Q9Y3Z3 (SAMH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SAM domain and HD domain-containing protein 1
EC=3.1.4.-

Alternative name(s):
Dendritic cell-derived IFNG-induced protein
Short name=DCIP
Monocyte protein 5
Short name=MOP-5

Gene names

Name:	SAMHD1
Synonyms:	MOP5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Putative nuclease involved in innate immune response by acting as a negative regulator of the cell-intrinsic antiviral response. May play a role in mediating proinflammatory responses to TNF-alpha signaling. Ref.12 Ref.18
Subcellular location	Nucleus Ref.18.
Tissue specificity	Expressed in heart, skeletal muscle, spleen, liver, small intestine, placenta, lung and peripheral blood leukocytes. No expression is seen in brain and thymus. Ref.1
Induction	By IFNG/IFN-gamma. Up-regulated in TNF treated lung fibroblasts. Ref.1 Ref.12
Involvement in disease	Aicardi-Goutieres syndrome 5 (AGS5) [MIM:612952]: A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.18 Chilblain lupus 2 (CHBL2) [MIM:614415]: A rare cutaneous form of lupus erythematosus. Affected individuals present with painful bluish-red papular or nodular lesions of the skin in acral locations precipitated by cold and wet exposure at temperatures less than 10 degrees centigrade. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19
Sequence similarities	Belongs to the SAMHD1 family. Contains 1 HD domain. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Biological process	Immunity Innate immunity
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Aicardi-Goutieres syndrome Disease mutation
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	defense response to virus Inferred from mutant phenotype Ref.18. Source: UniProtKB immune response Non-traceable author statement Ref.1. Source: UniProtKB innate immune response Inferred from electronic annotation. Source: UniProtKB-KW metabolic process Inferred from electronic annotation. Source: GOC regulation of innate immune response Inferred from mutant phenotype Ref.18. Source: UniProtKB
Cellular_component	nucleus Inferred from direct assay Ref.18. Source: UniProtKB
Molecular_function	RNA binding Inferred from direct assay PubMed 22461318. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: InterPro phosphoric diester hydrolase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DYSF	O75923	2	EBI-1054601,EBI-2799016
TIRAP	P58753	2	EBI-1054601,EBI-528644

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y3Z3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9Y3Z3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     113-136: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 626

626

SAM domain and HD domain-containing protein 1

PRO_0000153732

Regions

Domain

45 – 110

66

SAM

Domain

164 – 319

156

HD

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.8

Modified residue

18

1

Phosphoserine By similarity

Modified residue

21

1

Phosphothreonine By similarity

Modified residue

25

1

Phosphothreonine By similarity

Modified residue

592

1

Phosphothreonine Ref.9 Ref.10 Ref.11 Ref.13 Ref.15

Natural variations

Alternative sequence

113 – 136

24

Missing in isoform 2.

VSP_037841

Natural variant

123

1

H → P in AGS5. Ref.18

VAR_058481

Natural variant

143

1

R → C in AGS5. Ref.18

VAR_058482

Natural variant

143

1

R → H in AGS5. Ref.18

VAR_058483

Natural variant

145

1

R → Q in AGS5. Ref.18

VAR_058484

Natural variant

201

1

I → N in AGS5 and CHBL2. Ref.18 Ref.19

VAR_058485

Natural variant

209

1

G → S in AGS5. Ref.18

VAR_058486

Natural variant

254

1

M → V in AGS5. Ref.18

VAR_058487

Natural variant

369

1

L → S in AGS5. Ref.18

VAR_058488

Natural variant

385

1

M → V in AGS5. Ref.18

VAR_058489

Experimental info

Sequence conflict

394

1

D → G in AAF32407. Ref.1

Sequence conflict

394

1

D → G in CAB43368. Ref.3

Sequence conflict

404

1

G → E in AAH36450. Ref.7

Sequence conflict

494

1

K → E in AAF32407. Ref.1

Sequence conflict

494

1

K → E in CAB43368. Ref.3

Sequence conflict

546

1

A → V in AAH36450. Ref.7

Secondary structure

1

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626

Helix Strand Turn

Details...

