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IQCJ-SCHIP1 readthrough transcript protein

 IQIP1_HUMAN             Reviewed;         563 AA.
B3KU38; B3KRM0; O75543; Q00P30; Q00P31; Q7Z3Y3; Q8IY83; Q9P0W3; Q9P0W4;
Q9P0W5;
22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
22-NOV-2017, sequence version 2.
29-SEP-2021, entry version 75.
RecName: Full=IQCJ-SCHIP1 readthrough transcript protein {ECO:0000312|HGNC:HGNC:38842};
Name=IQCJ-SCHIP1 {ECO:0000312|HGNC:HGNC:38842};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:BAG53300.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IQCJ-SCHIP1-1 AND IQCJ-SCHIP1-2),
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=17045569; DOI=10.1016/j.bbrc.2006.09.136;
Kwasnicka-Crawford D.A., Carson A.R., Scherer S.W.;
"IQCJ-SCHIP1, a novel fusion transcript encoding a calmodulin-binding IQ
motif protein.";
Biochem. Biophys. Res. Commun. 350:890-899(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IQCJ-SCHIP1-1).
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, 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).
[5]
FUNCTION, AND INTERACTION WITH ANK3.
PubMed=25950943; DOI=10.1111/jnc.13158;
Papandreou M.J., Vacher H., Fache M.P., Klingler E., Rueda-Boroni F.,
Ferracci G., Debarnot C., Piperoglou C., Garcia Del Cano G., Goutebroze L.,
Dargent B.;
"CK2-regulated schwannomin-interacting protein IQCJ-SCHIP-1 association
with AnkG contributes to the maintenance of the axon initial segment.";
J. Neurochem. 134:527-537(2015).
-!- FUNCTION: May play a role in action potential conduction in myelinated
cells through the organization of molecular complexes at nodes of
Ranvier and axon initial segments (PubMed:25950943). May also play a
role in axon outgrowth and guidance (By similarity).
{ECO:0000250|UniProtKB:A0A088MLT8, ECO:0000269|PubMed:25950943}.
-!- SUBUNIT: Homooligomer (via coiled coil domain). Interacts (via IQ
domain) with calmodulin; the interaction is direct and lost in presence
of calcium (By similarity). Interacts with ANK3 (via ANK repeats);
required for localization at axon initial segments (AIS) and nodes of
Ranvier (PubMed:25950943). Interacts with SPTBN4. Interacts with KCNQ2
and KCNQ3 (By similarity). {ECO:0000250|UniProtKB:A0A088MLT8,
ECO:0000269|PubMed:25950943}.
-!- SUBCELLULAR LOCATION: Cell projection, axon
{ECO:0000250|UniProtKB:A0A088MLT8}. Cytoplasm
{ECO:0000269|PubMed:17045569}. Note=Localizes to the axon initial
segments (AIS) and nodes of Ranvier of neurons and is absent from
dendrites. {ECO:0000250|UniProtKB:A0A088MLT8}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=IQCJ-SCHIP1-1;
IsoId=B3KU38-1; Sequence=Displayed;
Name=IQCJ-SCHIP1-2;
IsoId=B3KU38-2; Sequence=VSP_059227;
Name=SCHIP1-1; Synonyms=SCHIP-1, SCHIP-1a;
IsoId=P0DPB3-1, Q9P0W5-1;
Sequence=External;
Name=SCHIP1-2; Synonyms=SCHIP-1-D241/253;
IsoId=P0DPB3-2, Q9P0W5-2;
Sequence=External;
Name=SCHIP1-3; Synonyms=SCHIP-1-D22/253;
IsoId=P0DPB3-3, Q9P0W5-3;
Sequence=External;
Name=SCHIP1-4;
IsoId=P0DPB3-4, Q9P0W5-4;
Sequence=External;
Name=IQCJ-1;
IsoId=Q1A5X6-1; Sequence=External;
Name=IQCJ-2;
IsoId=Q1A5X6-2; Sequence=External;
Name=IQCJ-3;
IsoId=Q1A5X6-3; Sequence=External;
-!- TISSUE SPECIFICITY: Highly expressed in brain and to a lower extent in
heart and kidney. {ECO:0000269|PubMed:17045569}.
