dbPTM

SAMH1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SAMH1_HUMAN
UniProt AC	Q9Y3Z3
Protein Name	Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
Gene Name	SAMHD1
Organism	Homo sapiens (Human).
Sequence Length	626
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. [PubMed: 18546154]
Protein Sequence	MQRADSEQPSKRPRCDDSPRTPSNTPSAEADWSPGLELHPDYKTWGPEQVCSFLRRGGFEEPVLLKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRLVQIHVDTMKVINDPIHGHIELHPLLVRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVHALGEKQPELQISERDVLCVQIAGLCHDLGHGPFSHMFDGRFIPLARPEVKWTHEQGSVMMFEHLINSNGIKPVMEQYGLIPEEDICFIKEQIVGPLESPVEDSLWPYKGRPENKSFLYEIVSNKRNGIDVDKWDYFARDCHHLGIQNNFDYKRFIKFARVCEVDNELRICARDKEVGNLYDMFHTRNSLHRRAYQHKVGNIIDTMITDAFLKADDYIEITGAGGKKYRISTAIDDMEAYTKLTDNIFLEILYSTDPKLKDAREILKQIEYRNLFKYVGETQPTGQIKIKREDYESLPKEVASAKPKVLLDVKLKAEDFIVDVINMDYGMQEKNPIDHVSFYCKTAPNRAIRITKNQVSQLLPEKFAEQLIRVYCKKVDRKSLYAARQYFVQWCADRNFTKPQDGDVIAPLITPQKKEWNDSTSVQNPTRLREASKSRVQLFKDDPM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MQRADSEQ -------CCCCCCCC	5.70	19413330
6	Phosphorylation	--MQRADSEQPSKRP --CCCCCCCCCCCCC	36.83	28450419
10	Phosphorylation	RADSEQPSKRPRCDD CCCCCCCCCCCCCCC	40.78	30242111
11	Ubiquitination	ADSEQPSKRPRCDDS CCCCCCCCCCCCCCC	73.44	-
18	Phosphorylation	KRPRCDDSPRTPSNT CCCCCCCCCCCCCCC	11.75	23401153
21	Phosphorylation	RCDDSPRTPSNTPSA CCCCCCCCCCCCCCC	34.16	23401153
23	Phosphorylation	DDSPRTPSNTPSAEA CCCCCCCCCCCCCCC	53.36	23401153
25	Phosphorylation	SPRTPSNTPSAEADW CCCCCCCCCCCCCCC	23.98	23927012
27	Phosphorylation	RTPSNTPSAEADWSP CCCCCCCCCCCCCCC	36.38	23927012
33	Phosphorylation	PSAEADWSPGLELHP CCCCCCCCCCCEECC	15.05	23927012
42	Phosphorylation	GLELHPDYKTWGPEQ CCEECCCCCCCCHHH	18.12	23927012
66 (in isoform 2)	Ubiquitination	-	46.28	-
66	Ubiquitination	FEEPVLLKNIRENEI CCCCEECCCCCCCCC	46.28	21890473
66 (in isoform 1)	Ubiquitination	-	46.28	21890473
74	O-linked_Glycosylation	NIRENEITGALLPCL CCCCCCCCCCHHHCC	15.38	23301498
84	O-linked_Glycosylation	LLPCLDESRFENLGV HHHCCCHHHHHHCCC	41.77	23301498
92	Phosphorylation	RFENLGVSSLGERKK HHHHCCCCCHHHHHH	20.32	23186163
93	Phosphorylation	FENLGVSSLGERKKL HHHCCCCCHHHHHHH	37.68	23403867
98	Ubiquitination	VSSLGERKKLLSYIQ CCCHHHHHHHHHHHH	43.39	-
99	Ubiquitination	SSLGERKKLLSYIQR CCHHHHHHHHHHHHH	61.96	21890473
99 (in isoform 1)	Ubiquitination	-	61.96	21890473
102	Phosphorylation	GERKKLLSYIQRLVQ HHHHHHHHHHHHHHH	30.53	28450419
