CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023799
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 
Protein Synonyms/Alias
 dNTPase; Dendritic cell-derived IFNG-induced protein; DCIP; Monocyte protein 5; MOP-5; SAM domain and HD domain-containing protein 1 
Gene Name
 SAMHD1 
Gene Synonyms/Alias
 MOP5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
66FEEPVLLKNIRENEIubiquitination[1, 2, 3, 4, 5, 6, 7]
99SSLGERKKLLSYIQRubiquitination[1, 5, 7]
148FQRLRYIKQLGGGYYubiquitination[1, 7]
294YKGRPENKSFLYEIVubiquitination[1, 7]
304LYEIVSNKRNGIDVDubiquitination[1, 7]
312RNGIDVDKWDYFARDubiquitination[1, 7]
446KDAREILKQIEYRNLubiquitination[1, 2, 5, 7]
455IEYRNLFKYVGETQPubiquitination[1, 7]
467TQPTGQIKIKREDYEubiquitination[1, 7]
486EVASAKPKVLLDVKLubiquitination[1, 7]
544VSQLLPEKFAEQLIRubiquitination[1, 7]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Host restriction nuclease that blocks early-stage virus replication in dendritic and other myeloid cells. May function by reducing the cellular dNTP levels to levels too low for retroviral reverse transcription to occur. May play a role in mediating proinflammatory responses to TNF-alpha signaling. 
Sequence Annotation
 DOMAIN 45 110 SAM.
 DOMAIN 164 319 HD.
 NP_BIND 137 145 dGTP.
 ACT_SITE 233 233 Probable.
 METAL 167 167 Zinc.
 METAL 206 206 Zinc.
 METAL 207 207 Zinc.
 METAL 311 311 Zinc.
 BINDING 164 164 Substrate.
 BINDING 210 210 Substrate.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 18 18 Phosphoserine (By similarity).
 MOD_RES 21 21 Phosphothreonine (By similarity).
 MOD_RES 25 25 Phosphothreonine (By similarity).
 MOD_RES 592 592 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; Aicardi-Goutieres syndrome; Alternative splicing; Antiviral defense; Complete proteome; Direct protein sequencing; Disease mutation; Hydrolase; Immunity; Innate immunity; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 626 AA 
Protein Sequence
MQRADSEQPS KRPRCDDSPR TPSNTPSAEA DWSPGLELHP DYKTWGPEQV CSFLRRGGFE 60
EPVLLKNIRE NEITGALLPC LDESRFENLG VSSLGERKKL LSYIQRLVQI HVDTMKVIND 120
PIHGHIELHP LLVRIIDTPQ FQRLRYIKQL GGGYYVFPGA SHNRFEHSLG VGYLAGCLVH 180
ALGEKQPELQ ISERDVLCVQ IAGLCHDLGH GPFSHMFDGR FIPLARPEVK WTHEQGSVMM 240
FEHLINSNGI KPVMEQYGLI PEEDICFIKE QIVGPLESPV EDSLWPYKGR PENKSFLYEI 300
VSNKRNGIDV DKWDYFARDC HHLGIQNNFD YKRFIKFARV CEVDNELRIC ARDKEVGNLY 360
DMFHTRNSLH RRAYQHKVGN IIDTMITDAF LKADDYIEIT GAGGKKYRIS TAIDDMEAYT 420
KLTDNIFLEI LYSTDPKLKD AREILKQIEY RNLFKYVGET QPTGQIKIKR EDYESLPKEV 480
ASAKPKVLLD VKLKAEDFIV DVINMDYGMQ EKNPIDHVSF YCKTAPNRAI RITKNQVSQL 540
LPEKFAEQLI RVYCKKVDRK SLYAARQYFV QWCADRNFTK PQDGDVIAPL ITPQKKEWND 600
STSVQNPTRL REASKSRVQL FKDDPM 626 
Gene Ontology
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0051607; P:defense response to virus; IMP:UniProtKB.
 GO:0006955; P:immune response; NAS:UniProtKB.
 GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
 GO:0008152; P:metabolic process; IEA:GOC.
 GO:0045088; P:regulation of innate immune response; IMP:UniProtKB. 
Interpro
 IPR003607; HD/PDEase_dom.
 IPR006674; HD_domain.
 IPR001660; SAM.
 IPR013761; SAM/pointed.
 IPR011510; SAM_2. 
Pfam
 PF01966; HD
 PF07647; SAM_2 
SMART
 SM00471; HDc
 SM00454; SAM 
PROSITE
 PS50105; SAM_DOMAIN 
PRINTS