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Protein FAM107A (Down-regulated in renal cell carcinoma 1) (Protein TU3A)

 F107A_HUMAN             Reviewed;         144 AA.
O95990; B3KNQ4; B7ZAY5; J3KR61; Q96NH4;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
12-SEP-2018, entry version 136.
RecName: Full=Actin-associated protein FAM107A {ECO:0000305};
AltName: Full=Down-regulated in renal cell carcinoma 1 {ECO:0000303|PubMed:10564580};
AltName: Full=Protein TU3A {ECO:0000303|PubMed:10702698};
Name=FAM107A {ECO:0000312|HGNC:HGNC:30827};
Synonyms=DRR1 {ECO:0000303|PubMed:10564580}, TU3A;
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), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND VARIANTS MET-15 AND LEU-19.
TISSUE=Ovary;
PubMed=10564580;
DOI=10.1002/(SICI)1098-2264(200001)27:1<1::AID-GCC1>3.0.CO;2-6;
Wang L., Darling J., Zhang J.-S., Liu W., Qian J., Bostwick D.,
Hartmann L., Jenkins R., Bardenhauer W., Schutte J., Opalka B.,
Smith D.I.;
"Loss of expression of the DRR1 gene at chromosomal segment 3p21.1 in
renal cell carcinoma.";
Genes Chromosomes Cancer 27:1-10(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10702698;
Yamato T., Orikasa K., Fukushige S., Orikasa S., Horii A.;
"Isolation and characterization of the novel gene, TU3A, in a commonly
deleted region on 3p14.3->p14.2 in renal cell carcinoma.";
Cytogenet. Cell Genet. 87:291-295(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
TISSUE=Fetal brain;
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=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[7]
SUBCELLULAR LOCATION.
PubMed=11256614; DOI=10.1093/embo-reports/kvd058;
Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.;
"Systematic subcellular localization of novel proteins identified by
large-scale cDNA sequencing.";
EMBO Rep. 1:287-292(2000).
[8]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
48-HIS--GLU-50; 65-PRO-GLU-66 AND 122-PRO-GLU-123.
PubMed=20543869; DOI=10.1038/onc.2010.216;
Le P.U., Angers-Loustau A., de Oliveira R.M., Ajlan A., Brassard C.L.,
Dudley A., Brent H., Siu V., Trinh G., Moelenkamp G., Wang J.,
Seyed Sadr M., Bedell B., Del Maestro R.F., Petrecca K.;
"DRR drives brain cancer invasion by regulating cytoskeletal-focal
adhesion dynamics.";
Oncogene 29:4636-4647(2010).
[9]
INTERACTION WITH ACTB AND PRDX1.
PubMed=21969592; DOI=10.1073/pnas.1103318108;
Schmidt M.V., Schuelke J.P., Liebl C., Stiess M., Avrabos C., Bock J.,
Wochnik G.M., Davies H.A., Zimmermann N., Scharf S.H., Truembach D.,
Wurst W., Zieglgaensberger W., Turck C., Holsboer F., Stewart M.G.,
Bradke F., Eder M., Mueller M.B., Rein T.;
"Tumor suppressor down-regulated in renal cell carcinoma 1 (DRR1) is a
stress-induced actin bundling factor that modulates synaptic efficacy
and cognition.";
Proc. Natl. Acad. Sci. U.S.A. 108:17213-17218(2011).
[10]
FUNCTION, INTERACTION WITH ACTB AND COMMD1, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 65-PRO-GLU-66; 74-ARG--ARG-76; 81-LYS--LYS-84 AND
122-PRO-GLU-123.
PubMed=28604741; DOI=10.1038/onc.2017.181;
Mu P., Akashi T., Lu F., Kishida S., Kadomatsu K.;
"A novel nuclear complex of DRR1, F-actin and COMMD1 involved in NF-
kappaB degradation and cell growth suppression in neuroblastoma.";
Oncogene 36:5745-5756(2017).
-!- FUNCTION: Stress-inducible actin-binding protein that plays a role
in synaptic and cognitive functions by modulating actin
filamentous (F-actin) dynamics. Mediates polymerization of
globular actin to F-actin. Also binds to, stabilizes and bundles
F-actin. Involved in synaptic function by regulating neurite
outgrowth in an actin-dependent manner and for the acquisition of
hippocampus-dependent cognitive function, such as learning and
long-term memory (By similarity). Plays a role in the actin and
microtubule cytoskeleton organization; negatively regulates focal
adhesion (FA) assembly promoting malignant glial cell migration in
an actin-, microtubule- and MAP1A-dependent manner
(PubMed:20543869). Also involved in neuroblastoma G1/S phase cell
cycle progression and cell proliferation inhibition by stimulating
ubiquitination of NF-kappa-B subunit RELA and NF-kappa-B
degradation in a COMMD1- and actin-dependent manner
(PubMed:10564580, PubMed:28604741). May play a role in tumor
development (PubMed:10564580). {ECO:0000250|UniProtKB:Q78TU8,
ECO:0000269|PubMed:10564580, ECO:0000269|PubMed:20543869,
ECO:0000269|PubMed:28604741}.
