Full text data of KLC4
KLC4
(KNSL8)
[Confidence: low (only semi-automatic identification from reviews)]
Kinesin light chain 4; KLC 4 (Kinesin-like protein 8)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Kinesin light chain 4; KLC 4 (Kinesin-like protein 8)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NSK0
ID KLC4_HUMAN Reviewed; 619 AA.
AC Q9NSK0; B3KNY4; B3KPI3; B3KSQ3; Q66K28; Q96EG6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Kinesin light chain 4;
DE Short=KLC 4;
DE AltName: Full=Kinesin-like protein 8;
GN Name=KLC4; Synonyms=KNSL8;
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] (ISOFORMS 1; 2 AND 3), AND
RP VARIANT HIS-72.
RC TISSUE=Adrenal gland, Brain, and Small intestine;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala, and Esophageal carcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Prostate, and Skin;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
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-590, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-590, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590 AND THR-612, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-590, AND
RP 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).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NSK0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NSK0-2; Sequence=VSP_037875, VSP_037876;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay. No
CC experimental confirmation available;
CC Name=3;
CC IsoId=Q9NSK0-3; Sequence=VSP_038083;
CC Name=4;
CC IsoId=Q9NSK0-4; Sequence=VSP_043324, VSP_043325;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the kinesin light chain family.
CC -!- SIMILARITY: Contains 7 TPR repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC86788.1; Type=Erroneous translation; Note=Wrong choice of CDS;
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DR EMBL; AK055293; BAG51496.1; -; mRNA.
DR EMBL; AK056393; BAG51695.1; -; mRNA.
DR EMBL; AK094102; BAG52815.1; -; mRNA.
DR EMBL; AK127018; BAC86788.1; ALT_SEQ; mRNA.
DR EMBL; AK127894; BAC87179.1; -; mRNA.
DR EMBL; AL162078; CAB82411.1; -; mRNA.
DR EMBL; AL136304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355385; CAI13781.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04149.1; -; Genomic_DNA.
DR EMBL; BC012357; AAH12357.1; -; mRNA.
DR EMBL; BC080637; AAH80637.1; -; mRNA.
DR EMBL; BC103727; AAI03728.1; -; mRNA.
DR EMBL; BX640717; CAE45836.1; -; mRNA.
DR PIR; T47147; T47147.
DR RefSeq; NP_612352.1; NM_138343.2.
DR RefSeq; NP_958929.1; NM_201521.1.
DR RefSeq; NP_958930.1; NM_201522.1.
DR RefSeq; NP_958931.1; NM_201523.1.
DR RefSeq; XP_005249529.1; XM_005249472.1.
DR RefSeq; XP_005249530.1; XM_005249473.1.
DR UniGene; Hs.655123; -.
DR ProteinModelPortal; Q9NSK0; -.
DR SMR; Q9NSK0; 192-495.
DR IntAct; Q9NSK0; 4.
DR MINT; MINT-4999921; -.
DR STRING; 9606.ENSP00000259708; -.
DR PhosphoSite; Q9NSK0; -.
DR DMDM; 116242607; -.
DR PaxDb; Q9NSK0; -.
DR PRIDE; Q9NSK0; -.
DR DNASU; 89953; -.
DR Ensembl; ENST00000259708; ENSP00000259708; ENSG00000137171.
DR Ensembl; ENST00000347162; ENSP00000340221; ENSG00000137171.
DR Ensembl; ENST00000394056; ENSP00000377620; ENSG00000137171.
DR Ensembl; ENST00000394058; ENSP00000377622; ENSG00000137171.
DR Ensembl; ENST00000458460; ENSP00000410358; ENSG00000137171.
DR Ensembl; ENST00000467906; ENSP00000418759; ENSG00000137171.
DR Ensembl; ENST00000479388; ENSP00000418031; ENSG00000137171.
DR GeneID; 89953; -.
DR KEGG; hsa:89953; -.
DR UCSC; uc003otv.1; human.
DR CTD; 89953; -.
DR GeneCards; GC06P043008; -.
DR HGNC; HGNC:21624; KLC4.
DR HPA; HPA030168; -.
DR HPA; HPA030169; -.
DR neXtProt; NX_Q9NSK0; -.
DR PharmGKB; PA134934134; -.
DR eggNOG; COG0457; -.
DR HOGENOM; HOG000261663; -.
DR HOVERGEN; HBG006217; -.
DR InParanoid; Q9NSK0; -.
