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Leucine-rich repeat protein SHOC-2 (Protein soc-2 homolog) (Protein sur-8 homolog)

 SHOC2_HUMAN             Reviewed;         582 AA.
Q9UQ13; A8K9W8; B3KR23; O76063; Q5VZS8; Q5VZS9;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
20-JUN-2001, sequence version 2.
18-JUL-2018, entry version 168.
RecName: Full=Leucine-rich repeat protein SHOC-2;
AltName: Full=Protein soc-2 homolog;
AltName: Full=Protein sur-8 homolog;
Name=SHOC2; Synonyms=KIAA0862;
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 1), AND INTERACTION WITH KRAS AND
NRAS.
PubMed=9674433; DOI=10.1016/S0092-8674(00)81227-1;
Sieburth D.S., Sun Q., Han M.;
"SUR-8, a conserved Ras-binding protein with leucine-rich repeats,
positively regulates Ras-mediated signaling in C. elegans.";
Cell 94:119-130(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9618511; DOI=10.1073/pnas.95.12.6903;
Selfors L.M., Schutzman J.L., Borland C.Z., Stern M.J.;
"Soc-2 encodes a leucine-rich repeat protein implicated in fibroblast
growth factor receptor signaling.";
Proc. Natl. Acad. Sci. U.S.A. 95:6903-6908(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 165-582 (ISOFORM 2).
TISSUE=Amygdala, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION.
PubMed=10783161;
Li W., Han M., Guan K.-L.;
"The leucine-rich repeat protein SUR-8 enhances MAP kinase activation
and forms a complex with Ras and Raf.";
Genes Dev. 14:895-900(2000).
[9]
INTERACTION WITH ERBIN.
PubMed=16301319; DOI=10.1074/jbc.M507360200;
Dai P., Xiong W.C., Mei L.;
"Erbin inhibits RAF activation by disrupting the sur-8-Ras-Raf
complex.";
J. Biol. Chem. 281:927-933(2006).
[10]
FUNCTION, INTERACTION WITH MRAS AND RAF1, AND IDENTIFICATION IN A
COMPLEX WITH PP1CA; PPP1CB; PPP1CC; RAF1 AND MRAS.
PubMed=16630891; DOI=10.1016/j.molcel.2006.03.027;
Rodriguez-Viciana P., Oses-Prieto J., Burlingame A., Fried M.,
McCormick F.;
"A phosphatase holoenzyme comprised of Shoc2/Sur8 and the catalytic
subunit of PP1 functions as an M-Ras effector to modulate Raf
activity.";
Mol. Cell 22:217-230(2006).
[11]
INVOLVEMENT IN NSLH1, VARIANT NSLH1 GLY-2, CHARACTERIZATION OF VARIANT
NSLH1 GLY-2, AND SUBCELLULAR LOCATION.
PubMed=19684605; DOI=10.1038/ng.425;
Cordeddu V., Di Schiavi E., Pennacchio L.A., Ma'ayan A., Sarkozy A.,
Fodale V., Cecchetti S., Cardinale A., Martin J., Schackwitz W.,
Lipzen A., Zampino G., Mazzanti L., Digilio M.C., Martinelli S.,
Flex E., Lepri F., Bartholdi D., Kutsche K., Ferrero G.B.,
Anichini C., Selicorni A., Rossi C., Tenconi R., Zenker M., Merlo D.,
Dallapiccola B., Iyengar R., Bazzicalupo P., Gelb B.D., Tartaglia M.;
"Mutation of SHOC2 promotes aberrant protein N-myristoylation and
causes Noonan-like syndrome with loose anagen hair.";
Nat. Genet. 41:1022-1026(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
VARIANT NSLH1 GLY-2.
PubMed=23918763; DOI=10.1002/ajmg.a.36098;
Gripp K.W., Zand D.J., Demmer L., Anderson C.E., Dobyns W.B.,
Zackai E.H., Denenberg E., Jenny K., Stabley D.L., Sol-Church K.;
"Expanding the SHOC2 mutation associated phenotype of Noonan syndrome
with loose anagen hair: structural brain anomalies and
myelofibrosis.";
Am. J. Med. Genet. A 161A:2420-2430(2013).
