Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Sterile alpha and TIR motif-containing protein 1 (Sterile alpha and Armadillo repeat protein) (Sterile alpha motif domain-containing protein 2) (MyD88-5) (SAM domain-containing protein 2) (Tir-1 homolog)

 SARM1_HUMAN             Reviewed;         724 AA.
Q6SZW1; O60277; Q7LGG3; Q9NXY5;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
27-SEP-2017, entry version 117.
RecName: Full=Sterile alpha and TIR motif-containing protein 1;
AltName: Full=Sterile alpha and Armadillo repeat protein;
AltName: Full=Sterile alpha motif domain-containing protein 2;
Short=MyD88-5;
Short=SAM domain-containing protein 2;
AltName: Full=Tir-1 homolog;
Flags: Precursor;
Name=SARM1; Synonyms=KIAA0524, SAMD2, SARM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=11386760; DOI=10.1006/geno.2001.6548;
Mink M., Fogelgren B., Olszewski K., Maroy P., Csiszar K.;
"A novel human gene (SARM) at chromosome 17q11 encodes a protein with
a SAM motif and structural similarity to Armadillo/beta-catenin that
is conserved in mouse, Drosophila, and Caenorhabditis elegans.";
Genomics 74:234-244(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Bousson J.-C., Casteran C., Tiraby G.;
"SARM1 isoforms nucleotide sequence.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-724.
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[4]
FUNCTION.
PubMed=15123841; DOI=10.1073/pnas.0308625101;
Liberati N.T., Fitzgerald K.A., Kim D.H., Feinbaum R., Golenbock D.T.,
Ausubel F.M.;
"Requirement for a conserved Toll/interleukin-1 resistance domain
protein in the Caenorhabditis elegans immune response.";
Proc. Natl. Acad. Sci. U.S.A. 101:6593-6598(2004).
[5]
FUNCTION, AND INTERACTION WITH TICAM1.
PubMed=16964262; DOI=10.1038/ni1382;
Carty M., Goodbody R., Schroeder M., Stack J., Moynagh P.N.,
Bowie A.G.;
"The human adaptor SARM negatively regulates adaptor protein TRIF-
dependent Toll-like receptor signaling.";
Nat. Immunol. 7:1074-1081(2006).
[6]
FUNCTION.
PubMed=16985498; DOI=10.1038/ni1006-1023;
O'Neill L.A.J.;
"DisSARMing Toll-like receptor signaling.";
Nat. Immunol. 7:1023-1025(2006).
[7]
TISSUE SPECIFICITY.
PubMed=17724133; DOI=10.1084/jem.20070868;
Kim Y., Zhou P., Qian L., Chuang J.Z., Lee J., Li C., Iadecola C.,
Nathan C., Ding A.;
"MyD88-5 links mitochondria, microtubules, and JNK3 in neurons and
regulates neuronal survival.";
J. Exp. Med. 204:2063-2074(2007).
[8]
REVIEW.
PubMed=18089857; DOI=10.1126/stke.4172007pe73;
Dalod M.;
"Studies of SARM1 uncover similarities between immune and neuronal
responses to danger.";
Sci. STKE 2007:PE73-PE73(2007).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=20306472; DOI=10.1002/eji.200940034;
Peng J., Yuan Q., Lin B., Panneerselvam P., Wang X., Luan X.L.,
Lim S.K., Leung B.P., Ho B., Ding J.L.;
"SARM inhibits both TRIF- and MyD88-mediated AP-1 activation.";
Eur. J. Immunol. 40:1738-1747(2010).
[10]
SUBCELLULAR LOCATION, MITOCHONDRIAL TRANSIT PEPTIDE CLEAVAGE SITE, AND
MUTAGENESIS OF LYS-11; ARG-14; ARG-22 AND ARG-27.
PubMed=22145856; DOI=10.1042/BJ20111653;
Panneerselvam P., Singh L.P., Ho B., Chen J., Ding J.L.;
"Targeting of pro-apoptotic TLR adaptor SARM to mitochondria:
definition of the critical region and residues in the signal
sequence.";
Biochem. J. 442:263-271(2012).
-!- FUNCTION: Negative regulator of MYD88- and TRIF-dependent toll-
like receptor signaling pathway which plays a pivotal role in
activating axonal degeneration following injury. Promotes
Wallerian degeneration an injury-induced axonal death pathway
which involves degeneration of an axon distal to the injury site.
