ID   KI13A_HUMAN             Reviewed;        1805 AA.
AC   Q9H1H9; A0JP21; A0JP22; F2Z382; Q5THQ2; Q5THQ3; Q9H193; Q9H194; Q9H1H8;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=Kinesin-like protein KIF13A;
DE   AltName: Full=Kinesin-like protein RBKIN;
GN   Name=KIF13A; Synonyms=RBKIN;
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] (ISOFORMS 3 AND 4), AND TISSUE SPECIFICITY.
RC   TISSUE=Fetal brain;
RX   PubMed=11374900; DOI=10.1006/geno.2001.6535;
RA   Jamain S., Quach H., Fellous M., Bourgeron T.;
RT   "Identification of the human KIF13A gene homologous to Drosophila kinesin-
RT   73 and candidate for schizophrenia.";
RL   Genomics 74:36-44(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Retina;
RX   PubMed=11861365;
RA   Chen D., Pajovic S., Duckett A., Brown V.D., Squire J.A., Gallie B.L.;
RT   "Genomic amplification in retinoblastoma narrowed to 0.6 megabase on
RT   chromosome 6p containing a kinesin-like gene, RBKIN.";
RL   Cancer Res. 62:967-971(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
RC   TISSUE=Glioblastoma;
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=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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [7]
RP   FUNCTION, INTERACTION WITH AP1G1 AND AP1G2, AND SUBCELLULAR LOCATION.
RX   PubMed=19841138; DOI=10.1083/jcb.200907122;
RA   Delevoye C., Hurbain I., Tenza D., Sibarita J.B., Uzan-Gafsou S., Ohno H.,
RA   Geerts W.J., Verkleij A.J., Salamero J., Marks M.S., Raposo G.;
RT   "AP-1 and KIF13A coordinate endosomal sorting and positioning during
RT   melanosome biogenesis.";
RL   J. Cell Biol. 187:247-264(2009).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ZFYVE26.
RX   PubMed=20208530; DOI=10.1038/ncb2036;
RA   Sagona A.P., Nezis I.P., Pedersen N.M., Liestol K., Poulton J.,
RA   Rusten T.E., Skotheim R.I., Raiborg C., Stenmark H.;
RT   "PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of
RT   FYVE-CENT to the midbody.";
RL   Nat. Cell Biol. 12:362-371(2010).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1287, 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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636; SER-1454; SER-1529;
RP   SER-1572 AND SER-1698, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1494 (ISOFORM 2),
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1481 (ISOFORMS 3 AND 4), AND
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).
CC   -!- FUNCTION: Plus end-directed microtubule-dependent motor protein
CC       involved in intracellular transport and regulating various processes
CC       such as mannose-6-phosphate receptor (M6PR) transport to the plasma
CC       membrane, endosomal sorting during melanosome biogenesis and
CC       cytokinesis. Mediates the transport of M6PR-containing vesicles from
CC       trans-Golgi network to the plasma membrane via direct interaction with
CC       the AP-1 complex. During melanosome maturation, required for delivering
CC       melanogenic enzymes from recycling endosomes to nascent melanosomes by
CC       creating peripheral recycling endosomal subdomains in melanocytes. Also
CC       required for the abcission step in cytokinesis: mediates translocation
CC       of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis.
CC       {ECO:0000269|PubMed:19841138, ECO:0000269|PubMed:20208530}.
CC   -!- SUBUNIT: Interacts with AP2B1 (By similarity). Interacts with ZFYVE26.
CC       Interacts with AP1G1 and AP1G2. {ECO:0000250,
CC       ECO:0000269|PubMed:19841138, ECO:0000269|PubMed:20208530}.
CC   -!- INTERACTION:
CC       Q9H1H9; Q9NQM4: DNAAF6; NbExp=3; IntAct=EBI-1759129, EBI-10239299;
CC       Q9H1H9-2; Q10567-3: AP1B1; NbExp=3; IntAct=EBI-12216695, EBI-11978055;
CC       Q9H1H9-2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-12216695, EBI-25882629;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome. Midbody. Endosome membrane. Golgi apparatus
CC       membrane {ECO:0000250}. Note=Recruited to the midbody during
CC       cytokinesis.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=RBKIN1;
CC         IsoId=Q9H1H9-1; Sequence=Displayed;
CC       Name=2; Synonyms=RBKIN2;
CC         IsoId=Q9H1H9-2; Sequence=VSP_002870;
CC       Name=3;
CC         IsoId=Q9H1H9-3; Sequence=VSP_021724, VSP_002870, VSP_021725,
CC                                  VSP_021726;
CC       Name=4;
CC         IsoId=Q9H1H9-4; Sequence=VSP_021724, VSP_002870;
CC       Name=5;
CC         IsoId=Q9H1H9-5; Sequence=VSP_045584, VSP_045585;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in heart,
CC       brain and skeletal muscle. {ECO:0000269|PubMed:11374900,
CC       ECO:0000269|PubMed:11861365}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at very low level in most fetal tissues,
CC       but at higher levels in skeletal muscle and lung.
