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E3 ubiquitin-protein ligase SH3RF1 (EC 2.3.2.27) (Plenty of SH3s) (Protein POSH) (RING finger protein 142) (RING-type E3 ubiquitin transferase SH3RF1) (SH3 domain-containing RING finger protein 1) (SH3 multiple domains protein 2)

 SH3R1_HUMAN             Reviewed;         888 AA.
Q7Z6J0; Q05BT2; Q8IW46; Q9HAM2; Q9P234;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 2.
30-AUG-2017, entry version 121.
RecName: Full=E3 ubiquitin-protein ligase SH3RF1;
EC=2.3.2.27;
AltName: Full=Plenty of SH3s;
Short=Protein POSH;
AltName: Full=RING finger protein 142;
AltName: Full=RING-type E3 ubiquitin transferase SH3RF1 {ECO:0000305};
AltName: Full=SH3 domain-containing RING finger protein 1;
AltName: Full=SH3 multiple domains protein 2;
Name=SH3RF1; Synonyms=KIAA1494, POSH, RNF142, SH3MD2;
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 MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 140-888 (ISOFORM 2).
TISSUE=Eye, and Ovary;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-712 (ISOFORM 1).
TISSUE=Embryo;
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 251-888 (ISOFORM 1).
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]
INTERACTION WITH MAP3K10; MAP3K11; DLK1; MAP2K4; MAP2K7; MAPK8 AND
MAPK9.
PubMed=12514131; DOI=10.1093/emboj/cdg021;
Xu Z., Kukekov N.V., Greene L.A.;
"POSH acts as a scaffold for a multiprotein complex that mediates JNK
activation in apoptosis.";
EMBO J. 22:252-261(2003).
[5]
INTERACTION WITH AKT1 AND AKT2.
PubMed=14504284; DOI=10.1074/jbc.M307357200;
Figueroa C., Tarras S., Taylor J., Vojtek A.B.;
"Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling
complex.";
J. Biol. Chem. 278:47922-47927(2003).
[6]
FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, FUNCTION IN HIV-1 PLASMA
MEMBRANE TARGETING, SUBCELLULAR LOCATION, AND SELF-UBIQUITINATION.
PubMed=15659549; DOI=10.1073/pnas.0408717102;
Alroy I., Tuvia S., Greener T., Gordon D., Barr H.M., Taglicht D.,
Mandil-Levin R., Ben-Avraham D., Konforty D., Nir A., Levius O.,
Bicoviski V., Dori M., Cohen S., Yaar L., Erez O., Propheta-Meiran O.,
Koskas M., Caspi-Bachar E., Alchanati I., Sela-Brown A., Moskowitz H.,
Tessmer U., Schubert U., Reiss Y.;
"The trans-Golgi network-associated human ubiquitin-protein ligase
POSH is essential for HIV type 1 production.";
Proc. Natl. Acad. Sci. U.S.A. 102:1478-1483(2005).
[7]
INTERACTION WITH SIAH1.
PubMed=16230351; DOI=10.1074/jbc.M509060200;
Xu Z., Sproul A., Wang W., Kukekov N., Greene L.A.;
"Siah1 interacts with the scaffold protein POSH to promote JNK
activation and apoptosis.";
J. Biol. Chem. 281:303-312(2006).
[8]
INTERACTION WITH MAPK8IP.
PubMed=16571722; DOI=10.1074/jbc.M601056200;
Kukekov N.V., Xu Z., Greene L.A.;
"Direct interaction of the molecular scaffolds POSH and JIP is
required for apoptotic activation of JNKs.";
J. Biol. Chem. 281:15517-15524(2006).
[9]
INTERACTION WITH AKT1 AND AKT2, PHOSPHORYLATION AT SER-304,
MUTAGENESIS OF SER-304, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17535800; DOI=10.1074/jbc.M704321200;
Lyons T.R., Thorburn J., Ryan P.W., Thorburn A., Anderson S.M.,
Kassenbrock C.K.;
"Regulation of the pro-apoptotic scaffolding protein POSH by Akt.";
J. Biol. Chem. 282:21987-21997(2007).
[10]
INTERACTION WITH HERP1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
VAL-14.
