RB6I2_HUMAN
ID RB6I2_HUMAN Reviewed; 1116 AA.
AC Q8IUD2; A2RU77; A7E295; D3DUP7; D3DUP8; Q6NVK2; Q8IUD3; Q8IUD4; Q8IUD5;
AC Q8NAS1; Q9NXN5; Q9UIK7; Q9UPS1;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=ELKS/Rab6-interacting/CAST family member 1;
DE Short=ERC-1;
DE AltName: Full=Rab6-interacting protein 2;
GN Name=ERC1; Synonyms=ELKS, KIAA1081, RAB6IP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND CHROMOSOMAL TRANSLOCATION WITH
RP RET.
RX PubMed=10337992;
RX DOI=10.1002/(sici)1098-2264(199906)25:2<97::aid-gcc4>3.0.co;2-l;
RA Nakata T., Kitamura Y., Shimizu K., Tanaka S., Fujimori M., Yokoyama S.,
RA Ito K., Emi M.;
RT "Fusion of a novel gene, ELKS, to RET due to translocation
RT t(10;12)(q11;p13) in a papillary thyroid carcinoma.";
RL Genes Chromosomes Cancer 25:97-103(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 5), AND TISSUE
RP SPECIFICITY.
RX PubMed=12203787; DOI=10.1002/gcc.10095;
RA Nakata T., Yokota T., Emi M., Minami S.;
RT "Differential expression of multiple isoforms of the ELKS mRNAs involved in
RT a papillary thyroid carcinoma.";
RL Genes Chromosomes Cancer 35:30-37(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-652 (ISOFORM 3).
RC TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1061 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [6]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [7]
RP PROTEIN SEQUENCE OF 254-269, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 733-1116 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 828-1116 (ISOFORMS 1/3).
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH CHUK; IKBKB; IKBKG AND NFKBIA.
RX PubMed=15218148; DOI=10.1126/science.1098387;
RA Ducut Sigala J.L., Bottero V., Young D.B., Shevchenko A., Mercurio F.,
RA Verma I.M.;
RT "Activation of transcription factor NF-kappaB requires ELKS, an IkappaB
RT kinase regulatory subunit.";
RL Science 304:1963-1967(2004).
RN [10]
RP INTERACTION WITH PPFIA1.
RX PubMed=12923177; DOI=10.1074/jbc.m307561200;
RA Ko J., Na M., Kim S., Lee J.R., Kim E.;
RT "Interaction of the ERC family of RIM-binding proteins with the liprin-
RT alpha family of multidomain proteins.";
RL J. Biol. Chem. 278:42377-42385(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-21 AND THR-1046, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-21, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND THR-38, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SDCCAG8.
RX PubMed=27224062; DOI=10.1371/journal.pone.0156081;
RA Airik R., Schueler M., Airik M., Cho J., Ulanowicz K.A., Porath J.D.,
RA Hurd T.W., Bekker-Jensen S., Schroeder J.M., Andersen J.S., Hildebrandt F.;
RT "SDCCAG8 interacts with RAB effector proteins RABEP2 and ERC1 and is
RT required for Hedgehog Signaling.";
RL PLoS ONE 11:E0156081-E0156081(2016).
CC -!- FUNCTION: Regulatory subunit of the IKK complex. Probably recruits
CC IkappaBalpha/NFKBIA to the complex. May be involved in the organization
CC of the cytomatrix at the nerve terminals active zone (CAZ) which
CC regulates neurotransmitter release. May be involved in vesicle
CC trafficking at the CAZ. May be involved in Rab-6 regulated endosomes to
CC Golgi transport. {ECO:0000269|PubMed:15218148}.
CC -!- SUBUNIT: Part of a complex with CHUK, IKBKB and IKBKG. Interacts with
CC CHUK, IKBKB and IKBKG. The interaction with IKBKG is independent of
CC CHUK and IKBKB. Interacts with NFKBIA. Isoform 4 interacts with PPFIA1,
CC and through its C-terminus with the PDZ domains of RIMS1 and RIMS2.
CC Interacts with ERC2/CAST1. Interacts with the GTB-bound forms of RAB6A
CC isoform 1 and isoform 2 and with RAB6B. The interaction was strongest
CC with RAB6B, followed by RAB6A isoform 2 and weakest with RAB6A isoform
CC 1 (By similarity). Interacts with SDCCAG8. {ECO:0000250,
CC ECO:0000269|PubMed:27224062}.
