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

E3 ubiquitin-protein ligase LNX (EC 2.3.2.27) (Ligand of Numb-protein X 1) (Numb-binding protein 1) (PDZ domain-containing RING finger protein 2) (RING-type E3 ubiquitin transferase LNX)

 LNX1_HUMAN              Reviewed;         728 AA.
Q8TBB1; Q4W5K7; Q8N4C2; Q96MJ7; Q9BY20;
28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
27-SEP-2017, entry version 151.
RecName: Full=E3 ubiquitin-protein ligase LNX;
EC=2.3.2.27;
AltName: Full=Ligand of Numb-protein X 1;
AltName: Full=Numb-binding protein 1;
AltName: Full=PDZ domain-containing RING finger protein 2;
AltName: Full=RING-type E3 ubiquitin transferase LNX {ECO:0000305};
Name=LNX1; Synonyms=LNX, PDZRN2; ORFNames=UNQ574/PRO1136;
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 2), AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=11521506; DOI=10.1023/A:1010269908398;
Xie Y., Zhao W., Wang W., Zhao S., Tang R., Ying K., Zhou Z., Mao Y.;
"Identification of a human LNX protein containing multiple PDZ
domains.";
Biochem. Genet. 39:117-126(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Prostate;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Placenta;
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).
[6]
INTERACTION WITH CXADR.
PubMed=12468544; DOI=10.1074/jbc.M205927200;
Sollerbrant K., Raschperger E., Mirza M., Engstroem U., Philipson L.,
Ljungdahl P.O., Pettersson R.F.;
"The Coxsackievirus and adenovirus receptor (CAR) forms a complex with
the PDZ domain-containing protein ligand-of-numb protein-X (LNX).";
J. Biol. Chem. 278:7439-7444(2003).
[7]
INTERACTION WITH NP9.
PubMed=15367597; DOI=10.1128/JVI.78.19.10310-10319.2004;
Armbruester V., Sauter M., Roemer K., Best B., Hahn S., Nty A.,
Schmid A., Philipp S., Mueller A., Mueller-Lantzsch N.;
"Np9 protein of human endogenous retrovirus K interacts with ligand of
numb protein X.";
J. Virol. 78:10310-10319(2004).
[8]
INTERACTION WITH MAGEB18 AND MAGEF1.
PubMed=20864041; DOI=10.1016/j.molcel.2010.08.029;
Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.;
"MAGE-RING protein complexes comprise a family of E3 ubiquitin
ligases.";
Mol. Cell 39:963-974(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, AND 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).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
and subsequent proteasomal degradation of NUMB. E3 ubiquitin
ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme
in the form of a thioester and then directly transfers the
ubiquitin to targeted substrates. Mediates ubiquitination of
isoform p66 and isoform p72 of NUMB, but not that of isoform p71
or isoform p65. {ECO:0000250|UniProtKB:O70263}.
-!- FUNCTION: Isoform 2 provides an endocytic scaffold for IGSF5/JAM4.
{ECO:0000250|UniProtKB:O70263}.
-!- 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 the phosphotyrosine interaction domain of
all isoforms of NUMB (By similarity). Interacts with MAGEB18 and
MAGEF1. Interacts with the Coxsackievirus and adenovirus receptor
CXADR. Interacts with endogenous retrovirus K protein Np9.