PubMed=17420289; DOI=10.1083/jcb.200611036;
Tuvia S., Taglicht D., Erez O., Alroy I., Alchanati I., Bicoviski V.,
Dori-Bachash M., Ben-Avraham D., Reiss Y.;
"The ubiquitin E3 ligase POSH regulates calcium homeostasis through
spatial control of Herp.";
J. Cell Biol. 177:51-61(2007).
[11]
FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE.
PubMed=19710010; DOI=10.1074/jbc.M109.041582;
Lin D.H., Yue P., Pan C.Y., Sun P., Zhang X., Han Z., Roos M.,
Caplan M., Giebisch G., Wang W.H.;
"POSH stimulates the ubiquitination and the clathrin-independent
endocytosis of ROMK1 channels.";
J. Biol. Chem. 284:29614-29624(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-532, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[14]
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).
-!- FUNCTION: Acts as a scaffold protein, contributes to Rac-induced
signal transduction such as JNKs (MAPK8 and MAPK9) activation and
induces apoptosis. Within a signaling complex, it probably
recruits protein kinases such as MAP3K10 or MAP3K11 which are in
turn activated leading to the sequential activation of MAP2K4,
MAP2K7 and JNKs (MAPK8 and MAPK9) (By similarity). May be involved
in targeting of HIV-1 GAG and GAG-POL polyproteins to the plasma
membrane. {ECO:0000250, ECO:0000269|PubMed:15659549,
ECO:0000269|PubMed:19710010}.
-!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part
of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-
conjugating enzymes such as UBE2D1 or UBE2N and then transfers it
to substrates. In the absence of an external substrate, it can
catalyze self-ubiquitination. Stimulates ubiquitination of
potassium channel KCNJ1, enhancing it's dynamin-dependent and
clathrin-independent endocytosis.
-!- FUNCTION: Plays an essential role in the targeting of HIV-1 Gag to
the plasma membrane, this function is dependent on it's RING
domain, and hence it's E3 ligase activity.
-!- 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 with Rac; in a GTP-dependent manner (By
similarity). Interacts with MAP3K10 and MAP3K11. Interacts with
MAPK8IP; this interaction leads to the PJAC complex (POSH-JIP or
SH3RF1/MAPK8IP apoptotic complex) with a 1:1 ratio. Interacts with
SIAH1. Interacts with HERP1. Probably part of a signaling complex
that may contain SH3RF1, MAPK8IP, DLK1, MAP2K4, MAP2K7, MAPK8,
MAPK9, AKT1 and AKT2. {ECO:0000250, ECO:0000269|PubMed:12514131,
ECO:0000269|PubMed:14504284, ECO:0000269|PubMed:16230351,
ECO:0000269|PubMed:16571722, ECO:0000269|PubMed:17420289,
ECO:0000269|PubMed:17535800}.
-!- INTERACTION:
P63000:RAC1; NbExp=2; IntAct=EBI-311339, EBI-413628;
O43255:SIAH2; NbExp=2; IntAct=EBI-311339, EBI-948141;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
Cell projection, lamellipodium. Cytoplasm. Golgi apparatus, trans-
Golgi network. Note=Colocalizes, with AKT2, in lamellipodia (By
similarity). Colocalizes, with HERP1, in trans-Golgi network.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q7Z6J0-1; Sequence=Displayed;
Name=2;
IsoId=Q7Z6J0-3; Sequence=VSP_033622, VSP_033623;
Note=No experimental confirmation available.;
-!- DOMAIN: The RING finger domain is responsible of ubiquitination
and proteasomal degradation.
-!- PTM: Phosphorylated at Ser-304 by AKT1 and AKT2. When
phosphorylated, it has reduced ability to bind Rac.
{ECO:0000269|PubMed:17535800}.
-!- PTM: Subject to ubiquitination and proteasomal degradation.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the SH3RF family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH33203.1; Type=Frameshift; Positions=182; Evidence={ECO:0000305};
Sequence=AAH33203.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH53671.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the middle of the protein.; Evidence={ECO:0000305};
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EMBL; BC033203; AAH33203.1; ALT_SEQ; mRNA.