103	Phosphorylation	ERKKLLSYIQRLVQI HHHHHHHHHHHHHHH	10.88	20068231
138	Phosphorylation	LLVRIIDTPQFQRLR HHEEECCCHHHHHHH	14.47	28450419
146	Phosphorylation	PQFQRLRYIKQLGGG HHHHHHHHHHHHCCC	19.64	21712546
148 (in isoform 1)	Ubiquitination	-	30.45	21890473
148	Ubiquitination	FQRLRYIKQLGGGYY HHHHHHHHHHCCCEE	30.45	21890473
155	Phosphorylation	KQLGGGYYVFPGASH HHHCCCEEECCCCCC	10.01	21712546
278	Phosphorylation	QIVGPLESPVEDSLW EEECCCCCCCCCCCC	41.76	23403867
280 (in isoform 2)	Ubiquitination	-	20.80	-
283	Phosphorylation	LESPVEDSLWPYKGR CCCCCCCCCCCCCCC	20.87	23403867
287	Phosphorylation	VEDSLWPYKGRPENK CCCCCCCCCCCCCCC	17.94	23403867
288	Ubiquitination	EDSLWPYKGRPENKS CCCCCCCCCCCCCCC	44.35	-
294	Acetylation	YKGRPENKSFLYEIV CCCCCCCCCHHHHHH	40.71	7234285
294 (in isoform 1)	Ubiquitination	-	40.71	21890473
294	Ubiquitination	YKGRPENKSFLYEIV CCCCCCCCCHHHHHH	40.71	21890473
295	Phosphorylation	KGRPENKSFLYEIVS CCCCCCCCHHHHHHC	31.87	24247654
304 (in isoform 1)	Ubiquitination	-	39.47	21890473
304	Ubiquitination	LYEIVSNKRNGIDVD HHHHHCCCCCCCCHH	39.47	21890473
312 (in isoform 1)	Ubiquitination	-	41.64	21890473
312	Ubiquitination	RNGIDVDKWDYFARD CCCCCHHHHHHHHHH	41.64	21890473
315	Phosphorylation	IDVDKWDYFARDCHH CCHHHHHHHHHHHHH	9.68	-
332	2-Hydroxyisobutyrylation	IQNNFDYKRFIKFAR CCCCCCHHHHHHHHH	42.55	-
332	Sumoylation	IQNNFDYKRFIKFAR CCCCCCHHHHHHHHH	42.55	-
384	Phosphorylation	KVGNIIDTMITDAFL HHHHHHHHHHHHHHH	10.48	20068231
387	Phosphorylation	NIIDTMITDAFLKAD HHHHHHHHHHHHHCC	15.51	20068231
405	Ubiquitination	EITGAGGKKYRISTA EEECCCCCEEEEEEE	45.79	-
405	2-Hydroxyisobutyrylation	EITGAGGKKYRISTA EEECCCCCEEEEEEE	45.79	-
407	Phosphorylation	TGAGGKKYRISTAID ECCCCCEEEEEEEEH	19.37	30576142
419	Phosphorylation	AIDDMEAYTKLTDNI EEHHHHHHHHHCCCC	7.36	21060948
420	Phosphorylation	IDDMEAYTKLTDNIF EHHHHHHHHHCCCCH	26.99	30576142
432	Phosphorylation	NIFLEILYSTDPKLK CCHHHHHHCCCHHHH	18.39	26503514
433	Phosphorylation	IFLEILYSTDPKLKD CHHHHHHCCCHHHHH	23.92	26503514
434	Phosphorylation	FLEILYSTDPKLKDA HHHHHHCCCHHHHHH	42.64	26503514
446	Ubiquitination	KDAREILKQIEYRNL HHHHHHHHHHHHHHH	55.69	21890473
446 (in isoform 1)	Ubiquitination	-	55.69	21890473
455 (in isoform 1)	Ubiquitination	-	42.04	21890473
455	Ubiquitination	IEYRNLFKYVGETQP HHHHHHHHHCCCCCC	42.04	21890473
467	Ubiquitination	TQPTGQIKIKREDYE CCCCCEEEEEHHHHH	34.00	21890473
467	Sumoylation	TQPTGQIKIKREDYE CCCCCEEEEEHHHHH	34.00	28112733
