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 02-SEP-2026, entry version 167. 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; Q13099: IFT88; NbExp=4; IntAct=EBI-717093, EBI-347427; CC Q96C92; Q9HC29: NOD2; NbExp=5; IntAct=EBI-717093, EBI-7445625; 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_001039707.2. [Q96C92-1] DR RefSeq; NP_001034797.1; NM_001039708.2. [Q96C92-4] DR RefSeq; NP_006634.3; NM_006643.4. [Q96C92-2] DR AlphaFoldDB; Q96C92; -. DR SMR; Q96C92; -. DR BioGRID; 116021; 206. DR CORUM; Q96C92; -. DR FunCoup; Q96C92; 1734. DR IntAct; Q96C92; 82. 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 jPOST; Q96C92; -. DR MassIVE; Q96C92; -. DR PaxDb; 9606-ENSP00000349929; -. DR PeptideAtlas; Q96C92; -. DR ProteomicsDB; 76166; -. [Q96C92-1] DR ProteomicsDB; 76167; -. [Q96C92-2] DR ProteomicsDB; 76168; -. [Q96C92-3] DR ProteomicsDB; 76169; -. [Q96C92-4] DR Pumba; Q96C92; -. DR Antibodypedia; 32151; 137 antibodies from 22 providers. DR DNASU; 10807; -. DR Ensembl; ENST00000298537.11; ENSP00000298537.7; ENSG00000165689.18. [Q96C92-2] DR Ensembl; ENST00000357365.8; ENSP00000349929.3; ENSG00000165689.18. [Q96C92-1] DR Ensembl; ENST00000371725.7; ENSP00000360790.3; ENSG00000165689.18. [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 AGR; HGNC:10667; -. DR ClinPGx; PA35597; -. 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 OpenTargets; ENSG00000165689; -. DR VEuPathDB; HostDB:ENSG00000165689; -. DR eggNOG; ENOG502QUJK; Eukaryota. DR GeneTree; ENSGT00390000000560; -. DR HOGENOM; CLU_051353_0_0_1; -. DR InParanoid; Q96C92; -. DR OMA; WSGSYHP; -. DR OrthoDB; 6499155at2759; -. DR PAN-GO; Q96C92; 8 GO annotations based on evolutionary models. DR PhylomeDB; Q96C92; -. DR PathwayCommons; Q96C92; -. DR SignaLink; Q96C92; -. DR SIGNOR; Q96C92; -. DR Agora; ENSG00000165689; -. DR BioGRID-ORCS; 10807; 26 hits in 1150 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 190 other cell types or tissues. DR ExpressionAtlas; Q96C92; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS: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: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:0032465; P:regulation of cytokinesis; IDA:UniProtKB. DR InterPro; IPR026757; ENTR1. DR InterPro; IPR063798; ENTR1_CC. DR PANTHER; PTHR31259; ENDOSOME-ASSOCIATED TRAFFICKING REGULATOR 1; 1. DR PANTHER; PTHR31259:SF6; ENDOSOME-ASSOCIATED-TRAFFICKING REGULATOR 1; 1. DR Pfam; PF29363; ENTR1; 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; Proteomics identification; KW 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 173..182 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 240..250 FT /note="Low complexity" 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 //