EMBL; BC041023; AAH41023.1; -; mRNA.
EMBL; BC053671; AAH53671.1; ALT_SEQ; mRNA.
EMBL; AK021429; BAB13822.1; -; mRNA.
EMBL; AB040927; BAA96018.1; -; mRNA.
CCDS; CCDS34099.1; -. [Q7Z6J0-1]
RefSeq; NP_065921.2; NM_020870.3. [Q7Z6J0-1]
UniGene; Hs.301804; -.
ProteinModelPortal; Q7Z6J0; -.
SMR; Q7Z6J0; -.
BioGrid; 121673; 20.
DIP; DIP-31636N; -.
ELM; Q7Z6J0; -.
IntAct; Q7Z6J0; 12.
MINT; MINT-2792302; -.
STRING; 9606.ENSP00000284637; -.
iPTMnet; Q7Z6J0; -.
PhosphoSitePlus; Q7Z6J0; -.
BioMuta; SH3RF1; -.
DMDM; 205830834; -.
EPD; Q7Z6J0; -.
MaxQB; Q7Z6J0; -.
PaxDb; Q7Z6J0; -.
PeptideAtlas; Q7Z6J0; -.
PRIDE; Q7Z6J0; -.
Ensembl; ENST00000284637; ENSP00000284637; ENSG00000154447. [Q7Z6J0-1]
GeneID; 57630; -.
KEGG; hsa:57630; -.
UCSC; uc003isa.2; human. [Q7Z6J0-1]
CTD; 57630; -.
DisGeNET; 57630; -.
GeneCards; SH3RF1; -.
HGNC; HGNC:17650; SH3RF1.
HPA; HPA074783; -.
neXtProt; NX_Q7Z6J0; -.
OpenTargets; ENSG00000154447; -.
PharmGKB; PA134915904; -.
eggNOG; ENOG410ITG6; Eukaryota.
eggNOG; ENOG410XS5R; LUCA.
GeneTree; ENSGT00760000119190; -.
HOGENOM; HOG000045564; -.
HOVERGEN; HBG069552; -.
InParanoid; Q7Z6J0; -.
KO; K12171; -.
OMA; GWYKGTH; -.
OrthoDB; EOG091G09B6; -.
PhylomeDB; Q7Z6J0; -.
TreeFam; TF105571; -.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q7Z6J0; -.
SIGNOR; Q7Z6J0; -.
UniPathway; UPA00143; -.
ChiTaRS; SH3RF1; human.
GeneWiki; SH3RF1; -.
GenomeRNAi; 57630; -.
PRO; PR:Q7Z6J0; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000154447; -.
CleanEx; HS_SH3RF1; -.
ExpressionAtlas; Q7Z6J0; baseline and differential.
Genevisible; Q7Z6J0; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:InterPro.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0046328; P:regulation of JNK cascade; IEA:InterPro.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001452; SH3_domain.
InterPro; IPR028502; SH3RF1.
InterPro; IPR018957; Znf_C3HC4_RING-type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
PANTHER; PTHR10663:SF236; PTHR10663:SF236; 1.
Pfam; PF00018; SH3_1; 1.
Pfam; PF14604; SH3_9; 3.
Pfam; PF00097; zf-C3HC4; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00184; RING; 1.
SMART; SM00326; SH3; 4.
SUPFAM; SSF50044; SSF50044; 4.
PROSITE; PS50002; SH3; 4.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell projection; Complete proteome; Cytoplasm;
Golgi apparatus; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; SH3 domain; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 888 E3 ubiquitin-protein ligase SH3RF1.
/FTId=PRO_0000334151.
DOMAIN 134 193 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 196 259 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 445 506 SH3 3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 829 888 SH3 4. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
ZN_FING 12 53 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 440 543 Interaction with AKT2. {ECO:0000250}.
COMPBIAS 397 403 Poly-Pro.
COMPBIAS 417 424 Poly-Ala.
COMPBIAS 657 662 Poly-Ala.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17535800}.
MOD_RES 532 532 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 735 735 Phosphoserine.
{ECO:0000250|UniProtKB:Q69ZI1}.
