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

Probable E3 ubiquitin-protein ligase DTX2 (EC 2.3.2.27) (Protein deltex-2) (Deltex2) (hDTX2) (RING finger protein 58) (RING-type E3 ubiquitin transferase DTX2)

 DTX2_HUMAN              Reviewed;         622 AA.
Q86UW9; Q4ZH49; Q6XM87; Q6XM88; Q96H69; Q9H890; Q9P200;
26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 3.
05-DEC-2018, entry version 146.
RecName: Full=Probable E3 ubiquitin-protein ligase DTX2;
EC=2.3.2.27 {ECO:0000250|UniProtKB:Q61010};
AltName: Full=Protein deltex-2;
Short=Deltex2;
Short=hDTX2;
AltName: Full=RING finger protein 58;
AltName: Full=RING-type E3 ubiquitin transferase DTX2 {ECO:0000305};
Name=DTX2; Synonyms=KIAA1528, RNF58;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2),
VARIANT GLU-384, SUBUNIT, AND IN VITRO UBIQUITIN LIGASE ACTIVITY.
PubMed=12670957; DOI=10.1074/jbc.M301157200;
Takeyama K., Aguiar R.C.T., Gu L., He C., Freeman G.J., Kutok J.L.,
Aster J.C., Shipp M.A.;
"The BAL-binding protein BBAP and related Deltex family members
exhibit ubiquitin-protein isopeptide ligase activity.";
J. Biol. Chem. 278:21930-21937(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-421.
Yi Z., Yi T., Wu Z.;
"cDNA cloning, characterization and expression analysis of DTX2, a
human WWE and RING-finger gene, in human embryos.";
DNA Seq. 17:175-180(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
GLU-384 AND ALA-421.
TISSUE=Brain;
PubMed=10819331; DOI=10.1093/dnares/7.2.143;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:143-150(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-421.
TISSUE=Thyroid;
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=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLU-384.
TISSUE=Brain, Lymph, and Muscle;
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=11564735; DOI=10.1074/jbc.M105245200;
Yamamoto N., Yamamoto S., Inagaki F., Kawaichi M., Fukamizu A.,
Kishi N., Matsuno K., Nakamura K., Weinmaster G., Okano H.,
Nakafuku M.;
"Role of Deltex-1 as a transcriptional regulator downstream of the
Notch receptor.";
J. Biol. Chem. 276:45031-45040(2001).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, 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).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[10]
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).
[11]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-213; ARG-215; ARG-233 AND
ARG-256, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Regulator of Notch signaling, a signaling pathway
involved in cell-cell communications that regulates a broad
spectrum of cell-fate determinations. Probably acts both as a
positive and negative regulator of Notch, depending on the
developmental and cell context. Mediates the antineural activity
of Notch, possibly by inhibiting the transcriptional activation
mediated by MATCH1. Functions as a ubiquitin ligase protein in
vitro, suggesting that it may regulate the Notch pathway via some
ubiquitin ligase activity.
-!- CATALYTIC ACTIVITY:
Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-
cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.; EC=2.3.2.27;
Evidence={ECO:0000250|UniProtKB:Q61010};
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homodimer. May form a heterodimer with other members of
the Deltex family. Interacts with NOTCH1.
{ECO:0000250|UniProtKB:Q61010}.