-!- SUBUNIT: Interacts with ACTB (PubMed:21969592, PubMed:28604741).
Interacts with COMMD1; this interaction stabilizes COMMD1 in the
nucleus (PubMed:28604741). Interacts with MAP1A (PubMed:20543869).
Interacts with PRDX1 (PubMed:21969592). Interacts with F-actin (By
similarity). {ECO:0000250|UniProtKB:Q78TU8,
ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:21969592,
ECO:0000269|PubMed:28604741}.
-!- INTERACTION:
Q96JN2-2:CCDC136; NbExp=3; IntAct=EBI-10192902, EBI-10171416;
A1L4K1:FSD2; NbExp=3; IntAct=EBI-10192902, EBI-5661036;
Q6A162:KRT40; NbExp=3; IntAct=EBI-10192902, EBI-10171697;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-10192902, EBI-741037;
Q9UJV3-2:MID2; NbExp=3; IntAct=EBI-10192902, EBI-10172526;
Q8ND90:PNMA1; NbExp=3; IntAct=EBI-10192902, EBI-302345;
Q6NUQ1:RINT1; NbExp=3; IntAct=EBI-10192902, EBI-726876;
O94972:TRIM37; NbExp=3; IntAct=EBI-10192902, EBI-741602;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-10192902, EBI-739895;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10564580,
ECO:0000269|PubMed:11256614, ECO:0000269|PubMed:20543869,
ECO:0000269|PubMed:28604741}. Cytoplasm, cytoskeleton, stress
fiber {ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:28604741}.
Cell junction, focal adhesion {ECO:0000269|PubMed:20543869}. Cell
projection, ruffle membrane {ECO:0000269|PubMed:20543869}. Cell
junction, synapse {ECO:0000250|UniProtKB:Q78TU8}. Note=Colocalizes
with F-actin and COMMD1 in the nucleus (PubMed:28604741).
Colocalizes with MAP1A along actin stress fibers and membrane
ruffles (PubMed:20543869). {ECO:0000269|PubMed:20543869,
ECO:0000269|PubMed:28604741}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O95990-1; Sequence=Displayed;
Name=2;
IsoId=O95990-2; Sequence=VSP_009232;
Note=May be due to an intron retention. No experimental
confirmation available.;
Name=3;
IsoId=O95990-3; Sequence=VSP_054803;
Name=4;
IsoId=O95990-4; Sequence=VSP_054804;
Note=Ref.4 (BAG51416) sequence is in conflict in position:
26:R->Q. {ECO:0000305};
-!- TISSUE SPECIFICITY: Widely expressed (PubMed:10564580). Expressed
in neurons (PubMed:20543869). Expressed in malignant glial tumors
(PubMed:20543869). Expression is reduced or absent in a number of
cancer cell lines (PubMed:10564580). {ECO:0000269|PubMed:10564580,
ECO:0000269|PubMed:20543869}.
-!- SIMILARITY: Belongs to the FAM107 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FAM107AID42728ch3p14.html";
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EMBL; AF089854; AAD16094.1; -; mRNA.
EMBL; AF089853; AAD16093.1; -; mRNA.
EMBL; AB023810; BAA83072.1; -; Genomic_DNA.
EMBL; AB023811; BAA82845.1; -; mRNA.
EMBL; AL050264; CAB43366.1; -; mRNA.
EMBL; AK054720; BAG51416.1; -; mRNA.
EMBL; AK055443; BAB70924.1; -; mRNA.
EMBL; AK316450; BAH14821.1; -; mRNA.
EMBL; AC116036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC119424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW65380.1; -; Genomic_DNA.
EMBL; BC010561; AAH10561.1; -; mRNA.
CCDS; CCDS2892.1; -. [O95990-1]
CCDS; CCDS63672.1; -. [O95990-3]
CCDS; CCDS63673.1; -. [O95990-4]
PIR; T08666; T08666.
RefSeq; NP_001070246.1; NM_001076778.2. [O95990-1]
RefSeq; NP_001269642.1; NM_001282713.1. [O95990-3]
RefSeq; NP_001269643.1; NM_001282714.1. [O95990-4]
RefSeq; NP_009108.1; NM_007177.3. [O95990-1]
UniGene; Hs.506357; -.
