ID KLC2_HUMAN Reviewed; 622 AA. AC Q9H0B6; B2RDY4; Q9H9C8; Q9HA20; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 15-JUN-2010, entry version 93. DE RecName: Full=Kinesin light chain 2; DE Short=KLC 2; GN Name=KLC2; 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 [LARGE SCALE MRNA]. RC TISSUE=Testis; RX MEDLINE=21154917; PubMed=11230166; DOI=10.1101/gr.GR1547R; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., RA Wambutt R., Korn B., Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and RT analysis of 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland, and 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lymph; 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; SER-508 AND RP SER-582, AND MASS SPECTROMETRY. RC TISSUE=Epithelium; 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND MASS RP SPECTROMETRY. RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-582 AND RP SER-589, AND MASS SPECTROMETRY. 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-582 AND RP SER-589, AND MASS SPECTROMETRY. 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582 AND SER-610, AND RP MASS SPECTROMETRY. RC TISSUE=T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing CC protein that may play a role in organelle transport. The light CC chain may function in coupling of cargo to the heavy chain or in CC the modulation of its ATPase activity (By similarity). CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two CC light chains (By similarity). CC -!- INTERACTION: CC P61981:YWHAG; NbExp=1; IntAct=EBI-726994, EBI-359832; CC P27348:YWHAQ; NbExp=1; IntAct=EBI-726994, EBI-359854; CC -!- SIMILARITY: Belongs to the kinesin light chain family. CC -!- SIMILARITY: Contains 6 TPR repeats. 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; AL136864; CAB66798.1; -; mRNA. DR EMBL; AK022449; BAB14039.1; -; mRNA. DR EMBL; AK022907; BAB14302.1; -; mRNA. DR EMBL; AK315725; BAG38081.1; -; mRNA. DR EMBL; BC034373; AAH34373.1; -; mRNA. DR IPI; IPI00021634; -. DR RefSeq; NP_001128246.1; -. DR RefSeq; NP_001128247.1; -. DR RefSeq; NP_001128248.1; -. DR RefSeq; NP_073733.1; -. DR UniGene; Hs.280792; -. DR PDB; 3CEQ; X-ray; 2.75 A; A/B=217-480. DR PDB; 3EDT; X-ray; 2.70 A; B/D/F/H=217-480. DR PDBsum; 3CEQ; -. DR PDBsum; 3EDT; -. DR IntAct; Q9H0B6; 6. DR STRING; Q9H0B6; -. DR PhosphoSite; Q9H0B6; -. DR PRIDE; Q9H0B6; -. DR Ensembl; ENST00000316924; ENSP00000314837; ENSG00000174996; Homo sapiens. DR Ensembl; ENST00000394067; ENSP00000377631; ENSG00000174996; Homo sapiens. DR Ensembl; ENST00000414181; ENSP00000391680; ENSG00000174996; Homo sapiens. DR Ensembl; ENST00000417856; ENSP00000399403; ENSG00000174996; Homo sapiens. DR GeneID; 64837; -. DR KEGG; hsa:64837; -. DR UCSC; uc001ohb.1; human. DR CTD; 64837; -. DR GeneCards; GC11P065781; -. DR