IGSF5/JAM4 interacts with isoform 2 through the second PDZ domain,
other isoforms may also interact with IGSF5/JAM4 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q9BWD1:ACAT2; NbExp=3; IntAct=EBI-739832, EBI-1047273;
Q96HD9:ACY3; NbExp=3; IntAct=EBI-739832, EBI-3916242;
Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-739832, EBI-741181;
Q96BJ3:AIDA; NbExp=3; IntAct=EBI-739832, EBI-4401674;
Q13155:AIMP2; NbExp=6; IntAct=EBI-739832, EBI-745226;
P09972:ALDOC; NbExp=7; IntAct=EBI-739832, EBI-2952751;
Q96Q83:ALKBH3; NbExp=3; IntAct=EBI-739832, EBI-6658697;
Q96GX9:APIP; NbExp=10; IntAct=EBI-739832, EBI-359248;
Q9BRG6:APOL4; NbExp=3; IntAct=EBI-739832, EBI-10296818;
Q8N5M1:ATPAF2; NbExp=8; IntAct=EBI-739832, EBI-1166928;
Q8WXE1:ATRIP; NbExp=3; IntAct=EBI-739832, EBI-747353;
P53004:BLVRA; NbExp=3; IntAct=EBI-739832, EBI-7410441;
Q9BXJ1:C1QTNF1; NbExp=3; IntAct=EBI-739832, EBI-750200;
P35219:CA8; NbExp=6; IntAct=EBI-739832, EBI-718700;
Q86XM0:CATSPERD; NbExp=3; IntAct=EBI-739832, EBI-10260328;
P83916:CBX1; NbExp=4; IntAct=EBI-739832, EBI-78129;
Q68D86:CCDC102B; NbExp=3; IntAct=EBI-739832, EBI-10171570;
Q96M63:CCDC114; NbExp=3; IntAct=EBI-739832, EBI-10173858;
Q8IYA8:CCDC36; NbExp=4; IntAct=EBI-739832, EBI-8638439;
P32320:CDA; NbExp=8; IntAct=EBI-739832, EBI-9250559;
Q9P209:CEP72; NbExp=3; IntAct=EBI-739832, EBI-739498;
Q96Q77:CIB3; NbExp=3; IntAct=EBI-739832, EBI-10292696;
Q14011:CIRBP; NbExp=3; IntAct=EBI-739832, EBI-538850;
P49759-3:CLK1; NbExp=4; IntAct=EBI-739832, EBI-11981867;
P49760:CLK2; NbExp=7; IntAct=EBI-739832, EBI-750020;
P38432:COIL; NbExp=2; IntAct=EBI-739832, EBI-945751;
Q96FN4:CPNE2; NbExp=3; IntAct=EBI-739832, EBI-7097057;
O75553:DAB1; NbExp=3; IntAct=EBI-739832, EBI-7875264;
P32321:DCTD; NbExp=3; IntAct=EBI-739832, EBI-739870;
Q9BTE7:DCUN1D5; NbExp=3; IntAct=EBI-739832, EBI-3924013;
P35638:DDIT3; NbExp=4; IntAct=EBI-739832, EBI-742651;
Q92841:DDX17; NbExp=3; IntAct=EBI-739832, EBI-746012;
Q06819:DIB1 (xeno); NbExp=3; IntAct=EBI-739832, EBI-166;
Q9ULA0:DNPEP; NbExp=5; IntAct=EBI-739832, EBI-748356;
Q92785:DPF2; NbExp=3; IntAct=EBI-739832, EBI-359932;
Q15056:EIF4H; NbExp=3; IntAct=EBI-739832, EBI-748492;
Q8TC92:ENOX1; NbExp=3; IntAct=EBI-739832, EBI-713221;
Q96B26:EXOSC8; NbExp=8; IntAct=EBI-739832, EBI-371922;
Q9NWS6:FAM118A; NbExp=3; IntAct=EBI-739832, EBI-8638992;
Q86V42:FAM124A; NbExp=3; IntAct=EBI-739832, EBI-744506;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-739832, EBI-10175124;
Q9NXK8:FBXL12; NbExp=3; IntAct=EBI-739832, EBI-719790;
