Full text data of KLC3
KLC3
(KLC2, KLC2L)
[Confidence: low (only semi-automatic identification from reviews)]
Kinesin light chain 3 (KLC2-like; kinesin light chain 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Kinesin light chain 3 (KLC2-like; kinesin light chain 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q6P597
ID KLC3_HUMAN Reviewed; 504 AA.
AC Q6P597; A0AVM3; A2RUT6; Q6GMU2; Q8NAL1; Q8WWJ9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-APR-2006, sequence version 2.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=Kinesin light chain 3;
DE AltName: Full=KLC2-like;
DE AltName: Full=kinesin light chain 2;
GN Name=KLC3; Synonyms=KLC2, KLC2L;
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 [GENOMIC DNA].
RC TISSUE=Fibroblast;
RX PubMed=8786141; DOI=10.1006/geno.1996.0303;
RA Lamerdin J.E., Stilwagen S.A., Ramirez M.H., Stubbs L., Carrano A.V.;
RT "Sequence analysis of the ERCC2 gene regions in human, mouse, and
RT hamster reveals three linked genes.";
RL Genomics 34:399-409(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Colon;
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-466 AND SER-502, AND
RP 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 [5]
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.,
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic 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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-498 AND
RP SER-502, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing
CC protein that may play a role in organelle transport.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light
CC chains. Associates with microtubulin in an ATP-dependent manner.
CC Interacts with KIF5C and ODF1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC Note=Elongating spermatid tail midpiece, localized in outer dense
CC fibers (ODFs) and associates with mitochondria (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P597-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P597-2; Sequence=VSP_017832;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q6P597-3; Sequence=VSP_017831;
CC -!- DOMAIN: The heptad repeat (HR) motif is sufficient for interaction
CC with kinesin heavy (KHL) chains and ODF1. The TPR region is
CC involved in mitochondrial binding (By similarity).
CC -!- SIMILARITY: Belongs to the kinesin light chain family.
CC -!- SIMILARITY: Contains 5 TPR repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L47234; AAL48324.1; -; Genomic_DNA.
DR EMBL; AK092481; BAC03901.1; -; mRNA.
DR EMBL; BC062998; AAH62998.2; -; mRNA.
DR EMBL; BC073841; AAH73841.1; -; mRNA.
DR EMBL; BC126418; AAI26419.1; -; mRNA.
DR EMBL; BC133037; AAI33038.1; -; mRNA.
DR RefSeq; NP_803136.2; NM_177417.2.
DR RefSeq; XP_005258596.1; XM_005258539.1.
DR UniGene; Hs.298079; -.
DR ProteinModelPortal; Q6P597; -.
DR SMR; Q6P597; 197-442.
DR IntAct; Q6P597; 2.
DR MINT; MINT-3318740; -.
DR STRING; 9606.ENSP00000375810; -.
DR PhosphoSite; Q6P597; -.
DR DMDM; 91207086; -.
DR PaxDb; Q6P597; -.
DR PRIDE; Q6P597; -.
DR DNASU; 147700; -.
DR Ensembl; ENST00000391946; ENSP00000375810; ENSG00000104892.
DR Ensembl; ENST00000470402; ENSP00000436019; ENSG00000104892.
DR Ensembl; ENST00000585434; ENSP00000466067; ENSG00000104892.
DR GeneID; 147700; -.
DR KEGG; hsa:147700; -.
DR UCSC; uc002pbf.1; human.
DR CTD; 147700; -.
DR GeneCards; GC19P045851; -.
DR HGNC; HGNC:20717; KLC3.
DR HPA; HPA052797; -.
DR MIM; 601334; gene.
DR neXtProt; NX_Q6P597; -.
DR PharmGKB; PA142671588; -.
DR eggNOG; COG0457; -.
DR HOGENOM; HOG000261663; -.
DR HOVERGEN; HBG006217; -.
DR InParanoid; Q6P597; -.
DR KO; K10407; -.
DR OMA; YGKRGRY; -.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR GeneWiki; KLC3; -.
DR GenomeRNAi; 147700; -.
DR NextBio; 85698; -.
DR PRO; PR:Q6P597; -.
DR ArrayExpress; Q6P597; -.
DR Bgee; Q6P597; -.
DR CleanEx; HS_KLC2; -.
DR CleanEx; HS_KLC3; -.
DR Genevestigator; Q6P597; -.