-!- INTERACTION:
O95870:ABHD16A; NbExp=5; IntAct=EBI-740376, EBI-348517;
Q9NXW9:ALKBH4; NbExp=9; IntAct=EBI-740376, EBI-8637516;
Q6P1W5:C1orf94; NbExp=3; IntAct=EBI-740376, EBI-946029;
Q8NI60:COQ8A; NbExp=3; IntAct=EBI-740376, EBI-745535;
Q9NRA8:EIF4ENIF1; NbExp=7; IntAct=EBI-740376, EBI-301024;
Q92567:FAM168A; NbExp=6; IntAct=EBI-740376, EBI-7957930;
Q14192:FHL2; NbExp=6; IntAct=EBI-740376, EBI-701903;
Q8IVS8:GLYCTK; NbExp=5; IntAct=EBI-740376, EBI-748515;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-740376, EBI-618309;
P19113:HDC; NbExp=6; IntAct=EBI-740376, EBI-10200283;
P49639:HOXA1; NbExp=4; IntAct=EBI-740376, EBI-740785;
P37235:HPCAL1; NbExp=3; IntAct=EBI-740376, EBI-749311;
Q9UM19:HPCAL4; NbExp=6; IntAct=EBI-740376, EBI-744820;
Q6P597:KLC3; NbExp=6; IntAct=EBI-740376, EBI-1643885;
Q6PEX3:KRTAP26-1; NbExp=3; IntAct=EBI-740376, EBI-3957672;
P61601:NCALD; NbExp=12; IntAct=EBI-740376, EBI-749635;
P62166:NCS1; NbExp=12; IntAct=EBI-740376, EBI-746987;
Q9H8W4:PLEKHF2; NbExp=3; IntAct=EBI-740376, EBI-742388;
P47897-2:QARS; NbExp=3; IntAct=EBI-740376, EBI-10209725;
Q93062:RBPMS; NbExp=7; IntAct=EBI-740376, EBI-740322;
Q8HWS3:RFX6; NbExp=4; IntAct=EBI-740376, EBI-746118;
Q9BQY4:RHOXF2; NbExp=3; IntAct=EBI-740376, EBI-372094;
Q9UFD9:RIMBP3; NbExp=3; IntAct=EBI-740376, EBI-10182375;
Q96IW7:SEC22A; NbExp=9; IntAct=EBI-740376, EBI-8652744;
Q15437:SEC23B; NbExp=6; IntAct=EBI-740376, EBI-742673;
Q99932:SPAG8; NbExp=3; IntAct=EBI-740376, EBI-954419;
Q9NZD8:SPG21; NbExp=6; IntAct=EBI-740376, EBI-742688;
Q86Y82:STX12; NbExp=5; IntAct=EBI-740376, EBI-2691717;
P63165:SUMO1; NbExp=3; IntAct=EBI-740376, EBI-80140;
Q9BYV2:TRIM54; NbExp=8; IntAct=EBI-740376, EBI-2130429;
Q15654:TRIP6; NbExp=3; IntAct=EBI-740376, EBI-742327;
P51668:UBE2D1; NbExp=6; IntAct=EBI-740376, EBI-743540;
P61077:UBE2D3; NbExp=8; IntAct=EBI-740376, EBI-348268;
Q9Y2X8:UBE2D4; NbExp=11; IntAct=EBI-740376, EBI-745527;
P62760:VSNL1; NbExp=9; IntAct=EBI-740376, EBI-740943;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11564735}.
Nucleus {ECO:0000269|PubMed:11564735}. Note=Predominantly
cytoplasmic. Partially nuclear. {ECO:0000269|PubMed:11564735}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=A;
IsoId=Q86UW9-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=Q86UW9-2; Sequence=VSP_008350;
-!- DOMAIN: The WWE domains are thought to mediate some protein-
protein interaction, and are frequently found in ubiquitin
ligases. {ECO:0000250}.
-!- SIMILARITY: Belongs to the Deltex family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA96052.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AY225124; AAP57518.1; -; mRNA.
EMBL; AY225125; AAP57519.1; -; mRNA.
EMBL; DQ010329; AAY27263.1; -; mRNA.
EMBL; AB040961; BAA96052.1; ALT_INIT; mRNA.
EMBL; AK023924; BAB14727.1; -; mRNA.
EMBL; AC005522; AAP21881.1; -; Genomic_DNA.
EMBL; AC007078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008856; AAH08856.1; -; mRNA.
EMBL; BC018555; AAH18555.1; -; mRNA.
EMBL; BC026059; AAH26059.1; -; mRNA.
EMBL; BC093079; AAH93079.1; -; mRNA.
CCDS; CCDS43605.1; -. [Q86UW9-2]
CCDS; CCDS5587.1; -. [Q86UW9-1]
RefSeq; NP_001096064.1; NM_001102594.1. [Q86UW9-1]
RefSeq; NP_001096065.1; NM_001102595.1. [Q86UW9-1]
RefSeq; NP_001096066.1; NM_001102596.1. [Q86UW9-2]
RefSeq; NP_065943.2; NM_020892.2. [Q86UW9-1]
RefSeq; XP_005250188.1; XM_005250131.1. [Q86UW9-1]
RefSeq; XP_005250189.1; XM_005250132.1. [Q86UW9-1]
RefSeq; XP_011514074.1; XM_011515772.1. [Q86UW9-1]
RefSeq; XP_011514075.1; XM_011515773.2. [Q86UW9-1]
RefSeq; XP_011514076.1; XM_011515774.1. [Q86UW9-1]
RefSeq; XP_011514077.1; XM_011515775.1. [Q86UW9-1]
RefSeq; XP_016867212.1; XM_017011723.1. [Q86UW9-1]
RefSeq; XP_016867213.1; XM_017011724.1. [Q86UW9-1]
RefSeq; XP_016867214.1; XM_017011725.1. [Q86UW9-1]
RefSeq; XP_016867215.1; XM_017011726.1. [Q86UW9-2]
RefSeq; XP_016867216.1; XM_017011727.1. [Q86UW9-2]
UniGene; Hs.187058; -.
