CKP2L_HUMAN
ID CKP2L_HUMAN Reviewed; 745 AA.
AC Q8IYA6; A8K915; B4DZE3; B7ZAC6; F5H0M5; Q53QF8; Q53RS8; Q8N1J8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cytoskeleton-associated protein 2-like;
DE AltName: Full=Radial fiber and mitotic spindle protein;
DE Short=Radmis;
GN Name=CKAP2L;
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] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP VAL-375.
RC TISSUE=Testis, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS SER-62 AND
RP SER-263.
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-375.
RC TISSUE=Testis;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-742 AND SER-745, 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 [5]
RP SUMOYLATION AT LYS-198, PHOSPHORYLATION AT TYR-204, AND MUTAGENESIS OF
RP LYS-198.
RC TISSUE=Cervix carcinoma;
RX PubMed=20388717; DOI=10.1074/jbc.m110.106955;
RA Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,
RA Eriksson J.E., Sistonen L.;
RT "In vivo identification of sumoylation sites by a signature tag and
RT cysteine-targeted affinity purification.";
RL J. Biol. Chem. 285:19324-19329(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-745, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-745, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [8]
RP INVOLVEMENT IN FLPIS, FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=25439729; DOI=10.1016/j.ajhg.2014.10.008;
RA Hussain M.S., Battaglia A., Szczepanski S., Kaygusuz E., Toliat M.R.,
RA Sakakibara S., Altmueller J., Thiele H., Nuernberg G., Moosa S., Yigit G.,
RA Beleggia F., Tinschert S., Clayton-Smith J., Vasudevan P., Urquhart J.E.,
RA Donnai D., Fryer A., Percin F., Brancati F., Dobbie A., Smigiel R.,
RA Gillessen-Kaesbach G., Wollnik B., Noegel A.A., Newman W.G., Nuernberg P.;
RT "Mutations in CKAP2L, the human homolog of the mouse Radmis gene, cause
RT Filippi syndrome.";
RL Am. J. Hum. Genet. 95:622-632(2014).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-198, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Microtubule-associated protein required for mitotic spindle
CC formation and cell-cycle progression in neural progenitor cells.
CC {ECO:0000269|PubMed:25439729}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:25439729}. Note=Uniformly distributed along each
CC microtubule bundle of spindles in addition to centrioles during
CC mitosis, expression promptly diminishes at interphase.
CC {ECO:0000269|PubMed:25439729}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IYA6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IYA6-2; Sequence=VSP_032219, VSP_032220;
CC Name=3;
CC IsoId=Q8IYA6-3; Sequence=VSP_053717;
CC -!- INDUCTION: Expression is cell-cycle dependent. Undetectable in
CC interphase and prophase, strong expression at the spindle pole
CC throughout metaphase to telophase. {ECO:0000269|PubMed:25439729}.
CC -!- DOMAIN: The KEN box is required for the association with the APC/C-Cdh1
CC complex, ubiquitination and degradation. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C).
CC {ECO:0000250}.
CC -!- DISEASE: Filippi syndrome (FLPIS) [MIM:272440]: A rare disorder
CC characterized by microcephaly, pre- and postnatal growth failure,
CC syndactyly, and distinctive facial features, including a broad nasal
CC bridge and underdeveloped alae nasi. Some affected individuals have
CC intellectual disability, seizures, undescended testicles in males, and
CC teeth and hair abnormalities. {ECO:0000269|PubMed:25439729}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the CKAP2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX93053.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK097948; BAC05202.1; -; mRNA.
DR EMBL; AK292530; BAF85219.1; -; mRNA.
DR EMBL; AK302875; BAG64055.1; -; mRNA.
DR EMBL; AK316241; BAH14612.1; -; mRNA.
DR EMBL; AC079922; AAY14923.1; -; Genomic_DNA.
DR EMBL; AC112235; AAX93053.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC036217; AAH36217.1; -; mRNA.
DR CCDS; CCDS2100.1; -. [Q8IYA6-1]
DR RefSeq; NP_001291290.1; NM_001304361.1. [Q8IYA6-3]
DR RefSeq; NP_689728.3; NM_152515.4. [Q8IYA6-1]
DR RefSeq; XP_011508968.1; XM_011510666.2. [Q8IYA6-3]
DR AlphaFoldDB; Q8IYA6; -.
DR SMR; Q8IYA6; -.
DR BioGRID; 127298; 14.
DR IntAct; Q8IYA6; 9.
DR STRING; 9606.ENSP00000305204; -.
DR GlyGen; Q8IYA6; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q8IYA6; -.
DR PhosphoSitePlus; Q8IYA6; -.
DR BioMuta; CKAP2L; -.
DR DMDM; 311033474; -.
DR EPD; Q8IYA6; -.
DR jPOST; Q8IYA6; -.
DR MassIVE; Q8IYA6; -.
DR MaxQB; Q8IYA6; -.
DR PaxDb; Q8IYA6; -.
DR PeptideAtlas; Q8IYA6; -.
DR PRIDE; Q8IYA6; -.
DR ProteomicsDB; 25385; -.
DR ProteomicsDB; 71132; -. [Q8IYA6-1]
DR ProteomicsDB; 71133; -. [Q8IYA6-2]
DR Antibodypedia; 33290; 75 antibodies from 16 providers.
DR DNASU; 150468; -.
DR Ensembl; ENST00000302450.11; ENSP00000305204.6; ENSG00000169607.13. [Q8IYA6-1]
DR GeneID; 150468; -.
DR KEGG; hsa:150468; -.
DR MANE-Select; ENST00000302450.11; ENSP00000305204.6; NM_152515.5; NP_689728.3.
DR UCSC; uc002tie.3; human. [Q8IYA6-1]
DR CTD; 150468; -.
