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Protein FAM83H

 FA83H_HUMAN             Reviewed;        1179 AA.
Q6ZRV2; A0JLS2; Q8N4W0;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
28-MAR-2018, entry version 105.
RecName: Full=Protein FAM83H {ECO:0000305};
Name=FAM83H {ECO:0000312|HGNC:HGNC:24797};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-1179.
TISSUE=Testis;
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 MRNA] OF 861-1179.
TISSUE=Placenta, and Prostate;
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1003, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[5]
FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN AI3A.
PubMed=18252228; DOI=10.1016/j.ajhg.2007.09.020;
Kim J.-W., Lee S.-K., Lee Z.H., Park J.-C., Lee K.-E., Lee M.-H.,
Park J.-T., Seo B.-M., Hu J.C.-C., Simmer J.P.;
"FAM83H mutations in families with autosomal-dominant hypocalcified
amelogenesis imperfecta.";
Am. J. Hum. Genet. 82:489-494(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; SER-647; SER-785
AND SER-1003, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647; SER-881; THR-883;
SER-892; SER-903; SER-936; SER-945; SER-1003; SER-1024 AND SER-1025,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; SER-914 AND
SER-1003, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-465; SER-523; SER-647;
SER-759; SER-785; SER-870; SER-881; SER-892; SER-903; SER-914;
SER-936; SER-945; SER-1003; THR-1040 AND SER-1048, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
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).
[11]
FUNCTION, INTERACTION WITH CSNK1A1 AND KRT18, SUBCELLULAR LOCATION,
REGION, AND MUTAGENESIS OF PHE-251 AND PHE-274.
PubMed=23902688; DOI=10.1242/jcs.129684;
Kuga T., Kume H., Kawasaki N., Sato M., Adachi J., Shiromizu T.,
Hoshino I., Nishimori T., Matsubara H., Tomonaga T.;
"A novel mechanism of keratin cytoskeleton organization through casein
kinase Ialpha and FAM83H in colorectal cancer.";
J. Cell Sci. 126:4721-4731(2013).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-514; SER-516;
SER-523; SER-647; SER-667; SER-785; SER-870; SER-881; SER-892;
SER-903; SER-914; SER-925; SER-936; SER-1003; SER-1025 AND SER-1147,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; THR-756; SER-813;
SER-914; SER-1003 AND SER-1068, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
VARIANT AI3A CYS-557.
PubMed=26142250; DOI=10.1016/j.archoralbio.2015.06.016;
Urzua B., Martinez C., Ortega-Pinto A., Adorno D., Morales-Bozo I.,
Riadi G., Jara L., Plaza A., Lefimil C., Lozano C., Reyes M.;
"Novel missense mutation of the FAM83H gene causes retention of
amelogenin and a mild clinical phenotype of hypocalcified enamel.";
Arch. Oral Biol. 60:1356-1367(2015).
-!- FUNCTION: May play a major role in the structural organization and
calcification of developing enamel (PubMed:18252228). May play a
role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to
keratin filaments. Thereby, it may regulate epithelial cell
migration (PubMed:23902688). {ECO:0000269|PubMed:18252228,
ECO:0000269|PubMed:23902688}.
-!- SUBUNIT: Interacts with CSNK1A1; recruits CSNK1A1 to keratin
filaments. Interacts with KRT18 and probably other keratins.
{ECO:0000269|PubMed:23902688}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:23902688}. Note=Colocalizes with keratin
filaments. {ECO:0000269|PubMed:23902688}.
-!- TISSUE SPECIFICITY: Expressed in the tooth follicle.
{ECO:0000269|PubMed:18252228}.
-!- DISEASE: Amelogenesis imperfecta 3A (AI3A) [MIM:130900]: An
autosomal dominant hypomineralized form of amelogenesis
imperfecta, a defect of enamel formation. AI3A is characterized by
enamel of normal thickness but soft and with cheesy consistency.
Enamel is lost from tooth soon after eruption.
{ECO:0000269|PubMed:18252228, ECO:0000269|PubMed:26142250}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the FAM83 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC87207.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AC105219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK127960; BAC87207.1; ALT_INIT; mRNA.
EMBL; BC007264; AAH07264.1; -; mRNA.
EMBL; BC033256; AAH33256.1; -; mRNA.
CCDS; CCDS6410.2; -.
RefSeq; NP_940890.3; NM_198488.3.