CC       {ECO:0000269|PubMed:11861365}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR   EMBL; AJ291578; CAC20442.1; -; mRNA.
DR   EMBL; AJ291579; CAC20443.1; -; mRNA.
DR   EMBL; AY014403; AAG38890.1; -; mRNA.
DR   EMBL; AY014404; AAG38891.1; -; mRNA.
DR   EMBL; AL023807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL138724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC062673; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC127115; AAI27116.1; -; mRNA.
DR   EMBL; BC127116; AAI27117.1; -; mRNA.
DR   CCDS; CCDS47380.1; -. [Q9H1H9-3]
DR   CCDS; CCDS47381.1; -. [Q9H1H9-1]
DR   CCDS; CCDS54967.1; -. [Q9H1H9-4]
DR   CCDS; CCDS54968.1; -. [Q9H1H9-2]
DR   CCDS; CCDS58998.1; -. [Q9H1H9-5]
DR   RefSeq; NP_001099036.1; NM_001105566.2. [Q9H1H9-2]
DR   RefSeq; NP_001099037.1; NM_001105567.2. [Q9H1H9-4]
DR   RefSeq; NP_001099038.1; NM_001105568.2. [Q9H1H9-3]
DR   RefSeq; NP_001230352.1; NM_001243423.1. [Q9H1H9-5]
DR   RefSeq; NP_071396.4; NM_022113.5. [Q9H1H9-1]
DR   AlphaFoldDB; Q9H1H9; -.
DR   SMR; Q9H1H9; -.
DR   BioGRID; 122019; 33.
DR   DIP; DIP-52276N; -.
DR   IntAct; Q9H1H9; 18.
DR   MINT; Q9H1H9; -.
DR   STRING; 9606.ENSP00000259711; -.
DR   GlyGen; Q9H1H9; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9H1H9; -.
DR   PhosphoSitePlus; Q9H1H9; -.
DR   BioMuta; KIF13A; -.
DR   DMDM; 118572662; -.
DR   EPD; Q9H1H9; -.
DR   jPOST; Q9H1H9; -.
DR   MassIVE; Q9H1H9; -.
DR   MaxQB; Q9H1H9; -.
DR   PaxDb; 9606-ENSP00000259711; -.
DR   PeptideAtlas; Q9H1H9; -.
DR   ProteomicsDB; 23911; -.
DR   ProteomicsDB; 80409; -. [Q9H1H9-1]
DR   ProteomicsDB; 80410; -. [Q9H1H9-2]
DR   ProteomicsDB; 80411; -. [Q9H1H9-3]
DR   ProteomicsDB; 80412; -. [Q9H1H9-4]
DR   Pumba; Q9H1H9; -.
DR   Antibodypedia; 25117; 105 antibodies from 19 providers.
DR   DNASU; 63971; -.
DR   Ensembl; ENST00000259711.11; ENSP00000259711.6; ENSG00000137177.20. [Q9H1H9-1]
DR   Ensembl; ENST00000378814.9; ENSP00000368091.5; ENSG00000137177.20. [Q9H1H9-3]
DR   Ensembl; ENST00000378826.6; ENSP00000368103.2; ENSG00000137177.20. [Q9H1H9-2]
DR   Ensembl; ENST00000378843.6; ENSP00000368120.2; ENSG00000137177.20. [Q9H1H9-4]
DR   Ensembl; ENST00000502704.2; ENSP00000425453.1; ENSG00000137177.20. [Q9H1H9-5]
DR   GeneID; 63971; -.
DR   KEGG; hsa:63971; -.
DR   MANE-Select; ENST00000259711.11; ENSP00000259711.6; NM_022113.6; NP_071396.4.
DR   UCSC; uc003ncf.4; human. [Q9H1H9-1]
DR   AGR; HGNC:14566; -.
DR   CTD; 63971; -.
DR   DisGeNET; 63971; -.
DR   GeneCards; KIF13A; -.
DR   HGNC; HGNC:14566; KIF13A.
