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

Protein mes-1 (Maternal-effect sterile protein 1)

 MES1_CAEEL              Reviewed;         966 AA.
G5EBL2;
20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
25-OCT-2017, entry version 59.
RecName: Full=Protein mes-1 {ECO:0000305};
AltName: Full=Maternal-effect sterile protein 1 {ECO:0000312|WormBase:F54F7.5};
Flags: Precursor;
Name=mes-1 {ECO:0000312|WormBase:F54F7.5};
ORFNames=F54F7.5 {ECO:0000312|WormBase:F54F7.5};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000312|EMBL:AAF13716.1}
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
PubMed=11003841;
Berkowitz L.A., Strome S.;
"MES-1, a protein required for unequal divisions of the germline in
early C. elegans embryos, resembles receptor tyrosine kinases and is
localized to the boundary between the germline and gut cells.";
Development 127:4419-4431(2000).
[2] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-89 AND SER-441.
PubMed=7555722;
Strome S., Martin P., Schierenberg E., Paulsen J.;
"Transformation of the germ line into muscle in mes-1 mutant embryos
of C. elegans.";
Development 121:2961-2972(1995).
[4] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=12110172; DOI=10.1016/S1534-5807(02)00185-5;
Bei Y., Hogan J., Berkowitz L.A., Soto M., Rocheleau C.E., Pang K.M.,
Collins J., Mello C.C.;
"SRC-1 and Wnt signaling act together to specify endoderm and to
control cleavage orientation in early C. elegans embryos.";
Dev. Cell 3:113-125(2002).
[5] {ECO:0000305}
FUNCTION.
PubMed=14534135; DOI=10.1242/dev.00790;
Tsou M.-F.B., Hayashi A., Rose L.S.;
"LET-99 opposes Galpha/GPR signaling to generate asymmetry for spindle
positioning in response to PAR and MES-1/SRC-1 signaling.";
Development 130:5717-5730(2003).
[6] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12730122; DOI=10.1101/gad.1081203;
Srinivasan D.G., Fisk R.M., Xu H., van den Heuvel S.;
"A complex of LIN-5 and GPR proteins regulates G protein signaling and
spindle function in C elegans.";
Genes Dev. 17:1225-1239(2003).
-!- FUNCTION: During early embryogenesis, controls asymmetric cell
division and the asymmetric localization of P granules of germline
precursor P2 and its descendant P3 (PubMed:7555722). Probably
upstream of tyrosine kinase src-1, plays a role in endoderm
development by controlling spindle orientation during EMS
blastomere cell division (PubMed:12110172). Controls EMS spindle
orientation probably by promoting lin-5 and gpr-1/2 enrichment at,
and let-99 exclusion from the junction between P2 and EMS cells
(PubMed:14534135, PubMed:12730122). {ECO:0000269|PubMed:12110172,
ECO:0000269|PubMed:12730122, ECO:0000269|PubMed:14534135,
ECO:0000269|PubMed:7555722}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11003841,
ECO:0000269|PubMed:12110172}; Single-pass type I membrane protein
{ECO:0000305}. Note=Localizes at the site of contact between EMS
and P2 cells in the 4-cell stage embryo, between P3 and E cells in
the 12-cell stage embryo and between P4 and Ep cells in the 26-
cell stage embryo. {ECO:0000269|PubMed:11003841,
ECO:0000269|PubMed:12110172}.
-!- DEVELOPMENTAL STAGE: Expressed at least in P2 germline cell at 4-
cell stage and up to 26-cell stage embryos (PubMed:11003841,
PubMed:12110172). Expressed only at L4 stage during larval
development and then accumulates in adults (PubMed:11003841).
{ECO:0000269|PubMed:11003841, ECO:0000269|PubMed:12110172}.
-!- DOMAIN: The protein kinase domain is predicted to be catalytically
inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- DISRUPTION PHENOTYPE: 71 percent of embryos of mutant mothers
develop into sterile adults with extra body muscle cells at the
restrictive temperature (25 degrees Celsius) (PubMed:7555722). Low
embryonic lethality (7-8 percent) (PubMed:7555722). Loss of lin-5
and grp-1/2 enrichment at the EMS/P2 cell boundaries at the 4-cell
embryonic stage (PubMed:12730122). Decrease in phosphotyrosine
