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Protein lin-28 homolog B (Lin-28B)

 LN28B_HUMAN             Reviewed;         250 AA.
Q6ZN17; A1L165; B2RPN6; Q5TCM4;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=Protein lin-28 homolog B;
Short=Lin-28B;
Name=LIN28B; Synonyms=CSDD2;
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).
Moss E.G., Kemper K.;
"Expression of Lin28A and Lin28B in post-implantation mouse embryos.";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Teratocarcinoma;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[6]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INDUCTION.
PubMed=16971064; DOI=10.1016/j.gene.2006.07.011;
Guo Y., Chen Y., Ito H., Watanabe A., Ge X., Kodama T., Aburatani H.;
"Identification and characterization of lin-28 homolog B (LIN28B) in
human hepatocellular carcinoma.";
Gene 384:51-61(2006).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND RNA-BINDING.
PubMed=18951094; DOI=10.1016/j.molcel.2008.09.014;
Heo I., Joo C., Cho J., Ha M., Han J., Kim V.N.;
"Lin28 mediates the terminal uridylation of let-7 precursor
MicroRNA.";
Mol. Cell 32:276-284(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
FUNCTION, AND RNA-BINDING.
PubMed=19703396; DOI=10.1016/j.cell.2009.08.002;
Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H.,
Han J., Kim V.N.;
"TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through
pre-microRNA uridylation.";
Cell 138:696-708(2009).
[10]
POSSIBLE INVOLVEMENT IN CANCERS.
PubMed=19483683; DOI=10.1038/ng.392;
Viswanathan S.R., Powers J.T., Einhorn W., Hoshida Y., Ng T.L.,
Toffanin S., O'Sullivan M., Lu J., Phillips L.A., Lockhart V.L.,
Shah S.P., Tanwar P.S., Mermel C.H., Beroukhim R., Azam M.,
Teixeira J., Meyerson M., Hughes T.P., Llovet J.M., Radich J.,
Mullighan C.G., Golub T.R., Sorensen P.H., Daley G.Q.;
"Lin28 promotes transformation and is associated with advanced human
malignancies.";
Nat. Genet. 41:843-848(2009).
[11]
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).
[12]
FUNCTION IN PRE-LET-7 REPRESSION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=22118463; DOI=10.1016/j.cell.2011.10.039;
Piskounova E., Polytarchou C., Thornton J.E., LaPierre R.J.,
Pothoulakis C., Hagan J.P., Iliopoulos D., Gregory R.I.;
"Lin28A and Lin28B inhibit let-7 microRNA biogenesis by distinct
mechanisms.";
Cell 147:1066-1079(2011).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-96; SER-105;
SER-110 AND SER-203, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 24-111, AND ZINC KNUCKLE
DOMAIN.
PubMed=22570413; DOI=10.1093/nar/gks355;
Mayr F., Schutz A., Doge N., Heinemann U.;
"The Lin28 cold-shock domain remodels pre-let-7 microRNA.";
Nucleic Acids Res. 40:7492-7506(2012).
-!- FUNCTION: Suppressor of microRNA (miRNA) biogenesis, including
that of let-7 and possibly of miR107, miR-143 and miR-200c. Binds
primary let-7 transcripts (pri-let-7), including pri-let-7g and
pri-let-7a-1, and sequester them in the nucleolus, away from the
microprocessor complex, hence preventing their processing into
mature miRNA (PubMed:22118463). Does not act on pri-miR21
(PubMed:22118463). The repression of let-7 expression is required
for normal development and contributes to maintain the pluripotent
state of embryonic stem cells by preventing let-7-mediated
differentiation. When overexpressed, recruits ZCCHC11/TUT4
uridylyltransferase to pre-let-7 transcripts, leading to their
terminal uridylation and degradation (PubMed:19703396). This
activity might not be relevant in vivo, as LIN28B-mediated
inhibition of let-7 miRNA maturation appears to be ZCCHC11-
independent (PubMed:22118463). Interaction with target pre-miRNAs
occurs via an 5'-GGAG-3' motif in the pre-miRNA terminal loop.