DR DisGeNET; 150468; -.
DR GeneCards; CKAP2L; -.
DR HGNC; HGNC:26877; CKAP2L.
DR HPA; ENSG00000169607; Group enriched (bone marrow, lymphoid tissue, testis).
DR MalaCards; CKAP2L; -.
DR MIM; 272440; phenotype.
DR MIM; 616174; gene.
DR neXtProt; NX_Q8IYA6; -.
DR OpenTargets; ENSG00000169607; -.
DR Orphanet; 3255; Filippi syndrome.
DR PharmGKB; PA144596448; -.
DR VEuPathDB; HostDB:ENSG00000169607; -.
DR eggNOG; ENOG502RZUT; Eukaryota.
DR GeneTree; ENSGT00530000063691; -.
DR HOGENOM; CLU_022701_0_0_1; -.
DR InParanoid; Q8IYA6; -.
DR OMA; QKSTQPC; -.
DR OrthoDB; 417608at2759; -.
DR PhylomeDB; Q8IYA6; -.
DR TreeFam; TF333003; -.
DR PathwayCommons; Q8IYA6; -.
DR SignaLink; Q8IYA6; -.
DR BioGRID-ORCS; 150468; 36 hits in 1077 CRISPR screens.
DR ChiTaRS; CKAP2L; human.
DR GenomeRNAi; 150468; -.
DR Pharos; Q8IYA6; Tbio.
DR PRO; PR:Q8IYA6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8IYA6; protein.
DR Bgee; ENSG00000169607; Expressed in ventricular zone and 116 other tissues.
DR ExpressionAtlas; Q8IYA6; baseline and differential.
DR Genevisible; Q8IYA6; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR InterPro; IPR029197; CKAP2_C.
DR Pfam; PF15297; CKAP2_C; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Intellectual disability;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..745
FT /note="Cytoskeleton-associated protein 2-like"
FT /id="PRO_0000324335"
FT REGION 25..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 185..187
FT /note="KEN box"
FT /evidence="ECO:0000250"
FT COMPBIAS 33..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:20388717"
FT MOD_RES 742
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..411
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032219"
FT VAR_SEQ 1..165
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053717"
FT VAR_SEQ 412
FT /note="Q -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032220"
FT VARIANT 19
FT /note="L -> F (in dbSNP:rs36093393)"
FT /id="VAR_039735"
FT VARIANT 26
FT /note="K -> R (in dbSNP:rs35593767)"
FT /id="VAR_039736"
FT VARIANT 62
FT /note="N -> S (in dbSNP:rs17042344)"
FT /evidence="ECO:0000269|PubMed:15815621"
FT /id="VAR_039737"
FT VARIANT 104
FT /note="T -> I (in dbSNP:rs13007595)"
FT /id="VAR_039738"
FT VARIANT 263
FT /note="R -> S (in dbSNP:rs17042341)"
FT /evidence="ECO:0000269|PubMed:15815621"
FT /id="VAR_039739"
FT VARIANT 375
FT /note="I -> V (in dbSNP:rs6731822)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_039740"
FT VARIANT 379
FT /note="P -> A (in dbSNP:rs2676126)"
FT /id="VAR_039741"
FT VARIANT 519
FT /note="S -> G (in dbSNP:rs36046436)"
FT /id="VAR_039742"
FT VARIANT 614
FT /note="L -> S (in dbSNP:rs3811040)"
FT /id="VAR_039743"
FT VARIANT 706
FT /note="E -> D (in dbSNP:rs3811039)"
FT /id="VAR_039744"
FT MUTAGEN 198
FT /note="K->R: Abrogates sumoylation."
FT /evidence="ECO:0000269|PubMed:20388717"
FT CONFLICT 375
FT /note="I -> A (in Ref. 1; BAH14612)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="L -> P (in Ref. 1; BAC05202)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="V -> A (in Ref. 1; BAF85219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 745 AA; 83587 MW; 46FE794CD9EBADD9 CRC64;
MVGPGPTAAA AVEERQRKLQ EYLAAKGKLK SQNTKPYLKS KNNCQNQPPS KSTIRPKNDV
TNHVVLPVKP KRSISIKLQP RPPNTAGSQK PKLEPPKLLG KRLTSECVSS NPYSKPSSKS
FQQCEAGSST TGELSRKPVG SLNIEQLKTT KQQLTDQGNG KCIDFMNNIH VENESLDNFL
KETNKENLLD ILTEPERKPD PKLYTRSKPK TDSYNQTKNS LVPKQALGKS SVNSAVLKDR
VNKQFVGETQ SRTFPVKSQQ LSRGADLARP GVKPSRTVPS HFIRTLSKVQ SSKKPVVKNI
KDIKVNRSQY ERPNETKIRS YPVTEQRVKH TKPRTYPSLL QGEYNNRHPN IKQDQKSSQV
CIPQTSCVLQ KSKAISQRPN LTVGRFNSAI PSTPSIRPNG TSGNKHNNNG FQQKAQTLDS
KLKKAVPQNH FLNKTAPKTQ ADVTTVNGTQ TNPNIKKKAT AEDRRKQLEE WQKSKGKTYK
RPPMELKTKR KVIKEMNISF WKSIEKEEEE KKAQLELSSK INNTLTECLN LIEGGVPSNE
ILNILSSIPE AEKFAKFWIC KAKLLASKGT FDVIGLYEEA IKNGATPIQE LRKVVLNILQ
DSNRTTEGIT SDSLVAETSI TSVEELAKKM ESVKSCLSPK EREQVTATPR IAKAEQHNYP
GIKLQIGPIP RINGMPEVQD MKFITPVRRS SRIERAVSRY PEMLQEHDLV VASLDELLEV
EETKCFIFRR NEALPVTLGF QTPES