CC -!- INTERACTION:
CC Q8IUD2-2; Q8R0S4: Cacnb4; Xeno; NbExp=2; IntAct=EBI-6920871, EBI-3647752;
CC Q8IUD2-3; PRO_0000037573 [P27958]; Xeno; NbExp=8; IntAct=EBI-9352449, EBI-3649474;
CC Q8IUD2-4; PRO_0000037573 [P27958]; Xeno; NbExp=3; IntAct=EBI-9352501, EBI-3649474;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:27224062}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q811U3}. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q811U3}. Note=Recruited on Golgi membranes by
CC RAB6A in a GTP-dependent manner (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=ELKS epsilon;
CC IsoId=Q8IUD2-1; Sequence=Displayed;
CC Name=2; Synonyms=ELKS beta;
CC IsoId=Q8IUD2-2; Sequence=VSP_011451, VSP_011452, VSP_011454,
CC VSP_011455;
CC Name=3; Synonyms=ELKS delta;
CC IsoId=Q8IUD2-3; Sequence=VSP_011451;
CC Name=4; Synonyms=ELKS alpha;
CC IsoId=Q8IUD2-4; Sequence=VSP_011451, VSP_011452, VSP_011453,
CC VSP_011454, VSP_011455;
CC Name=5; Synonyms=ELKS gamma;
CC IsoId=Q8IUD2-5; Sequence=VSP_011450, VSP_011452, VSP_011454,
CC VSP_011455;
CC -!- TISSUE SPECIFICITY: Widely expressed. Isoform 2 and isoform 4 are
CC abundantly expressed in brain. Isoform 1 and isoform 3 are
CC predominantly expressed in testis and thyroid, and isoform 1
CC predominates in other tissues tested. {ECO:0000269|PubMed:12203787}.
CC -!- DISEASE: Note=A chromosomal aberration involving ERC1/RAB6IP2 is found
CC in papillary thyroid carcinomas (PTCs). Translocation t(10;12)(q11;p13)
CC involving RET. In vitro, isoform 1, isoform 3 and isoform 5
CC participating in a ERC1-RET fusion protein activate tyrosine-protein
CC kinase activity. {ECO:0000269|PubMed:10337992}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH68006.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA83033.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA90975.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ELKSID503.html";
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DR EMBL; AB015617; BAA88763.1; -; mRNA.
DR EMBL; AB053469; BAC54108.1; -; mRNA.
DR EMBL; AB053468; BAC54107.1; -; mRNA.
DR EMBL; AB053470; BAC54109.1; -; mRNA.
DR EMBL; AB053471; BAC54110.1; -; mRNA.
DR EMBL; CH471116; EAW88932.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88934.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88936.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88938.1; -; Genomic_DNA.
DR EMBL; BC068006; AAH68006.1; ALT_SEQ; mRNA.
DR EMBL; BC132782; AAI32783.1; -; mRNA.
DR EMBL; BC132784; AAI32785.1; -; mRNA.
DR EMBL; BC150248; AAI50249.1; -; mRNA.
DR EMBL; AB029004; BAA83033.2; ALT_INIT; mRNA.
DR EMBL; AK000148; BAA90975.1; ALT_INIT; mRNA.
DR EMBL; AK092201; BAC03827.1; -; mRNA.
DR CCDS; CCDS53732.1; -. [Q8IUD2-3]
DR CCDS; CCDS8508.1; -. [Q8IUD2-1]
DR RefSeq; NP_829883.1; NM_178039.3. [Q8IUD2-3]
DR RefSeq; NP_829884.1; NM_178040.3. [Q8IUD2-1]
DR RefSeq; XP_011519243.1; XM_011520941.2. [Q8IUD2-1]
DR RefSeq; XP_016874553.1; XM_017019064.1. [Q8IUD2-1]
DR RefSeq; XP_016874556.1; XM_017019067.1. [Q8IUD2-3]
DR AlphaFoldDB; Q8IUD2; -.
DR SMR; Q8IUD2; -.
DR BioGRID; 116714; 145.
DR CORUM; Q8IUD2; -.
DR IntAct; Q8IUD2; 76.
DR MINT; Q8IUD2; -.
DR STRING; 9606.ENSP00000468263; -.
DR GlyGen; Q8IUD2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IUD2; -.
DR MetOSite; Q8IUD2; -.
DR PhosphoSitePlus; Q8IUD2; -.
DR BioMuta; ERC1; -.
DR DMDM; 51827892; -.
DR EPD; Q8IUD2; -.
DR jPOST; Q8IUD2; -.
DR MassIVE; Q8IUD2; -.
DR MaxQB; Q8IUD2; -.
DR PaxDb; Q8IUD2; -.