Mediates MYC-induced let-7 repression (By similarity). When
overexpressed, isoform 1 stimulates growth of the breast
adenocarcinoma cell line MCF-7. Isoform 2 has no effect on cell
growth. {ECO:0000250|UniProtKB:Q45KJ6,
ECO:0000269|PubMed:16971064, ECO:0000269|PubMed:18951094,
ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:22118463}.
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus
{ECO:0000269|PubMed:22118463}. Cytoplasm
{ECO:0000269|PubMed:16971064}. Note=Predominantly nucleolar
(PubMed:22118463). In Huh7 cells, predominantly cytoplasmic, with
only a subset of cells exhibiting strong nuclear staining;
however, the specificity of the polyclonal antibody used in these
experiments has not been not documented (PubMed:16971064).
{ECO:0000269|PubMed:16971064, ECO:0000269|PubMed:22118463}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6ZN17-1; Sequence=Displayed;
Name=2; Synonyms=LIN28BS;
IsoId=Q6ZN17-2; Sequence=VSP_027207;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed at high levels in the placenta and,
at mucher lower, in testis and fetal liver (PubMed:16971064).
Isoform 1 is only detected in placenta and in moderately and
poorly differentiated hepatocellular carcinoma cells (at protein
level). Isoform 2 is detected in fetal liver, non-tumor liver
tissues, as well as well-differentiated tumor tissues (at protein
level). Tends to be up-regulated in triple-negative
(ER-,PR-,HER2-) breast tumors, as well as in liver, ovarian, and
thyroid carcinomas (PubMed:22118463).
{ECO:0000269|PubMed:16971064, ECO:0000269|PubMed:22118463}.
-!- INDUCTION: Might be negatively regulated by the microRNA let-7b.
{ECO:0000269|PubMed:16971064}.
-!- DOMAIN: The tandem zinc fingers, also referred as zinc knuckle
domain (ZKD), mediate specific binding to the GGAG/GGUG motif
while the CSD shows only limited pyrimidine-rich sequence
specificity. Both domains bind single-stranded nucleic acids.
-!- SIMILARITY: Belongs to the lin-28 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/LIN28BID45723ch6q16.html";
-----------------------------------------------------------------------
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EMBL; DQ127228; AAZ38897.1; -; mRNA.
EMBL; AK131411; BAD18558.1; -; mRNA.
EMBL; Z95329; CAI21661.2; -; Genomic_DNA.
EMBL; AL135911; CAI21661.2; JOINED; Genomic_DNA.
EMBL; AL135911; CAI20969.2; -; Genomic_DNA.
EMBL; Z95329; CAI20969.2; JOINED; Genomic_DNA.
EMBL; CH471051; EAW48434.1; -; Genomic_DNA.
EMBL; BC127712; AAI27713.1; -; mRNA.
EMBL; BC127713; AAI27714.1; -; mRNA.
EMBL; BC137526; AAI37527.1; -; mRNA.
EMBL; BC137527; AAI37528.1; -; mRNA.
EMBL; BC141960; AAI41961.1; -; mRNA.
CCDS; CCDS34504.1; -. [Q6ZN17-1]
RefSeq; NP_001004317.1; NM_001004317.3. [Q6ZN17-1]
UniGene; Hs.23616; -.
PDB; 4A4I; X-ray; 1.95 A; A/B=24-111.
PDBsum; 4A4I; -.
ProteinModelPortal; Q6ZN17; -.
SMR; Q6ZN17; -.
BioGrid; 133142; 35.
IntAct; Q6ZN17; 5.
STRING; 9606.ENSP00000344401; -.
iPTMnet; Q6ZN17; -.
PhosphoSitePlus; Q6ZN17; -.
BioMuta; LIN28B; -.
DMDM; 74758701; -.
EPD; Q6ZN17; -.
MaxQB; Q6ZN17; -.
PaxDb; Q6ZN17; -.
PeptideAtlas; Q6ZN17; -.
PRIDE; Q6ZN17; -.
Ensembl; ENST00000345080; ENSP00000344401; ENSG00000187772. [Q6ZN17-1]
GeneID; 389421; -.
KEGG; hsa:389421; -.
UCSC; uc003pqv.2; human. [Q6ZN17-1]
CTD; 389421; -.
DisGeNET; 389421; -.
