KI13B_HUMAN
ID KI13B_HUMAN Reviewed; 1826 AA.
AC Q9NQT8; B4DGY5; B5MC45; F8VPJ2; O75134; Q9BYJ6;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Kinesin-like protein KIF13B;
DE AltName: Full=Kinesin-like protein GAKIN;
GN Name=KIF13B; Synonyms=GAKIN, KIAA0639;
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), AND INTERACTION WITH DLG1 AND DLG4.
RX PubMed=10859302; DOI=10.1074/jbc.m000715200;
RA Hanada T., Lin L., Tibaldi E.V., Reinherz E.L., Chishti A.H.;
RT "GAKIN, a novel kinesin-like protein associates with the human homologue of
RT the Drosophila discs large tumor suppressor in T lymphocytes.";
RL J. Biol. Chem. 275:28774-28784(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Nagase T., Ishikawa K.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1096-1826 (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1644, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1379; SER-1382; SER-1432 AND
RP SER-1438, AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1410, 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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH 14-3-3, MUTAGENESIS OF
RP SER-1381 AND SER-1410, AND PHOSPHORYLATION AT SER-1381 AND SER-1410.
RX PubMed=20194617; DOI=10.1128/mcb.01181-09;
RA Yoshimura Y., Terabayashi T., Miki H.;
RT "Par1b/MARK2 phosphorylates kinesin-like motor protein GAKIN/KIF13B to
RT regulate axon formation.";
RL Mol. Cell. Biol. 30:2206-2219(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661, 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661; SER-1381; SER-1391;
RP SER-1410; SER-1644 AND SER-1797, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1410; SER-1537; THR-1545;
RP SER-1559 AND SER-1797, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 STRUCTURE BY NMR OF 1684-1771.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CAP-Gly domain in human kinesin-like protein
RT KIF13B.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Involved in reorganization of the cortical cytoskeleton.
CC Regulates axon formation by promoting the formation of extra axons. May
CC be functionally important for the intracellular trafficking of MAGUKs
CC and associated protein complexes. {ECO:0000269|PubMed:20194617}.
CC -!- SUBUNIT: Binds to DLG1 and DLG4. Interacts (when phosphorylated at Ser-
CC 1381 and Ser-1410) with 14-3-3. {ECO:0000269|PubMed:10859302,
CC ECO:0000269|PubMed:20194617}.
CC -!- INTERACTION:
CC Q9NQT8; O75689: ADAP1; NbExp=6; IntAct=EBI-766408, EBI-714732;
CC Q9NQT8; Q12959-2: DLG1; NbExp=3; IntAct=EBI-766408, EBI-357500;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20194617}. Cell projection, axon
CC {ECO:0000269|PubMed:20194617}. Note=accumulates at the distal part of
CC the microtubules in the tips of axons, but not of dendrites.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NQT8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQT8-2; Sequence=VSP_056360, VSP_056361;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated at Ser-1381 and Ser-1410 by MARK2, promoting
CC interaction with 14-3-3 and inhibiting microtubule-dependent
CC accumulation and formation of axons. {ECO:0000269|PubMed:20194617}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31614.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF279865; AAF81263.1; -; mRNA.
DR EMBL; AB014539; BAA31614.3; ALT_INIT; mRNA.
DR EMBL; AK294837; BAG57946.1; -; mRNA.
DR EMBL; AC084262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL583912; CAC29496.1; -; mRNA.
DR CCDS; CCDS55217.1; -. [Q9NQT8-1]
DR RefSeq; NP_056069.2; NM_015254.3. [Q9NQT8-1]
DR PDB; 2COW; NMR; -; A=1685-1771.
DR PDB; 3FM8; X-ray; 2.30 A; A/B=440-545.
DR PDB; 3GBJ; X-ray; 2.10 A; A/B/C=4-352.
DR PDB; 3MDB; X-ray; 2.95 A; A/B=440-545.
DR PDBsum; 2COW; -.
DR PDBsum; 3FM8; -.
DR PDBsum; 3GBJ; -.
DR PDBsum; 3MDB; -.
DR AlphaFoldDB; Q9NQT8; -.
