KLC2_HUMAN
ID KLC2_HUMAN Reviewed; 622 AA.
AC Q9H0B6; A8MXL7; B2RDY4; Q9H9C8; Q9HA20;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Kinesin light chain 2 {ECO:0000305};
DE Short=KLC 2;
GN Name=KLC2 {ECO:0000312|HGNC:HGNC:20716};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX 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., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-582 AND SER-589, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-445; SER-581;
RP SER-582 AND SER-589, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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., Buerckstuemmer T.,
RA 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 [11]
RP FUNCTION, INTERACTION WITH PLEKHM2, AND SUBCELLULAR LOCATION.
RX PubMed=22172677; DOI=10.1016/j.devcel.2011.10.007;
RA Rosa-Ferreira C., Munro S.;
RT "Arl8 and SKIP act together to link lysosomes to kinesin-1.";
RL Dev. Cell 21:1171-1178(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582 AND SER-610, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-521; SER-581;
RP SER-582; SER-589; SER-608; SER-610 AND SER-615, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP INVOLVEMENT IN SPOAN.
RX PubMed=26385635; DOI=10.1093/hmg/ddv388;
RA Melo U.S., Macedo-Souza L.I., Figueiredo T., Muotri A.R., Gleeson J.G.,
RA Coux G., Armas P., Calcaterra N.B., Kitajima J.P., Amorim S., Olavio T.R.,
RA Griesi-Oliveira K., Coatti G.C., Rocha C.R., Martins-Pinheiro M.,
RA Menck C.F., Zaki M.S., Kok F., Zatz M., Santos S.;
RT "Overexpression of KLC2 due to a homozygous deletion in the non-coding
RT region causes SPOAN syndrome.";
RL Hum. Mol. Genet. 24:6877-6885(2015).
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC that plays a role in organelle transport. The light chain functions in
CC coupling of cargo to the heavy chain or in the modulation of its ATPase
CC activity (Probable). Through binding with PLEKHM2 and ARL8B, recruits
CC kinesin-1 to lysosomes and hence direct lysosomes movement toward
CC microtubule plus ends (PubMed:22172677). {ECO:0000269|PubMed:22172677,
CC ECO:0000305|PubMed:22172677}.
CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light
CC chains (Probable). Interacts (via TPR repeats) with PLEKHM2 (Probable).
CC {ECO:0000305, ECO:0000305|PubMed:22172677}.
CC -!- INTERACTION:
CC Q9H0B6; Q9BQS8: FYCO1; NbExp=2; IntAct=EBI-726994, EBI-2869338;
CC Q9H0B6; P63104: YWHAZ; NbExp=2; IntAct=EBI-726994, EBI-347088;
CC Q9H0B6; P0DTC9: N; Xeno; NbExp=4; IntAct=EBI-726994, EBI-25475856;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Lysosome
CC membrane {ECO:0000269|PubMed:22172677}; Peripheral membrane protein
CC {ECO:0000305|PubMed:22172677}; Cytoplasmic side
CC {ECO:0000305|PubMed:22172677}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H0B6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0B6-2; Sequence=VSP_043486;
CC -!- DISEASE: Spastic paraplegia, optic atrophy, and neuropathy (SPOAN)
CC [MIM:609541]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body. SPOAN is characterized
CC by spastic paraplegia with progressive joint contractures and spine
CC deformities, loss of independent ambulation by age 10 years, sub-normal
CC vision secondary to congenital optic atrophy, and neuropathy.
CC Inheritance is autosomal recessive. {ECO:0000269|PubMed:26385635}.
CC Note=The gene represented in this entry is involved in disease
CC pathogenesis. The disease is caused by a homozygous deletion in the
CC non-coding region of the KLC2 gene. {ECO:0000269|PubMed:26385635}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
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DR EMBL; AL136864; CAB66798.1; -; mRNA.
DR EMBL; AK022449; BAB14039.1; -; mRNA.
DR EMBL; AK022907; BAB14302.1; -; mRNA.
DR EMBL; AK094593; BAG52895.1; -; mRNA.
DR EMBL; AK315725; BAG38081.1; -; mRNA.
DR EMBL; AP000759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034373; AAH34373.1; -; mRNA.
DR CCDS; CCDS44653.1; -. [Q9H0B6-2]
DR CCDS; CCDS8130.1; -. [Q9H0B6-1]
DR RefSeq; NP_001128246.1; NM_001134774.1. [Q9H0B6-2]
DR RefSeq; NP_001128247.1; NM_001134775.1. [Q9H0B6-1]
DR RefSeq; NP_001128248.1; NM_001134776.1. [Q9H0B6-1]
DR RefSeq; NP_001305663.1; NM_001318734.1. [Q9H0B6-1]
DR RefSeq; NP_073733.1; NM_022822.2. [Q9H0B6-1]
DR RefSeq; XP_005274240.1; XM_005274183.1. [Q9H0B6-1]
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 AlphaFoldDB; Q9H0B6; -.
DR SMR; Q9H0B6; -.
DR BioGRID; 122313; 499.
DR DIP; DIP-40381N; -.
DR ELM; Q9H0B6; -.
DR IntAct; Q9H0B6; 67.
DR MINT; Q9H0B6; -.
DR STRING; 9606.ENSP00000399403; -.
DR GlyGen; Q9H0B6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H0B6; -.
DR MetOSite; Q9H0B6; -.
DR PhosphoSitePlus; Q9H0B6; -.
DR BioMuta; KLC2; -.
DR DMDM; 13878553; -.
DR EPD; Q9H0B6; -.
DR jPOST; Q9H0B6; -.
DR MassIVE; Q9H0B6; -.
DR MaxQB; Q9H0B6; -.
