ENTR1_HUMAN
ID ENTR1_HUMAN Reviewed; 435 AA.
AC Q96C92; A6NCP1; O60525; Q5SXN1; Q5SXN2; Q5SXN3; Q5SXN4; Q5SXN8; Q6V704;
AC Q9NVY5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Endosome-associated-trafficking regulator 1 {ECO:0000305};
DE AltName: Full=Antigen NY-CO-3 {ECO:0000303|PubMed:9610721};
DE AltName: Full=Serologically defined colon cancer antigen 3 {ECO:0000303|PubMed:23108400};
GN Name=ENTR1 {ECO:0000312|HGNC:HGNC:10667}; Synonyms=SDCCAG3;
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 [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS GLN-304
RP AND MET-379.
RA Lin L., Yu R., Cao L., Ke R., Li H., Zhou G., Shen C., Zhong G., Xiao W.,
RA Li M., Yang S.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ILE-428.
RC TISSUE=Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-435 (ISOFORMS 1/3), AND
RP VARIANT GLY-176.
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 221-412.
RC TISSUE=Colon carcinoma;
RX PubMed=9610721;
RX DOI=10.1002/(sici)1097-0215(19980529)76:5<652::aid-ijc7>3.0.co;2-p;
RA Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
RA Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
RT "Characterization of human colon cancer antigens recognized by autologous
RT antibodies.";
RL Int. J. Cancer 76:652-658(1998).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-243, 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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTPN13 AND GIT1,
RP IDENTIFICATION IN A COMPLEX WITH PTPN13 AND GIT1, PHOSPHORYLATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF PRO-190 AND GLU-194.
RX PubMed=23108400; DOI=10.1038/onc.2012.485;
RA Hagemann N., Ackermann N., Christmann J., Brier S., Yu F., Erdmann K.S.;
RT "The serologically defined colon cancer antigen-3 interacts with the
RT protein tyrosine phosphatase PTPN13 and is involved in the regulation of
RT cytokinesis.";
RL Oncogene 32:4602-4613(2013).
RN [13]
RP FUNCTION, INTERACTION WITH VPS35, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=25278552; DOI=10.1242/jcs.156299;
RA McGough I.J., Steinberg F., Gallon M., Yatsu A., Ohbayashi N., Heesom K.J.,
RA Fukuda M., Cullen P.J.;
RT "Identification of molecular heterogeneity in SNX27-retromer-mediated
RT endosome-to-plasma-membrane recycling.";
RL J. Cell Sci. 127:4940-4953(2014).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND SER-243, 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 [15]
RP INTERACTION WITH NOD2.
RX PubMed=27812135; DOI=10.1371/journal.pone.0165420;
RA Thiebaut R., Esmiol S., Lecine P., Mahfouz B., Hermant A., Nicoletti C.,
RA Parnis S., Perroy J., Borg J.P., Pascoe L., Hugot J.P., Ollendorff V.;
RT "Characterization and Genetic Analyses of New Genes Coding for NOD2
RT Interacting Proteins.";
RL PLoS ONE 11:E0165420-E0165420(2016).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH IFT88, AND DOMAIN.
RX PubMed=27767179; DOI=10.1038/srep35399;
RA Yu F., Sharma S., Skowronek A., Erdmann K.S.;
RT "The serologically defined colon cancer antigen-3 (SDCCAG3) is involved in
RT the regulation of ciliogenesis.";
RL Sci. Rep. 6:35399-35399(2016).
CC -!- FUNCTION: Endosome-associated protein that plays a role in membrane
CC receptor sorting, cytokinesis and ciliogenesis (PubMed:23108400,
CC PubMed:25278552, PubMed:27767179). Involved in the endosome-to-plasma
CC membrane trafficking and recycling of SNX27-retromer-dependent cargo
CC proteins, such as GLUT1 (PubMed:25278552). Involved in the regulation
CC of cytokinesis; the function may involve PTPN13 and GIT1
CC (PubMed:23108400). Plays a role in the formation of cilia
CC (PubMed:27767179). Involved in cargo protein localization, such as
CC PKD2, at primary cilia (PubMed:27767179). Involved in the presentation
CC of the tumor necrosis factor (TNF) receptor TNFRSF1A on the cell
CC surface, and hence in the modulation of the TNF-induced apoptosis (By
CC similarity). {ECO:0000250|UniProtKB:A2AIW0,
CC ECO:0000269|PubMed:23108400, ECO:0000269|PubMed:25278552,
CC ECO:0000269|PubMed:27767179}.