EuPathDB; HostDB:ENSG00000187772.6; -.
GeneCards; LIN28B; -.
HGNC; HGNC:32207; LIN28B.
HPA; HPA036630; -.
HPA; HPA061745; -.
MalaCards; LIN28B; -.
MIM; 611044; gene.
neXtProt; NX_Q6ZN17; -.
OpenTargets; ENSG00000187772; -.
Orphanet; 635; Neuroblastoma.
PharmGKB; PA142671543; -.
eggNOG; KOG3070; Eukaryota.
eggNOG; COG1278; LUCA.
GeneTree; ENSGT00880000137959; -.
HOGENOM; HOG000047091; -.
HOVERGEN; HBG081922; -.
InParanoid; Q6ZN17; -.
KO; K18754; -.
OrthoDB; EOG091G0RTY; -.
PhylomeDB; Q6ZN17; -.
TreeFam; TF316240; -.
SignaLink; Q6ZN17; -.
GenomeRNAi; 389421; -.
PRO; PR:Q6ZN17; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000187772; -.
CleanEx; HS_LIN28B; -.
ExpressionAtlas; Q6ZN17; baseline and differential.
Genevisible; Q6ZN17; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0010587; P:miRNA catabolic process; IMP:UniProtKB.
GO; GO:0031054; P:pre-miRNA processing; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
GO; GO:0031123; P:RNA 3'-end processing; IMP:UniProtKB.
CDD; cd04458; CSP_CDS; 1.
Gene3D; 4.10.60.10; -; 3.
InterPro; IPR011129; CSD.
InterPro; IPR002059; CSP_DNA-bd.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF00313; CSD; 1.
Pfam; PF00098; zf-CCHC; 2.
PRINTS; PR00050; COLDSHOCK.
SMART; SM00357; CSP; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
RNA-binding; RNA-mediated gene silencing; Zinc; Zinc-finger.
CHAIN 1 250 Protein lin-28 homolog B.
/FTId=PRO_0000253793.
DOMAIN 29 102 CSD.
ZN_FING 127 144 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 149 166 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
MOTIF 112 125 Bipartite nuclear localization signal.
{ECO:0000269|PubMed:22118463}.
MOTIF 239 250 Nucleolar localization signal.
{ECO:0000269|PubMed:22118463}.
METAL 129 129 Zinc 1. {ECO:0000250}.
METAL 132 132 Zinc 1. {ECO:0000250}.
METAL 137 137 Zinc 1. {ECO:0000250}.
METAL 142 142 Zinc 1. {ECO:0000250}.
METAL 151 151 Zinc 2. {ECO:0000250}.
METAL 154 154 Zinc 2. {ECO:0000250}.
METAL 159 159 Zinc 2. {ECO:0000250}.
METAL 164 164 Zinc 2. {ECO:0000250}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 70 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_027207.
STRAND 28 38 {ECO:0000244|PDB:4A4I}.
TURN 39 42 {ECO:0000244|PDB:4A4I}.
STRAND 43 51 {ECO:0000244|PDB:4A4I}.
STRAND 54 65 {ECO:0000244|PDB:4A4I}.
HELIX 66 68 {ECO:0000244|PDB:4A4I}.
STRAND 71 74 {ECO:0000244|PDB:4A4I}.
STRAND 82 88 {ECO:0000244|PDB:4A4I}.
STRAND 95 101 {ECO:0000244|PDB:4A4I}.
HELIX 102 104 {ECO:0000244|PDB:4A4I}.