levels at the site of contact between P2 and EMS cells
(PubMed:12110172). {ECO:0000269|PubMed:12110172,
ECO:0000269|PubMed:12730122, ECO:0000269|PubMed:7555722}.
-!- SIMILARITY: Belongs to the protein kinase superfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF200199; AAF13716.1; -; mRNA.
EMBL; BX284606; CAA91758.2; -; Genomic_DNA.
PIR; T22681; T22681.
RefSeq; NP_741906.1; NM_171780.4.
UniGene; Cel.6122; -.
ProteinModelPortal; G5EBL2; -.
SMR; G5EBL2; -.
IntAct; G5EBL2; 1.
STRING; 6239.F54F7.5; -.
EPD; G5EBL2; -.
PaxDb; G5EBL2; -.
EnsemblMetazoa; F54F7.5; F54F7.5; WBGene00003219.
GeneID; 181362; -.
KEGG; cel:CELE_F54F7.5; -.
CTD; 181362; -.
WormBase; F54F7.5; CE28237; WBGene00003219; mes-1.
eggNOG; ENOG410JKTY; Eukaryota.
eggNOG; ENOG411187E; LUCA.
GeneTree; ENSGT00390000006056; -.
OrthoDB; EOG093708VD; -.
PRO; PR:G5EBL2; -.
Proteomes; UP000001940; Chromosome X.
Bgee; WBGene00003219; -.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:WormBase.
GO; GO:0008356; P:asymmetric cell division; IMP:WormBase.
GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:WormBase.
GO; GO:0001708; P:cell fate specification; IMP:WormBase.
GO; GO:0003006; P:developmental process involved in reproduction; IMP:UniProtKB.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:UniProtKB.
GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:WormBase.
GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:WormBase.
GO; GO:0007276; P:gamete generation; IMP:WormBase.
GO; GO:0070986; P:left/right axis specification; IGI:UniProtKB.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
ATP-binding; Cell cycle; Cell division; Cell membrane;
Complete proteome; Glycoprotein; Membrane; Mitosis;
Nucleotide-binding; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 966 Protein mes-1. {ECO:0000255}.
/FTId=PRO_5005349097.
TOPO_DOM 20 470 Extracellular. {ECO:0000305}.
TRANSMEM 471 491 Helical. {ECO:0000255}.
TOPO_DOM 492 966 Cytoplasmic. {ECO:0000305}.
DOMAIN 656 966 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 662 670 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 685 685 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 214 214 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 251 251 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 372 372 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 89 89 G->E: In q367; 12 percent of mutant
mothers' progeny is sterile at the
permissive temperature (16 degrees
Celsius) and 79 percent at the
restrictive temperature (25 degrees
Celsius). Low levels of embryonic
lethality. {ECO:0000269|PubMed:7555722}.
MUTAGEN 441 441 S->N: In q222; 6 percent of mutant
mothers' progeny is sterile at the
permissive temperature (16 degrees
Celsius) and 77 percent at the
restrictive temperature (25 degrees
Celsius). Low levels of embryonic
lethality. {ECO:0000269|PubMed:7555722}.
SEQUENCE 966 AA; 108898 MW; 07B0000EBA14437F CRC64;
MKIHHFLTLL CTFLPLTTTA LTNSTPLSLL GPCYKRCVTK FGETKEQLTN AETISLEYDV
SNNTEFSLCK LGCNSHEYTD LNLAAFRYGQ LAYQKILTTV EDVPTRGTVL NDVFIVCLDT
SFMPSNNSAP SAKRLLSGTV LLVLDEDVAK ADNVFLIEVL ARNADKSAVQ VISQQWCYSS
NCNITFNAPT EVSSFDVRLR VSTFDSNGQV GGINFSKWHN INQILTKTFV DMSLKSVVWK
AEKAAANFVF NLTASDHVPA CSLQMIYRSS LSSELLHRNF YLDHTLEVFV NNLDFDKIYT
MQLAPSGTHD RSTPSLASAV IEIPPCRHLV DDYSMCAPPP VSSLSYNWNL SPTSEYELLI
KWKLLNYMDG LNVTEELSIP VAYFLLNAHP LITANNEQCE KYEKIRRVVS YGLRELVFHV
PDTDCNYEVE MTAVDTNQRI SEVKKIQVFR FNVPPYVSFL QASDIPTSVE LMAVVLATSA
IFALIALFLL YRKRKRDKKA RFQMYKDAEA GVSYDYVATT ESLGSVVQIR STNFRFEPVE
NIDGNIEAAL AQQQKFEGGT MNSMFRTYYN LDHPVKVPAH MAEASSDEDN GYENIRYSYF
GSELSDDVFE EDIYMTHKSL SIYCQDSPLT TPMAPIAPYE HFDDIPSHQY RNFQVHNFNE
RIEKQAYWLM ATVVDVVRRE LYSLKVPKDY TPETISAMRK ELEFLRTLAP HGNCRRFEGV
VIGRWDDLPR QVIGILIENT RGGTLRNYIA AVGSVFRNCS LATDHDSFAS QQDMNSTQHP
FDKLSTEADE NNSKKVKIQE ITDSLSIRFC QFAEQVSSAL EHLHSAGSVH TRVTTLNIYL
LHNYSDPFDM LPDQVVKLGN FGFAVQNSED VVLDDNLQPP EVIKGEKYEA RGDIWQFGLC
LAEMCSLGDL EQSEVGTLKS GHDTFKNLPS TQVLRDAAKR CLSARTRPSA SDLCGVFKSV
NVAATV