DR GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0008088; P:axon cargo transport; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR002151; Kinesin_light.
DR InterPro; IPR015390; Rabaptin_Rab5-bd_dom.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF09311; Rab5-bind; 1.
DR Pfam; PF00515; TPR_1; 1.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 4.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW Cytoskeleton; Microtubule; Motor protein; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1 504 Kinesin light chain 3.
FT /FTId=PRO_0000230785.
FT REPEAT 207 240 TPR 1.
FT REPEAT 249 282 TPR 2.
FT REPEAT 291 324 TPR 3.
FT REPEAT 333 366 TPR 4.
FT REPEAT 375 408 TPR 5.
FT COILED 90 150 Potential.
FT COMPBIAS 181 184 Poly-Glu.
FT COMPBIAS 190 196 Poly-Ala.
FT MOD_RES 466 466 Phosphoserine.
FT MOD_RES 498 498 Phosphothreonine.
FT MOD_RES 502 502 Phosphoserine.
FT VAR_SEQ 1 1 M -> MIPQTPHHCSPGAAM (in isoform 3).
FT /FTId=VSP_017831.
FT VAR_SEQ 163 163 Missing (in isoform 2).
FT /FTId=VSP_017832.
FT CONFLICT 352 352 V -> A (in Ref. 2; BAC03901).
SQ SEQUENCE 504 AA; 55364 MW; 3767D66C79EA3D49 CRC64;
MSVQVAAPGS AGLGPERLSP EELVRQTRQV VQGLEALRAE HHGLAGHLAE ALAGQGPAAG
LEMLEEKQQV VSHSLEAIEL GLGEAQVLLA LSAHVGALEA EKQRLRSQAR RLAQENVWLR
EELEETQRRL RASEESVAQL EEEKRHLEFL GQLRQYDPPA ESQQSESPPR RDSLASLFPS
EEEERKGPEA AGAAAAQQGG YEIPARLRTL HNLVIQYAGQ GRYEVAVPLC RQALEDLERS
SGHCHPDVAT MLNILALVYR DQNKYKEATD LLHDALQIRE QTLGPEHPAV AATLNNLAVL
YGKRGRYREA EPLCQRALEI REKVLGADHP DVAKQLNNLA LLCQNQGKFE DVERHYARAL
SIYEALGGPH DPNVAKTKNN LASAYLKQNK YQQAEELYKE ILHKEDLPAP LGAPNTGTAG
DAEQALRRSS SLSKIRESIR RGSEKLVSRL RGEAAAGAAG MKRAMSLNTL NVDAPRAPGT
QFPSWHLDKA PRTLSASTQD LSPH
//
ID KLC3_HUMAN Reviewed; 504 AA.
AC Q6P597; A0AVM3; A2RUT6; Q6GMU2; Q8NAL1; Q8WWJ9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-APR-2006, sequence version 2.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=Kinesin light chain 3;
DE AltName: Full=KLC2-like;
DE AltName: Full=kinesin light chain 2;
GN Name=KLC3; Synonyms=KLC2, KLC2L;
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 [GENOMIC DNA].
RC TISSUE=Fibroblast;
RX PubMed=8786141; DOI=10.1006/geno.1996.0303;
RA Lamerdin J.E., Stilwagen S.A., Ramirez M.H., Stubbs L., Carrano A.V.;
RT "Sequence analysis of the ERCC2 gene regions in human, mouse, and
RT hamster reveals three linked genes.";
RL Genomics 34:399-409(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Colon;
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-466 AND SER-502, AND
RP 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 [5]
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.,
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic 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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-498 AND
RP SER-502, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing
CC protein that may play a role in organelle transport.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light
CC chains. Associates with microtubulin in an ATP-dependent manner.
CC Interacts with KIF5C and ODF1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC Note=Elongating spermatid tail midpiece, localized in outer dense
CC fibers (ODFs) and associates with mitochondria (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P597-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P597-2; Sequence=VSP_017832;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q6P597-3; Sequence=VSP_017831;
CC -!- DOMAIN: The heptad repeat (HR) motif is sufficient for interaction
CC with kinesin heavy (KHL) chains and ODF1. The TPR region is
CC involved in mitochondrial binding (By similarity).
CC -!- SIMILARITY: Belongs to the kinesin light chain family.
CC -!- SIMILARITY: Contains 5 TPR repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L47234; AAL48324.1; -; Genomic_DNA.
