JKIP1_HUMAN
ID JKIP1_HUMAN Reviewed; 626 AA.
AC Q96N16; A6H2J2; A6H2J3; A6H2J4; A6H2J5; A8MTK6; B4DHZ8; B8ZZR7; D3DVT0;
AC Q86Y69; Q8N7G3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Janus kinase and microtubule-interacting protein 1;
DE AltName: Full=GABA-B receptor-binding protein;
DE AltName: Full=Multiple alpha-helices and RNA-linker protein 1;
DE Short=Marlin-1;
GN Name=JAKMIP1; Synonyms=GABABRBP, JAMIP1, MARLIN1;
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 [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH GABBR1,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=14718537; DOI=10.1074/jbc.m311737200;
RA Couve A., Restituito S., Brandon J.M., Charles K.J., Bawagan H.,
RA Freeman K.B., Pangalos M.N., Calver A.R., Moss S.J.;
RT "Marlin-1, a novel RNA-binding protein associates with GABA receptors.";
RL J. Biol. Chem. 279:13934-13943(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), TISSUE SPECIFICITY,
RP AND VARIANT ARG-251.
RC TISSUE=Brain;
RX PubMed=17761393; DOI=10.1016/j.gene.2007.07.001;
RA Costa V., Conte I., Ziviello C., Casamassimi A., Alfano G., Banfi S.,
RA Ciccodicola A.;
RT "Identification and expression analysis of novel Jakmip1 transcripts.";
RL Gene 402:1-8(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 6 AND 7).
RC TISSUE=Caudate nucleus, Teratocarcinoma, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP FUNCTION, INTERACTION WITH JAK1 AND TYK2, OLIGOMERIZATION, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=15277531; DOI=10.1074/jbc.m401915200;
RA Steindler C., Li Z., Algarte M., Alcover A., Libri V., Ragimbeau J.,
RA Pellegrini S.;
RT "Jamip1 (marlin-1) defines a family of proteins interacting with Janus
RT kinases and microtubules.";
RL J. Biol. Chem. 279:43168-43177(2004).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH GABBR1 AND KIF5B.
RX PubMed=17532644; DOI=10.1016/j.mcn.2007.04.008;
RA Vidal R.L., Ramirez O.A., Sandoval L., Koenig-Robert R., Haertel S.,
RA Couve A.;
RT "Marlin-1 and conventional kinesin link GABAB receptors to the cytoskeleton
RT and regulate receptor transport.";
RL Mol. Cell. Neurosci. 35:501-512(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382 AND THR-470, AND
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 [10]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-375.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Associates with microtubules and may play a role in the
CC microtubule-dependent transport of the GABA-B receptor. May play a role
CC in JAK1 signaling and regulate microtubule cytoskeleton rearrangements.
CC {ECO:0000269|PubMed:14718537, ECO:0000269|PubMed:15277531,
CC ECO:0000269|PubMed:17532644}.
CC -!- SUBUNIT: Homodimer. Forms a complex with GABBR1 and KIF5B/kinesin-1.
CC Interacts with JAK1 and TYK2. {ECO:0000269|PubMed:14718537,
CC ECO:0000269|PubMed:15277531, ECO:0000269|PubMed:17532644}.
CC -!- INTERACTION:
CC Q96N16; P51451: BLK; NbExp=3; IntAct=EBI-2680803, EBI-2105445;
CC Q96N16; Q96B23: C18orf25; NbExp=3; IntAct=EBI-2680803, EBI-742108;
CC Q96N16; Q9HC52: CBX8; NbExp=3; IntAct=EBI-2680803, EBI-712912;
CC Q96N16; P26196: DDX6; NbExp=3; IntAct=EBI-2680803, EBI-351257;
CC Q96N16; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-2680803, EBI-744099;
CC Q96N16; P42858: HTT; NbExp=10; IntAct=EBI-2680803, EBI-466029;
CC Q96N16; Q14005-2: IL16; NbExp=3; IntAct=EBI-2680803, EBI-17178971;
CC Q96N16; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-2680803, EBI-348259;
CC Q96N16; Q9Y3B7: MRPL11; NbExp=3; IntAct=EBI-2680803, EBI-5453723;
CC Q96N16; P20618: PSMB1; NbExp=3; IntAct=EBI-2680803, EBI-372273;
CC Q96N16; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-2680803, EBI-748391;
CC Q96N16; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-2680803, EBI-10241197;
CC Q96N16; O75604: USP2; NbExp=3; IntAct=EBI-2680803, EBI-743272;
CC Q96N16; P07947: YES1; NbExp=3; IntAct=EBI-2680803, EBI-515331;
CC Q96N16; Q9UHR6: ZNHIT2; NbExp=3; IntAct=EBI-2680803, EBI-2557592;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Membrane; Peripheral
CC membrane protein. Note=Colocalizes with the microtubule network.