-!- DEVELOPMENTAL STAGE: Isoform IQCJ-SCHIP1-1 and isoform IQCJ-SCHIP1-2
are expressed in fetal brain, kidney, spleen and skeletal muscle.
Isoform IQCJ-SCHIP1-2 is also detected in fetal heart and lung.
{ECO:0000269|PubMed:17045569}.
-!- MISCELLANEOUS: [Isoform IQCJ-SCHIP1-1]: Based on a naturally occurring
readthrough transcript which produces an IQCJ-SCHIP1 fusion protein.
{ECO:0000269|PubMed:17045569}.
-!- MISCELLANEOUS: [Isoform IQCJ-SCHIP1-2]: Based on a naturally occurring
readthrough transcript which produces an IQCJ-SCHIP1 fusion protein.
{ECO:0000269|PubMed:17045569}.
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EMBL; DQ157847; ABA42889.1; -; mRNA.
EMBL; DQ157848; ABA42890.1; -; mRNA.
EMBL; AK096479; BAG53300.1; -; mRNA.
EMBL; AC021654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC063955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC068770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC107312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC131150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS56289.1; -. [B3KU38-1]
CCDS; CCDS56291.1; -. [B3KU38-2]
RefSeq; NP_001184042.1; NM_001197113.1. [B3KU38-1]
RefSeq; NP_001184043.1; NM_001197114.1. [B3KU38-2]
SMR; B3KU38; -.
STRING; 9606.ENSP00000420182; -.
iPTMnet; B3KU38; -.
BioMuta; IQCJ-SCHIP1; -.
jPOST; B3KU38; -.
MassIVE; B3KU38; -.
PRIDE; B3KU38; -.
Antibodypedia; 78841; 107 antibodies.
DNASU; 100505385; -.
Ensembl; ENST00000476809; ENSP00000418692; ENSG00000283154. [B3KU38-2]
Ensembl; ENST00000485419; ENSP00000420182; ENSG00000283154. [B3KU38-1]
GeneID; 100505385; -.
KEGG; hsa:100505385; -.
CTD; 100505385; -.
DisGeNET; 100505385; -.
GeneCards; IQCJ-SCHIP1; -.
HGNC; HGNC:38842; IQCJ-SCHIP1.
HPA; ENSG00000283154; Tissue enhanced (brain).
neXtProt; NX_B3KU38; -.
OpenTargets; ENSG00000283154; -.
VEuPathDB; HostDB:ENSG00000283154; -.
eggNOG; KOG4847; Eukaryota.
GeneTree; ENSGT00390000011127; -.
OMA; CGTCVPE; -.
OrthoDB; 1290403at2759; -.
PathwayCommons; B3KU38; -.
BioGRID-ORCS; 100505385; 8 hits in 949 CRISPR screens.
ChiTaRS; IQCJ-SCHIP1; human.
GenomeRNAi; 100505385; -.
Pharos; B3KU38; Tdark.
PRO; PR:B3KU38; -.
Proteomes; UP000005640; Chromosome 3.
ExpressionAtlas; B3KU38; baseline and differential.
Genevisible; B3KU38; HS.
GO; GO:0043194; C:axon initial segment; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0051494; P:negative regulation of cytoskeleton organization; IMP:UniProtKB.
GO; GO:0035332; P:positive regulation of hippo signaling; IBA:GO_Central.
InterPro; IPR029362; IQCJ-SCHIP1_N.
InterPro; IPR039045; SCHIP_1.
InterPro; IPR015649; SCHIP_1_C.
PANTHER; PTHR13103; PTHR13103; 1.
Pfam; PF15157; IQCJ-SCHIP1; 1.
Pfam; PF10148; SCHIP-1; 1.
1: Evidence at protein level;
Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
Phosphoprotein; Reference proteome.
