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E3 ubiquitin-protein ligase TRIM13 (EC 2.3.2.27) (B-cell chronic lymphocytic leukemia tumor suppressor Leu5) (Leukemia-associated protein 5) (Putative tumor suppressor RFP2) (RING finger protein 77) (RING-type E3 ubiquitin transferase TRIM13) (Ret finger protein 2) (Tripartite motif-containing protein 13)

 TRI13_HUMAN             Reviewed;         407 AA.
O60858; B2RB49; Q5UBW0; Q5W0U8; Q5W0U9; Q9BQ47; Q9C021;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 2.
25-OCT-2017, entry version 167.
RecName: Full=E3 ubiquitin-protein ligase TRIM13;
EC=2.3.2.27;
AltName: Full=B-cell chronic lymphocytic leukemia tumor suppressor Leu5;
AltName: Full=Leukemia-associated protein 5;
AltName: Full=Putative tumor suppressor RFP2;
AltName: Full=RING finger protein 77;
AltName: Full=RING-type E3 ubiquitin transferase TRIM13 {ECO:0000305};
AltName: Full=Ret finger protein 2;
AltName: Full=Tripartite motif-containing protein 13;
Name=TRIM13; Synonyms=LEU5, RFP2, RNF77;
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 VARIANT THR-355.
TISSUE=Leukemia;
PubMed=9599022; DOI=10.1016/S0014-5793(98)00357-3;
Kapanadze B., Kashuba V., Baranova A., Rasool O., van Everdink W.J.,
Liu Y., Syomov A., Corcoran M., Poltaraus A., Brodyansky V.,
Syomova N., Kazakov A., Ibbotson R., van den Berg A., Gizatullin R.,
Fedorova L., Sulimova G., Zelenin A., Deaven L., Lehrach H.,
Grander D., Buys C., Oscier D., Zabarovsky E.R., Einhorn S.,
Yankovsky N.;
"A cosmid and cDNA fine physical map of a human chromosome 13q14
region frequently lost in B-cell chronic lymphocytic leukemia and
identification of a new putative tumor suppressor gene, Leu5.";
FEBS Lett. 426:266-270(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
1).
PubMed=11264177; DOI=10.1182/blood.V97.7.2098;
Migliazza A., Bosch F., Komatsu H., Cayanis E., Martinotti S.,
Toniato E., Guccione E., Qu X., Chien M., Murty V.V., Gaidano G.,
Inghirami G., Zhang P., Fischer S., Kalachikov S.M., Russo J.,
Edelman I., Efstratiadis A., Dalla-Favera R.;
"Nucleotide sequence, transcription map, and mutation analysis of the
13q14 chromosomal region deleted in B-cell chronic lymphocytic
leukemia.";
Blood 97:2098-2104(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT THR-355.
PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
Minucci S., Pelicci P.G., Ballabio A.;
"The tripartite motif family identifies cell compartments.";
EMBO J. 20:2140-2151(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=14499696; DOI=10.1016/S0165-4608(03)00126-2;
van Everdink W.J., Baranova A., Lummen C., Tyazhelova T., Looman M.W.,
Ivanov D., Verlind E., Pestova A., Faber H., van der Veen A.Y.,
Yankovsky N., Vellenga E., Buys C.H.;
"RFP2, c13ORF1, and FAM10A4 are the most likely tumor suppressor gene
candidates for B-cell chronic lymphocytic leukemia.";
Cancer Genet. Cytogenet. 146:48-57(2003).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT
THR-355.
Baranova A.V., Sangfelt O., Ivanov D.V., Borodina T.A.,
Yankovsky N.K.;
"RFP2 putative tumor suppressor gene: genomic organization, multiple
mRNA isoforms and evaluation as a B-cell chronic lymphocytic leukaemia
candidate.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Corcoran M.M., Hammarsund M., Grander D., Oscier D., Kapanadze B.,
Einhorn S., Sangfelt O.;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Corcoran M.M., Lerner M., Sangfelt O.;
"Alternative isoform of candidate tumor suppressor RFP2.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-355.
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[10]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Blood, and Lung;
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).
[12]
FUNCTION AS AN E3 UBIQUITIN LIGASE, AUTOUBIQUITINATION, SUBCELLULAR
LOCATION, MUTAGENESIS OF CYS-13, IDENTIFICATION BY MASS SPECTROMETRY,
AND INTERACTION WITH VCP.