[14]
VARIANT NSLH1 ILE-173, CHARACTERIZATION OF VARIANT NSLH1 ILE-173,
FUNCTION, INTERACTION WITH MRAS AND RAF1 AND PHOSPHATASE 1C, AND
SUBCELLULAR LOCATION.
PubMed=25137548; DOI=10.1002/humu.22634;
Hannig V., Jeoung M., Jang E.R., Phillips J.A. III, Galperin E.;
"A Novel SHOC2 Variant in Rasopathy.";
Hum. Mutat. 35:1290-1294(2014).
-!- FUNCTION: Regulatory subunit of protein phosphatase 1 (PP1c) that
acts as a M-Ras/MRAS effector and participates in MAPK pathway
activation. Upon M-Ras/MRAS activation, targets PP1c to
specifically dephosphorylate the 'Ser-259' inhibitory site of RAF1
kinase and stimulate RAF1 activity at specialized signaling
complexes. {ECO:0000269|PubMed:10783161,
ECO:0000269|PubMed:16630891, ECO:0000269|PubMed:25137548}.
-!- SUBUNIT: Interacts with M-Ras/MRAS, and RAF1. Forms a multiprotein
complex with Ras (M-Ras/MRAS), Raf (RAF1) and protein phosphatase
1 (PPP1CA, PPP1CB and PPP1CC). Interacts with ERBIN; disrupts the
interaction with RAF1 and Ras, leading to prevent activation of
the Ras signaling pathway. Specifically binds K-Ras/KRAS, M-
Ras/MRAS and N-Ras/NRAS but not H-Ras/HRAS.
{ECO:0000269|PubMed:16301319, ECO:0000269|PubMed:16630891,
ECO:0000269|PubMed:25137548, ECO:0000269|PubMed:9674433}.
-!- INTERACTION:
Q96RT1:ERBIN; NbExp=4; IntAct=EBI-993879, EBI-993903;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19684605,
ECO:0000269|PubMed:25137548}. Nucleus
{ECO:0000269|PubMed:19684605, ECO:0000269|PubMed:25137548}.
Note=Translocates from cytoplasm to nucleus upon growth factor
stimulation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UQ13-1; Sequence=Displayed;
Name=2;
IsoId=Q9UQ13-2; Sequence=VSP_038188;
Note=No experimental confirmation available.;
-!- DISEASE: Noonan syndrome-like disorder with loose anagen hair 1
(NSLH1) [MIM:607721]: A syndrome characterized by Noonan
dysmorphic features such as macrocephaly, high forehead,
hypertelorism, palpebral ptosis, low-set and posteriorly rotated
ears, short and webbed neck, pectus anomalies, in association with
pluckable, sparse, thin and slow-growing hair.
{ECO:0000269|PubMed:19684605, ECO:0000269|PubMed:23918763,
ECO:0000269|PubMed:25137548}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the SHOC2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA74885.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAG52235.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAH72813.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The matchmaker - Issue
121 of September 2010;
URL="https://web.expasy.org/spotlight/back_issues/121";
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EMBL; AF068920; AAC39856.1; -; mRNA.
EMBL; AF054828; AAC25698.1; -; mRNA.
EMBL; AB020669; BAA74885.2; ALT_INIT; mRNA.
EMBL; AK090820; BAG52235.1; ALT_INIT; mRNA.
EMBL; AK292833; BAF85522.1; -; mRNA.
EMBL; AL158163; CAH72812.1; -; Genomic_DNA.
EMBL; AL158163; CAH72813.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471066; EAW49548.1; -; Genomic_DNA.
EMBL; BC050445; AAH50445.1; -; mRNA.
CCDS; CCDS58095.1; -. [Q9UQ13-2]
CCDS; CCDS7568.1; -. [Q9UQ13-1]
RefSeq; NP_001255968.1; NM_001269039.2. [Q9UQ13-2]
RefSeq; NP_001311265.1; NM_001324336.1. [Q9UQ13-1]
RefSeq; NP_001311266.1; NM_001324337.1. [Q9UQ13-1]
RefSeq; NP_031399.2; NM_007373.3. [Q9UQ13-1]
RefSeq; XP_016872191.1; XM_017016702.1. [Q9UQ13-1]
RefSeq; XP_016872192.1; XM_017016703.1. [Q9UQ13-1]
RefSeq; XP_016872193.1; XM_017016704.1. [Q9UQ13-1]
UniGene; Hs.104315; -.