ProteinModelPortal; Q86UW9; -.
SMR; Q86UW9; -.
BioGrid; 125266; 46.
IntAct; Q86UW9; 125.
MINT; Q86UW9; -.
STRING; 9606.ENSP00000322885; -.
iPTMnet; Q86UW9; -.
PhosphoSitePlus; Q86UW9; -.
BioMuta; DTX2; -.
DMDM; 68067880; -.
EPD; Q86UW9; -.
MaxQB; Q86UW9; -.
PaxDb; Q86UW9; -.
PeptideAtlas; Q86UW9; -.
PRIDE; Q86UW9; -.
ProteomicsDB; 69923; -.
ProteomicsDB; 69924; -. [Q86UW9-2]
DNASU; 113878; -.
Ensembl; ENST00000324432; ENSP00000322885; ENSG00000091073. [Q86UW9-1]
Ensembl; ENST00000413936; ENSP00000390218; ENSG00000091073. [Q86UW9-1]
Ensembl; ENST00000430490; ENSP00000411986; ENSG00000091073. [Q86UW9-1]
Ensembl; ENST00000446820; ENSP00000392545; ENSG00000091073. [Q86UW9-2]
GeneID; 113878; -.
KEGG; hsa:113878; -.
UCSC; uc003uff.5; human. [Q86UW9-1]
CTD; 113878; -.
DisGeNET; 113878; -.
EuPathDB; HostDB:ENSG00000091073.19; -.
GeneCards; DTX2; -.
HGNC; HGNC:15973; DTX2.
HPA; HPA042931; -.
MIM; 613141; gene.
neXtProt; NX_Q86UW9; -.
OpenTargets; ENSG00000091073; -.
PharmGKB; PA27515; -.
eggNOG; ENOG410IEMS; Eukaryota.
eggNOG; ENOG4111EY2; LUCA.
GeneTree; ENSGT00940000157641; -.
HOGENOM; HOG000007352; -.
HOVERGEN; HBG007213; -.
InParanoid; Q86UW9; -.
KO; K06058; -.
OMA; ICYLPDC; -.
OrthoDB; EOG091G04KU; -.
PhylomeDB; Q86UW9; -.
Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
UniPathway; UPA00143; -.
ChiTaRS; DTX2; human.
GeneWiki; DTX2; -.
GenomeRNAi; 113878; -.
PRO; PR:Q86UW9; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000091073; Expressed in 142 organ(s), highest expression level in lower esophagus mucosa.
CleanEx; HS_DTX2; -.
ExpressionAtlas; Q86UW9; baseline and differential.
Genevisible; Q86UW9; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
CDD; cd09633; Deltex_C; 1.
Gene3D; 3.30.390.130; -; 1.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.30.720.50; -; 2.
InterPro; IPR039396; Deltex_C.
InterPro; IPR039399; Deltex_C_sf.
InterPro; IPR039398; Deltex_fam.
InterPro; IPR004170; WWE-dom.
InterPro; IPR018123; WWE-dom_subgr.
InterPro; IPR037197; WWE_dom_sf.
InterPro; IPR018957; Znf_C3HC4_RING-type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR12622; PTHR12622; 1.
Pfam; PF02825; WWE; 2.
Pfam; PF00097; zf-C3HC4; 1.
SMART; SM00184; RING; 1.
SMART; SM00678; WWE; 2.
SUPFAM; SSF117839; SSF117839; 2.
PROSITE; PS50918; WWE; 2.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Metal-binding; Methylation; Notch signaling pathway; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transferase;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 622 Probable E3 ubiquitin-protein ligase
DTX2.
/FTId=PRO_0000219083.
DOMAIN 8 97 WWE 1. {ECO:0000255|PROSITE-
ProRule:PRU00248}.
