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 28-JUL-2009, entry version 82. 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 [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. 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; 5. DR PhosphoSite; Q9H0B6; -. DR PRIDE; Q9H0B6; -. DR Ensembl; ENST00000316924; ENSP00000314837; ENSG00000174996; Homo sapiens. DR Ensembl; ENST00000394067; ENSP00000377631; ENSG00000174996; Homo sapiens. DR GeneID; 64837; -. DR UCSC; uc001ohb.1; human. DR GeneCards; GC11P065781; -. DR GeneCards; GC11P065782; -. DR H-InvDB; HIX0009825; -. DR HGNC; HGNC:20716; KLC2. DR MIM; 611729; gene. DR PharmGKB; PA142671587; -. DR HOGENOM; Q9H0B6; -. DR HOVERGEN; Q9H0B6; -. DR OMA; Q9H0B6; PAAEWSG. DR NextBio; 66920; -. DR ArrayExpress; Q9H0B6; -. DR Bgee; Q9H0B6; -. DR CleanEx; HS_KLC2; -. 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; IPR011990; TPR-like_helical. DR InterPro; IPR013026; TPR_region. 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; 4. 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 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). 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 //