DR PaxDb; Q9H0B6; -.
DR PeptideAtlas; Q9H0B6; -.
DR PRIDE; Q9H0B6; -.
DR ProteomicsDB; 80243; -. [Q9H0B6-1]
DR ProteomicsDB; 80244; -. [Q9H0B6-2]
DR Antibodypedia; 30085; 204 antibodies from 26 providers.
DR DNASU; 64837; -.
DR Ensembl; ENST00000316924.9; ENSP00000314837.5; ENSG00000174996.12. [Q9H0B6-1]
DR Ensembl; ENST00000394066.6; ENSP00000377630.2; ENSG00000174996.12. [Q9H0B6-2]
DR Ensembl; ENST00000394067.7; ENSP00000377631.2; ENSG00000174996.12. [Q9H0B6-1]
DR Ensembl; ENST00000417856.5; ENSP00000399403.1; ENSG00000174996.12. [Q9H0B6-1]
DR Ensembl; ENST00000421552.5; ENSP00000408484.1; ENSG00000174996.12. [Q9H0B6-2]
DR GeneID; 64837; -.
DR KEGG; hsa:64837; -.
DR MANE-Select; ENST00000394067.7; ENSP00000377631.2; NM_001318734.2; NP_001305663.1.
DR UCSC; uc001ohb.3; human. [Q9H0B6-1]
DR CTD; 64837; -.
DR DisGeNET; 64837; -.
DR GeneCards; KLC2; -.
DR HGNC; HGNC:20716; KLC2.
DR HPA; ENSG00000174996; Low tissue specificity.
DR MalaCards; KLC2; -.
DR MIM; 609541; phenotype.
DR MIM; 611729; gene.
DR neXtProt; NX_Q9H0B6; -.
DR OpenTargets; ENSG00000174996; -.
DR Orphanet; 320406; Spastic paraplegia-optic atrophy-neuropathy syndrome.
DR PharmGKB; PA142671587; -.
DR VEuPathDB; HostDB:ENSG00000174996; -.
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00940000161973; -.
DR HOGENOM; CLU_019953_0_0_1; -.
DR InParanoid; Q9H0B6; -.
DR OMA; GSQERCH; -.
DR OrthoDB; 511880at2759; -.
DR PhylomeDB; Q9H0B6; -.
DR TreeFam; TF314010; -.
DR PathwayCommons; Q9H0B6; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-5625970; RHO GTPases activate KTN1.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q9H0B6; -.
DR SIGNOR; Q9H0B6; -.
DR BioGRID-ORCS; 64837; 352 hits in 1081 CRISPR screens.
DR ChiTaRS; KLC2; human.
DR EvolutionaryTrace; Q9H0B6; -.
DR GeneWiki; KLC2; -.
DR GenomeRNAi; 64837; -.
DR Pharos; Q9H0B6; Tbio.
DR PRO; PR:Q9H0B6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9H0B6; protein.
DR Bgee; ENSG00000174996; Expressed in right hemisphere of cerebellum and 148 other tissues.
DR ExpressionAtlas; Q9H0B6; baseline and differential.
DR Genevisible; Q9H0B6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005871; C:kinesin complex; ISS:HGNC-UCL.
DR GO; GO:0016938; C:kinesin I complex; NAS:BHF-UCL.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0043005; C:neuron projection; IEA:GOC.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:LIFEdb.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0019894; F:kinesin binding; ISS:BHF-UCL.
DR GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR002151; Kinesin_light.
DR InterPro; IPR015792; Kinesin_light_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 2.
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; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Hereditary spastic paraplegia; Lysosome; Membrane; Microtubule;
KW Motor protein; Neurodegeneration; Neuropathy; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..622
FT /note="Kinesin light chain 2"
FT /id="PRO_0000215095"
FT REPEAT 198..231
FT /note="TPR 1"
FT REPEAT 240..273
FT /note="TPR 2"
FT REPEAT 282..315
FT /note="TPR 3"
FT REPEAT 324..357
FT /note="TPR 4"
FT REPEAT 366..399
FT /note="TPR 5"
FT REPEAT 449..482
FT /note="TPR 6"
FT REGION 145..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 78..143
FT /evidence="ECO:0000255"
FT COMPBIAS 145..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88448"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88448"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88448"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 77..153
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043486"
FT VARIANT 517
FT /note="P -> S (in dbSNP:rs2276036)"
FT /id="VAR_020379"
FT CONFLICT 6
FT /note="F -> Y (in Ref. 2; BAB14302)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="K -> R (in Ref. 2; BAB14039)"
FT /evidence="ECO:0000305"
FT HELIX 217..232
FT /evidence="ECO:0007829|PDB:3EDT"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:3EDT"
FT HELIX 237..252
FT /evidence="ECO:0007829|PDB:3EDT"
FT HELIX 256..273
FT /evidence="ECO:0007829|PDB:3EDT"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:3EDT"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:3EDT"
FT HELIX 298..316
FT /evidence="ECO:0007829|PDB:3EDT"
FT HELIX 321..335
FT /evidence="ECO:0007829|PDB:3EDT"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:3EDT"
FT HELIX 340..357
FT /evidence="ECO:0007829|PDB:3EDT"
FT HELIX 363..379
FT /evidence="ECO:0007829|PDB:3EDT"
FT HELIX 382..400
FT /evidence="ECO:0007829|PDB:3EDT"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:3EDT"
FT HELIX 411..420
FT /evidence="ECO:0007829|PDB:3EDT"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:3CEQ"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:3CEQ"
FT HELIX 446..461
FT /evidence="ECO:0007829|PDB:3EDT"
FT HELIX 465..476
FT /evidence="ECO:0007829|PDB:3EDT"
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
