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 12-OCT-2022, entry version 198. 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}. 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; 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; 508. DR DIP; DIP-40381N; -. DR ELM; Q9H0B6; -. DR IntAct; Q9H0B6; 73. 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; 203 antibodies from 25 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: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 //