CC -!- SUBUNIT: Found in a complex with ENTR1, PTPN13 and GIT1
CC (PubMed:23108400). Interacts with PTPN13 (via the FERM domain)
CC (PubMed:23108400). Interacts (via N-terminus) with GIT1 (via N- and C-
CC terminus); this interaction is direct (PubMed:23108400). Interacts with
CC NOD2 (PubMed:27812135). Interacts (via N-terminus) with IFT88
CC (PubMed:27767179). Interacts with VPS35 (PubMed:25278552).
CC {ECO:0000269|PubMed:23108400, ECO:0000269|PubMed:25278552,
CC ECO:0000269|PubMed:27767179, ECO:0000269|PubMed:27812135}.
CC -!- INTERACTION:
CC Q96C92-2; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-10178036, EBI-541426;
CC Q96C92-2; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-10178036, EBI-16429430;
CC Q96C92-2; P26196: DDX6; NbExp=3; IntAct=EBI-10178036, EBI-351257;
CC Q96C92-2; O00560: SDCBP; NbExp=3; IntAct=EBI-10178036, EBI-727004;
CC Q96C92-2; P0C1Z6-2: TFPT; NbExp=3; IntAct=EBI-10178036, EBI-10178002;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2AIW0}. Early
CC endosome {ECO:0000269|PubMed:23108400}. Endosome
CC {ECO:0000269|PubMed:25278552}. Recycling endosome
CC {ECO:0000269|PubMed:23108400}. Midbody {ECO:0000269|PubMed:23108400}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:23108400, ECO:0000269|PubMed:27767179}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:27767179}.
CC Note=Colocalizes in a WASHC2-dependent manner with the retromer CSC
CC complex at endosomes (PubMed:25278552). During cytokinesis colocalized
CC with PTPN13 at the midbody (PubMed:23108400). Colocalizes with IFT88
CC and gamma-tubulin at the basal body of primary cilia (PubMed:27767179).
CC Colocalizes with IFT88 and pericentrin at the centrosome
CC (PubMed:27767179). {ECO:0000269|PubMed:23108400,
CC ECO:0000269|PubMed:25278552, ECO:0000269|PubMed:27767179}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96C92-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96C92-2; Sequence=VSP_032177;
CC Name=3;
CC IsoId=Q96C92-3; Sequence=VSP_032176;
CC Name=4;
CC IsoId=Q96C92-4; Sequence=VSP_040477;
CC -!- TISSUE SPECIFICITY: Expressed in the colon (at protein level).
CC {ECO:0000269|PubMed:23108400}.
CC -!- DOMAIN: Tne N-terminal domain is necessary and sufficient for basal
CC body localization and ciliogenesis. {ECO:0000269|PubMed:27767179}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:23108400}.
CC -!- SIMILARITY: Belongs to the ENTR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91607.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY349357; AAQ56721.1; -; mRNA.
DR EMBL; CR597452; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL592301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88230.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88231.1; -; Genomic_DNA.
DR EMBL; BC014515; AAH14515.2; -; mRNA.
DR EMBL; AK001296; BAA91607.1; ALT_INIT; mRNA.
DR EMBL; AF039688; AAC18037.1; -; mRNA.
DR CCDS; CCDS43903.1; -. [Q96C92-4]
DR CCDS; CCDS43904.1; -. [Q96C92-1]
DR CCDS; CCDS6999.2; -. [Q96C92-2]
DR RefSeq; NP_001034796.1; NM_001039707.1. [Q96C92-1]
DR RefSeq; NP_001034797.1; NM_001039708.1. [Q96C92-4]
DR RefSeq; NP_006634.3; NM_006643.3. [Q96C92-2]
DR AlphaFoldDB; Q96C92; -.
DR SMR; Q96C92; -.
DR BioGRID; 116021; 188.
DR IntAct; Q96C92; 57.
DR MINT; Q96C92; -.
DR STRING; 9606.ENSP00000349929; -.
DR GlyGen; Q96C92; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96C92; -.
DR PhosphoSitePlus; Q96C92; -.
DR BioMuta; SDCCAG3; -.
DR DMDM; 172045853; -.
DR EPD; Q96C92; -.
DR jPOST; Q96C92; -.
DR MassIVE; Q96C92; -.
DR MaxQB; Q96C92; -.
DR PaxDb; Q96C92; -.
DR PeptideAtlas; Q96C92; -.
DR PRIDE; Q96C92; -.
DR ProteomicsDB; 76166; -. [Q96C92-1]
DR ProteomicsDB; 76167; -. [Q96C92-2]
DR ProteomicsDB; 76168; -. [Q96C92-3]
DR ProteomicsDB; 76169; -. [Q96C92-4]
DR Antibodypedia; 32151; 149 antibodies from 22 providers.
DR DNASU; 10807; -.
