KTN1_HUMAN
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 03-AUG-2022, entry version 180.
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};
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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; 231.
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; 198 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. [Q86UP2-1]
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. [Q86UP2-1]
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 sperm and 210 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
