KI13A_HUMAN
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 03-AUG-2022, entry version 173.
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; 28.
DR DIP; DIP-52276N; -.
DR IntAct; Q9H1H9; 14.
DR MINT; Q9H1H9; -.
DR STRING; 9606.ENSP00000259711; -.
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; Q9H1H9; -.
DR PeptideAtlas; Q9H1H9; -.
DR PRIDE; 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 Antibodypedia; 25117; 80 antibodies from 18 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 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; FIEHCAE; -.
DR OrthoDB; 76316at2759; -.
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 1086 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 190 other tissues.
DR ExpressionAtlas; Q9H1H9; baseline and differential.
DR Genevisible; Q9H1H9; HS.
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: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; cd00060; FHA; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR032923; KIF13A.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR027640; Kinesin-like_fam.
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; PTHR24115; PTHR24115; 1.
DR PANTHER; PTHR24115:SF458; PTHR24115:SF458; 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; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
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
