MTCL1_HUMAN
ID MTCL1_HUMAN Reviewed; 1905 AA.
AC Q9Y4B5; E9PAY7; Q6ZMQ9; Q8IWA9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 5.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Microtubule cross-linking factor 1;
DE AltName: Full=Coiled-coil domain-containing protein 165;
DE AltName: Full=PAR-1-interacting protein;
DE AltName: Full=SOGA family member 2;
GN Name=MTCL1; Synonyms=CCDC165, KIAA0802, SOGA2;
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 2), AND VARIANTS ARG-861
RP AND SER-1097.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLY-898.
RC TISSUE=Cerebellum;
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=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1417; SER-1421; THR-1675 AND
RP SER-1679, AND IDENTIFICATION BY 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549; SER-618; THR-621;
RP SER-776; SER-901; SER-923; SER-1385; SER-1388; THR-1417; SER-1421;
RP TYR-1427; SER-1561; SER-1578; SER-1583; SER-1592; SER-1661; THR-1667;
RP THR-1675; SER-1683; SER-1812 AND SER-1814, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-941 AND SER-975 (ISOFORM 4), VARIANT [LARGE SCALE
RP ANALYSIS] GLY-898, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-263; SER-685; SER-776
RP AND SER-1399, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975 (ISOFORM
RP 4), AND IDENTIFICATION BY 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 [13]
RP FUNCTION, SUBUNIT, INTERACTION WITH MARK2, ASSOCIATION WITH MICROTUBULES,
RP AND SUBCELLULAR LOCATION.
RX PubMed=23902687; DOI=10.1242/jcs.127845;
RA Sato Y., Akitsu M., Amano Y., Yamashita K., Ide M., Shimada K.,
RA Yamashita A., Hirano H., Arakawa N., Maki T., Hayashi I., Ohno S.,
RA Suzuki A.;
RT "The novel PAR-1-binding protein MTCL1 has crucial roles in organizing
RT microtubules in polarizing epithelial cells.";
RL J. Cell Sci. 126:4671-4683(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-87; SER-263; SER-549;
RP SER-776; SER-1278; SER-1385; SER-1514; SER-1523; SER-1791 AND SER-1808, AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Microtubule-associated factor involved in the late phase of
CC epithelial polarization and microtubule dynamics regulation. Plays a
CC role in the development and maintenance of non-centrosomal microtubule
CC bundles at the lateral membrane in polarized epithelial cells.
CC {ECO:0000269|PubMed:23902687}.
CC -!- SUBUNIT: Isoform 1 interacts with MARK2; the interaction increases
CC MARK2 microtubule-binding ability (By similarity). Homodimer.
CC Associates (via N- and C-terminus domains) with microtubule filaments.
CC Isoform 2 interacts with MARK2; the interaction is direct.
CC {ECO:0000250, ECO:0000269|PubMed:23902687}.
CC -!- SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000250}. Apical cell
CC membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:23902687}. Midbody {ECO:0000269|PubMed:23902687}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23902687}. Note=Colocalized
CC with microtubules at the base of cilia. Gradually accumulates on the
CC apicobasal microtubule bundles during epithelial cell polarization (By
CC similarity). Colocalized with the apicobasal microtubule bundles
CC running beneath the lateral membrane. Colocalized with microtubule
CC bundles in the spindle pole in mitotic cells and in the midbodies at
CC the end of cytokinesis. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Y4B5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4B5-2; Sequence=VSP_023550;
CC Name=3;
CC IsoId=Q9Y4B5-3; Sequence=VSP_023550, VSP_023551;
CC Name=4;
CC IsoId=Q9Y4B5-4; Sequence=VSP_023549, VSP_023552, VSP_023553,
CC VSP_023554;
CC -!- SIMILARITY: Belongs to the SOGA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34522.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB018345; BAA34522.2; ALT_INIT; mRNA.
DR EMBL; AK131528; BAD18666.1; -; mRNA.