Helix

42 – 44

3

Helix

46 – 57

12

Helix

62 – 70

9

Turn

75 – 80

6

Helix

83 – 88

6

Helix

94 – 108

15

Turn

109 – 112

4

Turn

121 – 123

3

Helix

130 – 136

7

Helix

139 – 142

4

Helix

143 – 146

4

Helix

151 – 153

3

Turn

154 – 156

3

Helix

164 – 185

22

Helix

187 – 189

3

Helix

193 – 205

13

Turn

206 – 209

4

Turn

212 – 214

3

Helix

215 – 219

5

Helix

221 – 225

5

Helix

233 – 247

15

Helix

251 – 256

6

Helix

261 – 273

13

Beta strand

288 – 290

3

Helix

292 – 299

8

Turn

304 – 306

3

Helix

310 – 323

14

Helix

331 – 336

6

Beta strand

338 – 352

15

Helix

353 – 355

3

Helix

356 – 372

17

Turn

373 – 375

3

Helix

377 – 391

15

Turn

392 – 396

5

Helix

402 – 404

3

Helix

409 – 414

6

Helix

416 – 419

4

Helix

425 – 432

8

Helix

439 – 450

12

Beta strand

455 – 460

6

Helix

470 – 475

6

Helix

476 – 481

6

Helix

495 – 497

3

Beta strand

498 – 504

7

Beta strand

523 – 525

3

Beta strand

548 – 555

8

Helix

559 – 574

16

Turn

575 – 577

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 13, 2002. Version 2. Checksum: 559CB6BB029E6558	FASTA	626	72,201
	10 20 30 40 50 60 MQRADSEQPS KRPRCDDSPR TPSNTPSAEA DWSPGLELHP DYKTWGPEQV CSFLRRGGFE 70 80 90 100 110 120 EPVLLKNIRE NEITGALLPC LDESRFENLG VSSLGERKKL LSYIQRLVQI HVDTMKVIND 130 140 150 160 170 180 PIHGHIELHP LLVRIIDTPQ FQRLRYIKQL GGGYYVFPGA SHNRFEHSLG VGYLAGCLVH 190 200 210 220 230 240 ALGEKQPELQ ISERDVLCVQ IAGLCHDLGH GPFSHMFDGR FIPLARPEVK WTHEQGSVMM 250 260 270 280 290 300 FEHLINSNGI KPVMEQYGLI PEEDICFIKE QIVGPLESPV EDSLWPYKGR PENKSFLYEI 310 320 330 340 350 360 VSNKRNGIDV DKWDYFARDC HHLGIQNNFD YKRFIKFARV CEVDNELRIC ARDKEVGNLY 370 380 390 400 410 420 DMFHTRNSLH RRAYQHKVGN IIDTMITDAF LKADDYIEIT GAGGKKYRIS TAIDDMEAYT 430 440 450 460 470 480 KLTDNIFLEI LYSTDPKLKD AREILKQIEY RNLFKYVGET QPTGQIKIKR EDYESLPKEV 490 500 510 520 530 540 ASAKPKVLLD VKLKAEDFIV DVINMDYGMQ EKNPIDHVSF YCKTAPNRAI RITKNQVSQL 550 560 570 580 590 600 LPEKFAEQLI RVYCKKVDRK SLYAARQYFV QWCADRNFTK PQDGDVIAPL ITPQKKEWND 610 620 STSVQNPTRL REASKSRVQL FKDDPM
	Isoform 2 [UniParc]. Checksum: 1C1BEBBF78784F57	FASTA	602	69,444
	10 20 30 40 50 60 MQRADSEQPS KRPRCDDSPR TPSNTPSAEA DWSPGLELHP DYKTWGPEQV CSFLRRGGFE 70 80 90 100 110 120 EPVLLKNIRE NEITGALLPC LDESRFENLG VSSLGERKKL LSYIQRLVQI HVDTPQFQRL 130 140 150 160 170 180 RYIKQLGGGY YVFPGASHNR FEHSLGVGYL AGCLVHALGE KQPELQISER DVLCVQIAGL 190 200 210 220 230 240 CHDLGHGPFS HMFDGRFIPL ARPEVKWTHE QGSVMMFEHL INSNGIKPVM EQYGLIPEED 250 260 270 280 290 300 ICFIKEQIVG PLESPVEDSL WPYKGRPENK SFLYEIVSNK RNGIDVDKWD YFARDCHHLG 310 320 330 340 350 360 IQNNFDYKRF IKFARVCEVD NELRICARDK EVGNLYDMFH TRNSLHRRAY QHKVGNIIDT 370 380 390 400 410 420 MITDAFLKAD DYIEITGAGG KKYRISTAID DMEAYTKLTD NIFLEILYST DPKLKDAREI 430 440 450 460 470 480 LKQIEYRNLF KYVGETQPTG QIKIKREDYE SLPKEVASAK PKVLLDVKLK AEDFIVDVIN 490 500 510 520 530 540 MDYGMQEKNP IDHVSFYCKT APNRAIRITK NQVSQLLPEK FAEQLIRVYC KKVDRKSLYA 550 560 570 580 590 600 ARQYFVQWCA DRNFTKPQDG DVIAPLITPQ KKEWNDSTSV QNPTRLREAS KSRVQLFKDD PM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of human homologue of mouse IFN-gamma induced protein from human dendritic cells." Li N., Zhang W., Cao X. Immunol. Lett. 74:221-224(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION. Tissue: Brain.