CHAIN 1..563
/note="IQCJ-SCHIP1 readthrough transcript protein"
/id="PRO_0000442334"
DOMAIN 47..67
/note="IQ"
REGION 63..150
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 164..295
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 312..336
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 384..430
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 419..563
/note="Required for interaction with ankyrins"
/evidence="ECO:0000250|UniProtKB:A0A088MLT8"
COILED 500..534
/evidence="ECO:0000255"
COMPBIAS 69..97
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 108..144
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 170..184
/note="Acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 185..199
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 315..333
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 399..415
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 193
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
VAR_SEQ 26..52
/note="Missing (in isoform IQCJ-SCHIP1-2)"
/id="VSP_059227"
CONFLICT 230
/note="Q -> R (in Ref. 2; BAG53300 and 1; ABA42890/
ABA42889)"
/evidence="ECO:0000305"
CONFLICT 536
/note="D -> A (in Ref. 2; BAG53300 and 1; ABA42890/
ABA42889)"
/evidence="ECO:0000305"
SEQUENCE 563 AA; 62248 MW; 54C0F2D21E4B2739 CRC64;
MRLEELKRLQ NPLEQVNDGK YSFENHQLAM DAENNIEKYP LNLQPLESKV KIIQRAWREY
LQRQEPLGKR SPSPPSVSSE KLSSSVSMNT FSDSSTPDYR EDGMDLGSDA GSSSSSSRAS
SQSNSTKVTP CSECKSSSSP GGSLDLVSAL EDYEEPFPVY QKKVIDEWAP EEDGEEEEEE
DERDQRGYRD DRSPAREPGD VSARTRSGGG GGRSATTAMP PPVPNGNLHQ HDPQDLRHNG
NVVVAGRPSC SRGPRRAIQK PQPAGGRRSG RGPAAGGLCL QPPDGGTCVP EEPPVPPMDW
EALEKHLAGL QFREQEVRNQ GQARTNSTSA QKNERESIRQ KLALGSFFDD GPGIYTSCSK
SGKPSLSSRL QSGMNLQICF VNDSGSDKDS DADDSKTETS LDTPLSPMSK QSSSYSDRDT
TEEESESLDD MDFLTRQKKL QAEAKMALAM AKPMAKMQVE VEKQNRKKSP VADLLPHMPH
ISECLMKRSL KPTDLRDMTI GQLQVIVNDL HSQIESLNEE LVQLLLIRDE LHTEQDAMLV
DIEDLTRHAE SQQKHMAEKM PAK


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Pathways :
WP1049: G Protein Signaling Pathways
WP1713: Two-component system
WP163: Cytoplasmic Ribosomal Proteins
WP1659: Glycine, serine and threonine metabolism
WP2371: Parkinsons Disease Pathway
WP540: Cytoplasmic Ribosomal Proteins
WP1665: Limonene and pinene degradation
WP525: Mitochondrial Unfolded-Protein Response
WP914: NLR proteins
WP1438: Influenza A virus infection
WP1892: Protein folding
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP2032: TSH signaling pathway
WP1887: Post-translational modification: synthesis of GPI-anchored proteins
WP1675: Nitrogen metabolism
WP813: G Protein Signaling Pathways
WP1531: Vitamin D synthesis
WP1032: NLR proteins
WP1616: ABC transporters
WP2199: Seed Development
WP1963: The effect of Glucocorticoids on target gene expression
WP1685: Peptidoglycan biosynthesis
WP288: NLR proteins
WP1692: Protein export
WP1239: Cytoplasmic Ribosomal Proteins

Related Genes :
[Iqcj-Schip1 Iqschfp Schip1] IQCJ-SCHIP1 readthrough transcript protein
[IQCJ-SCHIP1] IQCJ-SCHIP1 readthrough transcript protein
[SCHIP1] Schwannomin-interacting protein 1 (SCHIP-1)
