ID KTN1_HUMAN Reviewed; 1357 AA. AC Q86UP2; B4DZ88; Q13999; Q14707; Q15387; Q17RZ5; Q5GGW3; Q86W57; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 25-MAY-2022, entry version 179. DE RecName: Full=Kinectin; DE AltName: Full=CG-1 antigen; DE AltName: Full=Kinesin receptor; GN Name=KTN1; Synonyms=CG1, KIAA0004; 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 1). RC TISSUE=Lymphoid tissue; RX PubMed=7787243; DOI=10.1091/mbc.6.2.161; RA Fuetterer A., Kruppa G., Kraemer B., Lemke H., Kroenke M.; RT "Molecular cloning and characterization of human kinectin."; RL Mol. Biol. Cell 6:161-170(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Peripheral blood lymphocyte; RX PubMed=8039706; DOI=10.1016/0378-1119(94)90381-6; RA Print C.G., Leung E., Harrison J.E.B., Watson J.D., Krissansen G.W.; RT "Cloning of a gene encoding a human leukocyte protein characterised by RT extensive heptad repeats."; RL Gene 144:221-228(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Wang H.-C., Chen W.-F., Su Y.-R.; RT "Identification of a variant of Homo sapiens kinectin mRNA."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Bone marrow; RX PubMed=7584026; DOI=10.1093/dnares/1.1.27; RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., RA Nagase T., Seki N., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. I. The RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of RT randomly sampled cDNA clones from human immature myeloid cell line KG-1."; RL DNA Res. 1:27-35(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Testis; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-870 (ISOFORMS 1/2). RC TISSUE=Cerebellum, and Lung; 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 [8] RP PROTEIN SEQUENCE OF 191-195; 395-405; 545-554; 747-761 AND 811-823. RX PubMed=11973345; DOI=10.1242/jcs.115.10.2031; RA Tran H., Pankov R., Tran S.D., Hampton B., Burgess W.H., Yamada K.M.; RT "Integrin clustering induces kinectin accumulation."; RL J. Cell Sci. 115:2031-2040(2002). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 538-1357. RC TISSUE=Embryonic rhabdomyosarcoma; RA Behrends U., Gotz C., Mautner J.; RT "SEREX-defined rhabdomyosarcoma antigens."; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [10] RP CHROMOSOMAL LOCATION. RX PubMed=8575822; DOI=10.1007/bf00587304; RA Print C.G., Morris C.M., Spurr N.K., Rooke L., Krissansen G.W.; RT "The CG-1 gene, a member of the kinectin and ES/130 family, maps to human RT chromosome band 14q22."; RL Immunogenetics 43:227-229(1996). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153, AND IDENTIFICATION BY RP 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; THR-153 AND SER-156, 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND THR-153, AND RP IDENTIFICATION BY 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 [15] 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-77; THR-153 AND RP SER-1313, AND 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, AND IDENTIFICATION BY RP 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 [19] RP PHOSPHORYLATION AT SER-75. RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028; RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J., RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N., RA Pinna L.A., Pagliarini D.J., Dixon J.E.; RT "A single kinase generates the majority of the secreted phosphoproteome."; RL Cell 161:1619-1632(2015). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [21] RP VARIANTS [LARGE SCALE ANALYSIS] ARG-226 AND PRO-1316. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [22] RP VARIANT MET-1233. RX PubMed=27932480; DOI=10.1681/asn.2016040387; RG NephroS; RG UK study of Nephrotic Syndrome; RA Bierzynska A., Soderquest K., Dean P., Colby E., Rollason R., Jones C., RA Inward C.D., McCarthy H.J., Simpson M.A., Lord G.M., Williams M., RA Welsh G.I., Koziell A.B., Saleem M.A.; RT "MAGI2 mutations cause congenital nephrotic syndrome."; RL J. Am. Soc. Nephrol. 