RefSeq; XP_005250946.1; XM_005250889.3.
UniGene; Hs.67776; -.
UniGene; Hs.713170; -.
ProteinModelPortal; Q6ZRV2; -.
SMR; Q6ZRV2; -.
BioGrid; 130292; 66.
IntAct; Q6ZRV2; 33.
MINT; Q6ZRV2; -.
STRING; 9606.ENSP00000373565; -.
iPTMnet; Q6ZRV2; -.
PhosphoSitePlus; Q6ZRV2; -.
SwissPalm; Q6ZRV2; -.
BioMuta; FAM83H; -.
DMDM; 296439349; -.
EPD; Q6ZRV2; -.
MaxQB; Q6ZRV2; -.
PaxDb; Q6ZRV2; -.
PeptideAtlas; Q6ZRV2; -.
PRIDE; Q6ZRV2; -.
Ensembl; ENST00000388913; ENSP00000373565; ENSG00000180921.
Ensembl; ENST00000612192; ENSP00000478790; ENSG00000273889.
GeneID; 286077; -.
KEGG; hsa:286077; -.
UCSC; uc064rej.1; human.
CTD; 286077; -.
DisGeNET; 286077; -.
EuPathDB; HostDB:ENSG00000180921.6; -.
GeneCards; FAM83H; -.
H-InvDB; HIX0025555; -.
HGNC; HGNC:24797; FAM83H.
HPA; HPA024505; -.
HPA; HPA024604; -.
MalaCards; FAM83H; -.
MIM; 130900; phenotype.
MIM; 611927; gene.
neXtProt; NX_Q6ZRV2; -.
OpenTargets; ENSG00000180921; -.
Orphanet; 100032; Hypocalcified amelogenesis imperfecta.
PharmGKB; PA144596434; -.
eggNOG; ENOG410IEPN; Eukaryota.
eggNOG; ENOG410YB0T; LUCA.
GeneTree; ENSGT00760000119168; -.
HOGENOM; HOG000112488; -.
HOVERGEN; HBG107907; -.
InParanoid; Q6ZRV2; -.
OMA; EMDAFKR; -.
OrthoDB; EOG091G00UI; -.
PhylomeDB; Q6ZRV2; -.
TreeFam; TF330777; -.
GeneWiki; FAM83H; -.
GenomeRNAi; 286077; -.
PRO; PR:Q6ZRV2; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000180921; -.
CleanEx; HS_FAM83H; -.
ExpressionAtlas; Q6ZRV2; baseline and differential.
Genevisible; Q6ZRV2; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:1990254; F:keratin filament binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0044380; P:protein localization to cytoskeleton; IMP:UniProtKB.
InterPro; IPR012461; FAM83.
PANTHER; PTHR16181; PTHR16181; 1.
Pfam; PF07894; DUF1669; 1.
1: Evidence at protein level;
Amelogenesis imperfecta; Biomineralization; Complete proteome;
Cytoplasm; Cytoskeleton; Disease mutation; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 1179 Protein FAM83H.
/FTId=PRO_0000324488.
REGION 1 286 Mediates interaction with CSNK1A1 and is
required for FAM83H activity in keratin
cytoskeleton organization.
{ECO:0000269|PubMed:23902688}.
MOD_RES 465 465 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 514 514 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 516 516 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 647 647 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 667 667 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 756 756 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 759 759 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 785 785 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 813 813 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 870 870 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 881 881 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 883 883 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 892 892 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 894 894 Phosphothreonine.
{ECO:0000250|UniProtKB:Q148V8}.
MOD_RES 903 903 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 914 914 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 925 925 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 936 936 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 945 945 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 1003 1003 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1009 1009 Phosphoserine.
{ECO:0000250|UniProtKB:Q148V8}.
MOD_RES 1024 1024 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1025 1025 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1040 1040 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1048 1048 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1068 1068 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1147 1147 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 201 201 Q -> H (in dbSNP:rs9969600).
/FTId=VAR_062189.
VARIANT 557 557 G -> C (in AI3A; mild form;
dbSNP:rs312262803).
{ECO:0000269|PubMed:26142250}.
/FTId=VAR_073954.
MUTAGEN 251 251 F->A: No effect on interaction with
CSNK1A1 and function in keratin
cytoskeleton organization.
{ECO:0000269|PubMed:23902688}.