CC Localizes to the cell body and neurites of hippocampal neurons where it
CC accumulates in granules. Localizes to the tail and to a lower extent to
CC the head of sperm cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=Jakmip1A;
CC IsoId=Q96N16-1; Sequence=Displayed;
CC Name=2; Synonyms=Jakmip1B;
CC IsoId=Q96N16-2; Sequence=VSP_031997;
CC Name=3; Synonyms=Jakmip1C;
CC IsoId=Q96N16-3; Sequence=VSP_031991, VSP_031993;
CC Name=4; Synonyms=Jakmip1D;
CC IsoId=Q96N16-4; Sequence=VSP_031995, VSP_031996;
CC Name=5; Synonyms=Jakmip1E;
CC IsoId=Q96N16-5; Sequence=VSP_031990, VSP_031992, VSP_031997;
CC Name=6;
CC IsoId=Q96N16-6; Sequence=VSP_031989, VSP_031994;
CC Name=7;
CC IsoId=Q96N16-7; Sequence=VSP_031990;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in neural tissues and
CC lymphoid cells (at protein level). Isoform 2, isoform 3 and isoform 4
CC are specifically expressed in brain and retina. Isoform 1 and isoform 5
CC are also detected in liver, lung and skeletal muscle. Also detected in
CC testis and to a lower extent spleen and intestine.
CC {ECO:0000269|PubMed:15277531, ECO:0000269|PubMed:17761393}.
CC -!- MISCELLANEOUS: [Isoform 3]: Dubious isoform produced through aberrant
CC splice sites. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Dubious isoform produced through aberrant
CC splice sites. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the JAKMIP family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to bind single-stranded RNA molecules
CC and regulate GABA-B receptor expression. {ECO:0000305|PubMed:14718537}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC05325.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC05325.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AY382340; AAR26235.1; -; mRNA.
DR EMBL; AM412307; CAL80778.1; -; mRNA.
DR EMBL; AM412308; CAL80779.1; -; mRNA.
DR EMBL; AM412309; CAL80780.1; -; mRNA.
DR EMBL; AM412310; CAL80781.1; -; mRNA.
DR EMBL; AK056126; BAB71098.1; -; mRNA.
DR EMBL; AK098536; BAC05325.1; ALT_SEQ; mRNA.
DR EMBL; AK295339; BAG58310.1; -; mRNA.
DR EMBL; AC092442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471131; EAW82401.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82402.1; -; Genomic_DNA.
DR EMBL; BC047075; AAH47075.1; -; mRNA.
DR CCDS; CCDS3385.1; -. [Q96N16-1]
DR CCDS; CCDS47005.1; -. [Q96N16-2]
DR CCDS; CCDS77897.1; -. [Q96N16-7]
DR RefSeq; NP_001092903.1; NM_001099433.1. [Q96N16-2]
DR RefSeq; NP_001293062.1; NM_001306133.1. [Q96N16-1]
DR RefSeq; NP_001293063.1; NM_001306134.1. [Q96N16-7]
DR RefSeq; NP_653321.1; NM_144720.3. [Q96N16-1]
DR RefSeq; XP_011511702.1; XM_011513400.2. [Q96N16-7]
DR RefSeq; XP_016863282.1; XM_017007793.1. [Q96N16-2]
DR AlphaFoldDB; Q96N16; -.
DR SMR; Q96N16; -.
DR BioGRID; 127465; 33.
DR IntAct; Q96N16; 22.
DR MINT; Q96N16; -.