P31150:GDI1; NbExp=6; IntAct=EBI-739832, EBI-946999;
Q9H4A5:GOLPH3L; NbExp=3; IntAct=EBI-739832, EBI-4403434;
O75791:GRAP2; NbExp=4; IntAct=EBI-739832, EBI-740418;
P62993:GRB2; NbExp=3; IntAct=EBI-739832, EBI-401755;
Q4V328:GRIPAP1; NbExp=4; IntAct=EBI-739832, EBI-717919;
V9HW56:HEL-S-108; NbExp=3; IntAct=EBI-739832, EBI-10330141;
V9HWB8:HEL-S-30; NbExp=3; IntAct=EBI-739832, EBI-10215395;
V9HWF5:HEL-S-69p; NbExp=3; IntAct=EBI-739832, EBI-10330249;
V9HW80:HEL-S-70; NbExp=3; IntAct=EBI-739832, EBI-10175326;
Q6NT76:HMBOX1; NbExp=3; IntAct=EBI-739832, EBI-2549423;
Q9NP66:HMG20A; NbExp=4; IntAct=EBI-739832, EBI-740641;
Q9NSC5:HOMER3; NbExp=6; IntAct=EBI-739832, EBI-748420;
Q8IX15-3:HOMEZ; NbExp=3; IntAct=EBI-739832, EBI-10172004;
O75506:HSBP1; NbExp=7; IntAct=EBI-739832, EBI-748664;
Q9BT40:INPP5K; NbExp=3; IntAct=EBI-739832, EBI-749162;
Q9H1K1:ISCU; NbExp=3; IntAct=EBI-739832, EBI-1047335;
Q719H9:KCTD1; NbExp=5; IntAct=EBI-739832, EBI-9027502;
Q8WZ19:KCTD13; NbExp=3; IntAct=EBI-739832, EBI-742916;
Q8NC69:KCTD6; NbExp=3; IntAct=EBI-739832, EBI-2511344;
Q7L273:KCTD9; NbExp=4; IntAct=EBI-739832, EBI-4397613;
Q5T7B8-2:KIF24; NbExp=4; IntAct=EBI-739832, EBI-10213781;
Q9BVG8-5:KIFC3; NbExp=4; IntAct=EBI-739832, EBI-14069005;
Q53G59:KLHL12; NbExp=3; IntAct=EBI-739832, EBI-740929;
P19012:KRT15; NbExp=3; IntAct=EBI-739832, EBI-739566;
Q9BYR5:KRTAP4-2; NbExp=5; IntAct=EBI-739832, EBI-10172511;
Q9BYQ4:KRTAP9-2; NbExp=3; IntAct=EBI-739832, EBI-1044640;
Q9BQD3:KXD1; NbExp=3; IntAct=EBI-739832, EBI-739657;
Q6UWP7:LCLAT1; NbExp=3; IntAct=EBI-739832, EBI-10254507;
Q13094:LCP2; NbExp=4; IntAct=EBI-739832, EBI-346946;
O43679:LDB2; NbExp=4; IntAct=EBI-739832, EBI-2865580;
Q8TCE9:LGALS14; NbExp=3; IntAct=EBI-739832, EBI-10274069;
Q9Y333:LSM2; NbExp=3; IntAct=EBI-739832, EBI-347416;
Q96M61:MAGEB18; NbExp=13; IntAct=EBI-739832, EBI-741835;
P45984:MAPK9; NbExp=5; IntAct=EBI-739832, EBI-713568;
Q9Y316:MEMO1; NbExp=5; IntAct=EBI-739832, EBI-1104564;
Q8WXB1:METTL21A; NbExp=3; IntAct=EBI-739832, EBI-8652459;
Q9UJV3-2:MID2; NbExp=4; IntAct=EBI-739832, EBI-10172526;
Q96HT8:MRFAP1L1; NbExp=5; IntAct=EBI-739832, EBI-748896;
Q96QG7:MTMR9; NbExp=3; IntAct=EBI-739832, EBI-744593;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-739832, EBI-742948;
Q9H7P6:MVB12B; NbExp=3; IntAct=EBI-739832, EBI-6149062;
O95544:NADK; NbExp=3; IntAct=EBI-739832, EBI-743949;
Q9UJ70:NAGK; NbExp=2; IntAct=EBI-739832, EBI-372578;
O43639:NCK2; NbExp=3; IntAct=EBI-739832, EBI-713635;
Q8N987:NECAB1; NbExp=4; IntAct=EBI-739832, EBI-11956853;