DR KO; K10407; -.
DR OMA; MSKSRHR; -.
DR OrthoDB; EOG7TXKGD; -.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR GeneWiki; KLC4; -.
DR GenomeRNAi; 89953; -.
DR NextBio; 76452; -.
DR PRO; PR:Q9NSK0; -.
DR ArrayExpress; Q9NSK0; -.
DR Bgee; Q9NSK0; -.
DR CleanEx; HS_KLC4; -.
DR Genevestigator; Q9NSK0; -.
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:0003777; F:microtubule motor activity; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR002151; Kinesin_light.
DR InterPro; IPR015792; Kinesin_light_repeat.
DR InterPro; IPR015390; Rabaptin_Rab5-bd_dom.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF09311; Rab5-bind; 1.
DR Pfam; PF07719; TPR_2; 1.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 4.
DR PROSITE; PS01160; KINESIN_LIGHT; 3.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Cytoskeleton; Microtubule; Motor protein; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat; TPR repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 619 Kinesin light chain 4.
FT /FTId=PRO_0000215097.
FT REPEAT 55 88 TPR 1.
FT REPEAT 211 244 TPR 2.
FT REPEAT 253 286 TPR 3.
FT REPEAT 295 328 TPR 4.
FT REPEAT 337 370 TPR 5.
FT REPEAT 379 412 TPR 6.
FT REPEAT 464 497 TPR 7.
FT COILED 32 150 Potential.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 460 460 Phosphoserine.
FT MOD_RES 590 590 Phosphoserine.
FT MOD_RES 612 612 Phosphothreonine.
FT VAR_SEQ 1 1 M -> MEVTGFGVTRPGKVPQARM (in isoform 3).
FT /FTId=VSP_038083.
FT VAR_SEQ 87 131 VMLALASHLSTVESEKQKLRAQVRRLCQENQWLRDELAGTQ
FT QRLQ -> NLELRGCAHLGDAGSSQPPEHSGVGETEAAGSG
FT AAAMPGEPVAAG (in isoform 2).
FT /FTId=VSP_037875.
FT VAR_SEQ 132 619 Missing (in isoform 2).
FT /FTId=VSP_037876.
FT VAR_SEQ 295 315 AATLNNLAVLYGKRGKYKEAE -> SIPCPPHPTPRTPHHC
FT CFGLS (in isoform 4).
FT /FTId=VSP_043324.
FT VAR_SEQ 316 619 Missing (in isoform 4).
FT /FTId=VSP_043325.
FT VARIANT 72 72 R -> H (in dbSNP:rs11558979).
FT /FTId=VAR_049708.
FT CONFLICT 54 54 L -> LQTIECL (in Ref. 1; BAC87179).
FT CONFLICT 286 286 T -> S (in Ref. 1; BAG51695).
FT CONFLICT 366 366 I -> T (in Ref. 1; BAG51695).
FT CONFLICT 434 434 M -> L (in Ref. 1; BAG52815).
SQ SEQUENCE 619 AA; 68640 MW; 32DFC2A9A91B5574 CRC64;
MSGLVLGQRD EPAGHRLSQE EILGSTRLVS QGLEALRSEH QAVLQSLSQT IECLQQGGHE
EGLVHEKARQ LRRSMENIEL GLSEAQVMLA LASHLSTVES EKQKLRAQVR RLCQENQWLR
DELAGTQQRL QRSEQAVAQL EEEKKHLEFL GQLRQYDEDG HTSEEKEGDA TKDSLDDLFP
NEEEEDPSNG LSRGQGATAA QQGGYEIPAR LRTLHNLVIQ YAAQGRYEVA VPLCKQALED
LERTSGRGHP DVATMLNILA LVYRDQNKYK EAAHLLNDAL SIRESTLGPD HPAVAATLNN
LAVLYGKRGK YKEAEPLCQR ALEIREKVLG TNHPDVAKQL NNLALLCQNQ GKYEAVERYY
QRALAIYEGQ LGPDNPNVAR TKNNLASCYL KQGKYAEAET LYKEILTRAH VQEFGSVDDD
HKPIWMHAEE REEMSKSRHH EGGTPYAEYG GWYKACKVSS PTVNTTLRNL GALYRRQGKL
EAAETLEECA LRSRRQGTDP ISQTKVAELL GESDGRRTSQ EGPGDSVKFE GGEDASVAVE
WSGDGSGTLQ RSGSLGKIRD VLRRSSELLV RKLQGTEPRP SSSNMKRAAS LNYLNQPSAA
PLQVSRGLSA STMDLSSSS
//
ID KLC4_HUMAN Reviewed; 619 AA.