PubMed=17314412; DOI=10.1091/mbc.E06-03-0248;
Lerner M., Corcoran M., Cepeda D., Nielsen M.L., Zubarev R.,
Ponten F., Uhlen M., Hober S., Grander D., Sangfelt O.;
"The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin
ligase involved in ERAD.";
Mol. Biol. Cell 18:1670-1682(2007).
[13]
FUNCTION AS AN E3 UBIQUITIN LIGASE, AUTOUBIQUITINATION, SUBCELLULAR
LOCATION, MUTAGENESIS OF CYS-13, IDENTIFICATION BY MASS SPECTROMETRY,
AND INTERACTION WITH MDM2 AND AKT1.
PubMed=21333377; DOI=10.1016/j.ejcb.2010.12.001;
Joo H.M., Kim J.Y., Jeong J.B., Seong K.M., Nam S.Y., Yang K.H.,
Kim C.S., Kim H.S., Jeong M., An S., Jin Y.W.;
"Ret finger protein 2 enhances ionizing radiation-induced apoptosis
via degradation of AKT and MDM2.";
Eur. J. Cell Biol. 90:420-431(2011).
[14]
FUNCTION, AUTOUBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF
CYS-13, AND INTERACTION WITH SQSTM1.
PubMed=22178386; DOI=10.1016/j.bbamcr.2011.11.015;
Tomar D., Singh R., Singh A.K., Pandya C.D., Singh R.;
"TRIM13 regulates ER stress induced autophagy and clonogenic ability
of the cells.";
Biochim. Biophys. Acta 1823:316-326(2012).
-!- FUNCTION: E3 ubiquitin ligase involved in the retrotranslocation
and turnover of membrane and secretory proteins from the ER
through a set of processes named ER-associated degradation (ERAD).
This process acts on misfolded proteins as well as in the
regulated degradation of correctly folded proteins. Enhances
ionizing radiation-induced p53/TP53 stability and apoptosis via
ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity
through MDM2 and AKT1 proteasomal degradation. Regulates ER
stress-induced autophagy, and may act as a tumor suppressor.
{ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377,
ECO:0000269|PubMed:22178386}.
-!- CATALYTIC ACTIVITY: 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.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts (via C-terminal domain) with VCP. Interacts
with AKT1; the interaction ubiquitinates AKT1 and leads to its
proteasomal degradation. Interacts with MDM2; the interaction
ubiquitinates AKT1 and leads to its proteasomal degradation.
Interacts with p62/SQSTM1. {ECO:0000269|PubMed:17314412,
ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386}.
-!- INTERACTION:
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-9867345, EBI-10172181;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377,
ECO:0000269|PubMed:22178386}; Single-pass membrane protein
{ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377,
ECO:0000269|PubMed:22178386}. Note=Concentrates and colocalizes
with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic
reticulum.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Alpha;
IsoId=O60858-1; Sequence=Displayed;
Name=2; Synonyms=Beta;
IsoId=O60858-2; Sequence=VSP_005746, VSP_005747;
Name=3;
IsoId=O60858-3; Sequence=VSP_038142;
-!- DOMAIN: The coiled-coil domain is required for the induction of
autophagy during endoplasmic reticulum (ER) stress.
-!- DOMAIN: The RING-type zinc finger is required for auto-
polyubiquitination.
-!- DOMAIN: The C-terminal domain transmembrane domain is
indispensable for the localization to the ER.
-!- PTM: Auto-ubiquitinated; requires the RING-type zinc finger. Auto-
polyubiquitination leads to proteasomal degradation.
{ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377,
ECO:0000269|PubMed:22178386}.
-!- MISCELLANEOUS: Located on chromosome 13 within the minimal
deletion region for B-cell chronic lymphocytic leukemia.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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EMBL; AJ224819; CAA12136.1; -; mRNA.
EMBL; AF279660; AAK13059.1; -; Genomic_DNA.
EMBL; AF220127; AAG53500.1; -; mRNA.
EMBL; AF220128; AAG53501.1; -; mRNA.
EMBL; AY191002; AAO38979.1; -; mRNA.
EMBL; AF241849; AAK51624.1; -; Genomic_DNA.
EMBL; AF241850; AAF91315.1; -; mRNA.
EMBL; AY455758; AAR31110.1; -; mRNA.
EMBL; AY764035; AAV51406.1; -; mRNA.
EMBL; AK314496; BAG37096.1; -; mRNA.
EMBL; AL137060; CAC43391.1; -; Genomic_DNA.
EMBL; AL137060; CAH72825.1; -; Genomic_DNA.
EMBL; AL137060; CAH72826.1; -; Genomic_DNA.