DR EMBL; AK092481; BAC03901.1; -; mRNA.
DR EMBL; BC062998; AAH62998.2; -; mRNA.
DR EMBL; BC073841; AAH73841.1; -; mRNA.
DR EMBL; BC126418; AAI26419.1; -; mRNA.
DR EMBL; BC133037; AAI33038.1; -; mRNA.
DR RefSeq; NP_803136.2; NM_177417.2.
DR RefSeq; XP_005258596.1; XM_005258539.1.
DR UniGene; Hs.298079; -.
DR ProteinModelPortal; Q6P597; -.
DR SMR; Q6P597; 197-442.
DR IntAct; Q6P597; 2.
DR MINT; MINT-3318740; -.
DR STRING; 9606.ENSP00000375810; -.
DR PhosphoSite; Q6P597; -.
DR DMDM; 91207086; -.
DR PaxDb; Q6P597; -.
DR PRIDE; Q6P597; -.
DR DNASU; 147700; -.
DR Ensembl; ENST00000391946; ENSP00000375810; ENSG00000104892.
DR Ensembl; ENST00000470402; ENSP00000436019; ENSG00000104892.
DR Ensembl; ENST00000585434; ENSP00000466067; ENSG00000104892.
DR GeneID; 147700; -.
DR KEGG; hsa:147700; -.
DR UCSC; uc002pbf.1; human.
DR CTD; 147700; -.
DR GeneCards; GC19P045851; -.
DR HGNC; HGNC:20717; KLC3.
DR HPA; HPA052797; -.
DR MIM; 601334; gene.
DR neXtProt; NX_Q6P597; -.
DR PharmGKB; PA142671588; -.
DR eggNOG; COG0457; -.
DR HOGENOM; HOG000261663; -.
DR HOVERGEN; HBG006217; -.
DR InParanoid; Q6P597; -.
DR KO; K10407; -.
DR OMA; YGKRGRY; -.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR GeneWiki; KLC3; -.
DR GenomeRNAi; 147700; -.
DR NextBio; 85698; -.
DR PRO; PR:Q6P597; -.
DR ArrayExpress; Q6P597; -.
DR Bgee; Q6P597; -.
DR CleanEx; HS_KLC2; -.
DR CleanEx; HS_KLC3; -.
DR Genevestigator; Q6P597; -.
DR GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0008088; P:axon cargo transport; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR002151; Kinesin_light.
DR InterPro; IPR015390; Rabaptin_Rab5-bd_dom.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF09311; Rab5-bind; 1.
DR Pfam; PF00515; TPR_1; 1.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 4.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW Cytoskeleton; Microtubule; Motor protein; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1 504 Kinesin light chain 3.
FT /FTId=PRO_0000230785.
FT REPEAT 207 240 TPR 1.
FT REPEAT 249 282 TPR 2.
FT REPEAT 291 324 TPR 3.
FT REPEAT 333 366 TPR 4.
FT REPEAT 375 408 TPR 5.
FT COILED 90 150 Potential.
FT COMPBIAS 181 184 Poly-Glu.
FT COMPBIAS 190 196 Poly-Ala.
FT MOD_RES 466 466 Phosphoserine.
FT MOD_RES 498 498 Phosphothreonine.
FT MOD_RES 502 502 Phosphoserine.
FT VAR_SEQ 1 1 M -> MIPQTPHHCSPGAAM (in isoform 3).
FT /FTId=VSP_017831.
FT VAR_SEQ 163 163 Missing (in isoform 2).
FT /FTId=VSP_017832.
FT CONFLICT 352 352 V -> A (in Ref. 2; BAC03901).