DR SMR; Q9NQT8; -.
DR BioGRID; 116895; 128.
DR DIP; DIP-34586N; -.
DR IntAct; Q9NQT8; 15.
DR STRING; 9606.ENSP00000427900; -.
DR GlyGen; Q9NQT8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NQT8; -.
DR MetOSite; Q9NQT8; -.
DR PhosphoSitePlus; Q9NQT8; -.
DR SwissPalm; Q9NQT8; -.
DR BioMuta; KIF13B; -.
DR DMDM; 519668668; -.
DR EPD; Q9NQT8; -.
DR jPOST; Q9NQT8; -.
DR MassIVE; Q9NQT8; -.
DR MaxQB; Q9NQT8; -.
DR PaxDb; Q9NQT8; -.
DR PeptideAtlas; Q9NQT8; -.
DR PRIDE; Q9NQT8; -.
DR ProteomicsDB; 28292; -.
DR ProteomicsDB; 4171; -.
DR ProteomicsDB; 82187; -. [Q9NQT8-1]
DR Antibodypedia; 5396; 165 antibodies from 28 providers.
DR DNASU; 23303; -.
DR Ensembl; ENST00000524189.6; ENSP00000427900.1; ENSG00000197892.13. [Q9NQT8-1]
DR GeneID; 23303; -.
DR KEGG; hsa:23303; -.
DR MANE-Select; ENST00000524189.6; ENSP00000427900.1; NM_015254.4; NP_056069.2.
DR UCSC; uc003xhh.5; human. [Q9NQT8-1]
DR CTD; 23303; -.
DR DisGeNET; 23303; -.
DR GeneCards; KIF13B; -.
DR HGNC; HGNC:14405; KIF13B.
DR HPA; ENSG00000197892; Group enriched (brain, parathyroid gland).
DR MIM; 607350; gene.
DR neXtProt; NX_Q9NQT8; -.
DR OpenTargets; ENSG00000197892; -.
DR PharmGKB; PA30099; -.
DR VEuPathDB; HostDB:ENSG00000197892; -.
DR eggNOG; KOG0241; Eukaryota.
DR GeneTree; ENSGT00940000155500; -.
DR HOGENOM; CLU_001485_29_2_1; -.
DR InParanoid; Q9NQT8; -.
DR OMA; CKEVAVS; -.
DR OrthoDB; 76316at2759; -.
DR PhylomeDB; Q9NQT8; -.
DR TreeFam; TF105221; -.
DR PathwayCommons; Q9NQT8; -.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q9NQT8; -.
DR SIGNOR; Q9NQT8; -.
DR BioGRID-ORCS; 23303; 17 hits in 1077 CRISPR screens.
DR ChiTaRS; KIF13B; human.
DR EvolutionaryTrace; Q9NQT8; -.
DR GenomeRNAi; 23303; -.
DR Pharos; Q9NQT8; Tbio.
DR PRO; PR:Q9NQT8; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NQT8; protein.
DR Bgee; ENSG00000197892; Expressed in olfactory bulb and 205 other tissues.
DR ExpressionAtlas; Q9NQT8; baseline and differential.
DR Genevisible; Q9NQT8; HS.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; TAS:UniProtKB.
DR GO; GO:0050770; P:regulation of axonogenesis; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 2.30.30.190; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1826
FT /note="Kinesin-like protein KIF13B"
FT /id="PRO_0000125448"
FT DOMAIN 5..353
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 471..535
FT /note="FHA"
FT DOMAIN 1721..1763
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REGION 546..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1662..1698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 364..439
FT /evidence="ECO:0000255"
FT COILED 607..710
FT /evidence="ECO:0000255"
FT COILED 752..772
FT /evidence="ECO:0000255"
FT COILED 1096..1143
FT /evidence="ECO:0000255"
FT COMPBIAS 547..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1624
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1381
FT /note="Phosphoserine; by MARK2"
FT /evidence="ECO:0000269|PubMed:20194617,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1410
FT /note="Phosphoserine; by MARK2"
FT /evidence="ECO:0000269|PubMed:20194617,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1545
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..1460
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056360"
FT VAR_SEQ 1487..1507
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056361"
FT VARIANT 1471
FT /note="V -> I (in dbSNP:rs17526980)"
FT /id="VAR_055982"
FT MUTAGEN 1381
FT /note="S->A: Abolishes phosphorylation by MARK2; when
FT associated with A-1410."