HGNC; HGNC:20716; KLC2. DR MIM; 611729; gene. DR PharmGKB; PA142671587; -. DR eggNOG; prNOG12029; -. DR HOGENOM; HBG447230; -. DR HOVERGEN; HBG006217; -. DR InParanoid; Q9H0B6; -. DR OMA; AAEWSGD; -. DR OrthoDB; EOG9J6VBF; -. DR PhylomeDB; Q9H0B6; -. DR NextBio; 66920; -. DR ArrayExpress; Q9H0B6; -. DR Bgee; Q9H0B6; -. DR CleanEx; HS_KLC2; -. DR Genevestigator; Q9H0B6; -. DR GermOnline; ENSG00000174996; Homo sapiens. DR GO; GO:0005829; C:cytosol; ISS:HGNC. DR GO; GO:0005871; C:kinesin complex; ISS:HGNC. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR002151; Kinesin_light. DR InterPro; IPR015792; Kinesin_light_repeat. DR InterPro; IPR015390; Rabaptin_Rab5-bd. DR InterPro; IPR001440; TPR-1. DR InterPro; IPR013026; TPR-contain. DR InterPro; IPR011990; TPR-like_helical. DR InterPro; IPR019734; TPR_repeat. DR Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1. DR Pfam; PF09311; Rab5-bind; 1. DR Pfam; PF00515; TPR_1; 2. DR PRINTS; PR00381; KINESINLIGHT. DR SMART; SM00028; TPR; 4. DR PROSITE; PS01160; KINESIN_LIGHT; 2. DR PROSITE; PS50005; TPR; 5. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Complete proteome; Microtubule; KW Motor protein; Phosphoprotein; Polymorphism; Repeat; TPR repeat. FT CHAIN 1 622 Kinesin light chain 2. FT /FTId=PRO_0000215095. FT REPEAT 198 231 TPR 1. FT REPEAT 240 273 TPR 2. FT REPEAT 282 315 TPR 3. FT REPEAT 324 357 TPR 4. FT REPEAT 366 399 TPR 5. FT REPEAT 449 482 TPR 6. FT COILED 78 143 Potential. FT MOD_RES 445 445 Phosphoserine. FT MOD_RES 507 507 Phosphoserine. FT MOD_RES 508 508 Phosphoserine. FT MOD_RES 582 582 Phosphoserine. FT MOD_RES 589 589 Phosphoserine. FT MOD_RES 610 610 Phosphoserine. FT VARIANT 517 517 P -> S (in dbSNP:rs2276036). FT /FTId=VAR_020379. FT CONFLICT 6 6 F -> Y (in Ref. 2; BAB14302). FT CONFLICT 306 306 K -> R (in Ref. 2; BAB14039). FT HELIX 217 231 FT HELIX 237 252 FT HELIX 256 273 FT HELIX 279 291 FT HELIX 298 315 FT HELIX 321 335 FT HELIX 340 357 FT HELIX 363 378 FT HELIX 382 400 FT HELIX 411 420 FT HELIX 446 454 FT HELIX 458 461 FT HELIX 465 476 SQ SEQUENCE 622 AA; 68935 MW; 5B57ABE4DF6E396E CRC64; MAMMVFPREE KLSQDEIVLG TKAVIQGLET LRGEHRALLA PLVAPEAGEA EPGSQERCIL LRRSLEAIEL GLGEAQVILA LSSHLGAVES EKQKLRAQVR RLVQENQWLR EELAGTQQKL QRSEQAVAQL EEEKQHLLFM SQIRKLDEDA SPNEEKGDVP KDTLDDLFPN EDEQSPAPSP GGGDVSGQHG GYEIPARLRT LHNLVIQYAS QGRYEVAVPL CKQALEDLEK TSGHDHPDVA TMLNILALVY RDQNKYKEAA HLLNDALAIR EKTLGKDHPA VAATLNNLAV LYGKRGKYKE AEPLCKRALE IREKVLGKFH PDVAKQLSNL ALLCQNQGKA EEVEYYYRRA LEIYATRLGP DDPNVAKTKN NLASCYLKQG KYQDAETLYK EILTRAHEKE FGSVNGDNKP IWMHAEEREE SKDKRRDSAP YGEYGSWYKA CKVDSPTVNT TLRSLGALYR RQGKLEAAHT LEDCASRNRK QGLDPASQTK VVELLKDGSG RRGDRRSSRD MAGGAGPRSE SDLEDVGPTA EWNGDGSGSL RRSGSFGKLR DALRRSSEML VKKLQGGTPQ EPPNPRMKRA SSLNFLNKSV EEPTQPGGTG LSDSRTLSSS SMDLSRRSSL VG //