Q7Z6G3:NECAB2; NbExp=3; IntAct=EBI-739832, EBI-950070;
Q7Z6G3-2:NECAB2; NbExp=3; IntAct=EBI-739832, EBI-10172876;
Q9HC98:NEK6; NbExp=3; IntAct=EBI-739832, EBI-740364;
Q9Y5B8:NME7; NbExp=5; IntAct=EBI-739832, EBI-744782;
Q7Z3S9:NOTCH2NL; NbExp=5; IntAct=EBI-739832, EBI-945833;
O95848:NUDT14; NbExp=7; IntAct=EBI-739832, EBI-536866;
Q9NPJ8:NXT2; NbExp=3; IntAct=EBI-739832, EBI-752122;
Q969R2:OSBP2; NbExp=3; IntAct=EBI-739832, EBI-7405817;
Q9H4L5:OSBPL3; NbExp=4; IntAct=EBI-739832, EBI-1051317;
Q9UJX0:OSGIN1; NbExp=3; IntAct=EBI-739832, EBI-9057006;
Q15102:PAFAH1B3; NbExp=6; IntAct=EBI-739832, EBI-711522;
P22234:PAICS; NbExp=3; IntAct=EBI-739832, EBI-712261;
P30039:PBLD; NbExp=3; IntAct=EBI-739832, EBI-750589;
P61457:PCBD1; NbExp=6; IntAct=EBI-739832, EBI-740475;
Q8ND90:PNMA1; NbExp=6; IntAct=EBI-739832, EBI-302345;
Q96PV4:PNMA5; NbExp=4; IntAct=EBI-739832, EBI-10171633;
Q8WZA1:POMGNT1; NbExp=3; IntAct=EBI-739832, EBI-3912424;
P62937:PPIA; NbExp=3; IntAct=EBI-739832, EBI-437708;
P31321:PRKAR1B; NbExp=4; IntAct=EBI-739832, EBI-2805516;
Q9NZ81:PRR13; NbExp=4; IntAct=EBI-739832, EBI-740924;
Q03393:PTS; NbExp=3; IntAct=EBI-739832, EBI-712344;
O75771:RAD51D; NbExp=6; IntAct=EBI-739832, EBI-1055693;
Q9Y620:RAD54B; NbExp=3; IntAct=EBI-739832, EBI-740830;
P38159:RBMX; NbExp=3; IntAct=EBI-739832, EBI-743526;
P0DJD3:RBMY1A1; NbExp=3; IntAct=EBI-739832, EBI-8638511;
Q15415:RBMY1J; NbExp=4; IntAct=EBI-739832, EBI-8642021;
O75679:RFPL3; NbExp=3; IntAct=EBI-739832, EBI-10188956;
Q96HH0:ROBO3; NbExp=3; IntAct=EBI-739832, EBI-10288358;
Q9HAT0:ROPN1; NbExp=3; IntAct=EBI-739832, EBI-1378139;
P49247:RPIA; NbExp=3; IntAct=EBI-739832, EBI-744831;
Q6ZNE9:RUFY4; NbExp=5; IntAct=EBI-739832, EBI-10181525;
Q9Y230:RUVBL2; NbExp=5; IntAct=EBI-739832, EBI-352939;
P21673:SAT1; NbExp=8; IntAct=EBI-739832, EBI-711613;
Q8WYJ6:SEPT1; NbExp=4; IntAct=EBI-739832, EBI-693002;
Q96ES7:SGF29; NbExp=3; IntAct=EBI-739832, EBI-743117;
Q9BV90:SNRNP25; NbExp=3; IntAct=EBI-739832, EBI-9675976;
P62306:SNRPF; NbExp=3; IntAct=EBI-739832, EBI-356900;
Q8NA61-2:SPERT; NbExp=6; IntAct=EBI-739832, EBI-11524851;
P12931:SRC; NbExp=6; IntAct=EBI-739832, EBI-621482;
O43805:SSNA1; NbExp=5; IntAct=EBI-739832, EBI-2515299;
Q6ZMT1:STAC2; NbExp=3; IntAct=EBI-739832, EBI-948802;
Q86TI0:TBC1D1; NbExp=4; IntAct=EBI-739832, EBI-1644036;
Q5QJ74:TBCEL; NbExp=3; IntAct=EBI-739832, EBI-10244795;
Q9BT49:THAP7; NbExp=3; IntAct=EBI-739832, EBI-741350;
Q96CG3:TIFA; NbExp=3; IntAct=EBI-739832, EBI-740711;
Q13077:TRAF1; NbExp=6; IntAct=EBI-739832, EBI-359224;