FT /evidence="ECO:0000269|PubMed:20194617"
FT MUTAGEN 1410
FT /note="S->A: Abolishes phosphorylation by MARK2; when
FT associated with A-1389."
FT /evidence="ECO:0000269|PubMed:20194617"
FT CONFLICT 55
FT /note="V -> C (in Ref. 1; AAF81263)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="V -> A (in Ref. 1; AAF81263)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="F -> L (in Ref. 1; AAF81263)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="V -> A (in Ref. 1; AAF81263)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="K -> E (in Ref. 1; AAF81263)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="H -> N (in Ref. 1; AAF81263)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="H -> L (in Ref. 1; AAF81263)"
FT /evidence="ECO:0000305"
FT CONFLICT 858
FT /note="S -> P (in Ref. 1; AAF81263)"
FT /evidence="ECO:0000305"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:3GBJ"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:3GBJ"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:3GBJ"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:3GBJ"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3GBJ"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3GBJ"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3GBJ"
FT HELIX 76..92
FT /evidence="ECO:0007829|PDB:3GBJ"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:3GBJ"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:3GBJ"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:3GBJ"
FT HELIX 122..137
FT /evidence="ECO:0007829|PDB:3GBJ"
FT STRAND 142..154
FT /evidence="ECO:0007829|PDB:3GBJ"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3GBJ"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:3GBJ"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:3GBJ"
FT STRAND 222..235
FT /evidence="ECO:0007829|PDB:3GBJ"
FT STRAND 241..253
FT /evidence="ECO:0007829|PDB:3GBJ"
FT HELIX 272..292
FT /evidence="ECO:0007829|PDB:3GBJ"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:3GBJ"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:3GBJ"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:3GBJ"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:3GBJ"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:3GBJ"
FT HELIX 337..350
FT /evidence="ECO:0007829|PDB:3GBJ"
FT STRAND 449..452
FT /evidence="ECO:0007829|PDB:3FM8"
FT TURN 457..460
FT /evidence="ECO:0007829|PDB:3MDB"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:3FM8"
FT STRAND 469..476
FT /evidence="ECO:0007829|PDB:3FM8"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:3FM8"
FT STRAND 493..497
FT /evidence="ECO:0007829|PDB:3FM8"
FT STRAND 503..507
FT /evidence="ECO:0007829|PDB:3FM8"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:3FM8"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:3FM8"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:3FM8"