ProteinModelPortal; Q9UQ13; -.
SMR; Q9UQ13; -.
BioGrid; 113729; 21.
IntAct; Q9UQ13; 12.
MINT; Q9UQ13; -.
STRING; 9606.ENSP00000358464; -.
iPTMnet; Q9UQ13; -.
PhosphoSitePlus; Q9UQ13; -.
BioMuta; SHOC2; -.
DMDM; 14423936; -.
EPD; Q9UQ13; -.
PaxDb; Q9UQ13; -.
PeptideAtlas; Q9UQ13; -.
PRIDE; Q9UQ13; -.
ProteomicsDB; 85490; -.
ProteomicsDB; 85491; -. [Q9UQ13-2]
Ensembl; ENST00000265277; ENSP00000265277; ENSG00000108061. [Q9UQ13-2]
Ensembl; ENST00000369452; ENSP00000358464; ENSG00000108061. [Q9UQ13-1]
GeneID; 8036; -.
KEGG; hsa:8036; -.
UCSC; uc001kzl.5; human. [Q9UQ13-1]
CTD; 8036; -.
DisGeNET; 8036; -.
EuPathDB; HostDB:ENSG00000108061.11; -.
GeneCards; SHOC2; -.
HGNC; HGNC:15454; SHOC2.
HPA; HPA009164; -.
MalaCards; SHOC2; -.
MIM; 602775; gene.
MIM; 607721; phenotype.
neXtProt; NX_Q9UQ13; -.
OpenTargets; ENSG00000108061; -.
Orphanet; 2701; Noonan syndrome-like disorder with loose anagen hair.
PharmGKB; PA37960; -.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00840000129686; -.
HOGENOM; HOG000116557; -.
HOVERGEN; HBG055661; -.
InParanoid; Q9UQ13; -.
KO; K19613; -.
OMA; NQFTSYP; -.
OrthoDB; EOG091G05NZ; -.
PhylomeDB; Q9UQ13; -.
TreeFam; TF315742; -.
SignaLink; Q9UQ13; -.
SIGNOR; Q9UQ13; -.
ChiTaRS; SHOC2; human.
GeneWiki; SHOC2; -.
GenomeRNAi; 8036; -.
PRO; PR:Q9UQ13; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000108061; -.
CleanEx; HS_SHOC2; -.
ExpressionAtlas; Q9UQ13; baseline and differential.
Genevisible; Q9UQ13; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000164; C:protein phosphatase type 1 complex; IDA:UniProtKB.
GO; GO:0008157; F:protein phosphatase 1 binding; IDA:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IDA:UniProtKB.
GO; GO:0019888; F:protein phosphatase regulator activity; TAS:UniProtKB.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; NAS:UniProtKB.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; NAS:UniProtKB.
Gene3D; 3.80.10.10; -; 4.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
Pfam; PF13855; LRR_8; 4.
SMART; SM00369; LRR_TYP; 16.
PROSITE; PS51450; LRR; 17.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Disease mutation;
Leucine-rich repeat; Nucleus; Reference proteome; Repeat.
CHAIN 1 582 Leucine-rich repeat protein SHOC-2.
/FTId=PRO_0000097737.
REPEAT 101 122 LRR 1.
REPEAT 124 145 LRR 2.
REPEAT 147 169 LRR 3.
REPEAT 170 191 LRR 4.
REPEAT 193 214 LRR 5.
REPEAT 216 237 LRR 6.
REPEAT 239 260 LRR 7.
REPEAT 262 283 LRR 8.
REPEAT 285 307 LRR 9.
REPEAT 308 329 LRR 10.
REPEAT 332 353 LRR 11.
REPEAT 356 377 LRR 12.
REPEAT 380 400 LRR 13.
REPEAT 403 424 LRR 14.
REPEAT 426 448 LRR 15.
REPEAT 449 470 LRR 16.
REPEAT 472 494 LRR 17.
REPEAT 495 516 LRR 18.
REPEAT 518 540 LRR 19.