DR EMBL; AP000864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040542; AAH40542.2; -; mRNA.
DR CCDS; CCDS11841.1; -. [Q9Y4B5-3]
DR RefSeq; NP_056025.2; NM_015210.3. [Q9Y4B5-3]
DR RefSeq; XP_005258156.1; XM_005258099.4.
DR AlphaFoldDB; Q9Y4B5; -.
DR SMR; Q9Y4B5; -.
DR BioGRID; 116859; 87.
DR IntAct; Q9Y4B5; 37.
DR MINT; Q9Y4B5; -.
DR STRING; 9606.ENSP00000352927; -.
DR GlyGen; Q9Y4B5; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9Y4B5; -.
DR PhosphoSitePlus; Q9Y4B5; -.
DR BioMuta; MTCL1; -.
DR DMDM; 384872711; -.
DR EPD; Q9Y4B5; -.
DR jPOST; Q9Y4B5; -.
DR MassIVE; Q9Y4B5; -.
DR MaxQB; Q9Y4B5; -.
DR PaxDb; Q9Y4B5; -.
DR PeptideAtlas; Q9Y4B5; -.
DR PRIDE; Q9Y4B5; -.
DR ProteomicsDB; 86147; -. [Q9Y4B5-1]
DR ProteomicsDB; 86148; -. [Q9Y4B5-2]
DR ProteomicsDB; 86149; -. [Q9Y4B5-3]
DR ProteomicsDB; 86150; -. [Q9Y4B5-4]
DR Antibodypedia; 48434; 33 antibodies from 14 providers.
DR DNASU; 23255; -.
DR Ensembl; ENST00000306329.15; ENSP00000305027.11; ENSG00000168502.17. [Q9Y4B5-1]
DR Ensembl; ENST00000359865.7; ENSP00000352927.3; ENSG00000168502.17. [Q9Y4B5-3]
DR Ensembl; ENST00000400050.7; ENSP00000382924.4; ENSG00000168502.17. [Q9Y4B5-3]
DR Ensembl; ENST00000517570.5; ENSP00000429556.1; ENSG00000168502.17. [Q9Y4B5-2]
DR Ensembl; ENST00000518815.1; ENSP00000463465.1; ENSG00000168502.17. [Q9Y4B5-4]
DR GeneID; 23255; -.
DR KEGG; hsa:23255; -.
DR UCSC; uc002knq.2; human. [Q9Y4B5-1]
DR CTD; 23255; -.
DR DisGeNET; 23255; -.
DR GeneCards; MTCL1; -.
DR HGNC; HGNC:29121; MTCL1.
DR HPA; ENSG00000168502; Tissue enhanced (brain, retina).
DR MIM; 615766; gene.
DR neXtProt; NX_Q9Y4B5; -.
DR OpenTargets; ENSG00000168502; -.
DR PharmGKB; PA128394616; -.
DR VEuPathDB; HostDB:ENSG00000168502; -.
DR eggNOG; KOG4787; Eukaryota.
DR GeneTree; ENSGT00950000182982; -.
DR HOGENOM; CLU_002595_0_0_1; -.
DR InParanoid; Q9Y4B5; -.
DR OMA; KDLHARP; -.
DR OrthoDB; 34629at2759; -.
DR PhylomeDB; Q9Y4B5; -.
DR TreeFam; TF331853; -.
DR PathwayCommons; Q9Y4B5; -.
DR SignaLink; Q9Y4B5; -.
DR BioGRID-ORCS; 23255; 7 hits in 1074 CRISPR screens.
DR ChiTaRS; MTCL1; human.
DR GeneWiki; KIAA0802; -.
DR GenomeRNAi; 23255; -.
DR Pharos; Q9Y4B5; Tbio.
DR PRO; PR:Q9Y4B5; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9Y4B5; protein.
DR Bgee; ENSG00000168502; Expressed in cerebellar cortex and 156 other tissues.
DR ExpressionAtlas; Q9Y4B5; baseline and differential.