[2]	"Molecular and biological characterization of a novel monocyte protein, MOP-5." Takayama K., Yoshimoto M. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Platelet.
[3]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Placenta and Trachea.
[5]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[8]	Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-10, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: T-cell.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Dendritic cell-derived interferon-gamma-induced protein mediates tumor necrosis factor-alpha stimulation of human lung fibroblasts." Liao W., Bao Z., Cheng C., Mok Y.-K., Wong W.S. Proteomics 8:2640-2650(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, MASS SPECTROMETRY, FUNCTION.
[13]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, MASS SPECTROMETRY.
[14]	"Cerebral arterial stenoses and stroke: novel features of Aicardi-Goutieres syndrome caused by the Arg164X mutation in SAMHD1 are associated with altered cytokine expression." Thiele H., du Moulin M., Barczyk K., George C., Schwindt W., Nurnberg G., Frosch M., Kurlemann G., Roth J., Nurnberg P., Rutsch F. Hum. Mutat. 31:E1836-E1850(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN AGS5.
[15]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"Solution structure of the N-terminal SAM-domain of the SAM domain and HD domain containing protein 1 (dendritic cell-derived IFNG-induced protein) (DCIP) (monocyte protein 5) (MOP-5)." RIKEN structural genomics initiative (RSGI) Submitted (JUL-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 23-118.
[18]	"Mutations involved in Aicardi-Goutieres syndrome implicate SAMHD1 as regulator of the innate immune response." Rice G.I., Bond J., Asipu A., Brunette R.L., Manfield I.W., Carr I.M., Fuller J.C., Jackson R.M., Lamb T., Briggs T.A., Ali M., Gornall H., Couthard L.R., Aeby A., Attard-Montalto S.P., Bertini E., Bodemer C., Brockmann K. , Brueton L.A., Corry P.C., Desguerre I., Fazzi E., Cazorla A.G., Gener B., Hamel B.C.J., Heiberg A., Hunter M., van der Knaap M.S., Kumar R., Lagae L., Landrieu P.G., Lourenco C.M., Marom D., McDermott M.F., van der Merwe W., Orcesi S., Prendiville J.S., Rasmussen M., Shalev S.A., Soler D.M., Shinawi M., Spiegel R., Tan T.Y., Vanderver A., Wakeling E.L., Wassmer E., Whittaker E., Lebon P., Stetson D.B., Bonthron D.T., Crow Y.J. Nat. Genet. 41:829-832(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AGS5 PRO-123; CYS-143; HIS-143; GLN-145; ASN-201; SER-209; VAL-254; SER-369 AND VAL-385, FUNCTION, SUBCELLULAR LOCATION.
[19]	"Autosomal dominant inheritance of a heterozygous mutation in SAMHD1 causing familial chilblain lupus." Ravenscroft J.C., Suri M., Rice G.I., Szynkiewicz M., Crow Y.J. Am. J. Med. Genet. A 155:235-237(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CHBL2 ASN-201.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF228421 mRNA. Translation: AAF32407.1.
AB013847 mRNA. Translation: BAB18916.1.
AL050267 mRNA. Translation: CAB43368.1.
AK027811 mRNA. Translation: BAB55386.1.
AK304187 mRNA. Translation: BAG65067.1.
AL079335, AL365505 Genomic DNA. Translation: CAI42293.1.
AL365505, AL079335 Genomic DNA. Translation: CAI95179.1.
CH471077 Genomic DNA. Translation: EAW76090.1.
CH471077 Genomic DNA. Translation: EAW76091.1.
BC036450 mRNA. Translation: AAH36450.1.