467 (in isoform 1)	Ubiquitination	-	34.00	21890473
469	Sumoylation	PTGQIKIKREDYESL CCCEEEEEHHHHHHC	44.74	28112733
469	Sumoylation	PTGQIKIKREDYESL CCCEEEEEHHHHHHC	44.74	-
478	Ubiquitination	EDYESLPKEVASAKP HHHHHCCHHHHCCCC	70.84	-
482	Phosphorylation	SLPKEVASAKPKVLL HCCHHHHCCCCEEEE	41.84	-
486 (in isoform 1)	Ubiquitination	-	44.82	21890473
486	Ubiquitination	EVASAKPKVLLDVKL HHHCCCCEEEEEEEE	44.82	21890473
492	Sumoylation	PKVLLDVKLKAEDFI CEEEEEEEECHHHEE	43.89	28112733
507	Phosphorylation	VDVINMDYGMQEKNP EEEECCCCCCCCCCC	12.06	-
519	Phosphorylation	KNPIDHVSFYCKTAP CCCCCEEEEEECCCC	13.69	23401153
521	Phosphorylation	PIDHVSFYCKTAPNR CCCEEEEEECCCCCC	5.87	27080861
534	Ubiquitination	NRAIRITKNQVSQLL CCEEEEEHHHHHHHC	42.91	-
544	Ubiquitination	VSQLLPEKFAEQLIR HHHHCCHHHHHHHHH	48.19	21890473
544 (in isoform 1)	Ubiquitination	-	48.19	21890473
553	Phosphorylation	AEQLIRVYCKKVDRK HHHHHHHHHHHCCHH	6.68	-
560	Ubiquitination	YCKKVDRKSLYAARQ HHHHCCHHHHHHHHH	40.11	-
563	Phosphorylation	KVDRKSLYAARQYFV HCCHHHHHHHHHHHH	12.81	25367160
579	Phosphorylation	WCADRNFTKPQDGDV HHHCCCCCCCCCCCE	45.42	-
592	Phosphorylation	DVIAPLITPQKKEWN CEEEEEECCCCCCCC	27.61	19664994
595	Sumoylation	APLITPQKKEWNDST EEEECCCCCCCCCCC	54.59	-
596	Ubiquitination	PLITPQKKEWNDSTS EEECCCCCCCCCCCC	63.82	-
601	O-linked_Glycosylation	QKKEWNDSTSVQNPT CCCCCCCCCCCCCHH	21.26	23301498
601	Phosphorylation	QKKEWNDSTSVQNPT CCCCCCCCCCCCCHH	21.26	28450419
602	Phosphorylation	KKEWNDSTSVQNPTR CCCCCCCCCCCCHHH	35.46	28857561
603	Phosphorylation	KEWNDSTSVQNPTRL CCCCCCCCCCCHHHH	26.17	28450419
608	Phosphorylation	STSVQNPTRLREASK CCCCCCHHHHHHHHH	50.30	28450419
616	Phosphorylation	RLREASKSRVQLFKD HHHHHHHHHCHHCCC	34.88	23186163
622	Sumoylation	KSRVQLFKDDPM--- HHHCHHCCCCCC---	70.57	-
622	Sumoylation	KSRVQLFKDDPM--- HHHCHHCCCCCC---	70.57	28112733

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
278	S	Phosphorylation	Kinase	UL97	P16788	PSP
592	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
592	T	Phosphorylation	Kinase	CDK2	P24941	PSP
592	T	Phosphorylation	Kinase	UL97	P16788	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	DCAF1	Q9Y4B6	PMID:23677995

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
592	T	Phosphorylation	17081983
(Microbial infection) Phosphorylation at Thr-592 by Epstein-Barr virus kinase BGLF4 and human cytomegalovirus/HCMV UL97 leads to a reduced level of dCTPase and dTTPase activity and the loss of viral restriction.