MUTAGEN 274 274 F->A: Decreased interaction with CSNK1A1
and loss of function in keratin
cytoskeleton organization.
{ECO:0000269|PubMed:23902688}.
CONFLICT 605 605 E -> V (in Ref. 2; BAC87207).
{ECO:0000305}.
SEQUENCE 1179 AA; 127122 MW; D35A1822D8E517F0 CRC64;
MARRSQSSSQ GDNPLAPGYL PPHYKEYYRL AVDALAEGGS EAYSRFLATE GAPDFLCPEE
LEHVSRHLRP PQYVTREPPE GSLLDVDMDG SSGTYWPVNS DQAVPELDLG WPLTFGFQGT
EVTTLVQPPP PDSPSIKDEA RRMIRSAQQV VAVVMDMFTD VDLLSEVLEA AARRVPVYIL
LDEMNAQHFL DMADKCRVNL QHVDFLRVRT VAGPTYYCRT GKSFKGHVKE KFLLVDCAVV
MSGSYSFMWS FEKIHRSLAH VFQGELVSSF DEEFRILFAQ SEPLVPSAAA LARMDAYALA
PYAGAGPLVG VPGVGAPTPF SFPKRAHLLF PPPREEGLGF PSFLDPDRHF LSAFRREEPP
RMPGGALEPH AGLRPLSRRL EAEAGPAGEL AGARGFFQAR HLEMDAFKRH SFATEGAGAV
ENFAAARQVS RQTFLSHGDD FRFQTSHFHR DQLYQQQYQW DPQLTPARPQ GLFEKLRGGR
AGFADPDDFT LGAGPRFPEL GPDGHQRLDY VPSSASREVR HGSDPAFAPG PRGLEPSGAP
RPNLTQRFPC QAAARPGPDP APEAEPERRG GPEGRAGLRR WRLASYLSGC HGEDGGDDGL
PAPMEAEAYE DDVLAPGGRA PAGDLLPSAF RVPAAFPTKV PVPGPGSGGN GPEREGPEEP
GLAKQDSFRS RLNPLVQRSS RLRSSLIFST SQAEGAAGAA AATEKVQLLH KEQTVSETLG
PGGEAVRSAA STKVAELLEK YKGPARDPGG GAGAITVASH SKAVVSQAWR EEVAAPGAVG
GERRSLESCL LDLRDSFAQQ LHQEAERQPG AASLTAAQLL DTLGRSGSDR LPSRFLSAQS
HSTSPQGLDS PLPLEGSGAH QVLHNESKGS PTSAYPERKG SPTPGFSTRR GSPTTGFIEQ
KGSPTSAYPE RRGSPVPPVP ERRSSPVPPV PERRGSLTLT ISGESPKAGP AEEGPSGPME
VLRKGSLRLR QLLSPKGERR MEDEGGFPVP QENGQPESPR RLSLGQGDST EAATEERGPR
ARLSSATANA LYSSNLRDDT KAILEQISAH GQKHRAVPAP SPGPTHNSPE LGRPPAAGVL
APDMSDKDKC SAIFRSDSLG TQGRLSRTLP ASAEERDRLL RRMESMRKEK RVYSRFEVFC
KKEEASSPGA GEGPAEEGTR DSKVGKFVPK ILGTFKSKK


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053237A Fam83h 250ul
044964A Fam83h 250ul
i007445 FAM83H-set siRNA_Lentivectors 4x500ng
i007445a FAM83H siRNA_Lentivectors 500ng
i007445b FAM83H siRNA_Lentivectors 500ng
i007445d FAM83H siRNA_Lentivectors 500ng
i007445c FAM83H siRNA_Lentivectors 500ng
MT-h07425 FAM83H 3&_39;UTR Lenti-reporter-Luc Vector 1ug
bs-16018R-HRP Rabbit Anti-FAM83H Polyclonal Antibody 100ul
bs-16018R Rabbit Anti-FAM83H Polyclonal Antibody 100ul
FAM84B FAM83H Gene family with sequence similarity 83, member H
bs-16018R-Biotin Rabbit Anti-FAM83H Polyclonal Antibody 100ul
FAM83H FAM83F Gene family with sequence similarity 83, member F
CSB-EL008346MO Mouse family with sequence similarity 83, member H (FAM83H) ELISA kit, Species Mouse, Sample Type serum, plasma 96T


 

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