DR STRING; 9606.ENSP00000386711; -.
DR iPTMnet; Q96N16; -.
DR PhosphoSitePlus; Q96N16; -.
DR BioMuta; JAKMIP1; -.
DR DMDM; 74732477; -.
DR EPD; Q96N16; -.
DR jPOST; Q96N16; -.
DR MassIVE; Q96N16; -.
DR MaxQB; Q96N16; -.
DR PaxDb; Q96N16; -.
DR PeptideAtlas; Q96N16; -.
DR PRIDE; Q96N16; -.
DR ProteomicsDB; 4263; -.
DR ProteomicsDB; 77442; -. [Q96N16-1]
DR ProteomicsDB; 77443; -. [Q96N16-2]
DR ProteomicsDB; 77444; -. [Q96N16-3]
DR ProteomicsDB; 77445; -. [Q96N16-4]
DR ProteomicsDB; 77446; -. [Q96N16-5]
DR ProteomicsDB; 77447; -. [Q96N16-6]
DR Antibodypedia; 22639; 175 antibodies from 28 providers.
DR DNASU; 152789; -.
DR Ensembl; ENST00000282924.9; ENSP00000282924.5; ENSG00000152969.20. [Q96N16-1]
DR Ensembl; ENST00000409021.9; ENSP00000386711.3; ENSG00000152969.20. [Q96N16-2]
DR Ensembl; ENST00000409371.8; ENSP00000387042.3; ENSG00000152969.20. [Q96N16-5]
DR Ensembl; ENST00000409831.5; ENSP00000386925.1; ENSG00000152969.20. [Q96N16-1]
DR Ensembl; ENST00000410077.2; ENSP00000386745.2; ENSG00000152969.20. [Q96N16-7]
DR GeneID; 152789; -.
DR KEGG; hsa:152789; -.
DR MANE-Select; ENST00000409021.9; ENSP00000386711.3; NM_001099433.2; NP_001092903.1. [Q96N16-2]
DR UCSC; uc003giu.5; human. [Q96N16-1]
DR CTD; 152789; -.
DR DisGeNET; 152789; -.
DR GeneCards; JAKMIP1; -.
DR HGNC; HGNC:26460; JAKMIP1.
DR HPA; ENSG00000152969; Tissue enhanced (brain, pituitary gland, retina).
DR MIM; 611195; gene.
DR neXtProt; NX_Q96N16; -.
DR OpenTargets; ENSG00000152969; -.
DR PharmGKB; PA143485508; -.
DR VEuPathDB; HostDB:ENSG00000152969; -.
DR eggNOG; ENOG502QS6X; Eukaryota.
DR GeneTree; ENSGT00940000153713; -.
DR HOGENOM; CLU_020294_1_0_1; -.
DR InParanoid; Q96N16; -.
DR OMA; IEEKHSF; -.
DR OrthoDB; 727914at2759; -.
DR PhylomeDB; Q96N16; -.
DR TreeFam; TF331900; -.
DR PathwayCommons; Q96N16; -.
DR SignaLink; Q96N16; -.
DR SIGNOR; Q96N16; -.
DR BioGRID-ORCS; 152789; 9 hits in 1077 CRISPR screens.
DR GenomeRNAi; 152789; -.
DR Pharos; Q96N16; Tbio.
DR PRO; PR:Q96N16; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q96N16; protein.
DR Bgee; ENSG00000152969; Expressed in caudate nucleus and 124 other tissues.
DR ExpressionAtlas; Q96N16; baseline and differential.
DR Genevisible; Q96N16; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0050811; F:GABA receptor binding; IDA:MGI.
DR GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR024836; JAKMIP.
DR InterPro; IPR031994; JAKMIP_C.
DR PANTHER; PTHR18935; PTHR18935; 1.
