCCC		46.2125619855
603PhosphorylationDIIAPLITPLKWNNK
CCEECEECCCCCCCC		30.1925521595
620AcetylationSCLQEVSKVKTCLKF
HHHHHHHCHHHHHCC		53.5823806337
620MalonylationSCLQEVSKVKTCLKF
HHHHHHHCHHHHHCC		53.5826320211
634PhosphorylationF--------------
C--------------		24719451
651Acetylation-------------------------------
-------------------------------		-
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 SAMH1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
634TPhosphorylation

17242355
634TPhosphorylation

17242355
634TPhosphorylation

17242355
634TPhosphorylation

17242355
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 SAMH1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNA2_HUMANCCNA2physical
24623419
CCNB1_HUMANCCNB1physical
24623419
CDK1_HUMANCDK1physical
24623419
CDK2_HUMANCDK2physical
24623419
CD97_HUMANCD97physical
26496610
RT27_HUMANMRPS27physical
26496610
CHTOP_HUMANCHTOPphysical
26496610
RM04_HUMANMRPL4physical
26496610
K1522_HUMANKIAA1522physical
26496610
NOL9_HUMANNOL9physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SAMH1_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-18; THR-21; SER-24;THR-25 AND THR-29, AND MASS SPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, AND MASSSPECTROMETRY.

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