REPEAT 542 563 LRR 20.
VAR_SEQ 234 279 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038188.
VARIANT 2 2 S -> G (in NSLH1; creates a N-
myristoylation site, resulting in
myristoylation of the protein and
aberrant targeting to the plasma
membrane; dbSNP:rs267607048).
{ECO:0000269|PubMed:19684605,
ECO:0000269|PubMed:23918763}.
/FTId=VAR_060199.
VARIANT 173 173 M -> I (in NSLH1; significantly decreases
ERK1/2 activity; does not affect
cytoplasm and nucleus localization; does
not affect SHOC2-MRAS-RAF1 complex
assembly; impairs interaction with
phosphatase 1c; dbSNP:rs730881020).
{ECO:0000269|PubMed:25137548}.
/FTId=VAR_074030.
CONFLICT 475 475 K -> E (in Ref. 4; BAF85522).
{ECO:0000305}.
CONFLICT 535 535 F -> L (in Ref. 3; BAA74885).
{ECO:0000305}.
SEQUENCE 582 AA; 64888 MW; F3F828646642A855 CRC64;
MSSSLGKEKD SKEKDPKVPS AKEREKEAKA SGGFGKESKE KEPKTKGKDA KDGKKDSSAA
QPGVAFSVDN TIKRPNPAPG TRKKSSNAEV IKELNKCREE NSMRLDLSKR SIHILPSSIK
ELTQLTELYL YSNKLQSLPA EVGCLVNLMT LALSENSLTS LPDSLDNLKK LRMLDLRHNK
LREIPSVVYR LDSLTTLYLR FNRITTVEKD IKNLSKLSML SIRENKIKQL PAEIGELCNL
ITLDVAHNQL EHLPKEIGNC TQITNLDLQH NELLDLPDTI GNLSSLSRLG LRYNRLSAIP
RSLAKCSALE ELNLENNNIS TLPESLLSSL VKLNSLTLAR NCFQLYPVGG PSQFSTIYSL
NMEHNRINKI PFGIFSRAKV LSKLNMKDNQ LTSLPLDFGT WTSMVELNLA TNQLTKIPED
VSGLVSLEVL ILSNNLLKKL PHGLGNLRKL RELDLEENKL ESLPNEIAYL KDLQKLVLTN
NQLTTLPRGI GHLTNLTHLG LGENLLTHLP EEIGTLENLE ELYLNDNPNL HSLPFELALC
SKLSIMSIEN CPLSHLPPQI VAGGPSFIIQ FLKMQGPYRA MV


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SHOC2_MOUSE ELISA Kit FOR Leucine-rich repeat protein SHOC-2; organism: Mouse; gene name: Shoc2 96T
EIAAB14615 Afh,Fbl3a,F-box and leucine-rich repeat protein 3A,F-box_LRR-repeat protein 3,F-box_LRR-repeat protein 3A,Fbxl3,Fbxl3a,Mouse,Mus musculus,Ovtm,Protein after-hours,Protein overtime
EIAAB14621 FBL4,FBL5,F-box and leucine-rich repeat protein 5,F-box protein FBL4_FBL5,F-box_LRR-repeat protein 5,FBXL5,FLR1,Homo sapiens,Human,p45SKP2-like protein
20-372-60235 F-box and leucine-rich repeat protein 4 (FBXL4) - Mouse monoclonal anti-human FBXL4 antibody; F-box and leucine-rich repeat protein 4; F-box protein FBL4_FBL5 Monoclonal 0.1 mg
EIAAB30918 Homo sapiens,Human,KIAA0931,PH domain leucine-rich repeat-containing protein phosphatase 2,PH domain leucine-rich repeat-containing protein phosphatase-like,PHLPP2,PHLPPL,PHLPP-like
EIAAB14613 FBL2,FBL3,F-box and leucine-rich repeat protein 2,F-box protein FBL2_FBL3,F-box_LRR-repeat protein 2,FBXL2,Homo sapiens,Human
EIAAB14617 FBL4,FBL5,F-box and leucine-rich repeat protein 4,F-box protein FBL4_FBL5,F-box_LRR-repeat protein 4,FBXL4,Homo sapiens,Human


 

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