UniGene; Hs.729396; -.
ProteinModelPortal; O95990; -.
BioGrid; 116341; 52.
IntAct; O95990; 31.
STRING; 9606.ENSP00000354270; -.
BioMuta; FAM107A; -.
PaxDb; O95990; -.
PeptideAtlas; O95990; -.
PRIDE; O95990; -.
ProteomicsDB; 51166; -.
ProteomicsDB; 51167; -. [O95990-2]
DNASU; 11170; -.
Ensembl; ENST00000360997; ENSP00000354270; ENSG00000168309. [O95990-1]
Ensembl; ENST00000394481; ENSP00000377991; ENSG00000168309. [O95990-1]
Ensembl; ENST00000447756; ENSP00000400858; ENSG00000168309. [O95990-3]
Ensembl; ENST00000464064; ENSP00000419529; ENSG00000168309. [O95990-2]
Ensembl; ENST00000474531; ENSP00000419124; ENSG00000168309. [O95990-4]
GeneID; 11170; -.
KEGG; hsa:11170; -.
UCSC; uc003dko.5; human. [O95990-1]
CTD; 11170; -.
DisGeNET; 11170; -.
EuPathDB; HostDB:ENSG00000168309.16; -.
GeneCards; FAM107A; -.
HGNC; HGNC:30827; FAM107A.
HPA; HPA055888; -.
MIM; 608295; gene.
neXtProt; NX_O95990; -.
OpenTargets; ENSG00000168309; -.
PharmGKB; PA143485464; -.
eggNOG; ENOG410IX5W; Eukaryota.
eggNOG; ENOG4111Z4D; LUCA.
GeneTree; ENSGT00390000011228; -.
HOGENOM; HOG000048230; -.
HOVERGEN; HBG002824; -.
InParanoid; O95990; -.
OMA; LMNHKRG; -.
PhylomeDB; O95990; -.
TreeFam; TF325943; -.
SIGNOR; O95990; -.
ChiTaRS; FAM107A; human.
GeneWiki; FAM107A; -.
GenomeRNAi; 11170; -.
PRO; PR:O95990; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000168309; Expressed in 223 organ(s), highest expression level in entorhinal cortex.
CleanEx; HS_FAM107A; -.
ExpressionAtlas; O95990; baseline and differential.
Genevisible; O95990; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB.
GO; GO:0050890; P:cognition; ISS:UniProtKB.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:UniProtKB.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; IDA:UniProtKB.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
InterPro; IPR009533; DUF1151.
PANTHER; PTHR16768; PTHR16768; 1.
Pfam; PF06625; DUF1151; 1.
1: Evidence at protein level;
Actin-binding; Alternative splicing; Cell cycle; Cell junction;
Cell membrane; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Growth regulation; Membrane; Nucleus;
Polymorphism; Reference proteome; Stress response; Synapse.
CHAIN 1 144 Actin-associated protein FAM107A.
/FTId=PRO_0000080014.
COILED 66 112 {ECO:0000255}.
MOTIF 74 84 Nuclear localization signal.
{ECO:0000269|PubMed:28604741}.
VAR_SEQ 1 1 M -> MAQRLGEWARGPSDATGLYRAVLLRSAAM (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054803.
VAR_SEQ 1 1 M -> MGAAQGKKKTYSPQARFHSENEKQRRNGSAAM (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054804.
VAR_SEQ 110 144 LEKPPEKEEDHAPEFIKVRENLRRIATLTSEEREL -> VG
DGHPAGTTHPPGLSSREELCCGHS (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_009232.
VARIANT 15 15 L -> M (in ovarian cancer and renal cell
carcinoma cell lines).
{ECO:0000269|PubMed:10564580}.
/FTId=VAR_017238.
VARIANT 19 19 P -> L (in renal cell carcinoma cell
line). {ECO:0000269|PubMed:10564580}.
/FTId=VAR_017239.
VARIANT 89 89 A -> S (in dbSNP:rs1043942).
/FTId=VAR_049016.
VARIANT 141 141 E -> Q (in dbSNP:rs11539086).
/FTId=VAR_049017.
MUTAGEN 48 50 Missing: Increases nuclear and diffused
cytoplasm localization, decreases
interaction with MAP1A, alters actin
cytoskeleton organization and decreases
focal adhesion (FA) disassembly and cell
migration. {ECO:0000269|PubMed:20543869}.
MUTAGEN 65 66 PE->AA: Increases diffused cytoplasm
localization, loss of interaction with
ACTB and colocalization with nuclear F-
actin, decreases COMMD1 protein stability
and ubiquitination of NF-kappa-B subunit
RELA and decreases focal adhesion (FA)
disassembly and cell migration; when
associated with 122-A-A-123.