Can activate neuronal death in response to stress. Regulates
dendritic arborization through the MAPK4-JNK pathway. Involved in
innate immune response. Inhibits both TICAM1/TRIF- and MYD88-
dependent activation of JUN/AP-1, TRIF-dependent activation of NF-
kappa-B and IRF3, and the phosphorylation of MAPK14/p38.
{ECO:0000269|PubMed:15123841, ECO:0000269|PubMed:16964262,
ECO:0000269|PubMed:16985498, ECO:0000269|PubMed:20306472}.
-!- SUBUNIT: Interacts with TICAM1/TRIF and thereby interferes with
TICAM1/TRIF function. Interacts with MAPK10/JNK3 and SDC2 (via
cytoplasmic domain) (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q99836:MYD88; NbExp=5; IntAct=EBI-11693532, EBI-447677;
Q86XR7:TICAM2; NbExp=2; IntAct=EBI-11693532, EBI-525927;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, axon
{ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell
junction, synapse {ECO:0000250}. Mitochondrion. Note=Associated
with microtubules. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6SZW1-1; Sequence=Displayed;
Name=2;
IsoId=Q6SZW1-2; Sequence=VSP_013603;
-!- TISSUE SPECIFICITY: Predominantly expressed in brain, kidney and
liver. Expressed at lower level in placenta.
{ECO:0000269|PubMed:11386760, ECO:0000269|PubMed:17724133}.
-!- INDUCTION: Up-regulated by lipopolysaccharides (LPS).
{ECO:0000269|PubMed:20306472}.
-!- CAUTION: Was initially (PubMed:11386760) reported to contain ARM
repeats. Such repeats are however not predicted by any detection
method. {ECO:0000305|PubMed:11386760}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ290445; CAB90355.1; -; mRNA.
EMBL; AY444166; AAR17520.1; -; mRNA.
EMBL; AB011096; BAA25450.1; -; mRNA.
CCDS; CCDS11230.2; -. [Q6SZW1-1]
RefSeq; NP_055892.2; NM_015077.3. [Q6SZW1-1]
UniGene; Hs.743510; -.
ProteinModelPortal; Q6SZW1; -.
SMR; Q6SZW1; -.
BioGrid; 116726; 27.
IntAct; Q6SZW1; 5.
STRING; 9606.ENSP00000406738; -.
iPTMnet; Q6SZW1; -.
PhosphoSitePlus; Q6SZW1; -.
BioMuta; SARM1; -.
DMDM; 83288284; -.
EPD; Q6SZW1; -.
MaxQB; Q6SZW1; -.
PaxDb; Q6SZW1; -.
PeptideAtlas; Q6SZW1; -.
PRIDE; Q6SZW1; -.
Ensembl; ENST00000585482; ENSP00000468032; ENSG00000004139. [Q6SZW1-1]
GeneID; 23098; -.
KEGG; hsa:23098; -.
UCSC; uc032ezg.2; human. [Q6SZW1-1]
CTD; 23098; -.
DisGeNET; 23098; -.
EuPathDB; HostDB:ENSG00000004139.13; -.
GeneCards; SARM1; -.
H-InvDB; HIX0013645; -.
HGNC; HGNC:17074; SARM1.
HPA; HPA024359; -.
HPA; HPA024759; -.
MIM; 607732; gene.
neXtProt; NX_Q6SZW1; -.
OpenTargets; ENSG00000004139; -.
PharmGKB; PA134971180; -.
eggNOG; KOG3678; Eukaryota.
eggNOG; ENOG410XQ4A; LUCA.
GeneTree; ENSGT00390000004155; -.
HOGENOM; HOG000008460; -.
HOVERGEN; HBG079166; -.
InParanoid; Q6SZW1; -.
OMA; CIAAFYL; -.
OrthoDB; EOG091G01TX; -.
PhylomeDB; Q6SZW1; -.
Reactome; R-HSA-166166; MyD88-independent TLR3/TLR4 cascade.
Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-HSA-937072; TRAF6 mediated induction of TAK1 complex.
SIGNOR; Q6SZW1; -.
ChiTaRS; SARM1; human.
GenomeRNAi; 23098; -.
PRO; PR:Q6SZW1; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000004139; -.
CleanEx; HS_SARM1; -.
ExpressionAtlas; Q6SZW1; baseline and differential.