DR Genevisible; Q9Y4B5; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0097427; C:microtubule bundle; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR InterPro; IPR027882; DUF4482.
DR InterPro; IPR027881; SOGA.
DR Pfam; PF14818; DUF4482; 1.
DR Pfam; PF11365; SOGA; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..1905
FT /note="Microtubule cross-linking factor 1"
FT /id="PRO_0000280113"
FT REGION 1..508
FT /note="Necessary for self-assembly, microtubule bundling
FT activity and apicobasal microtubule organization"
FT /evidence="ECO:0000250"
FT REGION 1..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..249
FT /note="Necessary for colocalization and binding with
FT microtubules"
FT /evidence="ECO:0000250"
FT REGION 544..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1382
FT /note="Necessary for interaction with MARK2 and apicobasal
FT microtubule bundle formation in polarized epithelial cells"
FT /evidence="ECO:0000269|PubMed:23902687"
FT REGION 1346..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1485..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1773
FT /note="Necessary for colocalization and binding with
FT microtubules"
FT REGION 1707..1756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1782..1842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1863..1905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 330..404
FT /evidence="ECO:0000255"
FT COILED 432..483
FT /evidence="ECO:0000255"
FT COILED 513..718
FT /evidence="ECO:0000255"
FT COILED 1143..1201
FT /evidence="ECO:0000255"
FT COILED 1238..1278
FT /evidence="ECO:0000255"
FT COMPBIAS 21..35
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..268
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1722..1756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHU5"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHU5"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 621
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1417
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 1421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 1427
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1667
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1675
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 1679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 1683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1791
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1812
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1814
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..1004
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023549"
FT VAR_SEQ 1..360
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9872452"
FT /id="VSP_023550"
FT VAR_SEQ 989
FT /note="E -> ELRGPPVLPEQSVSIEELQGQLVQAARLHQEETETFTNKIHK (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023551"
FT VAR_SEQ 1187
FT /note="Q -> QNCCGYPRINIEEETLGFTRLPAGSTVKTLKSLGLQRLE (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023552"
FT VAR_SEQ 1273..1300
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023553"