VAR_SEQ 394 441 TLNPPLPPPPLLAATVLASTPPGATAAAAAAGMGPRPMAGS
TDQIAHL -> APPPLLLLLEWDRGPWQDPLTRLHIYGRRL
APVCMLLYIHTLLGKRIN (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_033622.
VAR_SEQ 442 888 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_033623.
VARIANT 663 663 P -> S (in dbSNP:rs3811813).
/FTId=VAR_043342.
MUTAGEN 14 14 V->A: Loss of Ubl activity.
{ECO:0000269|PubMed:17420289}.
MUTAGEN 304 304 S->A: Decreased level of phosphorylation
and no change in the ability to induce
apoptosis. {ECO:0000269|PubMed:17535800}.
MUTAGEN 304 304 S->D: Decreased level of phosphorylation
and Rac-binding ability and important
loss of the ability to induce apoptosis.
{ECO:0000269|PubMed:17535800}.
MUTAGEN 304 304 S->E: Decreased Rac-binding ability.
{ECO:0000269|PubMed:17535800}.
SEQUENCE 888 AA; 93129 MW; B3018000F03D0CF1 CRC64;
MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VGSRNELRCP ECRTLVGSGV
EELPSNILLV RLLDGIKQRP WKPGPGGGSG TNCTNALRSQ SSTVANCSSK DLQSSQGGQQ
PRVQSWSPPV RGIPQLPCAK ALYNYEGKEP GDLKFSKGDI IILRRQVDEN WYHGEVNGIH
GFFPTNFVQI IKPLPQPPPQ CKALYDFEVK DKEADKDCLP FAKDDVLTVI RRVDENWAEG
MLADKIGIFP ISYVEFNSAA KQLIEWDKPP VPGVDAGECS SAAAQSSTAP KHSDTKKNTK
KRHSFTSLTM ANKSSQASQN RHSMEISPPV LISSSNPTAA ARISELSGLS CSAPSQVHIS
TTGLIVTPPP SSPVTTGPSF TFPSDVPYQA ALGTLNPPLP PPPLLAATVL ASTPPGATAA
AAAAGMGPRP MAGSTDQIAH LRPQTRPSVY VAIYPYTPRK EDELELRKGE MFLVFERCQD
GWFKGTSMHT SKIGVFPGNY VAPVTRAVTN ASQAKVPMST AGQTSRGVTM VSPSTAGGPA
QKLQGNGVAG SPSVVPAAVV SAAHIQTSPQ AKVLLHMTGQ MTVNQARNAV RTVAAHNQER
PTAAVTPIQV QNAAGLSPAS VGLSHHSLAS PQPAPLMPGS ATHTAAISIS RASAPLACAA
AAPLTSPSIT SASLEAEPSG RIVTVLPGLP TSPDSASSAC GNSSATKPDK DSKKEKKGLL
KLLSGASTKR KPRVSPPASP TLEVELGSAE LPLQGAVGPE LPPGGGHGRA GSCPVDGDGP
VTTAVAGAAL AQDAFHRKAS SLDSAVPIAP PPRQACSSLG PVLNESRPVV CERHRVVVSY
PPQSEAELEL KEGDIVFVHK KREDGWFKGT LQRNGKTGLF PGSFVENI


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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
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
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
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
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
EIAAB07154 Checkpoint with forkhead and RING finger domains protein,CHFR,E3 ubiquitin-protein ligase CHFR,Homo sapiens,Human,RING finger protein 196,RNF196
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
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
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
EIAAB34425 E3 ubiquitin-protein ligase RFWD3,Homo sapiens,Human,RFWD3,RING finger and WD repeat domain-containing protein 3,RING finger protein 201,RNF201
EIAAB34369 E3 ubiquitin-protein ligase rififylin,FYVE-RING finger protein Sakura,Rat,Rattus norvegicus,Rffl,RING finger and FYVE-like domain-containing protein 1
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
EIAAB34426 E3 ubiquitin-protein ligase RFWD3,Mouse,Mus musculus,Rfwd3,RING finger and WD repeat domain-containing protein 3,RING finger protein 201,Rnf201


 

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