EMBL; CH471075; EAX08844.1; -; Genomic_DNA.
EMBL; CH471075; EAX08845.1; -; Genomic_DNA.
EMBL; BC003579; AAH03579.1; -; mRNA.
EMBL; BC063407; AAH63407.1; -; mRNA.
CCDS; CCDS41888.1; -. [O60858-3]
CCDS; CCDS9423.1; -. [O60858-1]
RefSeq; NP_001007279.1; NM_001007278.2. [O60858-3]
RefSeq; NP_005789.2; NM_005798.4. [O60858-1]
RefSeq; NP_434698.1; NM_052811.3. [O60858-1]
RefSeq; NP_998755.1; NM_213590.2. [O60858-1]
UniGene; Hs.436922; -.
ProteinModelPortal; O60858; -.
SMR; O60858; -.
BioGrid; 115501; 31.
IntAct; O60858; 6.
STRING; 9606.ENSP00000298772; -.
DrugBank; DB01565; Dihydromorphine.
DrugBank; DB01548; Diprenorphine.
DrugBank; DB01497; Etorphine.
iPTMnet; O60858; -.
PhosphoSitePlus; O60858; -.
BioMuta; TRIM13; -.
EPD; O60858; -.
MaxQB; O60858; -.
PaxDb; O60858; -.
PeptideAtlas; O60858; -.
PRIDE; O60858; -.
DNASU; 10206; -.
Ensembl; ENST00000356017; ENSP00000348299; ENSG00000204977. [O60858-3]
Ensembl; ENST00000378182; ENSP00000367424; ENSG00000204977. [O60858-1]
Ensembl; ENST00000420995; ENSP00000412943; ENSG00000204977. [O60858-1]
Ensembl; ENST00000457662; ENSP00000399206; ENSG00000204977. [O60858-1]
GeneID; 10206; -.
KEGG; hsa:10206; -.
UCSC; uc001vdp.2; human. [O60858-1]
CTD; 10206; -.
DisGeNET; 10206; -.
EuPathDB; HostDB:ENSG00000204977.9; -.
GeneCards; TRIM13; -.
HGNC; HGNC:9976; TRIM13.
HPA; HPA000367; -.
MIM; 605661; gene.
neXtProt; NX_O60858; -.
OpenTargets; ENSG00000204977; -.
PharmGKB; PA162406947; -.
eggNOG; ENOG410ITG5; Eukaryota.
eggNOG; ENOG410YH9X; LUCA.
GeneTree; ENSGT00760000118878; -.
HOVERGEN; HBG056536; -.
InParanoid; O60858; -.
KO; K12003; -.
OMA; QPLNIFC; -.
OrthoDB; EOG091G06VP; -.
PhylomeDB; O60858; -.
TreeFam; TF331669; -.
Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
UniPathway; UPA00143; -.
GenomeRNAi; 10206; -.
PRO; PR:O60858; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000204977; -.
CleanEx; HS_TRIM13; -.
ExpressionAtlas; O60858; baseline and differential.
Genevisible; O60858; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
GO; GO:1904264; F:ubiquitin protein ligase activity involved in ERAD pathway; TAS:Reactome.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:1902187; P:negative regulation of viral release from host cell; IDA:UniProtKB.
GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
GO; GO:0010942; P:positive regulation of cell death; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0016239; P:positive regulation of macroautophagy; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0010332; P:response to gamma radiation; IEP:UniProtKB.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
CDD; cd00021; BBOX; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR027370; Znf-RING_LisH.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00643; zf-B_box; 1.
Pfam; PF13445; zf-RING_UBOX; 1.
SMART; SM00336; BBOX; 1.
SMART; SM00184; RING; 1.
PROSITE; PS50119; ZF_BBOX; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome;
Endoplasmic reticulum; Membrane; Metal-binding; Polymorphism;
Reference proteome; Transferase; Transmembrane; Transmembrane helix;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 407 E3 ubiquitin-protein ligase TRIM13.
/FTId=PRO_0000056028.
TRANSMEM 317 337 Helical. {ECO:0000255}.
ZN_FING 10 58 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 89 131 B box-type. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
COILED 172 200 {ECO:0000255}.
VAR_SEQ 1 1 M -> MDVM (in isoform 3).
{ECO:0000303|Ref.7}.
/FTId=VSP_038142.
VAR_SEQ 175 175 L -> D (in isoform 2).
{ECO:0000303|PubMed:11331580}.
/FTId=VSP_005746.
VAR_SEQ 176 407 Missing (in isoform 2).