Genevisible; Q6SZW1; HS.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; IEA:Ensembl.
GO; GO:0005874; C:microtubule; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0034128; P:negative regulation of MyD88-independent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
GO; GO:1901214; P:regulation of neuron death; ISS:UniProtKB.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
InterPro; IPR000157; TIR_dom.
Pfam; PF07647; SAM_2; 2.
Pfam; PF13676; TIR_2; 1.
SMART; SM00454; SAM; 2.
SMART; SM00255; TIR; 1.
SUPFAM; SSF47769; SSF47769; 2.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS50105; SAM_DOMAIN; 2.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell projection;
Complete proteome; Cytoplasm; Differentiation; Immunity;
Innate immunity; Mitochondrion; Neurogenesis; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Synapse; Transit peptide.
TRANSIT 1 27 Mitochondrion.
CHAIN 28 724 Sterile alpha and TIR motif-containing
protein 1.
/FTId=PRO_0000097589.
DOMAIN 412 476 SAM 1. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
DOMAIN 486 548 SAM 2. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
DOMAIN 559 657 TIR.
MOD_RES 548 548 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PDS3}.
MOD_RES 558 558 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PDS3}.
VAR_SEQ 1 106 MVLTLLLSAYKLCRFFAMSGPRPGAERLAVPGPDGGGGTGP
WWAAGGRGPREVSPGAGTEVQDALERALPELQQALSALKQA
GGARAVGAGLAEVFQLVEEAWLLP -> MGAVARAHGGLRV
ARARESVAGGRHRGAGRPGARAAGAAAGLVRAEAGGRRAGR
GRRPGRGLPTGGGGLAAA (in isoform 2).
{ECO:0000303|PubMed:11386760}.
/FTId=VSP_013603.
VARIANT 23 23 P -> R (in dbSNP:rs7212814).
/FTId=VAR_061702.
MUTAGEN 11 11 K->A: No effect on mitochondrial
localization.
{ECO:0000269|PubMed:22145856}.
MUTAGEN 14 14 R->A: Loss in ability to localize to
mitochondria and reduction in apoptotic
activity. {ECO:0000269|PubMed:22145856}.
MUTAGEN 22 22 R->A: No effect on mitochondrial
localization.
{ECO:0000269|PubMed:22145856}.
MUTAGEN 27 27 R->A: No effect on mitochondrial
localization.
{ECO:0000269|PubMed:22145856}.
SEQUENCE 724 AA; 79388 MW; 6391EA4C31EF6604 CRC64;
MVLTLLLSAY KLCRFFAMSG PRPGAERLAV PGPDGGGGTG PWWAAGGRGP REVSPGAGTE
VQDALERALP ELQQALSALK QAGGARAVGA GLAEVFQLVE EAWLLPAVGR EVAQGLCDAI
RLDGGLDLLL RLLQAPELET RVQAARLLEQ ILVAENRDRV ARIGLGVILN LAKEREPVEL
ARSVAGILEH MFKHSEETCQ RLVAAGGLDA VLYWCRRTDP ALLRHCALAL GNCALHGGQA
VQRRMVEKRA AEWLFPLAFS KEDELLRLHA CLAVAVLATN KEVEREVERS GTLALVEPLV
ASLDPGRFAR CLVDASDTSQ GRGPDDLQRL VPLLDSNRLE AQCIGAFYLC AEAAIKSLQG
KTKVFSDIGA IQSLKRLVSY STNGTKSALA KRALRLLGEE VPRPILPSVP SWKEAEVQTW
LQQIGFSKYC ESFREQQVDG DLLLRLTEEE LQTDLGMKSG ITRKRFFREL TELKTFANYS
TCDRSNLADW LGSLDPRFRQ YTYGLVSCGL DRSLLHRVSE QQLLEDCGIH LGVHRARILT
AAREMLHSPL PCTGGKPSGD TPDVFISYRR NSGSQLASLL KVHLQLHGFS VFIDVEKLEA
GKFEDKLIQS VMGARNFVLV LSPGALDKCM QDHDCKDWVH KEIVTALSCG KNIVPIIDGF
EWPEPQVLPE DMQAVLTFNG IKWSHEYQEA TIEKIIRFLQ GRSSRDSSAG SDTSLEGAAP
MGPT


Related products :

Catalog number Product name Quantity
EIAAB37300 Homo sapiens,Human,KIAA0524,SAM domain-containing protein 2,SAMD2,SARM,SARM1,Sterile alpha and Armadillo repeat protein,Sterile alpha and TIR motif-containing protein 1,Sterile alpha motif domain-cont