28:1614-1621(2017). CC -!- FUNCTION: Receptor for kinesin thus involved in kinesin-driven vesicle CC motility. Accumulates in integrin-based adhesion complexes (IAC) upon CC integrin aggregation by fibronectin. CC -!- SUBUNIT: Parallel homodimers formed between the membrane-bound and the CC cytosolic form, and also between 2 cytosolic forms. {ECO:0000250}. CC -!- INTERACTION: CC Q86UP2; Q12983: BNIP3; NbExp=3; IntAct=EBI-359761, EBI-749464; CC Q86UP2; Q9BXN2: CLEC7A; NbExp=3; IntAct=EBI-359761, EBI-3939278; CC Q86UP2; P50222: MEOX2; NbExp=3; IntAct=EBI-359761, EBI-748397; CC Q86UP2; O43765: SGTA; NbExp=3; IntAct=EBI-359761, EBI-347996; CC Q86UP2; Q8N205: SYNE4; NbExp=3; IntAct=EBI-359761, EBI-7131783; CC Q86UP2-3; Q12983: BNIP3; NbExp=3; IntAct=EBI-12007212, EBI-749464; CC Q86UP2-3; P09693: CD3G; NbExp=3; IntAct=EBI-12007212, EBI-3862428; CC Q86UP2-3; P34810: CD68; NbExp=3; IntAct=EBI-12007212, EBI-2826276; CC Q86UP2-3; Q8WTT0: CLEC4C; NbExp=3; IntAct=EBI-12007212, EBI-12913226; CC Q86UP2-3; O15552: FFAR2; NbExp=3; IntAct=EBI-12007212, EBI-2833872; CC Q86UP2-3; P43628: KIR2DL3; NbExp=3; IntAct=EBI-12007212, EBI-8632435; CC Q86UP2-3; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-12007212, EBI-2820517; CC Q86UP2-3; P20645: M6PR; NbExp=3; IntAct=EBI-12007212, EBI-2907262; CC Q86UP2-3; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-12007212, EBI-373355; CC Q86UP2-3; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-12007212, EBI-16427978; CC Q86UP2-3; O43765: SGTA; NbExp=3; IntAct=EBI-12007212, EBI-347996; CC Q86UP2-3; P27105: STOM; NbExp=3; IntAct=EBI-12007212, EBI-1211440; CC Q86UP2-3; Q96L08: SUSD3; NbExp=3; IntAct=EBI-12007212, EBI-18194029; CC Q86UP2-3; Q8TBG9: SYNPR; NbExp=3; IntAct=EBI-12007212, EBI-10273251; CC Q86UP2-3; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-12007212, EBI-11724423; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type CC II membrane protein. Note=Vesicle membrane protein anchored to the CC endoplasmic reticulum. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=Q86UP2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86UP2-2; Sequence=VSP_007981, VSP_007982; CC Name=3; CC IsoId=Q86UP2-3; Sequence=VSP_043207, VSP_007982; CC Name=4; CC IsoId=Q86UP2-4; Sequence=VSP_007982; CC -!- TISSUE SPECIFICITY: High levels in peripheral blood lymphocytes, testis CC and ovary, lower levels in spleen, thymus, prostate, small intestine CC and colon. CC -!- SIMILARITY: Belongs to the kinectin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH50555.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAA02794.2; Type=Erroneous initiation; Note=Extended 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; Z22551; CAA80271.1; -; mRNA. DR EMBL; L25616; AAB65853.1; -; mRNA. DR EMBL; AY264265; AAP20418.1; -; mRNA. DR EMBL; D13629; BAA02794.2; ALT_INIT; mRNA. DR EMBL; AK302797; BAG64000.1; -; mRNA. DR EMBL; AL138499; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL355773; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC050555; AAH50555.1; ALT_SEQ; mRNA. DR EMBL; BC112337; AAI12338.1; -; mRNA. DR EMBL; BC117132; AAI17133.1; -; mRNA. DR EMBL; BC143720; AAI43721.1; -; mRNA. DR EMBL; AY536375; AAT66048.1; -; mRNA. DR CCDS; CCDS41957.1; -. [Q86UP2-1] DR CCDS; CCDS41958.1; -. [Q86UP2-2] DR CCDS; CCDS41959.1; -. [Q86UP2-3] DR PIR; I53799; I53799. DR PIR; S32763; S32763. DR RefSeq; NP_001072989.1; NM_001079521.1. [Q86UP2-1] DR RefSeq; NP_001072990.1; NM_001079522.1. [Q86UP2-3] DR RefSeq; NP_001257943.1; NM_001271014.1. [Q86UP2-4] DR RefSeq; NP_004977.2; NM_004986.3. [Q86UP2-2] DR RefSeq; XP_006720201.1; XM_006720138.2. [Q86UP2-1] DR