AC Q9NSK0; B3KNY4; B3KPI3; B3KSQ3; Q66K28; Q96EG6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Kinesin light chain 4;
DE Short=KLC 4;
DE AltName: Full=Kinesin-like protein 8;
GN Name=KLC4; Synonyms=KNSL8;
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] (ISOFORMS 1; 2 AND 3), AND
RP VARIANT HIS-72.
RC TISSUE=Adrenal gland, Brain, and Small intestine;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala, and Esophageal carcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Prostate, and Skin;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
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-590, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-590, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590 AND THR-612, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-590, AND
RP 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).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NSK0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NSK0-2; Sequence=VSP_037875, VSP_037876;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay. No
CC experimental confirmation available;
CC Name=3;
CC IsoId=Q9NSK0-3; Sequence=VSP_038083;
CC Name=4;
CC IsoId=Q9NSK0-4; Sequence=VSP_043324, VSP_043325;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the kinesin light chain family.
CC -!- SIMILARITY: Contains 7 TPR repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC86788.1; Type=Erroneous translation; Note=Wrong choice of CDS;
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DR EMBL; AK055293; BAG51496.1; -; mRNA.
DR EMBL; AK056393; BAG51695.1; -; mRNA.
DR EMBL; AK094102; BAG52815.1; -; mRNA.
DR EMBL; AK127018; BAC86788.1; ALT_SEQ; mRNA.
DR EMBL; AK127894; BAC87179.1; -; mRNA.
DR EMBL; AL162078; CAB82411.1; -; mRNA.
DR EMBL; AL136304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355385; CAI13781.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04149.1; -; Genomic_DNA.
DR EMBL; BC012357; AAH12357.1; -; mRNA.
DR EMBL; BC080637; AAH80637.1; -; mRNA.
DR EMBL; BC103727; AAI03728.1; -; mRNA.
DR EMBL; BX640717; CAE45836.1; -; mRNA.
DR PIR; T47147; T47147.
DR RefSeq; NP_612352.1; NM_138343.2.
DR RefSeq; NP_958929.1; NM_201521.1.
DR RefSeq; NP_958930.1; NM_201522.1.
DR RefSeq; NP_958931.1; NM_201523.1.
DR RefSeq; XP_005249529.1; XM_005249472.1.
DR RefSeq; XP_005249530.1; XM_005249473.1.
DR UniGene; Hs.655123; -.
DR ProteinModelPortal; Q9NSK0; -.
DR SMR; Q9NSK0; 192-495.
DR IntAct; Q9NSK0; 4.
DR MINT; MINT-4999921; -.
DR STRING; 9606.ENSP00000259708; -.
DR PhosphoSite; Q9NSK0; -.
DR DMDM; 116242607; -.
DR PaxDb; Q9NSK0; -.
DR PRIDE; Q9NSK0; -.
DR DNASU; 89953; -.
DR Ensembl; ENST00000259708; ENSP00000259708; ENSG00000137171.
DR Ensembl; ENST00000347162; ENSP00000340221; ENSG00000137171.
DR Ensembl; ENST00000394056; ENSP00000377620; ENSG00000137171.
DR Ensembl; ENST00000394058; ENSP00000377622; ENSG00000137171.
DR Ensembl; ENST00000458460; ENSP00000410358; ENSG00000137171.
DR Ensembl; ENST00000467906; ENSP00000418759; ENSG00000137171.
DR Ensembl; ENST00000479388; ENSP00000418031; ENSG00000137171.
DR GeneID; 89953; -.
DR KEGG; hsa:89953; -.
DR UCSC; uc003otv.1; human.
DR CTD; 89953; -.
DR GeneCards; GC06P043008; -.
DR HGNC; HGNC:21624; KLC4.
DR HPA; HPA030168; -.
DR HPA; HPA030169; -.
DR neXtProt; NX_Q9NSK0; -.
DR PharmGKB; PA134934134; -.
DR eggNOG; COG0457; -.
DR HOGENOM; HOG000261663; -.
DR HOVERGEN; HBG006217; -.
DR InParanoid; Q9NSK0; -.
DR KO; K10407; -.
DR OMA; MSKSRHR; -.
DR OrthoDB; EOG7TXKGD; -.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR GeneWiki; KLC4; -.