18-661-15183 Sterile alpha and TIR motif-containing protein 1 - Sterile alpha and Armadillo repeat protein; Tir-1 homolog Polyclonal 0.1 mg
EIAAB38727 Homo sapiens,hSmaug2,Human,Protein Smaug homolog 2,SAM domain-containing protein 4B,SAMD4B,Smaug 2,SMAUG2,Sterile alpha motif domain-containing protein 4B
EIAAB38725 Homo sapiens,hSmaug1,Human,KIAA1053,Protein Smaug homolog 1,SAM domain-containing protein 4A,SAMD4,SAMD4A,Smaug 1,SMAUG1,Sterile alpha motif domain-containing protein 4A
ANS1B_MOUSE Mouse ELISA Kit FOR Ankyrin repeat and sterile alpha motif domain-containing protein 1B 96T
CSB-EL001805RA Rat Ankyrin repeat and sterile alpha motif domain-containing protein 1B(ANKS1B) ELISA kit 96T
EIAAB37228 Major retinal SAM domain-containing protein,Mouse,Mr-s,Mus musculus,SAM domain-containing protein 11,Samd11,Sterile alpha motif domain-containing protein 11
CSB-EL001805HU Human Ankyrin repeat and sterile alpha motif domain-containing protein 1B(ANKS1B) ELISA kit 96T
CSB-EL001805RA Rat Ankyrin repeat and sterile alpha motif domain-containing protein 1B(ANKS1B) ELISA kit SpeciesRat 96T
CSB-EL001805MO Mouse Ankyrin repeat and sterile alpha motif domain-containing protein 1B(ANKS1B) ELISA kit 96T
EIAAB37254 Homo sapiens,Human,SAM domain-containing protein 8,SAMD8,SMSr,Sphingomyelin synthase-related protein 1,Sterile alpha motif domain-containing protein 8
CSB-EL001805MO Mouse Ankyrin repeat and sterile alpha motif domain-containing protein 1B(ANKS1B) ELISA kit SpeciesMouse 96T
CSB-EL001805HU Human Ankyrin repeat and sterile alpha motif domain-containing protein 1B(ANKS1B) ELISA kit SpeciesHuman 96T
EIAAB37231 Homo sapiens,HSD42,HSD-42,Human,SAM domain-containing protein 13,SAMD13,Sterile alpha motif domain-containing protein 13
EIAAB37225 C20orf136,Homo sapiens,Human,SAM domain-containing protein 10,SAMD10,Sterile alpha motif domain-containing protein 10
EIAAB37249 Homo sapiens,Human,SAM domain-containing protein 5,SAMD5,SAMDC1,Sterile alpha motif domain-containing protein 5
EIAAB37245 Atherin,Oryctolagus cuniculus,Rabbit,SAM domain-containing protein 1,SAMD1,Sterile alpha motif domain-containing protein 1
EIAAB37246 Atherin,Homo sapiens,Human,SAM domain-containing protein 1,SAMD1,Sterile alpha motif domain-containing protein 1
EIAAB37235 C14orf174,FAM15A,Homo sapiens,Human,SAM domain-containing protein 15,SAMD15,Sterile alpha motif domain-containing protein 15
EIAAB37227 Homo sapiens,Human,SAM domain-containing protein 11,SAMD11,Sterile alpha motif domain-containing protein 11
EIAAB37234 Homo sapiens,Human,SAM domain-containing protein 14,SAMD14,Sterile alpha motif domain-containing protein 14
EIAAB37229 Homo sapiens,Human,SAM domain-containing protein 12,SAMD12,Sterile alpha motif domain-containing protein 12
EIAAB37248 Gm623,Mouse,Mus musculus,SAM domain-containing protein 3,Samd3,Sterile alpha motif domain-containing protein 3
EIAAB37240 Kiaa2005,Mouse,Mus musculus,SAM domain-containing protein 9-like,Samd9l,Sterile alpha motif domain-containing protein 9-like
EIAAB37253 Homo sapiens,Human,SAM domain-containing protein 7,SAMD7,Sterile alpha motif domain-containing protein 7


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur