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Leucine-rich repeat-containing protein 4 (Brain tumor-associated protein BAG) (Nasopharyngeal carcinoma-associated gene 14 protein) (Netrin-G2 ligand) (NGL-2)

 LRRC4_HUMAN             Reviewed;         653 AA.
Q9HBW1; A4D0Y9; Q14DU9; Q6ZMI8; Q96A85;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 2.
20-JUN-2018, entry version 155.
RecName: Full=Leucine-rich repeat-containing protein 4;
AltName: Full=Brain tumor-associated protein BAG;
AltName: Full=Nasopharyngeal carcinoma-associated gene 14 protein;
AltName: Full=Netrin-G2 ligand;
Short=NGL-2;
Flags: Precursor;
Name=LRRC4; Synonyms=BAG; ORFNames=NAG14, UNQ554/PRO1111;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=15967442; DOI=10.1016/j.febslet.2005.05.058;
Zhang Q., Wang J., Fan S., Wang L., Cao L., Tang K., Peng C., Li Z.,
Li W., Gan K., Liu Z., Li X., Shen S., Li G.;
"Expression and functional characterization of LRRC4, a novel brain-
specific member of the LRR superfamily.";
FEBS Lett. 579:3674-3682(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Wang J.;
Thesis (2000), Zhongshan Medical University / Guangzhou, China.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
STRUCTURE BY NMR OF 351-442.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the Ig-like domain of human leucine-rich
repeat-containing protein 4.";
Submitted (OCT-2006) to the PDB data bank.
[8]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-444 IN COMPLEX WITH NTNG2,
AND DISULFIDE BONDS.
PubMed=21946559; DOI=10.1038/emboj.2011.346;
Seiradake E., Coles C.H., Perestenko P.V., Harlos K., McIlhinney R.A.,
Aricescu A.R., Jones E.Y.;
"Structural basis for cell surface patterning through NetrinG-NGL
interactions.";
EMBO J. 30:4479-4488(2011).
[9]
VARIANT [LARGE SCALE ANALYSIS] ALA-579.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Synaptic adhesion protein. Regulates the formation of
exitatory synapses through the recruitment of pre-and-postsynaptic
proteins. Organize the lamina/pathway-specific differentiation of
dendrites. Plays a important role for auditory synaptic responses.
Involved in the suppression of glioma (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Interacts with DLG4 (By similarity). Interacts (via LRR
repeats) with NTNG2. Forms a complex with DLG4 and with NMDA
receptors. {ECO:0000250, ECO:0000269|PubMed:21946559}.
-!- INTERACTION:
Q9Y2I2:NTNG1; NbExp=2; IntAct=EBI-7444327, EBI-7444396;
Q96CW9:NTNG2; NbExp=4; IntAct=EBI-7444327, EBI-750795;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein. Cell junction, synapse, postsynaptic cell membrane
{ECO:0000250}. Note=LRRC4 and DLG4 are interdependent for synaptic
localization. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Specifically expressed in brain.
{ECO:0000269|PubMed:15967442}.
-!- DOMAIN: The last 4 C-terminal residues bind to the first 2 PDZ
domains of DLG4. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
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EMBL; AF196976; AAG28019.2; -; mRNA.
EMBL; AJ297858; CAC82651.1; -; mRNA.
EMBL; AY358307; AAQ88674.1; -; mRNA.
EMBL; AK172751; BAD18737.1; -; mRNA.
EMBL; AK314047; BAG36756.1; -; mRNA.
EMBL; CH236947; EAL24316.1; -; Genomic_DNA.
EMBL; BC111561; AAI11562.1; -; mRNA.
EMBL; BC111745; AAI11746.1; -; mRNA.
CCDS; CCDS5799.1; -.
RefSeq; NP_071426.1; NM_022143.4.
RefSeq; XP_011514763.1; XM_011516461.2.
RefSeq; XP_016867994.1; XM_017012505.1.
UniGene; Hs.655003; -.
PDB; 2DL9; NMR; -; A=353-442.
PDB; 3ZYI; X-ray; 2.60 A; A=1-444.
PDBsum; 2DL9; -.
PDBsum; 3ZYI; -.
ProteinModelPortal; Q9HBW1; -.
SMR; Q9HBW1; -.
BioGrid; 122061; 13.
IntAct; Q9HBW1; 3.
MINT; Q9HBW1; -.
STRING; 9606.ENSP00000249363; -.
iPTMnet; Q9HBW1; -.
PhosphoSitePlus; Q9HBW1; -.
BioMuta; LRRC4; -.
DMDM; 51701696; -.
EPD; Q9HBW1; -.
PaxDb; Q9HBW1; -.
PeptideAtlas; Q9HBW1; -.
PRIDE; Q9HBW1; -.
ProteomicsDB; 81601; -.
Ensembl; ENST00000249363; ENSP00000249363; ENSG00000128594.
GeneID; 64101; -.
KEGG; hsa:64101; -.
UCSC; uc003vmk.4; human.
CTD; 64101; -.
DisGeNET; 64101; -.
EuPathDB; HostDB:ENSG00000128594.7; -.
GeneCards; LRRC4; -.
HGNC; HGNC:15586; LRRC4.
HPA; HPA051100; -.
MIM; 610486; gene.
neXtProt; NX_Q9HBW1; -.
OpenTargets; ENSG00000128594; -.
PharmGKB; PA30463; -.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000118831; -.
HOGENOM; HOG000252924; -.
HOVERGEN; HBG052359; -.
InParanoid; Q9HBW1; -.
KO; K16351; -.
OMA; SWWLREY; -.
OrthoDB; EOG091G037N; -.
PhylomeDB; Q9HBW1; -.
TreeFam; TF324303; -.
EvolutionaryTrace; Q9HBW1; -.
GeneWiki; LRRC4; -.
GenomeRNAi; 64101; -.
PRO; PR:Q9HBW1; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000128594; -.
CleanEx; HS_LRRC4; -.
ExpressionAtlas; Q9HBW1; baseline and differential.
Genevisible; Q9HBW1; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0004860; F:protein kinase inhibitor activity; IBA:GO_Central.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IBA:GO_Central.
GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
GO; GO:0097119; P:postsynaptic density protein 95 clustering; IEA:Ensembl.
GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR026882; Lrrc4.
InterPro; IPR000372; LRRNT.
PANTHER; PTHR24369:SF9; PTHR24369:SF9; 1.
Pfam; PF07679; I-set; 1.
Pfam; PF13855; LRR_8; 3.
SMART; SM00409; IG; 1.
SMART; SM00408; IGc2; 1.
SMART; SM00369; LRR_TYP; 7.
SMART; SM00082; LRRCT; 1.
SMART; SM00013; LRRNT; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51450; LRR; 7.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain;
Leucine-rich repeat; Membrane; Polymorphism;
Postsynaptic cell membrane; Reference proteome; Repeat; Signal;
Synapse; Transmembrane; Transmembrane helix.
SIGNAL 1 38 {ECO:0000255}.
CHAIN 39 653 Leucine-rich repeat-containing protein 4.
/FTId=PRO_0000014833.
TOPO_DOM 39 527 Extracellular. {ECO:0000255}.
TRANSMEM 528 548 Helical. {ECO:0000255}.
TOPO_DOM 549 653 Cytoplasmic. {ECO:0000255}.
DOMAIN 39 75 LRRNT.
REPEAT 76 97 LRR 1.
REPEAT 100 121 LRR 2.
REPEAT 124 145 LRR 3.
REPEAT 148 169 LRR 4.
REPEAT 172 194 LRR 5.
REPEAT 197 218 LRR 6.
REPEAT 219 240 LRR 7.
REPEAT 243 264 LRR 8.
REPEAT 267 288 LRR 9.
DOMAIN 300 352 LRRCT.
DOMAIN 353 442 Ig-like.
COMPBIAS 455 526 Thr-rich.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 388 388 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 434 434 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 440 440 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 447 447 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 450 450 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 46 52 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21946559}.
DISULFID 50 61 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21946559}.
DISULFID 304 329 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21946559}.
DISULFID 306 350 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21946559}.
DISULFID 374 424 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21946559}.
VARIANT 579 579 T -> A (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035519.
CONFLICT 4 4 L -> S (in Ref. 4; BAD18737).
{ECO:0000305}.
CONFLICT 253 257 QVSLI -> H (in Ref. 2; CAC82651).
{ECO:0000305}.
CONFLICT 300 300 N -> D (in Ref. 4; BAD18737).
{ECO:0000305}.
CONFLICT 315 315 L -> F (in Ref. 4; BAD18737).
{ECO:0000305}.
STRAND 50 52 {ECO:0000244|PDB:3ZYI}.
STRAND 54 56 {ECO:0000244|PDB:3ZYI}.
STRAND 58 60 {ECO:0000244|PDB:3ZYI}.
STRAND 78 81 {ECO:0000244|PDB:3ZYI}.
TURN 92 97 {ECO:0000244|PDB:3ZYI}.
STRAND 103 105 {ECO:0000244|PDB:3ZYI}.
TURN 116 121 {ECO:0000244|PDB:3ZYI}.
STRAND 127 129 {ECO:0000244|PDB:3ZYI}.
TURN 140 142 {ECO:0000244|PDB:3ZYI}.
STRAND 143 145 {ECO:0000244|PDB:3ZYI}.
STRAND 151 153 {ECO:0000244|PDB:3ZYI}.
TURN 164 169 {ECO:0000244|PDB:3ZYI}.
STRAND 175 177 {ECO:0000244|PDB:3ZYI}.
TURN 189 194 {ECO:0000244|PDB:3ZYI}.
STRAND 200 202 {ECO:0000244|PDB:3ZYI}.
STRAND 222 224 {ECO:0000244|PDB:3ZYI}.
STRAND 231 233 {ECO:0000244|PDB:3ZYI}.
HELIX 235 238 {ECO:0000244|PDB:3ZYI}.
STRAND 246 248 {ECO:0000244|PDB:3ZYI}.
TURN 259 264 {ECO:0000244|PDB:3ZYI}.
STRAND 270 272 {ECO:0000244|PDB:3ZYI}.
STRAND 294 296 {ECO:0000244|PDB:3ZYI}.
TURN 306 308 {ECO:0000244|PDB:3ZYI}.
HELIX 309 318 {ECO:0000244|PDB:3ZYI}.
STRAND 328 332 {ECO:0000244|PDB:3ZYI}.
TURN 333 337 {ECO:0000244|PDB:3ZYI}.
HELIX 345 347 {ECO:0000244|PDB:3ZYI}.
STRAND 362 365 {ECO:0000244|PDB:2DL9}.
STRAND 370 372 {ECO:0000244|PDB:2DL9}.
STRAND 380 385 {ECO:0000244|PDB:3ZYI}.
TURN 387 389 {ECO:0000244|PDB:2DL9}.
STRAND 390 393 {ECO:0000244|PDB:2DL9}.
STRAND 399 403 {ECO:0000244|PDB:2DL9}.
STRAND 405 407 {ECO:0000244|PDB:2DL9}.
STRAND 409 413 {ECO:0000244|PDB:2DL9}.
TURN 416 418 {ECO:0000244|PDB:2DL9}.
STRAND 420 427 {ECO:0000244|PDB:3ZYI}.
STRAND 432 440 {ECO:0000244|PDB:3ZYI}.
SEQUENCE 653 AA; 72717 MW; 38159C81F6850E37 CRC64;
MKLLWQVTVH HHTWNAILLP FVYLTAQVWI LCAAIAAAAS AGPQNCPSVC SCSNQFSKVV
CTRRGLSEVP QGIPSNTRYL NLMENNIQMI QADTFRHLHH LEVLQLGRNS IRQIEVGAFN
GLASLNTLEL FDNWLTVIPS GAFEYLSKLR ELWLRNNPIE SIPSYAFNRV PSLMRLDLGE
LKKLEYISEG AFEGLFNLKY LNLGMCNIKD MPNLTPLVGL EELEMSGNHF PEIRPGSFHG
LSSLKKLWVM NSQVSLIERN AFDGLASLVE LNLAHNNLSS LPHDLFTPLR YLVELHLHHN
PWNCDCDILW LAWWLREYIP TNSTCCGRCH APMHMRGRYL VEVDQASFQC SAPFIMDAPR
DLNISEGRMA ELKCRTPPMS SVKWLLPNGT VLSHASRHPR ISVLNDGTLN FSHVLLSDTG
VYTCMVTNVA GNSNASAYLN VSTAELNTSN YSFFTTVTVE TTEISPEDTT RKYKPVPTTS
TGYQPAYTTS TTVLIQTTRV PKQVAVPATD TTDKMQTSLD EVMKTTKIII GCFVAVTLLA
AAMLIVFYKL RKRHQQRSTV TAARTVEIIQ VDEDIPAATS AAATAAPSGV SGEGAVVLPT
IHDHINYNTY KPAHGAHWTE NSLGNSLHPT VTTISEPYII QTHTKDKVQE TQI


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18-003-43413 JmjC domain-containing histone demethylation protein 1A - EC 1.14.11.27; [Histone-H3]-lysine-36 demethylase 1A; F-box_LRR-repeat protein 11; F-box and leucine-rich repeat protein 11; F-box protein FBL 0.05 mg Aff Pur
EIAAB44217 E2IG4,E2-induced gene 4 protein,Homo sapiens,Human,Leucine-rich repeat-containing protein 54,LRRC54,TSK,TSKU,Tsukushi,Tsukushin,UNQ850_PRO1788
EIAAB43191 C9orf127,Homo sapiens,Human,Nasopharyngeal carcinoma-associated gene 6 protein,NGX6,Protein NAG-5,Protein NGX6,TMEM8B,Transmembrane protein 8B
FBXL19 FBXL17 Gene F-box and leucine-rich repeat protein 17
FBXL22 FBXL20 Gene F-box and leucine-rich repeat protein 20
FBXL8 FBXL6 Gene F-box and leucine-rich repeat protein 6
FBXL16 FBXL14 Gene F-box and leucine-rich repeat protein 14
FBXL15 FBXL13 Gene F-box and leucine-rich repeat protein 13
FBXL18 FBXL16 Gene F-box and leucine-rich repeat protein 16
FBXL2 FBXL18 Gene F-box and leucine-rich repeat protein 18
FBXL20 FBXL19 Gene F-box and leucine-rich repeat protein 19


 

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