Related products :

Catalog number Product name Quantity
EIAAB46789 Mouse,Mus musculus,Oocyte-specific maternal effect factor,Zar1,Zygote arrest protein 1
EIAAB46787 Oocyte-specific maternal effect factor,Rat,Rattus norvegicus,Zar1,Zygote arrest protein 1
EIAAB46788 Homo sapiens,Human,Oocyte-specific maternal effect factor,ZAR1,Zygote arrest protein 1
EIAAB06053 Ccndbp1,Cyclin-D1-binding protein 1,Dip1,Gcip,Grap2 and cyclin-D-interacting protein,Maid,Maternal Id-like protein,Mouse,Mus musculus,SSEC-8,Stage specific embryonic cDNA-8 protein
EIAAB45941 Homo sapiens,Human,hVPS35,Maternal-embryonic 3,MEM3,TCCCTA00141,Vacuolar protein sorting-associated protein 35,Vesicle protein sorting 35,VPS35
EIAAB45942 Maternal-embryonic 3,Mem3,Mouse,Mus musculus,Vacuolar protein sorting-associated protein 35,Vesicle protein sorting 35,Vps35
EIAAB26336 Mater,Mater protein,Maternal antigen that embryos require,Mouse,Mus musculus,NACHT, LRR and PYD domains-containing protein 5,Nalp5,Nlrp5,Ooplasm-specific protein 1,OP1
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
27-610 SUV39H1, a human homolog of the Drosophila position effect variegation modifier Su (var)3-9 and of the S. pombe silencing factor clr4, encodes a heterochromatic protein that transiently accumulates at 0.1 mg
26-815 Strong TKTL1 protein expression has been correlated with a certain type of glucose metabolism (aerobic glycolysis; Warburg effect) and to cells which are affected by chronic complications of diabetic 0.05 mg
MR-003 ///NEW Antibody 2-Step Effect Universal Anti-Mouse_ Anti-Rabbit IgG 2-Step Effect Universal 50ml
MR-003 ///NEW Antibody 2-Step Effect Universal Anti-Mouse_ Anti-Rabbit IgG 2-Step Effect Universal 100ml
20-372-60123 maternal G10 transcript. mRNA (cDNA clone MGC 39264 IMAGE 5087938). - Mouse monoclonal anti-human G10 antibody; Protein G10 homolog; EDG-2 Monoclonal 0.1 mg
EIAAB37254 Homo sapiens,Human,SAM domain-containing protein 8,SAMD8,SMSr,Sphingomyelin synthase-related protein 1,Sterile alpha motif domain-containing protein 8
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
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
EIAAB37225 C20orf136,Homo sapiens,Human,SAM domain-containing protein 10,SAMD10,Sterile alpha motif domain-containing protein 10
EIAAB37231 Homo sapiens,HSD42,HSD-42,Human,SAM domain-containing protein 13,SAMD13,Sterile alpha motif domain-containing protein 13
EIAAB37246 Atherin,Homo sapiens,Human,SAM domain-containing protein 1,SAMD1,Sterile alpha motif domain-containing protein 1
EIAAB37245 Atherin,Oryctolagus cuniculus,Rabbit,SAM domain-containing protein 1,SAMD1,Sterile alpha motif domain-containing protein 1
EIAAB37249 Homo sapiens,Human,SAM domain-containing protein 5,SAMD5,SAMDC1,Sterile alpha motif domain-containing protein 5
EIAAB37235 C14orf174,FAM15A,Homo sapiens,Human,SAM domain-containing protein 15,SAMD15,Sterile alpha motif domain-containing protein 15
EIAAB38723 Protein Smaug homolog 1,Rat,Rattus norvegicus,Samd4a,Smaug 1,Smaug1,Sterile alpha motif domain-containing protein 4A


 

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