DOMAIN 98 174 WWE 2. {ECO:0000255|PROSITE-
ProRule:PRU00248}.
ZN_FING 412 473 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
MOD_RES 213 213 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 215 215 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 233 233 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 249 249 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 256 256 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 360 360 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 337 383 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_008350.
VARIANT 94 94 A -> T (in dbSNP:rs2462312).
/FTId=VAR_016920.
VARIANT 384 384 G -> E (in dbSNP:rs1638152).
{ECO:0000269|PubMed:10819331,
ECO:0000269|PubMed:12670957,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_016921.
VARIANT 421 421 T -> A (in dbSNP:rs6979487).
{ECO:0000269|PubMed:10819331,
ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.2}.
/FTId=VAR_016922.
SEQUENCE 622 AA; 67246 MW; ABE1398204F2273A CRC64;
MAMAPSPSLV QVYTSPAAVA VWEWQDGLGT WHPYSATVCS FIEQQFVQQK GQRFGLGSLA
HSIPLGQADP SLAPYIIDLP SWTQFRQDTG TMRAVRRHLF PQHSAPGRGV VWEWLSDDGS
WTAYEASVCD YLEQQVARGN QLVDLAPLGY NYTVNYTTHT QTNKTSSFCR SVRRQAGPPY
PVTTIIAPPG HTGVACSCHQ CLSGSRTGPV SGRYRHSMTN LPAYPVPQHP PHRTASVFGT
HQAFAPYNKP SLSGARSAPR LNTTNAWGAA PPSLGSQPLY RSSLSHLGPQ HLPPGSSTSG
AVSASLPSGP SSSPGSVPAT VPMQMPKPSR VQQALAGMTS VLMSAIGLPV CLSRAPQPTS
PPASRLASKS HGSVKRLRKM SVKGATPKPE PEPEQVIKNY TEELKVPPDE DCIICMEKLS
TASGYSDVTD SKAIGSLAVG HLTKCSHAFH LLCLLAMYCN GNKDGSLQCP SCKTIYGEKT
GTQPQGKMEV LRFQMSLPGH EDCGTILIVY SIPHGIQGPE HPNPGKPFTA RGFPRQCYLP
DNAQGRKVLE LLKVAWKRRL IFTVGTSSTT GETDTVVWNE IHHKTEMDRN ITGHGYPDPN
YLQNVLAELA AQGVTEDCLE QQ


Related products :

Catalog number Product name Quantity
EIAAB12010 Deltex2,DTX2,hDTX2,Homo sapiens,Human,KIAA1528,Protein deltex-2,RING finger protein 58,RNF58
EIAAB43998 GERP,Glioblastoma-expressed RING finger protein,Homo sapiens,Human,Probable E3 ubiquitin-protein ligase TRIM8,RING finger protein 27,RNF27,TRIM8,Tripartite motif-containing protein 8
EIAAB43999 Gerp,Glioblastoma-expressed RING finger protein,Mouse,Mus musculus,Probable E3 ubiquitin-protein ligase TRIM8,RING finger protein 27,Rnf27,Trim8,Tripartite motif-containing protein 8
EIAAB45299 E3 ubiquitin-protein ligase UHRF2,Homo sapiens,Human,NIRF,Np95_ICBP90-like RING finger protein,Np95-like RING finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,RING finger protein 107
EIAAB34367 CARP-2,Caspase regulator CARP2,Caspases-8 and -10-associated RING finger protein 2,E3 ubiquitin-protein ligase rififylin,Fring,FYVE-RING finger protein Sakura,Homo sapiens,Human,RFFL,RING finger and F
EIAAB43947 E3 ubiquitin-protein ligase TRIM63,Homo sapiens,Human,IRF,Iris RING finger protein,MuRF1,MURF1,MuRF-1,Muscle-specific RING finger protein 1,RING finger protein 28,RNF28,SMRZ,Striated muscle RING zinc
EIAAB35413 E3 ubiquitin-protein ligase RNF138,hNARF,Homo sapiens,HSD4,HSD-4,Human,NARF,Nemo-like kinase-associated RING finger protein,NLK-associated RING finger protein,RING finger protein 138,RNF138
EIAAB35571 CARP-1,Caspase regulator CARP1,Caspases-8 and -10-associated RING finger protein 1,E3 ubiquitin-protein ligase RNF34,FYVE-RING finger protein Momo,Homo sapiens,hRFI,Human,Human RING finger homologous
EIAAB45298 E3 ubiquitin-protein ligase UHRF2,Mouse,Mus musculus,NIRF,Nirf,Np95-like ring finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,Ubiquitin-like PHD and RING finger domain-containing pr