DR Ensembl; ENST00000298537.11; ENSP00000298537.7; ENSG00000165689.17. [Q96C92-2]
DR Ensembl; ENST00000357365.8; ENSP00000349929.3; ENSG00000165689.17. [Q96C92-1]
DR Ensembl; ENST00000371725.7; ENSP00000360790.3; ENSG00000165689.17. [Q96C92-4]
DR GeneID; 10807; -.
DR KEGG; hsa:10807; -.
DR MANE-Select; ENST00000357365.8; ENSP00000349929.3; NM_001039707.2; NP_001034796.1.
DR UCSC; uc004chi.4; human. [Q96C92-1]
DR CTD; 10807; -.
DR DisGeNET; 10807; -.
DR GeneCards; ENTR1; -.
DR HGNC; HGNC:10667; ENTR1.
DR HPA; ENSG00000165689; Low tissue specificity.
DR MIM; 618289; gene.
DR neXtProt; NX_Q96C92; -.
DR OpenTargets; ENSG00000165689; -.
DR PharmGKB; PA35597; -.
DR VEuPathDB; HostDB:ENSG00000165689; -.
DR eggNOG; ENOG502QUJK; Eukaryota.
DR GeneTree; ENSGT00390000000560; -.
DR HOGENOM; CLU_051353_0_0_1; -.
DR InParanoid; Q96C92; -.
DR OMA; LEYPQPF; -.
DR OrthoDB; 1429935at2759; -.
DR PhylomeDB; Q96C92; -.
DR TreeFam; TF335840; -.
DR PathwayCommons; Q96C92; -.
DR SignaLink; Q96C92; -.
DR BioGRID-ORCS; 10807; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; SDCCAG3; human.
DR GenomeRNAi; 10807; -.
DR Pharos; Q96C92; Tbio.
DR PRO; PR:Q96C92; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q96C92; protein.
DR Bgee; ENSG00000165689; Expressed in left testis and 188 other tissues.
DR ExpressionAtlas; Q96C92; baseline and differential.
DR Genevisible; Q96C92; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:1903566; P:positive regulation of protein localization to cilium; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032465; P:regulation of cytokinesis; IDA:UniProtKB.
DR InterPro; IPR026757; ENTR1.
DR PANTHER; PTHR31259; PTHR31259; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endosome; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..435
FT /note="Endosome-associated-trafficking regulator 1"
FT /id="PRO_0000324285"
FT REGION 136..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..198
FT /note="Required for interaction with PTPN13"
FT /evidence="ECO:0000269|PubMed:23108400"
FT REGION 225..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 261..371
FT /evidence="ECO:0000255"
FT COMPBIAS 143..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_032176"
FT VAR_SEQ 24..96
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_040477"
FT VAR_SEQ 75..97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032177"
FT VARIANT 157
FT /note="L -> V (in dbSNP:rs7047681)"
FT /id="VAR_039687"
FT VARIANT 176
FT /note="E -> G (in dbSNP:rs17851182)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_039688"
FT VARIANT 304
FT /note="R -> Q (in dbSNP:rs3812577)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_039689"
FT VARIANT 379
FT /note="V -> M (in dbSNP:rs1131992)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_039690"
FT VARIANT 428
FT /note="V -> I (in dbSNP:rs17855450)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_039691"
FT MUTAGEN 190
FT /note="P->A: Disrupts interaction with PTPN13."
FT /evidence="ECO:0000269|PubMed:23108400"
FT MUTAGEN 194
FT /note="E->A: Disrupts interaction with PTPN13."
FT /evidence="ECO:0000269|PubMed:23108400"
FT CONFLICT 7
FT /note="R -> H (in Ref. 4; AAH14515)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="N -> T (in Ref. 1; AAQ56721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 47961 MW; 03EBD9512232B5E3 CRC64;
MSGYQRRPGA TPLSRARSLA IPDAPAFYER RSCLPQLNCE RPHGRDLDSP FFGIRPAFMC
YVPSPVLASV GDTDFGYGKG KCSKQSPSGA HGTHFGDDRF EDLEEANPFS FREFLKTKNL
GLSKEDPASR IYAKEASRHS LGLDHNSPPS QTGGYGLEYQ QPFFEDPTGA GDLLDEEEDE
DTGWSGAYLP SAIEQTHPER VPAGTSPCST YLSFFSTPSE LAGPESLPSW ALSDTDSRVS
PASPAGSPSA DFAVHGESLG DRHLRTLQIS YDALKDENSK LRRKLNEVQS FSEAQTEMVR
TLERKLEAKM IKEESDYHDL ESVVQQVEQN LELMTKRAVK AENHVVKLKQ EISLLQAQVS
NFQRENEALR CGQGASLTVV KQNADVALQN LRVVMNSAQA SIKQLVSGAE TLNLVAEILK
SIDRISEVKD EEEDS