SEQUENCE 250 AA; 27084 MW; DEF2920C5F1D0BBD CRC64;
MAEGGASKGG GEEPGKLPEP AEEESQVLRG TGHCKWFNVR MGFGFISMIN REGSPLDIPV
DVFVHQSKLF MEGFRSLKEG EPVEFTFKKS SKGLESIRVT GPGGSPCLGS ERRPKGKTLQ
KRKPKGDRCY NCGGLDHHAK ECSLPPQPKK CHYCQSIMHM VANCPHKNVA QPPASSQGRQ
EAESQPCTST LPREVGGGHG CTSPPFPQEA RAEISERSGR SPQEASSTKS SIAPEEQSKK
GPSVQKRKKT


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EIAAB34392 Fox-1 homolog B,Fox-1 homolog Fxh,Fox2,Fxh,Hexaribonucleotide-binding protein 2,Hrnbp2,Mouse,Mus musculus,Rbfox2,Rbm9,RNA binding protein fox-1 homolog 2,RNA-binding motif protein 9,RNA-binding protei
U1313b CLIA Bos taurus,Bovine,HBV X-interacting protein homolog,HBX-interacting protein homolog,HBXIP,Hepatitis B virus X-interacting protein homolog 96T
U1313m CLIA HBV X-interacting protein homolog,HBX-interacting protein homolog,Hbxip,Hepatitis B virus X-interacting protein homolog,Mouse,Mus musculus,Xip 96T
E1313b ELISA Bos taurus,Bovine,HBV X-interacting protein homolog,HBX-interacting protein homolog,HBXIP,Hepatitis B virus X-interacting protein homolog 96T
E1313m ELISA kit HBV X-interacting protein homolog,HBX-interacting protein homolog,Hbxip,Hepatitis B virus X-interacting protein homolog,Mouse,Mus musculus,Xip 96T
E1313b ELISA kit Bos taurus,Bovine,HBV X-interacting protein homolog,HBX-interacting protein homolog,HBXIP,Hepatitis B virus X-interacting protein homolog 96T
E1313m ELISA HBV X-interacting protein homolog,HBX-interacting protein homolog,Hbxip,Hepatitis B virus X-interacting protein homolog,Mouse,Mus musculus,Xip 96T
EIAAB05142 Cage1,CAGE-1,Cancer_testis antigen 3 homolog,Cancer-associated gene 1 protein homolog,CT3 homolog,Ctag3,Mouse,Mus musculus
EIAAB05141 Cage1,CAGE-1,Cancer_testis antigen 3 homolog,Cancer-associated gene 1 protein homolog,CT3 homolog,Ctag3,Rat,Rattus norvegicus
18-003-43993 LAG1 longevity assurance homolog 4 - Translocating chain-associating membrane protein homolog 1; TRAM homolog 1 Polyclonal 0.1 mg Protein A
EIAAB08651 Coenzyme Q biosynthesis protein 7 homolog,COQ7,Homo sapiens,Human,Timing protein clk-1 homolog,Ubiquinone biosynthesis protein COQ7 homolog
EIAAB40490 Homo sapiens,Human,N-Sec1,p67,Protein unc-18 homolog 1,Protein unc-18 homolog A,STXBP1,Syntaxin-binding protein 1,Unc18-1,UNC18A,Unc-18A
EIAAB34215 Dp1,GP106,Mouse,Mus musculus,Polyposis locus protein 1 homolog,Protein TB2 homolog,Receptor expression-enhancing protein 5,Reep5
EIAAB38308 Homo sapiens,Human,KIAA0862,Leucine-rich repeat protein SHOC-2,Protein soc-2 homolog,Protein sur-8 homolog,SHOC2
EIAAB40489 N-Sec1,p67,Protein unc-18 homolog 1,Protein unc-18 homolog A,Rat,Rattus norvegicus,rbSec1,Stxbp1,Syntaxin-binding protein 1,Unc18-1,Unc18a,Unc-18A
EIAAB40497 Mouse,Munc18-2,Mus musculus,MUSEC1,Protein unc-18 homolog 2,Protein unc-18 homolog B,Stxbp2,Syntaxin-binding protein 2,Unc18-2,Unc18b,Unc-18B
EIAAB13308 CTF7 homolog 1,ECO1 homolog 1,EFO1,EFO1p,ESCO1,ESO1 homolog 1,Establishment factor-like protein 1,Establishment of cohesion 1 homolog 1,hEFO1,Homo sapiens,Human,KIAA1911,N-acetyltransferase ESCO1
E1313p ELISA HBV X-interacting protein homolog,HBX-interacting protein homolog,HBXIP,Hepatitis B virus X-interacting protein homolog,Pig,Sus scrofa 96T
E1313p ELISA kit HBV X-interacting protein homolog,HBX-interacting protein homolog,HBXIP,Hepatitis B virus X-interacting protein homolog,Pig,Sus scrofa 96T


 

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