RefSeq; XP_006720202.1; XM_006720139.2. [Q86UP2-4] DR RefSeq; XP_011535053.1; XM_011536751.2. [Q86UP2-1] DR RefSeq; XP_011535055.1; XM_011536753.1. [Q86UP2-3] DR RefSeq; XP_016876767.1; XM_017021278.1. [Q86UP2-1] DR RefSeq; XP_016876771.1; XM_017021282.1. [Q86UP2-2] DR RefSeq; XP_016876772.1; XM_017021283.1. [Q86UP2-2] DR AlphaFoldDB; Q86UP2; -. DR SMR; Q86UP2; -. DR BioGRID; 110092; 222. DR CORUM; Q86UP2; -. DR DIP; DIP-27585N; -. DR IntAct; Q86UP2; 103. DR MINT; Q86UP2; -. DR STRING; 9606.ENSP00000378725; -. DR GlyGen; Q86UP2; 8 sites. DR iPTMnet; Q86UP2; -. DR MetOSite; Q86UP2; -. DR PhosphoSitePlus; Q86UP2; -. DR SwissPalm; Q86UP2; -. DR BioMuta; KTN1; -. DR DMDM; 34098465; -. DR EPD; Q86UP2; -. DR jPOST; Q86UP2; -. DR MassIVE; Q86UP2; -. DR MaxQB; Q86UP2; -. DR PaxDb; Q86UP2; -. DR PeptideAtlas; Q86UP2; -. DR PRIDE; Q86UP2; -. DR ProteomicsDB; 69841; -. [Q86UP2-1] DR ProteomicsDB; 69842; -. [Q86UP2-2] DR ProteomicsDB; 69843; -. [Q86UP2-3] DR Antibodypedia; 127; 191 antibodies from 26 providers. DR DNASU; 3895; -. DR Ensembl; ENST00000395308.5; ENSP00000378719.1; ENSG00000126777.18. [Q86UP2-3] DR Ensembl; ENST00000395309.7; ENSP00000378720.4; ENSG00000126777.18. [Q86UP2-3] DR Ensembl; ENST00000395311.5; ENSP00000378722.1; ENSG00000126777.18. [Q86UP2-3] DR Ensembl; ENST00000395314.8; ENSP00000378725.3; ENSG00000126777.18. DR Ensembl; ENST00000413890.6; ENSP00000394992.2; ENSG00000126777.18. [Q86UP2-3] DR Ensembl; ENST00000438792.6; ENSP00000391964.2; ENSG00000126777.18. [Q86UP2-2] DR Ensembl; ENST00000459737.5; ENSP00000432149.1; ENSG00000126777.18. DR GeneID; 3895; -. DR KEGG; hsa:3895; -. DR MANE-Select; ENST00000395314.8; ENSP00000378725.3; NM_001079521.2; NP_001072989.1. DR UCSC; uc001xcb.4; human. [Q86UP2-1] DR CTD; 3895; -. DR DisGeNET; 3895; -. DR GeneCards; KTN1; -. DR HGNC; HGNC:6467; KTN1. DR HPA; ENSG00000126777; Low tissue specificity. DR MIM; 600381; gene. DR neXtProt; NX_Q86UP2; -. DR OpenTargets; ENSG00000126777; -. DR PharmGKB; PA30256; -. DR VEuPathDB; HostDB:ENSG00000126777; -. DR eggNOG; ENOG502QSIW; Eukaryota. DR GeneTree; ENSGT00940000158237; -. DR HOGENOM; CLU_005719_0_0_1; -. DR InParanoid; Q86UP2; -. DR OMA; KECMAET; -. DR PhylomeDB; Q86UP2; -. DR TreeFam; TF333579; -. DR PathwayCommons; Q86UP2; -. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-5625970; RHO GTPases activate KTN1. DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013408; RHOG GTPase cycle. DR Reactome; R-HSA-9696264; RND3 GTPase cycle. DR Reactome; R-HSA-9696270; RND2 GTPase cycle. DR SignaLink; Q86UP2; -. DR SIGNOR; Q86UP2; -. DR BioGRID-ORCS; 3895; 14 hits in 1080 CRISPR screens. DR ChiTaRS; KTN1; human. DR GeneWiki; KTN1; -. DR GenomeRNAi; 3895; -. DR Pharos; Q86UP2; Tbio. DR PRO; PR:Q86UP2; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q86UP2; protein. DR Bgee; ENSG00000126777; Expressed in testis and 255 other tissues. DR ExpressionAtlas; Q86UP2; baseline and differential. DR Genevisible; Q86UP2; HS. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0019894; F:kinesin binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0007018; P:microtubule-based movement; NAS:ProtInc. DR GO; GO:0015031; P:protein transport; IEA:InterPro. DR InterPro; IPR024854; Kinectin. DR InterPro; IPR007794; Rib_rcpt_KP. DR PANTHER; PTHR18864; PTHR18864; 1. DR Pfam; PF05104; Rib_recp_KP_reg; 1. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Direct protein sequencing; KW Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1..1357 FT /note="Kinectin" FT /id="PRO_0000084337" FT TOPO_DOM 1..6 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 7..29 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 30..1357 FT /note="Lumenal" FT /evidence="ECO:0000255" FT REGION 48..81 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 103..218 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 330..1356 FT /evidence="ECO:0000255" FT COMPBIAS 63..81 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 109..139 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 162..186 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 194..218 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 75 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 77 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 153 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 156 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1084 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1313 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CARBOHYD 172 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 435 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 772 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 904 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1055 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1088 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1263 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1329 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 832..854 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043207" FT VAR_SEQ 1031..1059 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7584026, FT ECO:0000303|PubMed:8039706" FT /id="VSP_007981" FT VAR_SEQ 1232..1259 FT /note="Missing (in isoform 2, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7584026, FT ECO:0000303|PubMed:8039706" FT /id="VSP_007982" FT VARIANT 226 FT /note="P -> R (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035931" FT VARIANT 282 FT /note="V -> M (in dbSNP:rs2274073)" FT /id="VAR_016206" FT VARIANT 1233 FT /note="L -> M (in dbSNP:rs372815686)" FT /evidence="ECO:0000269|PubMed:27932480" FT /id="VAR_079266" FT VARIANT 1316 FT /note="T -> P (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035932" FT CONFLICT 15 FT /note="S -> P (in Ref. 4; BAA02794)" FT /evidence="ECO:0000305" FT CONFLICT 210 FT /note="Missing (in Ref. 1; CAA80271)" FT /evidence="ECO:0000305" FT CONFLICT 373 FT /note="I -> M (in Ref. 1; CAA80271)" FT /evidence="ECO:0000305" FT CONFLICT 939 FT /note="E -> G (in Ref. 1; CAA80271)" FT /evidence="ECO:0000305" SQ SEQUENCE 1357 AA; 156275 MW; 971FCDF8AA8FC88E CRC64; MEFYESAYFI VLIPSIVITV IFLFFWLFMK ETLYDEVLAK QKREQKLIPT KTDKKKAEKK KNKKKEIQNG NLHESDSESV PRDFKLSDAL AVEDDQVAPV PLNVVETSSS VRERKKKEKK QKPVLEEQVI KESDASKIPG KKVEPVPVTK QPTPPSEAAA SKKKPGQKKS KNGSDDQDKK VETLMVPSKR QEALPLHQET KQESGSGKKK ASSKKQKTEN VFVDEPLIHA TTYIPLMDNA DSSPVVDKRE VIDLLKPDQV EGIQKSGTKK LKTETDKENA EVKFKDFLLS LKTMMFSEDE ALCVVDLLKE KSGVIQDALK KSSKGELTTL IHQLQEKDKL LAAVKEDAAA TKDRCKQLTQ EMMTEKERSN VVITRMKDRI GTLEKEHNVF QNKIHVSYQE TQQMQMKFQQ VREQMEAEIA HLKQENGILR DAVSNTTNQL ESKQSAELNK LRQDYARLVN ELTEKTGKLQ QEEVQKKNAE QAATQLKVQL QEAERRWEEV QSYIRKRTAE HEAAQQDLQS KFVAKENEVQ SLHSKLTDTL VSKQQLEQRL MQLMESEQKR VNKEESLQMQ VQDILEQNEA LKAQIQQFHS QIAAQTSASV LAEELHKVIA EKDKQIKQTE DSLASERDRL TSKEEELKDI QNMNFLLKAE VQKLQALANE QAAAAHELEK MQQSVYVKDD KIRLLEEQLQ HEISNKMEEF KILNDQNKAL KSEVQKLQTL VSEQPNKDVV EQMEKCIQEK DEKLKTVEEL LETGLIQVAT KEEELNAIRT ENSSLTKEVQ DLKAKQNDQV SFASLVEELK KVIHEKDGKI KSVEELLEAE LLKVANKEKT VQDLKQEIKA LKEEIGNVQL EKAQQLSITS KVQELQNLLK GKEEQMNTMK AVLEEKEKDL ANTGKWLQDL QEENESLKAH VQEVAQHNLK EASSASQFEE LEIVLKEKEN ELKRLEAMLK ERESDLSSKT QLLQDVQDEN KLFKSQIEQL KQQNYQQASS FPPHEELLKV ISEREKEISG LWNELDSLKD AVEHQRKKNN DLREKNWEAM EALASTEKML QDKVNKTSKE RQQQVEAVEL EAKEVLKKLF PKVSVPSNLS YGEWLHGFEK KAKECMAGTS GSEEVKVLEH KLKEADEMHT LLQLECEKYK SVLAETEGIL QKLQRSVEQE ENKWKVKVDE SHKTIKQMQS SFTSSEQELE RLRSENKDIE NLRREREHLE MELEKAEMER STYVTEVREL KDLLTELQKK LDDSYSEAVR QNEELNLLKA QLNETLTKLR TEQNERQKVA GDLHKAQQSL ELIQSKIVKA AGDTTVIENS DVSPETESSE KETMSVSLNQ TVTQLQQLLQ AVNQQLTKEK EHYQVLE //