Q12933:TRAF2; NbExp=5; IntAct=EBI-739832, EBI-355744;
Q9HCM9:TRIM39; NbExp=3; IntAct=EBI-739832, EBI-739510;
Q9BYV2:TRIM54; NbExp=5; IntAct=EBI-739832, EBI-2130429;
Q15645:TRIP13; NbExp=6; IntAct=EBI-739832, EBI-358993;
Q53H54:TRMT12; NbExp=3; IntAct=EBI-739832, EBI-10242598;
P22803:TRX2 (xeno); NbExp=3; IntAct=EBI-739832, EBI-19598;
Q99816:TSG101; NbExp=4; IntAct=EBI-739832, EBI-346882;
Q96PN8:TSSK3; NbExp=5; IntAct=EBI-739832, EBI-3918381;
Q9Y3C0:WASHC3; NbExp=4; IntAct=EBI-739832, EBI-712969;
P25631:YCR051W (xeno); NbExp=3; IntAct=EBI-739832, EBI-2347265;
O43167:ZBTB24; NbExp=4; IntAct=EBI-739832, EBI-744471;
O43298:ZBTB43; NbExp=3; IntAct=EBI-739832, EBI-740718;
Q8TBK6:ZCCHC10; NbExp=3; IntAct=EBI-739832, EBI-597063;
Q9NTW7:ZFP64; NbExp=3; IntAct=EBI-739832, EBI-745730;
Q9UDV6:ZNF212; NbExp=4; IntAct=EBI-739832, EBI-1640204;
Q9P0T4:ZNF581; NbExp=5; IntAct=EBI-739832, EBI-745520;
O00488:ZNF593; NbExp=3; IntAct=EBI-739832, EBI-726769;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8TBB1-1; Sequence=Displayed;
Name=2;
IsoId=Q8TBB1-2; Sequence=VSP_005733;
-!- TISSUE SPECIFICITY: Expressed in heart, placenta, kidney, pancreas
and brain. {ECO:0000269|PubMed:11521506}.
-!- DOMAIN: The NPXY motif is required for the interaction with the
PID domain of NUMB. It is however not sufficient.
-!- DOMAIN: The PDZ 1 domain participates in the interaction with the
PID domain of NUMB, and participates in the isoform-specific
ubiquitination of NUMB. The PDZ 2 domain of isoform 2 participates
in the interaction with IGSF5/JAM4, other isoforms containing this
domain may also interact with IGSF5/JAM4 (By similarity).
{ECO:0000250}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF237782; AAK15039.1; -; mRNA.
EMBL; AY358326; AAQ88692.1; -; mRNA.
EMBL; AK056823; BAB71291.1; -; mRNA.
EMBL; AC058822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC095040; AAY41000.1; -; Genomic_DNA.
EMBL; BC022983; AAH22983.1; -; mRNA.
EMBL; BC034737; AAH34737.1; -; mRNA.
CCDS; CCDS3492.1; -. [Q8TBB1-2]
CCDS; CCDS47057.1; -. [Q8TBB1-1]
RefSeq; NP_001119800.1; NM_001126328.2. [Q8TBB1-1]
RefSeq; NP_116011.2; NM_032622.2. [Q8TBB1-2]
RefSeq; XP_005265842.1; XM_005265785.4. [Q8TBB1-1]
RefSeq; XP_016864265.1; XM_017008776.1. [Q8TBB1-1]
UniGene; Hs.518760; -.
PDB; 3B76; X-ray; 1.75 A; A/B=504-594.
PDBsum; 3B76; -.
ProteinModelPortal; Q8TBB1; -.
SMR; Q8TBB1; -.
BioGrid; 124219; 238.
ELM; Q8TBB1; -.
IntAct; Q8TBB1; 408.
MINT; MINT-1441889; -.
STRING; 9606.ENSP00000263925; -.
iPTMnet; Q8TBB1; -.
PhosphoSitePlus; Q8TBB1; -.
