ID KTN1_HUMAN Reviewed; 1357 AA. AC Q86UP2; Q13999; Q14707; Q15387; Q17RZ5; Q86W57; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 31-OCT-2012, entry version 99. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Lymphoid tissue; RX MEDLINE=95306853; PubMed=7787243; 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 MEDLINE=94314220; 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 MEDLINE=96051387; PubMed=7584026; DOI=10.1093/dnares/1.1.27; RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., RA Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. I. RT The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by RT analysis of randomly sampled cDNA clones from human immature myeloid RT cell line KG-1."; RL DNA Res. 1:27-35(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22459283; 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., RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., RA 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., RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., RA Quetier F., Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-870 (ISOFORMS 1/2). RC TISSUE=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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 191-195; 395-405; 545-554; 747-761 AND 811-823. RX MEDLINE=21969647; PubMed=11973345; 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 [8] RP CHROMOSOMAL LOCATION. RX MEDLINE=96163023; PubMed=8575822; DOI=10.1007/s002510050050; 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 RT human chromosome band 14q22."; RL Immunogenetics 43:227-229(1996). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-77 AND THR-153, RP AND MASS SPECTROMETRY. 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [10] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-309, AND MASS RP SPECTROMETRY. RC TISSUE=Mammary cancer; RX PubMed=17370265; DOI=10.1002/pmic.200600410; RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; RT "Tryptic digestion of ubiquitin standards reveals an improved strategy RT for identifying ubiquitinated proteins by mass spectrometry."; RL Proteomics 7:868-874(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=19007248; DOI=10.1021/ac801708p; RA Wang B., Malik R., Nigg E.A., Korner R.; RT "Evaluation of the low-specificity protease elastase for large-scale RT phosphoproteome analysis."; RL Anal. Chem. 80:9526-9533(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; THR-153 AND SER-156, RP AND MASS SPECTROMETRY. 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153, AND MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). 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., RA Buerckstuemmer T., 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 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., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Receptor for kinesin thus involved in kinesin-driven CC vesicle motility. Accumulates in integrin-based adhesion complexes CC (IAC) upon integrin aggregation by fibronectin. CC -!- SUBUNIT: Parallel homodimers formed between the membrane-bound and CC the cytosolic form, and also between 2 cytosolic forms (By CC similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC type II membrane protein. Note=Vesicle membrane protein anchored CC to the endoplasmic reticulum. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; 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 -!- TISSUE SPECIFICITY: High levels in peripheral blood lymphocytes, CC testis and ovary, lower levels in spleen, thymus, prostate, small CC intestine and colon. CC -!- SIMILARITY: Belongs to the kinectin family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH50555.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; CC Sequence=BAA02794.2; Type=Erroneous initiation; Note=Translation N-terminally shortened; 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; 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 IPI; IPI00328753; -. DR IPI; IPI00337736; -. DR PIR; I53799; I53799. DR PIR; S32763; S32763. DR RefSeq; NP_001072989.1; NM_001079521.1. DR RefSeq; NP_001072990.1; NM_001079522.1. DR RefSeq; NP_004977.2; NM_004986.3. DR UniGene; Hs.509414; -. DR ProteinModelPortal; Q86UP2; -. DR DIP; DIP-27585N; -. DR IntAct; Q86UP2; 4. DR MINT; MINT-1149569; -. DR STRING; Q86UP2; -. DR PhosphoSite; Q86UP2; -. DR DMDM; 34098465; -. DR PRIDE; Q86UP2; -. DR DNASU; 3895; -. DR Ensembl; ENST00000395308; ENSP00000378719; ENSG00000126777. DR Ensembl; ENST00000395309; ENSP00000378720; ENSG00000126777. DR Ensembl; ENST00000395311; ENSP00000378722; ENSG00000126777. DR Ensembl; ENST00000395314; ENSP00000378725; ENSG00000126777. DR Ensembl; ENST00000413890; ENSP00000394992; ENSG00000126777. DR Ensembl; ENST00000416613; ENSP00000388807; ENSG00000126777. DR Ensembl; ENST00000438792; ENSP00000391964; ENSG00000126777. DR Ensembl; ENST00000459737; ENSP00000432149; ENSG00000126777. DR GeneID; 3895; -. DR KEGG; hsa:3895; -. DR UCSC; uc001xcb.3; human. DR UCSC; uc001xce.3; human. DR CTD; 3895; -. DR GeneCards; GC14P056046; -. DR HGNC; HGNC:6467; KTN1. DR HPA; CAB015331; -. DR HPA; HPA003178; -. DR HPA; HPA017876; -. DR MIM; 600381; gene. DR neXtProt; NX_Q86UP2; -. DR PharmGKB; PA30256; -. DR eggNOG; NOG149793; -. DR HOGENOM; HOG000113267; -. DR HOVERGEN; HBG007851; -. DR InParanoid; Q86UP2; -. DR OMA; IQNMNFL; -. DR PhylomeDB; Q86UP2; -. DR GenomeRNAi; 3895; -. DR NextBio; 15287; -. DR ArrayExpress; Q86UP2; -. DR Bgee; Q86UP2; -. DR CleanEx; HS_KTN1; -. DR Genevestigator; Q86UP2; -. DR GermOnline; ENSG00000126777; Homo sapiens. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:ProtInc. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0007018; P:microtubule-based movement; NAS:ProtInc. DR InterPro; IPR024854; Kinectin. DR PANTHER; PTHR18864; PTHR18864; 1. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Complete proteome; KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; KW Isopeptide bond; Membrane; Phosphoprotein; Polymorphism; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT CHAIN 1 1357 Kinectin. FT /FTId=PRO_0000084337. FT TOPO_DOM 1 6 Cytoplasmic (Potential). FT TRANSMEM 7 29 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 30 1357 Lumenal (Potential). FT COILED 330 1356 Potential. FT MOD_RES 75 75 Phosphoserine. FT MOD_RES 77 77 Phosphoserine. FT MOD_RES 153 153 Phosphothreonine. FT MOD_RES 156 156 Phosphoserine. FT CARBOHYD 172 172 N-linked (GlcNAc...) (Potential). FT CARBOHYD 435 435 N-linked (GlcNAc...) (Potential). FT CARBOHYD 772 772 N-linked (GlcNAc...) (Potential). FT CARBOHYD 904 904 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1055 1055 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1088 1088 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1263 1263 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1329 1329 N-linked (GlcNAc...) (Potential). FT CROSSLNK 309 309 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT VAR_SEQ 832 854 Missing (in isoform 3). FT /FTId=VSP_043207. FT VAR_SEQ 1031 1059 Missing (in isoform 2). FT /FTId=VSP_007981. FT VAR_SEQ 1232 1259 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_007982. FT VARIANT 226 226 P -> R (in a breast cancer sample; FT somatic mutation). FT /FTId=VAR_035931. FT VARIANT 282 282 V -> M (in dbSNP:rs2274073). FT /FTId=VAR_016206. FT VARIANT 1316 1316 T -> P (in a breast cancer sample; FT somatic mutation). FT /FTId=VAR_035932. FT CONFLICT 15 15 S -> P (in Ref. 4; BAA02794). FT CONFLICT 210 210 Missing (in Ref. 1; CAA80271). FT CONFLICT 373 373 I -> M (in Ref. 1; CAA80271). FT CONFLICT 939 939 E -> G (in Ref. 1; CAA80271). 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 //