[Schip1] Schwannomin-interacting protein 1 (SCHIP-1)
[Schip1 CG5375] Schwannomin-interacting protein 1 homolog
[Eef1akmt4-Ece2] EEF1AKMT4-ECE2 readthrough transcript protein (EC 3.4.24.71) [Includes: Methyltransferase-like region (EC 2.1.1.-); Endothelin-converting enzyme 2 region (EC 3.4.24.71)]
[EEF1AKMT4-ECE2] EEF1AKMT4-ECE2 readthrough transcript protein (EC 3.4.24.71) [Includes: Methyltransferase-like region (EC 2.1.1.-); Endothelin-converting enzyme 2 region (EC 3.4.24.71)]
[EEF1AKMT4-ECE2] EEF1AKMT4-ECE2 readthrough transcript protein (EC 3.4.24.71) [Includes: Methyltransferase-like region (EC 2.1.1.-); Endothelin-converting enzyme 2 region (EC 3.4.24.71)]
[ANK3] Ankyrin-3 (ANK-3) (Ankyrin-G)
[Ank3] Ankyrin-3 (ANK-3) (Ankyrin-G)
[Kcnq3] Potassium voltage-gated channel subfamily KQT member 3 (KQT-like 3) (Potassium channel subunit alpha KvLQT3) (Voltage-gated potassium channel subunit Kv7.3)
[Kcnq2 Kqt2] Potassium voltage-gated channel subfamily KQT member 2 (KQT-like 2) (Potassium channel subunit alpha KvLQT2) (Voltage-gated potassium channel subunit Kv7.2)
[Kcnq3] Potassium voltage-gated channel subfamily KQT member 3 (KQT-like 3) (Potassium channel subunit alpha KvLQT3) (Voltage-gated potassium channel subunit Kv7.3)
[Ank3] Ankyrin-3 (ANK-3) (Ankyrin-G)
[ZHX1-C8orf76 C8orf76] Zinc fingers and homeoboxes protein 1, isoform 2 (ZHX1-C8orf76 readthrough transcript protein)
[Schip1] Schip1 protein (Schwannomin-interacting protein 1)
[NF2 SCH] Merlin (Moesin-ezrin-radixin-like protein) (Neurofibromin-2) (Schwannomerlin) (Schwannomin)
[Kcnq2] Potassium voltage-gated channel subfamily KQT member 2 (KQT-like 2) (Potassium channel subunit alpha KvLQT2) (Voltage-gated potassium channel subunit Kv7.2)
[KCNQ3] Potassium voltage-gated channel subfamily KQT member 3 (KQT-like 3) (Potassium channel subunit alpha KvLQT3) (Voltage-gated potassium channel subunit Kv7.3)
[KCNQ2] Potassium voltage-gated channel subfamily KQT member 2 (KQT-like 2) (Neuroblastoma-specific potassium channel subunit alpha KvLQT2) (Voltage-gated potassium channel subunit Kv7.2)
[Schip1] Schip1 protein (Fragment)
[Schip1] Schwannomin-interacting protein 1
[ex CG4114] Protein expanded
[Tao Tao-1 CG14217] Serine/threonine-protein kinase Tao (EC 2.7.11.1)
[SCOC SCOCO HRIHFB2072] Short coiled-coil protein
[Mer EMR2 CG14228] Moesin/ezrin/radixin homolog 2 (Ezrin-moesin-radixin 2) (Merlin) (dMerlin)
[hpo CG11228] Serine/threonine-protein kinase hippo (EC 2.7.11.1) (Drosophila homolog of MST1 and MST2) (STE20-like kinase MST) (dMST)
[PSMD4 MCB1] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Antisecretory factor 1) (AF) (ASF) (Multiubiquitin chain-binding protein)
[yki CG4005] Transcriptional coactivator yorkie (Protein yorkie) (Transcriptional coactivator YAP1 homolog)
[KCNQ3] Potassium voltage-gated channel subfamily KQT member 3 (KQT-like 3) (Potassium channel subunit alpha KvLQT3) (Voltage-gated potassium channel subunit Kv7.3)

Bibliography :
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