DR Pfam; PF16034; JAKMIP_CC3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Membrane;
KW Microtubule; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..626
FT /note="Janus kinase and microtubule-interacting protein 1"
FT /id="PRO_0000323008"
FT REGION 1..365
FT /note="Mediates association with microtubules"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..626
FT /note="Mediates interaction with TYK2 and GABBR1"
FT /evidence="ECO:0000269|PubMed:14718537,
FT ECO:0000269|PubMed:15277531"
FT REGION 452..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..255
FT /evidence="ECO:0000255"
FT COILED 284..413
FT /evidence="ECO:0000255"
FT COILED 490..604
FT /evidence="ECO:0000255"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..208
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031989"
FT VAR_SEQ 44..208
FT /note="Missing (in isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17761393"
FT /id="VSP_031990"
FT VAR_SEQ 374..431
FT /note="QASLKRHTSLNDLSLTRDEQEIEFLRLQVLEQQHVIDDLSLERERLLRSKRH
FT RGKSLK -> HGAAAAGPAENPRTGGQTGVSEAAPERTGGKVFVPFFVFLTSIHSVALM
FT TSVSQELGL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17761393"
FT /id="VSP_031991"
FT VAR_SEQ 415..434
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17761393"
FT /id="VSP_031992"
FT VAR_SEQ 432..626
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17761393"
FT /id="VSP_031993"
FT VAR_SEQ 494..520
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031994"
FT VAR_SEQ 495..569
FT /note="YQALQRAYALLQEQVGGTLDAEREARTREQLQADLLRCQAKIEDLEKLLVEK
FT GQDSKWVEEKQLLIRTNQDLLEK -> DLQAAVEKVRRQILRQSREFDSQILRERMELL
FT QQAQQRIRELEDKLEFQKRHLKELEEKFLFLFLFFSLAFILWP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17761393"
FT /id="VSP_031995"
FT VAR_SEQ 570..626
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17761393"
FT /id="VSP_031996"
FT VAR_SEQ 603..626
FT /note="VRDSICCKLSNGADILFEPKLKFM -> ERERRSPAFNLQITTFPENHSSAL
FT QLFCHQEGVKDVNVSELMKKLDILGDNGNLRNEEQVAIIQAGTVLALCEKWLKQIEGTE
FT AALTQKMLDLEKEKDLFSRQKGYLEEELDYRKQALDQAYLKIQDLEATLYTALQQEPGR
FT RAGEALSEGQREDLQAAVEKVRRQILRQSREFDSQILRERMELLQQAQQRIRELEDKLE
FT FQKRHLKELEEKFLFLFLFFSLAFILWP (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:17761393"
FT /id="VSP_031997"
FT VARIANT 251
FT /note="K -> R (in dbSNP:rs772311401)"
FT /evidence="ECO:0000269|PubMed:17761393"
FT /id="VAR_039471"
FT VARIANT 375
FT /note="A -> V (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs199693515)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_039472"
FT CONFLICT 163
FT /note="K -> N (in Ref. 6; AAH47075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 73209 MW; 6A8E164E8A2A7EFB CRC64;
MSKKGRSKGE KPEMETDAVQ MANEELRAKL TSIQIEFQQE KSKVGKLRER LQEAKLEREQ
EQRRHTAYIS ELKAKLHEEK TKELQALREG LIRQHEQEAA RTAKIKEGEL QRLQATLNVL
RDGAADKVKT ALLTEAREEA RRAFDGERLR LQQEILELKA ARKQAEEALS NCMQADKTKA
ADLRAAYQAH QDEVHRIKRE CERDIRRLMD EIKGKDRVIL ALEKELGVQA GQTQKLLLQK
EALDEQLVQV KEAERHHSSP KRELPPGIGD MVELMGVQDQ HMDERDVRRF QLKIAELNSV
IRKLEDRNTL LADERNELLK RSRETEVQLK PLVEKNKRMN KKNEDLLQSI QRMEEKIKNL
TRENVEMKEK LSAQASLKRH TSLNDLSLTR DEQEIEFLRL QVLEQQHVID DLSLERERLL
RSKRHRGKSL KPPKKHVVET FFGFDEESVD SETLSETSYN TDRTDRTPAT PEEDLDDATA
REEADLRFCQ LTREYQALQR AYALLQEQVG GTLDAEREAR TREQLQADLL RCQAKIEDLE
KLLVEKGQDS KWVEEKQLLI RTNQDLLEKI YRLEMEENQL KNEMQDAKDQ NELLEFRVLE
LEVRDSICCK LSNGADILFE PKLKFM