{ECO:0000303|PubMed:11331580}.
/FTId=VSP_005747.
VARIANT 355 355 S -> T (in dbSNP:rs1056543).
{ECO:0000269|PubMed:11331580,
ECO:0000269|PubMed:15057823,
ECO:0000269|PubMed:9599022,
ECO:0000269|Ref.5}.
/FTId=VAR_013512.
MUTAGEN 13 13 C->A: Absence of polyubiquitination.
Stability of protein increased. No
enhanced apoptosis on ionizing radiation
induction. No ubiquitination of AKT1 or
MDM2. Decreased p53/TP53 stability. No
effect on induction of autophagy during
ER stress. {ECO:0000269|PubMed:17314412,
ECO:0000269|PubMed:21333377,
ECO:0000269|PubMed:22178386}.
SEQUENCE 407 AA; 46988 MW; 94B624345124AEBF CRC64;
MELLEEDLTC PICCSLFDDP RVLPCSHNFC KKCLEGILEG SVRNSLWRPA PFKCPTCRKE
TSATGINSLQ VNYSLKGIVE KYNKIKISPK MPVCKGHLGQ PLNIFCLTDM QLICGICATR
GEHTKHVFCS IEDAYAQERD AFESLFQSFE TWRRGDALSR LDTLETSKRK SLQLLTKDSD
KVKEFFEKLQ HTLDQKKNEI LSDFETMKLA VMQAYDPEIN KLNTILQEQR MAFNIAEAFK
DVSEPIVFLQ QMQEFREKIK VIKETPLPPS NLPASPLMKN FDTSQWEDIK LVDVDKLSLP
QDTGTFISKI PWSFYKLFLL ILLLGLVIVF GPTMFLEWSL FDDLATWKGC LSNFSSYLTK
TADFIEQSVF YWEQVTDGFF IFNERFKNFT LVVLNNVAEF VCKYKLL


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EIAAB43851 B-cell chronic lymphocytic leukemia tumor suppressor Leu5,E3 ubiquitin-protein ligase TRIM13,Homo sapiens,Human,LEU5,Leukemia-associated protein 5,Putative tumor suppressor RFP2,Ret finger protein 2,R
18-003-42487 Ret finger protein 2 - Leukemia-associated protein 5; B-cell chronic lymphocytic leukemia tumor suppressor Leu5; Putative tumor suppressor RFP2; Tripartite motif-containing protein 13; RING finger pro 0.05 mg Aff Pur
18-003-42488 Ret finger protein 2 - Leukemia-associated protein 5; B-cell chronic lymphocytic leukemia tumor suppressor Leu5; Putative tumor suppressor RFP2; Tripartite motif-containing protein 13; RING finger pro 0.1 mg Protein A
EIAAB43850 E3 ubiquitin-protein ligase TRIM13,Mouse,Mus musculus,Putative tumor suppressor RFP2,Ret finger protein 2,Rfp2,Trim13,Tripartite motif-containing protein 13
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
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
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
EIAAB43939 Homo sapiens,Human,RING finger protein 104,RNF104,TRIM57,TRIM59,Tripartite motif-containing protein 59,TSBF1,Tumor suppressor TSBF-1
29-844 RNF40 contains a RING finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein was reported to interact with the tumor suppressor protein RB1. Studies of the 0.1 mg
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
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
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
EIAAB43946 E3 ubiquitin-protein ligase TRIM63,Mouse,MuRF1,Murf1,MuRF-1,Mus musculus,Muscle RING finger protein 1,Muscle-specific RING finger protein 1,Rf1,Trim63,Tripartite motif-containing protein 63
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
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
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
EIAAB43990 BERP,Brain-expressed RING finger protein,Homo sapiens,Human,RING finger protein 22,RING finger protein 97,RNF22,RNF97,TRIM3,Tripartite motif-containing protein 3
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
EIAAB43847 E3 ubiquitin-protein ligase TRIM11,Homo sapiens,Human,Protein BIA1,RING finger protein 92,RNF92,TRIM11,Tripartite motif-containing protein 11
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
EIAAB43955 E3 ubiquitin-protein ligase TRIM68,GC109,Homo sapiens,Human,RING finger protein 137,RNF137,SS56,SS-56,SSA protein SS-56,TRIM68,Tripartite motif-containing protein 68
EIAAB43957 Mouse,Mus musculus,RING finger B-box coiled-coil transcription factor,RING finger protein 36,Rnf36,Testis-specific RING finger protein,Trif,Trim69,Tripartite motif-containing protein 69
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


 

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