BioMuta; LNX1; -.
DMDM; 29840786; -.
PaxDb; Q8TBB1; -.
PeptideAtlas; Q8TBB1; -.
PRIDE; Q8TBB1; -.
DNASU; 84708; -.
Ensembl; ENST00000263925; ENSP00000263925; ENSG00000072201. [Q8TBB1-1]
Ensembl; ENST00000306888; ENSP00000302879; ENSG00000072201. [Q8TBB1-2]
GeneID; 84708; -.
KEGG; hsa:84708; -.
UCSC; uc003haf.5; human. [Q8TBB1-1]
CTD; 84708; -.
DisGeNET; 84708; -.
EuPathDB; HostDB:ENSG00000072201.13; -.
GeneCards; LNX1; -.
HGNC; HGNC:6657; LNX1.
HPA; HPA002235; -.
HPA; HPA071091; -.
MIM; 609732; gene.
neXtProt; NX_Q8TBB1; -.
OpenTargets; ENSG00000072201; -.
PharmGKB; PA30419; -.
eggNOG; KOG3528; Eukaryota.
eggNOG; ENOG4110362; LUCA.
GeneTree; ENSGT00760000119017; -.
HOGENOM; HOG000261605; -.
HOVERGEN; HBG039539; -.
InParanoid; Q8TBB1; -.
KO; K10692; -.
OMA; HSPEENH; -.
OrthoDB; EOG091G0CBZ; -.
PhylomeDB; Q8TBB1; -.
TreeFam; TF330709; -.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; Q8TBB1; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q8TBB1; -.
GeneWiki; LNX1; -.
GenomeRNAi; 84708; -.
PRO; PR:Q8TBB1; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000072201; -.
CleanEx; HS_LNX1; -.
ExpressionAtlas; Q8TBB1; baseline and differential.
Genevisible; Q8TBB1; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IEA:Ensembl.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001478; PDZ.
InterPro; IPR018957; Znf_C3HC4_RING-type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00595; PDZ; 4.
Pfam; PF00097; zf-C3HC4; 1.
SMART; SM00228; PDZ; 4.
SMART; SM00184; RING; 1.
SUPFAM; SSF50156; SSF50156; 4.
PROSITE; PS50106; PDZ; 4.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Metal-binding; Phosphoprotein; Reference proteome; Repeat;
Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 728 E3 ubiquitin-protein ligase LNX.
/FTId=PRO_0000055913.
DOMAIN 274 359 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 381 464 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 507 593 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 638 724 PDZ 4. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
ZN_FING 41 79 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 186 244 Interaction with MAGEB18.
{ECO:0000269|PubMed:20864041}.
MOTIF 181 184 NPXY motif.
MOD_RES 441 441 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 127 MNQPESANDPEPLCAVCGQAHSLEENHFYSYPEEVDDDLIC
HICLQALLDPLDTPCGHTYCTLCLTNFLVEKDFCPMDRKPL
VLQHCKKSSILVNKLLNKLLVTCPFREHCTQVLQRCDLEHH
FQTS -> MKALLLLVLPWLSPANYIDNVGNLHFLYSEL
(in isoform 2).
{ECO:0000303|PubMed:11521506,
ECO:0000303|PubMed:12975309,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_005733.
CONFLICT 132 132 S -> F (in Ref. 1; AAK15039).
{ECO:0000305}.
CONFLICT 321 321 G -> R (in Ref. 3; BAB71291).
{ECO:0000305}.
CONFLICT 366 366 N -> T (in Ref. 3; BAB71291).
{ECO:0000305}.
CONFLICT 411 411 V -> A (in Ref. 3; BAB71291).
{ECO:0000305}.
STRAND 504 511 {ECO:0000244|PDB:3B76}.
STRAND 520 524 {ECO:0000244|PDB:3B76}.
STRAND 535 540 {ECO:0000244|PDB:3B76}.
HELIX 545 549 {ECO:0000244|PDB:3B76}.
STRAND 557 561 {ECO:0000244|PDB:3B76}.
HELIX 566 568 {ECO:0000244|PDB:3B76}.