SQ SEQUENCE 504 AA; 55364 MW; 3767D66C79EA3D49 CRC64;
MSVQVAAPGS AGLGPERLSP EELVRQTRQV VQGLEALRAE HHGLAGHLAE ALAGQGPAAG
LEMLEEKQQV VSHSLEAIEL GLGEAQVLLA LSAHVGALEA EKQRLRSQAR RLAQENVWLR
EELEETQRRL RASEESVAQL EEEKRHLEFL GQLRQYDPPA ESQQSESPPR RDSLASLFPS
EEEERKGPEA AGAAAAQQGG YEIPARLRTL HNLVIQYAGQ GRYEVAVPLC RQALEDLERS
SGHCHPDVAT MLNILALVYR DQNKYKEATD LLHDALQIRE QTLGPEHPAV AATLNNLAVL
YGKRGRYREA EPLCQRALEI REKVLGADHP DVAKQLNNLA LLCQNQGKFE DVERHYARAL
SIYEALGGPH DPNVAKTKNN LASAYLKQNK YQQAEELYKE ILHKEDLPAP LGAPNTGTAG
DAEQALRRSS SLSKIRESIR RGSEKLVSRL RGEAAAGAAG MKRAMSLNTL NVDAPRAPGT
QFPSWHLDKA PRTLSASTQD LSPH
//
MIM
601334
*RECORD*
*FIELD* NO
601334
*FIELD* TI
*601334 KINESIN LIGHT CHAIN 3; KLC3
;;KINESIN LIGHT CHAIN 2-LIKE; KLC2L;;
KNS2B
*FIELD* TX
read more
CLONING
Lamerdin et al. (1996) reported the comparative analysis of 91.6 kb of
sequence including 54.3 kb encompassing the human ERCC2 locus (126340)
on 19q13.2-q13.3, the syntenic region in the mouse (32.6 kb), and a
further 4.7 kb of sequence 3-prime of the previously reported ERCC2
region in the hamster. In addition to ERCC2, the analysis revealed the
presence of 2 previously undescribed genes, one of which was KLC3, in
all 3 species. KLC3, which Lamerdin et al. (1996) had designated KLC2,
was most similar to the kinesin light chain gene in sea urchin. The
deduced human protein contains 504 amino acids and shows significant
sequence identity with the human KLC1 protein (600025).
GENE STRUCTURE
Lamerdin et al. (1996) found by sequence comparison that the human,
mouse, and hamster KLC3 genes share 12 conserved exons; the human gene
contains 10 (as well as 1 alternate exon), the mouse contains 11, and
the hamster 8.
MAPPING
By sequence analysis, Lamerdin et al. (1996) identified the KLC3 gene on
chromosome 19q13.2-q13.3.
*FIELD* RF
1. Lamerdin, J. E.; Stilwagen, S. A.; Ramirez, M. H.; Stubbs, L.;
Carrano, A. V.: Sequence analysis of the ERCC2 gene regions in human,
mouse, and hamster reveals three linked genes. Genomics 34: 399-409,
1996.
*FIELD* CD
Victor A. McKusick: 7/5/1996
*FIELD* ED
carol: 03/10/2009
carol: 3/9/2009
alopez: 1/10/2006
mark: 7/8/1996
*RECORD*
*FIELD* NO
601334
*FIELD* TI
*601334 KINESIN LIGHT CHAIN 3; KLC3
;;KINESIN LIGHT CHAIN 2-LIKE; KLC2L;;
KNS2B
*FIELD* TX
read more
CLONING
Lamerdin et al. (1996) reported the comparative analysis of 91.6 kb of
sequence including 54.3 kb encompassing the human ERCC2 locus (126340)
on 19q13.2-q13.3, the syntenic region in the mouse (32.6 kb), and a
further 4.7 kb of sequence 3-prime of the previously reported ERCC2
region in the hamster. In addition to ERCC2, the analysis revealed the
presence of 2 previously undescribed genes, one of which was KLC3, in
all 3 species. KLC3, which Lamerdin et al. (1996) had designated KLC2,
was most similar to the kinesin light chain gene in sea urchin. The
deduced human protein contains 504 amino acids and shows significant
sequence identity with the human KLC1 protein (600025).
GENE STRUCTURE
Lamerdin et al. (1996) found by sequence comparison that the human,
mouse, and hamster KLC3 genes share 12 conserved exons; the human gene
contains 10 (as well as 1 alternate exon), the mouse contains 11, and
the hamster 8.
MAPPING
By sequence analysis, Lamerdin et al. (1996) identified the KLC3 gene on
chromosome 19q13.2-q13.3.
*FIELD* RF
1. Lamerdin, J. E.; Stilwagen, S. A.; Ramirez, M. H.; Stubbs, L.;
Carrano, A. V.: Sequence analysis of the ERCC2 gene regions in human,
mouse, and hamster reveals three linked genes. Genomics 34: 399-409,
1996.
*FIELD* CD
Victor A. McKusick: 7/5/1996
*FIELD* ED
carol: 03/10/2009
carol: 3/9/2009
alopez: 1/10/2006
mark: 7/8/1996