DR PeptideAtlas; Q8IUD2; -.
DR PRIDE; Q8IUD2; -.
DR ProteomicsDB; 70547; -. [Q8IUD2-1]
DR ProteomicsDB; 70548; -. [Q8IUD2-2]
DR ProteomicsDB; 70549; -. [Q8IUD2-3]
DR ProteomicsDB; 70550; -. [Q8IUD2-4]
DR ProteomicsDB; 70551; -. [Q8IUD2-5]
DR Antibodypedia; 10295; 183 antibodies from 33 providers.
DR DNASU; 23085; -.
DR Ensembl; ENST00000347735.10; ENSP00000340054.6; ENSG00000082805.21. [Q8IUD2-4]
DR Ensembl; ENST00000360905.9; ENSP00000354158.3; ENSG00000082805.21. [Q8IUD2-1]
DR Ensembl; ENST00000397203.7; ENSP00000380386.4; ENSG00000082805.21. [Q8IUD2-1]
DR Ensembl; ENST00000440394.7; ENSP00000410064.2; ENSG00000082805.21. [Q8IUD2-2]
DR Ensembl; ENST00000543086.7; ENSP00000438546.1; ENSG00000082805.21. [Q8IUD2-3]
DR Ensembl; ENST00000545948.5; ENSP00000442976.1; ENSG00000082805.21. [Q8IUD2-5]
DR Ensembl; ENST00000589028.6; ENSP00000468263.1; ENSG00000082805.21. [Q8IUD2-1]
DR GeneID; 23085; -.
DR KEGG; hsa:23085; -.
DR MANE-Select; ENST00000360905.9; ENSP00000354158.3; NM_178040.4; NP_829884.1.
DR UCSC; uc001qjb.3; human. [Q8IUD2-1]
DR CTD; 23085; -.
DR DisGeNET; 23085; -.
DR GeneCards; ERC1; -.
DR HGNC; HGNC:17072; ERC1.
DR HPA; ENSG00000082805; Low tissue specificity.
DR MalaCards; ERC1; -.
DR MIM; 607127; gene.
DR neXtProt; NX_Q8IUD2; -.
DR OpenTargets; ENSG00000082805; -.
DR Orphanet; 146; Differentiated thyroid carcinoma.
DR Orphanet; 280325; Distal monosomy 12p.
DR PharmGKB; PA134970875; -.
DR VEuPathDB; HostDB:ENSG00000082805; -.
DR eggNOG; KOG4809; Eukaryota.
DR GeneTree; ENSGT00650000093320; -.
DR HOGENOM; CLU_009304_0_0_1; -.
DR InParanoid; Q8IUD2; -.
DR OrthoDB; 446752at2759; -.
DR PhylomeDB; Q8IUD2; -.
DR TreeFam; TF324969; -.
DR PathwayCommons; Q8IUD2; -.
DR SignaLink; Q8IUD2; -.
DR SIGNOR; Q8IUD2; -.
DR BioGRID-ORCS; 23085; 9 hits in 1081 CRISPR screens.
DR ChiTaRS; ERC1; human.
DR GeneWiki; ERC1; -.
DR GenomeRNAi; 23085; -.
DR Pharos; Q8IUD2; Tbio.
DR PRO; PR:Q8IUD2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8IUD2; protein.
DR Bgee; ENSG00000082805; Expressed in sural nerve and 198 other tissues.
DR ExpressionAtlas; Q8IUD2; baseline and differential.
DR Genevisible; Q8IUD2; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008385; C:IkappaB kinase complex; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; TAS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:ParkinsonsUK-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0030165; F:PDZ domain binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031267; F:small GTPase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0007252; P:I-kappaB phosphorylation; IDA:UniProtKB.
DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; IBA:GO_Central.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:ParkinsonsUK-UCL.
DR InterPro; IPR019323; ELKS/CAST.
DR InterPro; IPR037245; FIP-RBD_C_sf.
DR InterPro; IPR019018; Rab-bd_FIP-RBD.
DR Pfam; PF10174; Cast; 3.
DR Pfam; PF09457; RBD-FIP; 1.
DR SUPFAM; SSF144270; SSF144270; 1.
DR PROSITE; PS51511; FIP_RBD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Cell projection;
KW Chromosomal rearrangement; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Synapse; Transport.