HELIX 571 579 {ECO:0000244|PDB:3B76}.
STRAND 583 594 {ECO:0000244|PDB:3B76}.
SEQUENCE 728 AA; 80629 MW; 5590E8D8976AE093 CRC64;
MNQPESANDP EPLCAVCGQA HSLEENHFYS YPEEVDDDLI CHICLQALLD PLDTPCGHTY
CTLCLTNFLV EKDFCPMDRK PLVLQHCKKS SILVNKLLNK LLVTCPFREH CTQVLQRCDL
EHHFQTSCKG ASHYGLTKDR KRRSQDGCPD GCASLTATAP SPEVSAAATI SLMTDEPGLD
NPAYVSSAED GQPAISPVDS GRSNRTRARP FERSTIRSRS FKKINRALSV LRRTKSGSAV
ANHADQGREN SENTTAPEVF PRLYHLIPDG EITSIKINRV DPSESLSIRL VGGSETPLVH
IIIQHIYRDG VIARDGRLLP GDIILKVNGM DISNVPHNYA VRLLRQPCQV LWLTVMREQK
FRSRNNGQAP DAYRPRDDSF HVILNKSSPE EQLGIKLVRK VDEPGVFIFN VLDGGVAYRH
GQLEENDRVL AINGHDLRYG SPESAAHLIQ ASERRVHLVV SRQVRQRSPD IFQEAGWNSN
GSWSPGPGER SNTPKPLHPT ITCHEKVVNI QKDPGESLGM TVAGGASHRE WDLPIYVISV
EPGGVISRDG RIKTGDILLN VDGVELTEVS RSEAVALLKR TSSSIVLKAL EVKEYEPQED
CSSPAALDSN HNMAPPSDWS PSWVMWLELP RCLYNCKDIV LRRNTAGSLG FCIVGGYEEY
NGNKPFFIKS IVEGTPAYND GRIRCGDILL AVNGRSTSGM IHACLARLLK ELKGRITLTI
VSWPGTFL


Related products :

Catalog number Product name Quantity
EIAAB33290 E3 ubiquitin-protein ligase PDZRN3,Homo sapiens,Human,KIAA1095,Ligand of Numb protein X 3,LNX3,PDZ domain-containing RING finger protein 3,PDZRN3,Protein SEMACAP3,Semaphorin cytoplasmic domain-associa
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
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
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
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
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
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
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
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
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
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
EIAAB33292 Homo sapiens,Human,Ligand of Numb protein X 4,LNX4,PDZ domain-containing RING finger protein 4,PDZRN4,SEMACAP3-like protein,SEMCAP3L
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
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
EIAAB34369 E3 ubiquitin-protein ligase rififylin,FYVE-RING finger protein Sakura,Rat,Rattus norvegicus,Rffl,RING finger and FYVE-like domain-containing protein 1
EIAAB34425 E3 ubiquitin-protein ligase RFWD3,Homo sapiens,Human,RFWD3,RING finger and WD repeat domain-containing protein 3,RING finger protein 201,RNF201
EIAAB34426 E3 ubiquitin-protein ligase RFWD3,Mouse,Mus musculus,Rfwd3,RING finger and WD repeat domain-containing protein 3,RING finger protein 201,Rnf201
EIAAB45297 E3 ubiquitin-protein ligase UHRF1,Mouse,Mus musculus,Np95,Nuclear protein 95,Nuclear zinc finger protein Np95,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing P
EIAAB35496 E3 ubiquitin-protein ligase RNF216,Homo sapiens,Human,RING finger protein 216,RNF216,Triad domain-containing protein 3,TRIAD3,UBCE7IP1,Ubiquitin-conjugating enzyme 7-interacting protein 1,ZIN,Zinc fin
EIAAB35497 E3 ubiquitin-protein ligase RNF216,Mouse,Mus musculus,RING finger protein 216,Rnf216,Triad domain-containing protein 3,Triad3,Ubce7ip1,UbcM4-interacting protein 83,Ubiquitin-conjugating enzyme 7-inter
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
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


 

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 Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | 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

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
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 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
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | 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
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

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