DR   HPA; ENSG00000137177; Tissue enhanced (skeletal).
DR   MIM; 605433; gene.
DR   neXtProt; NX_Q9H1H9; -.
DR   OpenTargets; ENSG00000137177; -.
DR   PharmGKB; PA30098; -.
DR   VEuPathDB; HostDB:ENSG00000137177; -.
DR   eggNOG; KOG0241; Eukaryota.
DR   GeneTree; ENSGT00940000157508; -.
DR   HOGENOM; CLU_001485_29_2_1; -.
DR   InParanoid; Q9H1H9; -.
DR   OMA; GQENHNL; -.
DR   OrthoDB; 126886at2759; -.
DR   PhylomeDB; Q9H1H9; -.
DR   TreeFam; TF105221; -.
DR   PathwayCommons; Q9H1H9; -.
DR   Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   SignaLink; Q9H1H9; -.
DR   SIGNOR; Q9H1H9; -.
DR   BioGRID-ORCS; 63971; 16 hits in 1164 CRISPR screens.
DR   ChiTaRS; KIF13A; human.
DR   GeneWiki; KIF13A; -.
DR   GenomeRNAi; 63971; -.
DR   Pharos; Q9H1H9; Tbio.
DR   PRO; PR:Q9H1H9; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9H1H9; Protein.
DR   Bgee; ENSG00000137177; Expressed in tendon of biceps brachii and 192 other cell types or tissues.
DR   ExpressionAtlas; Q9H1H9; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR   GO; GO:0032588; C:trans-Golgi network membrane; ISS: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; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR   GO; GO:0008333; P:endosome to lysosome transport; IMP:UniProtKB.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR   GO; GO:0032438; P:melanosome organization; IMP:UniProtKB.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0072383; P:plus-end-directed vesicle transport along microtubule; ISS:UniProtKB.
DR   GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR   GO; GO:0035459; P:vesicle cargo loading; IMP:UniProtKB.
DR   CDD; cd22729; FHA_KIF13A; 1.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   PANTHER; PTHR47117:SF1; STAR-RELATED LIPID TRANSFER PROTEIN 9; 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; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   Genevisible; Q9H1H9; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Endosome; Golgi apparatus; Membrane; Microtubule;
KW   Motor protein; Nucleotide-binding; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..1805
FT                   /note="Kinesin-like protein KIF13A"
FT                   /id="PRO_0000125446"
FT   DOMAIN          5..352
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   DOMAIN          469..519
FT                   /note="FHA"
FT   REGION          556..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1385..1404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1507..1531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1612..1645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1749..1779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          359..436
FT                   /evidence="ECO:0000255"
FT   COILED          602..775
FT                   /evidence="ECO:0000255"
FT   COILED          1100..1138
FT                   /evidence="ECO:0000255"
FT   COILED          1518..1547
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        556..571
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1753..1770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         102..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MOD_RES         636
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1287
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         1454
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1490
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQW7"
FT   MOD_RES         1529
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1572
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1648
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQW7"
FT   MOD_RES         1698
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         50..70
FT                   /note="KPPKVFAFDYCFWSMDESNTT -> LVTVAHISNSSTLGGQGKRIT (in
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045584"
FT   VAR_SEQ         71..1805