FT TURN 535..537
FT /evidence="ECO:0007829|PDB:3FM8"
FT STRAND 538..543
FT /evidence="ECO:0007829|PDB:3FM8"
FT STRAND 1706..1708
FT /evidence="ECO:0007829|PDB:2COW"
FT STRAND 1710..1712
FT /evidence="ECO:0007829|PDB:2COW"
FT STRAND 1714..1721
FT /evidence="ECO:0007829|PDB:2COW"
FT STRAND 1724..1728
FT /evidence="ECO:0007829|PDB:2COW"
FT STRAND 1730..1734
FT /evidence="ECO:0007829|PDB:2COW"
FT STRAND 1736..1738
FT /evidence="ECO:0007829|PDB:2COW"
FT STRAND 1743..1746
FT /evidence="ECO:0007829|PDB:2COW"
FT STRAND 1760..1762
FT /evidence="ECO:0007829|PDB:2COW"
FT HELIX 1764..1766
FT /evidence="ECO:0007829|PDB:2COW"
SQ SEQUENCE 1826 AA; 202789 MW; 7A336B3C5BDA21E6 CRC64;
MGDSKVKVAV RIRPMNRRET DLHTKCVVDV DANKVILNPV NTNLSKGDAR GQPKVFAYDH
CFWSMDESVK EKYAGQDIVF KCLGENILQN AFDGYNACIF AYGQTGSGKS YTMMGTADQP
GLIPRLCSGL FERTQKEENE EQSFKVEVSY MEIYNEKVRD LLDPKGSRQT LKVREHSVLG
PYVDGLSKLA VTSYKDIESL MSEGNKSRTV AATNMNEESS RSHAVFKITL THTLYDVKSG
TSGEKVGKLS LVDLAGSERA TKTGAAGDRL KEGSNINKSL TTLGLVISAL ADQSAGKNKN
KFVPYRDSVL TWLLKDSLGG NSKTAMVATV SPAADNYDET LSTLRYADRA KHIVNHAVVN
EDPNARIIRD LREEVEKLRE QLTKAEAMKS PELKDRLEES EKLIQEMTVT WEEKLRKTEE
IAQERQKQLE SLGISLQSSG IKVGDDKCFL VNLNADPALN ELLVYYLKEH TLIGSANSQD
IQLCGMGILP EHCIIDITSE GQVMLTPQKN TRTFVNGSSV SSPIQLHHGD RILWGNNHFF
RLNLPKKKKK AEREDEDQDP SMKNENSSEQ LDVDGDSSSE VSSEVNFNYE YAQMEVTMKA
LGSNDPMQSI LNSLEQQHEE EKRSALERQR LMYEHELEQL RRRLSPEKQN CRSMDRFSFH
SPSAQQRLRQ WAEEREATLN NSLMRLREQI VKANLLVREA NYIAEELDKR TEYKVTLQIP
ASSLDANRKR GSLLSEPAIQ VRRKGKGKQI WSLEKLDNRL LDMRDLYQEW KECEEDNPVI
RSYFKRADPF YDEQENHSLI GVANVFLESL FYDVKLQYAV PIINQKGEVA GRLHVEVMRL
SGDVGERIAG GDEVAEVSFE KETQENKLVC MVKILQATGL PQHLSHFVFC KYSFWDQQEP
VIVAPEVDTS SSSVSKEPHC MVVFDHCNEF SVNITEDFIE HLSEGALAIE VYGHKINDPR
KNPALWDLGI IQAKTRSLRD RWSEVTRKLE FWVQILEQNE NGEYCPVEVI SAKDVPTGGI
FQLRQGQSRR VQVEVKSVQE SGTLPLMEEC ILSVGIGCVK VRPLRAPRTH ETFHEEEEDM
DSYQDRDLER LRRKWLNALT KRQEYLDQQL QKLVSKRDKT EDDADREAQL LEMRLTLTEE
RNAVMVPSAG SGIPGAPAEW TPVPGMETHI PVIFLDLNAD DFSSQDNLDD PEAGGWDATL
TGEEEEEFFE LQIVKQHDGE VKAEASWDSA VHGCPQLSRG TPVDERLFLI VRVTVQLSHP
ADMQLVLRKR ICVNVHGRQG FAQSLLKKMS HRSSIPGCGV TFEIVSNIPE DAQGVEEREA
LARMAANVEN PASADSEAYI EKYLRSVLAV ENLLTLDRLR QEVAVKEQLT GKGKLSRRSI
SSPNVNRLSG SRQDLIPSYS LGSNKGRWES QQDVSQTTVS RGIAPAPALS VSPQNNHSPD
PGLSNLAASY LNPVKSFVPQ MPKLLKSLFP VRDEKRGKRP SPLAHQPVPR IMVQSASPDI
RVTRMEEAQP EMGPDVLVQT MGAPALKICD KPAKVPSPPP VIAVTAVTPA PEAQDGPPSP
LSEASSGYFS HSVSTATLSD ALGPGLDAAA PPGSMPTAPE AEPEAPISHP PPPTAVPAEE
PPGPQQLVSP GRERPDLEAP APGSPFRVRR VRASELRSFS RMLAGDPGCS PGAEGNAPAP
GAGGQALASD SEEADEVPEW LREGEFVTVG AHKTGVVRYV GPADFQEGTW VGVELDLPSG
KNDGSIGGKQ YFRCNPGYGL LVRPSRVRRA TGPVRRRSTG LRLGAPEARR SATLSGSATN
LASLTAALAK ADRSHKNPEN RKSWAS