FT CHAIN 1..1116
FT /note="ELKS/Rab6-interacting/CAST family member 1"
FT /id="PRO_0000097176"
FT DOMAIN 1046..1108
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 144..988
FT /evidence="ECO:0000255"
FT COILED 1060..1100
FT /evidence="ECO:0000255"
FT COMPBIAS 31..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 719..720
FT /note="Breakpoint for translocation to form ERC1-RET
FT oncogene"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MI1"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 38
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MI1"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1005
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811U3"
FT MOD_RES 1046
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 224..523
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12203787"
FT /id="VSP_011450"
FT VAR_SEQ 440..467
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10337992,
FT ECO:0000303|PubMed:10470851, ECO:0000303|PubMed:12203787,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_011451"
FT VAR_SEQ 783
FT /note="E -> ESLTS (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10337992,
FT ECO:0000303|PubMed:10470851, ECO:0000303|PubMed:12203787,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_011452"
FT VAR_SEQ 830..873
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10337992"
FT /id="VSP_011453"
FT VAR_SEQ 1009..1016
FT /note="IIQPLLEL -> DEEEGIWA (in isoform 2, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:10337992,
FT ECO:0000303|PubMed:10470851, ECO:0000303|PubMed:12203787,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_011454"
FT VAR_SEQ 1017..1116
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10337992,
FT ECO:0000303|PubMed:10470851, ECO:0000303|PubMed:12203787,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_011455"
FT VARIANT 50
FT /note="S -> G (in dbSNP:rs35037408)"
FT /id="VAR_051304"
FT VARIANT 1032
FT /note="T -> A (in dbSNP:rs12319376)"
FT /id="VAR_051305"
FT CONFLICT 828
FT /note="L -> G (in Ref. 8; BAA90975)"
FT /evidence="ECO:0000305"
FT CONFLICT 892
FT /note="K -> R (in Ref. 8; BAC03827)"
FT /evidence="ECO:0000305"
FT CONFLICT 910
FT /note="T -> I (in Ref. 8; BAC03827)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="S -> G (in Ref. 8; BAA90975)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1116 AA; 128086 MW; CCB70380AA7C6E69 CRC64;
MYGSARSVGK VEPSSQSPGR SPRLPRSPRL GHRRTNSTGG SSGSSVGGGS GKTLSMENIQ
SLNAAYATSG PMYLSDHENV GSETPKSTMT LGRSGGRLPY GVRMTAMGSS PNIASSGVAS
DTIAFGEHHL PPVSMASTVP HSLRQARDNT IMDLQTQLKE VLRENDLLRK DVEVKESKLS
SSMNSIKTFW SPELKKERAL RKDEASKITI WKEQYRVVQE ENQHMQMTIQ ALQDELRIQR
DLNQLFQQDS SSRTGEPCVA ELTEENFQRL HAEHERQAKE LFLLRKTLEE MELRIETQKQ
TLNARDESIK KLLEMLQSKG LSAKATEEDH ERTRRLAEAE MHVHHLESLL EQKEKENSML
REEMHRRFEN APDSAKTKAL QTVIEMKDSK ISSMERGLRD LEEEIQMLKS NGALSTEERE
EEMKQMEVYR SHSKFMKNKV EQLKEELSSK EAQWEELKKK AAGLQAEIGQ VKQELSRKDT
ELLALQTKLE TLTNQFSDSK QHIEVLKESL TAKEQRAAIL QTEVDALRLR LEEKETMLNK
KTKQIQDMAE EKGTQAGEIH DLKDMLDVKE RKVNVLQKKI ENLQEQLRDK EKQMSSLKER
VKSLQADTTN TDTALTTLEE ALAEKERTIE RLKEQRDRDE REKQEEIDNY KKDLKDLKEK
VSLLQGDLSE KEASLLDLKE HASSLASSGL KKDSRLKTLE IALEQKKEEC LKMESQLKKA
HEAALEARAS PEMSDRIQHL EREITRYKDE SSKAQAEVDR LLEILKEVEN EKNDKDKKIA
ELERQVKDQN KKVANLKHKE QVEKKKSAQM LEEARRREDN LNDSSQQLQD SLRKKDDRIE
ELEEALRESV QITAEREMVL AQEESARTNA EKQVEELLMA MEKVKQELES MKAKLSSTQQ
SLAEKETHLT NLRAERRKHL EEVLEMKQEA LLAAISEKDA NIALLELSSS KKKTQEEVAA
LKREKDRLVQ QLKQQTQNRM KLMADNYEDD HFKSSHSNQT NHKPSPDQII QPLLELDQNR
SKLKLYIGHL TTLCHDRDPL ILRGLTPPAS YNLDDDQAAW ENELQKMTRG QLQDELEKGE
RDNAELQEFA NAILQQIADH CPDILEQVVN ALEESS