{ECO:0000269|PubMed:28604741}.
MUTAGEN 74 76 RRR->AAA: Decreases nuclear localization
and ubiquitination of NF-kappa-B subunit
RELA. {ECO:0000269|PubMed:28604741}.
MUTAGEN 81 84 KKKK->AAAA: Decreases nuclear
localization.
{ECO:0000269|PubMed:28604741}.
MUTAGEN 122 123 PE->AA: Increases diffused cytoplasm
localization, loss of interaction with
ACTB and colocalization with nuclear F-
actin, decreases COMMD1 protein stability
and ubiquitination of NF-kappa-B subunit
RELA and decreases focal adhesion (FA)
disassembly and cell migration; when
associated with 65-A-A-66.
{ECO:0000269|PubMed:28604741}.
SEQUENCE 144 AA; 17455 MW; 90C192C723D68A36 CRC64;
MYSEIQRERA DIGGLMARPE YREWNPELIK PKKLLNPVKA SRSHQELHRE LLMNHRRGLG
VDSKPELQRV LEHRRRNQLI KKKKEELEAK RLQCPFEQEL LRRQQRLNQL EKPPEKEEDH
APEFIKVREN LRRIATLTSE EREL


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EIAAB11533 Cell cycle progression restoration gene 3 protein,CPR3,Dj3,DnaJ homolog subfamily A member 2,DNAJA2,Dnj3,HIRA-interacting protein 4,HIRIP4,Homo sapiens,Human,Renal carcinoma antigen NY-REN-14
MEDCLA319-01 Renal Cell Carcinoma Marker, Proximal Nephrogenic Renal Ag.,Carb. dom. of a 200kD gp200, Cl 66.4.C2,Mab anti_Hu; prfn 0.1 ml.
MEDCLA319-1 Renal Cell Carcinoma Marker, Proximal Nephrogenic Renal Ag.,Carb. dom. of a 200kD gp200, Cl 66.4.C2,Mab anti_Hu; prfn 1 ml.
E-EL-MK0438 Monkey TU3A (TU3A Protein) ELISA Kit 96T
E-EL-H0953 Human TU3A (TU3A Protein) ELISA Kit 96T
E-EL-Ch0235 Chicken TU3A (TU3A Protein) ELISA Kit 96T
E-EL-P0551 Porcine TU3A (TU3A Protein) ELISA Kit 96T
20-272-191562 Renal Cell Carcinoma (gp200). prediluted - Mouse monoclonal [SPM314] to Renal Cell Carcinoma (gp200). prediluted Monoclonal 7 ml
18-272-195109 UBE3A - Rabbit polyclonal to UBE3A; EC 6.3.2.-; E6AP ubiquitin-protein ligase; Oncogenic protein-associated protein E6-AP; Human papillomavirus E6-associated protein; Renal carcinoma antigen NY-REN-54 0.05 mg
18-272-195110 UBE3A - Rabbit polyclonal to UBE3A; EC 6.3.2.-; E6AP ubiquitin-protein ligase; Oncogenic protein-associated protein E6-AP; Human papillomavirus E6-associated protein; Renal carcinoma antigen NY-REN-54 0.05 mg
E2195h Cell proliferation-inducing gene 19 protein,Homo sapiens,Human,LDH muscle subunit,LDHA,LDH-A,LDH-M,L-lactate dehydrogenase A chain,PIG19,Renal carcinoma antigen NY-REN-59
TS1109 Human renal clear cell carcinoma (70 cases) and normal renal (10 cases) Tissue Section 1 slide
TA1036 Human renal clear cell carcinoma (70 cases) and normal renal (10 cases) tissues array
TS1068 Human renal clear cell carcinoma (90 cases) and normal renal (10 cases) Tissue Section 1 slide
U2195h CLIA Cell proliferation-inducing gene 19 protein,Homo sapiens,Human,LDH muscle subunit,LDHA,LDH-A,LDH-M,L-lactate dehydrogenase A chain,PIG19,Renal carcinoma antigen NY-REN-59 96T
U2195h CLIA kit Cell proliferation-inducing gene 19 protein,Homo sapiens,Human,LDH muscle subunit,LDHA,LDH-A,LDH-M,L-lactate dehydrogenase A chain,PIG19,Renal carcinoma antigen NY-REN-59 96T
E2195h ELISA Cell proliferation-inducing gene 19 protein,Homo sapiens,Human,LDH muscle subunit,LDHA,LDH-A,LDH-M,L-lactate dehydrogenase A chain,PIG19,Renal carcinoma antigen NY-REN-59 96T


 

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