DR GenomeRNAi; 89953; -.
DR NextBio; 76452; -.
DR PRO; PR:Q9NSK0; -.
DR ArrayExpress; Q9NSK0; -.
DR Bgee; Q9NSK0; -.
DR CleanEx; HS_KLC4; -.
DR Genevestigator; Q9NSK0; -.
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:0003777; F:microtubule motor activity; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR002151; Kinesin_light.
DR InterPro; IPR015792; Kinesin_light_repeat.
DR InterPro; IPR015390; Rabaptin_Rab5-bd_dom.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF09311; Rab5-bind; 1.
DR Pfam; PF07719; TPR_2; 1.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 4.
DR PROSITE; PS01160; KINESIN_LIGHT; 3.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Cytoskeleton; Microtubule; Motor protein; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat; TPR repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 619 Kinesin light chain 4.
FT /FTId=PRO_0000215097.
FT REPEAT 55 88 TPR 1.
FT REPEAT 211 244 TPR 2.
FT REPEAT 253 286 TPR 3.
FT REPEAT 295 328 TPR 4.
FT REPEAT 337 370 TPR 5.
FT REPEAT 379 412 TPR 6.
FT REPEAT 464 497 TPR 7.
FT COILED 32 150 Potential.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 460 460 Phosphoserine.
FT MOD_RES 590 590 Phosphoserine.
FT MOD_RES 612 612 Phosphothreonine.
FT VAR_SEQ 1 1 M -> MEVTGFGVTRPGKVPQARM (in isoform 3).
FT /FTId=VSP_038083.
FT VAR_SEQ 87 131 VMLALASHLSTVESEKQKLRAQVRRLCQENQWLRDELAGTQ
FT QRLQ -> NLELRGCAHLGDAGSSQPPEHSGVGETEAAGSG
FT AAAMPGEPVAAG (in isoform 2).
FT /FTId=VSP_037875.
FT VAR_SEQ 132 619 Missing (in isoform 2).
FT /FTId=VSP_037876.
FT VAR_SEQ 295 315 AATLNNLAVLYGKRGKYKEAE -> SIPCPPHPTPRTPHHC
FT CFGLS (in isoform 4).
FT /FTId=VSP_043324.
FT VAR_SEQ 316 619 Missing (in isoform 4).
FT /FTId=VSP_043325.
FT VARIANT 72 72 R -> H (in dbSNP:rs11558979).
FT /FTId=VAR_049708.
FT CONFLICT 54 54 L -> LQTIECL (in Ref. 1; BAC87179).
FT CONFLICT 286 286 T -> S (in Ref. 1; BAG51695).
FT CONFLICT 366 366 I -> T (in Ref. 1; BAG51695).
FT CONFLICT 434 434 M -> L (in Ref. 1; BAG52815).
SQ SEQUENCE 619 AA; 68640 MW; 32DFC2A9A91B5574 CRC64;
MSGLVLGQRD EPAGHRLSQE EILGSTRLVS QGLEALRSEH QAVLQSLSQT IECLQQGGHE
EGLVHEKARQ LRRSMENIEL GLSEAQVMLA LASHLSTVES EKQKLRAQVR RLCQENQWLR
DELAGTQQRL QRSEQAVAQL EEEKKHLEFL GQLRQYDEDG HTSEEKEGDA TKDSLDDLFP
NEEEEDPSNG LSRGQGATAA QQGGYEIPAR LRTLHNLVIQ YAAQGRYEVA VPLCKQALED
LERTSGRGHP DVATMLNILA LVYRDQNKYK EAAHLLNDAL SIRESTLGPD HPAVAATLNN
LAVLYGKRGK YKEAEPLCQR ALEIREKVLG TNHPDVAKQL NNLALLCQNQ GKYEAVERYY
QRALAIYEGQ LGPDNPNVAR TKNNLASCYL KQGKYAEAET LYKEILTRAH VQEFGSVDDD
HKPIWMHAEE REEMSKSRHH EGGTPYAEYG GWYKACKVSS PTVNTTLRNL GALYRRQGKL
EAAETLEECA LRSRRQGTDP ISQTKVAELL GESDGRRTSQ EGPGDSVKFE GGEDASVAVE
WSGDGSGTLQ RSGSLGKIRD VLRRSSELLV RKLQGTEPRP SSSNMKRAAS LNYLNQPSAA
PLQVSRGLSA STMDLSSSS
//