IPI

IPI00294739.
IPI00943982.

PIR

T08686.

RefSeq

NP_056289.2. NM_015474.3.

UniGene

Hs.580681.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E8O	NMR	-	A	23-118	[»]
3U1N	X-ray	3.10	A/B/C/D	120-626	[»]

ProteinModelPortal

Q9Y3Z3.

ModBase

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Protein-protein interaction databases

DIP

DIP-50704N.

IntAct

Q9Y3Z3. 6 interactions.

MINT

MINT-2823520.

STRING

9606.ENSP00000262878.

PTM databases

PhosphoSite

Q9Y3Z3.

Polymorphism databases

DMDM

22257047.

Proteomic databases

PaxDb

Q9Y3Z3.

PeptideAtlas

Q9Y3Z3.

PRIDE

Q9Y3Z3.

Protocols and materials databases

DNASU

25939.

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000262878; ENSP00000262878; ENSG00000101347.

GeneID

25939.

KEGG

hsa:25939.

UCSC

uc002xgh.2. human.

Organism-specific databases

CTD

25939.

GeneCards

GC20M035518.

HGNC

HGNC:15925. SAMHD1.

HPA

HPA047072.

MIM

606754. gene.
612952. phenotype.
614415. phenotype.

neXtProt

NX_Q9Y3Z3.

Orphanet

51. Aicardi-Goutieres syndrome.
276410. Cerebral vasculopathy with early-onset stroke.
90280. Chilblain lupus.

PharmGKB

PA34938.

GenAtlas

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Phylogenomic databases

eggNOG

COG1078.

HOVERGEN

HBG054208.

InParanoid

Q9Y3Z3.

OMA

QVCSFLR.

OrthoDB

EOG4MGS7B.

PhylomeDB

Q9Y3Z3.

Gene expression databases

ArrayExpress

Q9Y3Z3.

Bgee

Q9Y3Z3.

CleanEx

HS_SAMHD1.

Genevestigator

Q9Y3Z3.

GermOnline

ENSG00000101347. Homo sapiens.

Family and domain databases

Gene3D

1.10.150.50. 1 hit.
1.10.3210.10. 2 hits.

InterPro

IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
[Graphical view]

Pfam

PF01966. HD. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]

SMART

SM00471. HDc. 1 hit.
SM00454. SAM. 1 hit.
[Graphical view]

SUPFAM

SSF47769. SAM_homology. 1 hit.

PROSITE

PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q9Y3Z3.

GenomeRNAi

25939.

NextBio

47504.

SOURCE

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Entry information

Entry name

SAMH1_HUMAN

Accession

Primary (citable) accession number: Q9Y3Z3
Secondary accession number(s): B4E2A5 , E1P5V2, Q5JXG8, Q8N491, Q9H004, Q9H005, Q9H3U9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 2002
Last sequence update:	August 13, 2002
Last modified:	May 29, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.