18-003-42502 Ubiquitin ligase protein RING2 - EC 6.3.2.-; RING finger protein 2; RING finger protein 1B; RING1b; RING finger protein BAP-1; DinG protein; Huntingtin-interacting protein 2-interacting protein 3; HIP 0.1 mg Protein A
18-003-42501 Ubiquitin ligase protein RING2 - EC 6.3.2.-; RING finger protein 2; RING finger protein 1B; RING1b; RING finger protein BAP-1; DinG protein; Huntingtin-interacting protein 2-interacting protein 3; HIP 0.05 mg Aff Pur
EIAAB35549 E3 ubiquitin-protein ligase RLIM,Homo sapiens,Human,LIM domain-interacting RING finger protein,Renal carcinoma antigen NY-REN-43,RING finger LIM domain-binding protein,RING finger protein 12,RLIM,R-LI
EIAAB45296 Ac2-121,E3 ubiquitin-protein ligase UHRF1,Liver regeneration-related protein LRRG126,Rat,Rattus norvegicus,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing PHD
EIAAB33372 Kiaa0161,Mouse,Mus musculus,Probable E3 ubiquitin-protein ligase RNF144A,RING finger protein 144A,Rnf144,Rnf144a,Ubce7ip4,UbcM4-interacting protein 4,Ubiquitin-conjugating enzyme 7-interacting protein
EIAAB33371 Homo sapiens,Human,KIAA0161,Probable E3 ubiquitin-protein ligase RNF144A,RING finger protein 144A,RNF144,RNF144A,UBCE7IP4,UbcM4-interacting protein 4,Ubiquitin-conjugating enzyme 7-interacting protein
EIAAB24904 D15S9,Homo sapiens,Human,MKRN3,Probable E3 ubiquitin-protein ligase makorin-3,RING finger protein 63,RNF63,Zinc finger protein 127,ZNF127
EIAAB24906 Homo sapiens,Human,Makorin RING finger protein pseudogene 4,Makorin RING finger protein pseudogene 5,MKRN4,MKRN4P,MKRNP5,Putative E3 ubiquitin-protein ligase makorin-4,RING finger protein 64,RNF64,Zin
EIAAB38244 E3 ubiquitin-protein ligase SH3RF1,Homo sapiens,Human,KIAA1494,Plenty of SH3s,POSH,Protein POSH,RING finger protein 142,RNF142,SH3 domain-containing RING finger protein 1,SH3 multiple domains protein
EIAAB38246 Heart protein phosphatase 1-binding protein,HEPP1,Homo sapiens,Human,Putative E3 ubiquitin-protein ligase SH3RF2,RING finger protein 158,RNF158,SH3 domain-containing RING finger protein 2,SH3RF2
EIAAB35550 E3 ubiquitin-protein ligase RLIM,LIM domain-interacting RING finger protein,Mouse,Mus musculus,RING finger LIM domain-binding protein,RING finger protein 12,Rlim,R-LIM,Rnf12
EIAAB35482 Dorfin,Double ring-finger protein,E3 ubiquitin-protein ligase RNF19A,Gametogenesis-expressed protein GEG-154,Geg-154,Mouse,Mus musculus,RING finger protein 19A,Rnf19,Rnf19a,UBCM4-interacting protein 1
EIAAB34424 Constitutive photomorphogenesis protein 1 homolog,COP1,E3 ubiquitin-protein ligase RFWD2,hCOP1,Homo sapiens,Human,RFWD2,RING finger and WD repeat domain protein 2,RING finger protein 200,RNF200
EIAAB43861 E3 ubiquitin-protein ligase TRIM17,Homo sapiens,Human,RBCC,RING finger protein 16,RNF16,TERF,Testis RING finger protein,TRIM17,Tripartite motif-containing protein 17
EIAAB33374 E3 ubiquitin-protein ligase RNF144B,Homo sapiens,Human,IBR domain-containing protein 2,IBRDC2,p53-inducible RING finger protein,P53RFP,RING finger protein 144B,RNF144B
EIAAB12011 Deltex2,Dtx2,mDTX2,Mouse,Mus musculus,Protein deltex-2


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | 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 | 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 | 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 | Gentaur