592	T	Phosphorylation	17081983
In contrast, phosphorylation at Thr-592 promotes DNA end resection at stalled replication forks in response to DNA damage.
592	T	Phosphorylation	17081983
Phosphorylation at Thr-592 by CDK1 acts as a switch to control deoxynucleoside triphosphate (dNTPase)-dependent and -independent functions.
592	T	Phosphorylation	17081983
Phosphorylation at Thr-592 takes place in cycling cells: it reduces the stability of the homotetramer, impairing the dNTPase activity and subsequent ability to restrict infection by viruses.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DCAF1_HUMAN	VPRBP	physical	22362772
DDB1_HUMAN	DDB1	physical	22362772
VPX_SIVG1	vpx	physical	22362772
A4_HUMAN	APP	physical	21832049
VPX_SIVG1	vpx	physical	23874389
IMB1_HUMAN	KPNB1	physical	23874389
IF4B_HUMAN	EIF4B	physical	22863883
GANAB_HUMAN	GANAB	physical	22863883
PUR2_HUMAN	GART	physical	22863883
HS105_HUMAN	HSPH1	physical	22863883
PLAK_HUMAN	JUP	physical	22863883
PLOD2_HUMAN	PLOD2	physical	22863883
ANM3_HUMAN	PRMT3	physical	22863883
RANB3_HUMAN	RANBP3	physical	22863883
RL24_HUMAN	RPL24	physical	22863883
SF01_HUMAN	SF1	physical	22863883
SPT5H_HUMAN	SUPT5H	physical	22863883
TRM1_HUMAN	TRMT1	physical	22863883
XPO7_HUMAN	XPO7	physical	22863883
CCNA2_HUMAN	CCNA2	physical	24623419
CDK2_HUMAN	CDK2	physical	24623419
SKP2_HUMAN	SKP2	physical	24623419
CDK1_HUMAN	CDK1	physical	24623419
FA13B_HUMAN	FAM13B	physical	25423367
SAMH1_HUMAN	SAMHD1	physical	25423367
EF1A1_HUMAN	EEF1A1	physical	25423367
ACTB_HUMAN	ACTB	physical	25423367
RBX1_HUMAN	RBX1	physical	25423367
CUL4A_HUMAN	CUL4A	physical	25423367
CCNL2_HUMAN	CCNL2	physical	25532805
2AAA_HUMAN	PPP2R1A	physical	26496610
2A5E_HUMAN	PPP2R5E	physical	26496610
SMRD2_HUMAN	SMARCD2	physical	26496610
STX3_HUMAN	STX3	physical	26496610
SF01_HUMAN	SF1	physical	26496610
AKA12_HUMAN	AKAP12	physical	26496610
MTCL1_HUMAN	MTCL1	physical	26496610
RGAP1_HUMAN	RACGAP1	physical	26496610
KANL3_HUMAN	KANSL3	physical	26496610
ZMAT3_HUMAN	ZMAT3	physical	26496610
SOGA1_HUMAN	SOGA1	physical	26496610
RSBNL_HUMAN	RSBN1L	physical	26496610
GSK3A_HUMAN	GSK3A	physical	28514442
GSK3B_HUMAN	GSK3B	physical	28514442
CDK2_HUMAN	CDK2	physical	28514442
NAA10_HUMAN	NAA10	physical	28514442
IMA1_HUMAN	KPNA2	physical	24712655
VPX_HV2BE	HIV2gp3	physical	24712655
VPX_SIVG1	vpx	physical	24712655

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612952	Aicardi-Goutieres syndrome 5 (AGS5)
614415	Chilblain lupus 2 (CHBL2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SAMH1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-592, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND THR-592, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-592, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-592, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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 THR-592, AND MASSSPECTROMETRY.	18691976 [Abstract]
"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 THR-592, AND MASSSPECTROMETRY.	17081983 [Abstract]

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