FT VAR_SEQ 1894..1905
FT /note="NQTVLLTAPWGL -> ELPCSALAPSLEPCFSRPERPANRRPPSRWAPHSPT
FT ASQPQSPGDPTSLEEHGGEEPPEEQPHRDASLHGLSQYNSL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023554"
FT VARIANT 602
FT /note="M -> T (in dbSNP:rs35739383)"
FT /id="VAR_055942"
FT VARIANT 861
FT /note="Q -> R (in dbSNP:rs1965665)"
FT /evidence="ECO:0000269|PubMed:9872452"
FT /id="VAR_031073"
FT VARIANT 898
FT /note="D -> G (in dbSNP:rs3744979)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0007744|PubMed:18669648"
FT /id="VAR_031074"
FT VARIANT 1097
FT /note="G -> S (in dbSNP:rs12386117)"
FT /evidence="ECO:0000269|PubMed:9872452"
FT /id="VAR_031075"
FT VARIANT 1211
FT /note="K -> Q (in dbSNP:rs11874468)"
FT /id="VAR_031076"
FT MOD_RES Q9Y4B5-4:941
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9Y4B5-4:975
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
SQ SEQUENCE 1905 AA; 209526 MW; BD7455BB2B822CE0 CRC64;
METLNGPAGG GAPDAKLQPP GQHHRHHHLH PVAERRRLHR APSPARPFLK DLHARPAAPG
PAVPSSGRAP APAAPRSPNL AGKAPPSPGS LAAPGRLSRR SGGVPGAKDK PPPGAGARAA
GGAKAALGSR RAARVAPAEP LSRAGKPPGA EPPSAAAKGR KAKRGSRAPP ARTVGPPTPA
ARIPAVTLAV TSVAGSPARC SRISHTDSSS DLSDCPSEPL SDEQRLLPAA SSDAESGTGS
SDREPPRGAP TPSPAARGAP PGSPEPPALL AAPLAAGACP GGRSIPSGVS GGFAGPGVAE
DVRGRSPPER PVPGTPKEPS LGEQSRLVPA AEEEELLREM EELRSENDYL KDELDELRAE
MEEMRDSYLE EDVYQLQELR RELDRANKNC RILQYRLRKA EQKSLKVAET GQVDGELIRS
LEQDLKVAKD VSVRLHHELK TVEEKRAKAE DENETLRQQM IEVEISKQAL QNELERLKES
SLKRRSTREM YKEKKTFNQD DSADLRCQLQ FAKEEAFLMR KKMAKLGREK DELEQELQKY
KSLYGDVDSP LPTGEAGGPP STREAELKLR LKLVEEEANI LGRKIVELEV ENRGLKAEME
DMRGQQEREG PGRDHAPSIP TSPFGDSLES STELRRHLQF VEEEAELLRR SISEIEDHNR
QLTHELSKFK FEPPREPGWL GEGASPGAGG GAPLQEELKS ARLQISELSG KVLKLQHENH
ALLSNIQRCD LAAHLGLRAP SPRDSDAESD AGKKESDGEE SRLPQPKREG PVGGESDSEE
MFEKTSGFGS GKPSEASEPC PTELLKARED SEYLVTLKHE AQRLERTVER LITDTDSFLH
DAGLRGGAPL PGPGLQGEEE QGEGDQQEPQ LLGTINAKMK AFKKELQAFL EQVNRIGDGL
SPLPHLTESS SFLSTVTSVS RDSPIGNLGK ELGPDLQSRL KEQLEWQLGP ARGDERESLR
LRAARELHRR ADGDTGSHGL GGQTCFSLEM EEEHLYALRW KELEMHSLAL QNTLHERTWS
DEKNLMQQEL RSLKQNIFLF YVKLRWLLKH WRQGKQMEEE GEEFTEGEHP ETLSRLGELG
VQGGHQADGP DHDSDRGCGF PVGEHSPHSR VQIGDHSLRL QTADRGQPHK QVVENQQLFS
AFKALLEDFR AELREDERAR LRLQQQYASD KAAWDVEWAV LKCRLEQLEE KTENKLGELG
SSAESKGALK KEREVHQKLL ADSHSLVMDL RWQIHHSEKN WNREKVELLD RLDRDRQEWE
RQKKEFLWRI EQLQKENSPR RGGSFLCDQK DGNVRPFPHQ GSLRMPRPVA MWPCADADSI
PFEDRPLSKL KESDRCSASE NLYLDALSLD DEPEEPPAHR PEREFRNRLP EEEENHKGNL
QRAVSVSSMS EFQRLMDISP FLPEKGLPST SSKEDVTPPL SPDDLKYIEE FNKSWDYTPN
RGHNGGGPDL WADRTEVGRA GHEDSTEPFP DSSWYLTTSV TMTTDTMTSP EHCQKQPLRS
HVLTEQSGLR VLHSPPAVRR VDSITAAGGE GPFPTSRARG SPGDTKGGPP EPMLSRWPCT
SPRHSRDYVE GARRPLDSPL CTSLGFASPL HSLEMSKNLS DDMKEVAFSV RNAICSGPGE
LQVKDMACQT NGSRTMGTQT VQTISVGLQT EALRGSGVTS SPHKCLTPKA GGGATPVSSP
SRSLRSRQVA PAIEKVQAKF ERTCCSPKYG SPKLQRKPLP KADQPNNRTS PGMAQKGYSE
SAWARSTTTR ESPVHTTIND GLSSLFNIID HSPVVQDPFQ KGLRAGSRSR SAEPRPELGP
GQETGTNSRG RSPSPIGVGS EMCREEGGEG TPVKQDLSAP PGYTLTENVA RILNKKLLEH
ALKEERRQAA HGPPGLHSDS HSLGDTAEPG PMENQTVLLT APWGL