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045585"
FT   VAR_SEQ         1071..1083
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11374900,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021724"
FT   VAR_SEQ         1493..1527
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11374900,
FT                   ECO:0000303|PubMed:11861365, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_002870"
FT   VAR_SEQ         1792..1797
FT                   /note="VIIPEA -> GGTTSR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11374900"
FT                   /id="VSP_021725"
FT   VAR_SEQ         1798..1805
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11374900"
FT                   /id="VSP_021726"
FT   VARIANT         1415
FT                   /note="M -> V (in dbSNP:rs17689215)"
FT                   /id="VAR_029389"
FT   VARIANT         1600
FT                   /note="F -> S (in dbSNP:rs12211658)"
FT                   /id="VAR_049699"
FT   CONFLICT        674
FT                   /note="S -> G (in Ref. 2; AAG38890/AAG38891)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        925
FT                   /note="T -> A (in Ref. 2; AAG38890/AAG38891)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1185
FT                   /note="L -> P (in Ref. 2; AAG38890/AAG38891)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1521
FT                   /note="S -> N (in Ref. 2; AAG38890)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q9H1H9-2:1494
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         Q9H1H9-3:1481
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         Q9H1H9-4:1481
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
SQ   SEQUENCE   1805 AA;  202308 MW;  5E5A6C6941DC67CC CRC64;
     MSDTKVKVAV RVRPMNRREL ELNTKCVVEM EGNQTVLHPP PSNTKQGERK PPKVFAFDYC
     FWSMDESNTT KYAGQEVVFK CLGEGILEKA FQGYNACIFA YGQTGSGKSF SMMGHAEQLG
     LIPRLCCALF KRISLEQNES QTFKVEVSYM EIYNEKVRDL LDPKGSRQSL KVREHKVLGP
     YVDGLSQLAV TSFEDIESLM SEGNKSRTVA ATNMNEESSR SHAVFNIIIT QTLYDLQSGN
     SGEKVSKVSL VDLAGSERVS KTGAAGERLK EGSNINKSLT TLGLVISSLA DQAAGKGKSK
     FVPYRDSVLT WLLKDNLGGN SQTSMIATIS PAADNYEETL STLRYADRAK RIVNHAVVNE
     DPNAKVIREL REEVEKLREQ LSQAEAMKAP ELKEKLEESE KLIKELTVTW EEKLRKTEEI
     AQERQRQLES MGISLEMSGI KVGDDKCYLV NLNADPALNE LLVYYLKDHT RVGADTSQDI
     QLFGIGIQPQ HCEIDIASDG DVTLTPKENA RSCVNGTLVC STTQLWHGDR ILWGNNHFFR
     INLPKRKRRD WLKDFEKETG PPEHDLDAAS EASSEPDYNY EFAQMEVIMK TLNSNDPVQN
     VVQVLEKQYL EEKRSALEEQ RLMYERELEQ LRQQLSPDRQ PQSSGPDRLA YSSQTAQQKV
     TQWAEERDEL FRQSLAKLRE QLVKANTLVR EANFLAEEMS KLTDYQVTLQ IPAANLSANR
     KRGAIVSEPA IQVRRKGKST QVWTIEKLEN KLIDMRDLYQ EWKEKVPEAK RLYGKRGDPF
     YEAQENHNLI GVANVFLECL FCDVKLQYAV PIISQQGEVA GRLHVEVMRV TGAVPERVVE
     DDSSENSSES GSLEVVDSSG EIIHRVKKLT CRVKIKEATG LPLNLSNFVF CQYTFWDQCE
     STVAAPVVDP EVPSPQSKDA QYTVTFSHCK DYVVNVTEEF LEFISDGALA IEVWGHRCAG
     NGSSIWEVDS LHAKTRTLHD RWNEVTRRIE MWISILELNE LGEYAAVELH QAKDVNTGGI
     FQLRQGHSRR VQVTVKPVQH SGTLPLMVEA ILSVSIGCVT ARSTKLQRGL DSYQRDDEDG
     DDMDSYQEED LNCVRERWSD ALIKRREYLD EQIKKVSNKT EKTEDDVERE AQLVEQWVGL
     TEERNAVLVP APGSGIPGAP ADWIPPPGME THIPVLFLDL NADDLSANEQ LVGPHASGVN
     SILPKEHGSQ FFYLPIIKHS DDEVSATASW DSSVHDSVHL NRVTPQNERI YLIVKTTVQL
     SHPAAMELVL RKRIAANIYN KQSFTQSLKR RISLKNIFYS CGVTYEIVSN IPKATEEIED
     RETLALLAAR SENEGTSDGE TYIEKYTRGV LQVENILSLE RLRQAVTVKE ALSTKARHIR
     RSLSTPNVHN VSSSRPDLSG FDEDDKGWPE NQLDMSDYSS SYQDVACYGT LPRDSPRRNK
     EGCTSETPHA LTVSPFKAFS PQPPKFFKPL MPVKEEHKKR IALEARPLLS QESMPPPQAH
     NPGCIVPSGS NGSSMPVEHN SKREKKIDSE EEENELEAIN RKLISSQPYV PVEFADFSVY
     NASLENREWF SSKVDLSNSR VLEKEVSRSP TTSSITSGYF SHSASNATLS DMVVPSSDSS
     DQLAIQTKDA DSTEHSTPSL VHDFRPSSNK ELTEVEKGLV KDKIIVVPLK ENSALAKGSP
     SSQSIPEKNS KSLCRTGSCS ELDACPSKIS QPARGFCPRE VTVEHTTNIL EDHSFTEFMG
     VSEGKDFDGL TDSSAGELSS RRSLPNKTGG KTVSDGLHHP SQLHSKLEND QVIIPEAAFW
     VLCCQ
//