DUSTY_HUMAN
ID DUSTY_HUMAN Reviewed; 929 AA.
AC Q6XUX3; B7ZL64; O75060; Q17R94; Q5RKT0; Q6IN87; Q6P997; Q86Y03; Q9P1S5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Dual serine/threonine and tyrosine protein kinase;
DE EC=2.7.12.1;
DE AltName: Full=Dusty protein kinase;
DE Short=Dusty PK;
DE AltName: Full=RIP-homologous kinase;
DE AltName: Full=Receptor-interacting serine/threonine-protein kinase 5;
DE AltName: Full=Sugen kinase 496;
DE Short=SgK496;
GN Name=DSTYK; Synonyms=KIAA0472, RIP5, RIPK5, SGK496; ORFNames=HDCMD38P;
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), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=17123648; DOI=10.1016/j.bbaexp.2006.10.004;
RA Peng J., Dong W., Chen Y., Mo R., Cheng J.-F., Hui C.-C., Mohandas N.,
RA Huang C.-H.;
RT "Dusty protein kinases: primary structure, gene evolution, tissue specific
RT expression and unique features of the catalytic domain.";
RL Biochim. Biophys. Acta 1759:562-572(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Dendritic cell;
RA Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT "A novel gene from human dendritic cell.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Eye, Muscle, Placenta, and Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-929 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-681.
RX PubMed=15178406; DOI=10.1016/j.bbrc.2004.04.194;
RA Zha J., Zhou Q., Xu L.G., Chen D., Li L., Zhai Z., Shu H.B.;
RT "RIP5 is a RIP-homologous inducer of cell death.";
RL Biochem. Biophys. Res. Commun. 319:298-303(2004).
RN [7]
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 [8]
RP IDENTIFICATION BY 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 [9]
RP INVOLVEMENT IN CAKUT1, VARIANTS CAKUT1 GLN-29; GLY-200 AND LEU-843,
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23862974; DOI=10.1056/nejmoa1214479;
RA Sanna-Cherchi S., Sampogna R.V., Papeta N., Burgess K.E., Nees S.N.,
RA Perry B.J., Choi M., Bodria M., Liu Y., Weng P.L., Lozanovski V.J.,
RA Verbitsky M., Lugani F., Sterken R., Paragas N., Caridi G., Carrea A.,
RA Dagnino M., Materna-Kiryluk A., Santamaria G., Murtas C.,
RA Ristoska-Bojkovska N., Izzi C., Kacak N., Bianco B., Giberti S.,
RA Gigante M., Piaggio G., Gesualdo L., Kosuljandic Vukic D., Vukojevic K.,
RA Saraga-Babic M., Saraga M., Gucev Z., Allegri L., Latos-Bielenska A.,
RA Casu D., State M., Scolari F., Ravazzolo R., Kiryluk K., Al-Awqati Q.,
RA D'Agati V.D., Drummond I.A., Tasic V., Lifton R.P., Ghiggeri G.M.,
RA Gharavi A.G.;
RT "Mutations in DSTYK and dominant urinary tract malformations.";
RL N. Engl. J. Med. 369:621-629(2013).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN SPG23.
RX PubMed=28157540; DOI=10.1016/j.ajhg.2017.01.014;
RA Lee J.Y., Hsu C.K., Michael M., Nanda A., Liu L., McMillan J.R.,
RA Pourreyron C., Takeichi T., Tolar J., Reid E., Hayday T., Blumen S.C.,
RA Abu-Mouch S., Straussberg R., Basel-Vanagaite L., Barhum Y., Zouabi Y.,
RA Al-Ajmi H., Huang H.Y., Lin T.C., Akiyama M., Lee J.Y., McLean W.H.,
RA Simpson M.A., Parsons M., McGrath J.A.;
RT "Large intragenic deletion in DSTYK underlies autosomal-recessive
RT complicated spastic paraparesis, SPG23.";
RL Am. J. Hum. Genet. 100:364-370(2017).
CC -!- FUNCTION: Acts as a positive regulator of ERK phosphorylation
CC downstream of fibroblast growth factor-receptor activation
CC (PubMed:23862974, PubMed:28157540). Involved in the regulation of both
CC caspase-dependent apoptosis and caspase-independent cell death
CC (PubMed:15178406). In the skin, it plays a predominant role in
CC suppressing caspase-dependent apoptosis in response to UV stress in a
CC range of dermal cell types (PubMed:28157540).
CC {ECO:0000269|PubMed:15178406, ECO:0000269|PubMed:23862974,
CC ECO:0000269|PubMed:28157540}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17123648,
CC ECO:0000269|PubMed:23862974}. Cell membrane
CC {ECO:0000250|UniProtKB:Q6XUX1}. Apical cell membrane
CC {ECO:0000269|PubMed:23862974}. Basolateral cell membrane
CC {ECO:0000269|PubMed:23862974}. Cell junction
CC {ECO:0000250|UniProtKB:Q6XUX1}. Note=Detected at apical cell-cell
CC junctions. Colocalized with FGF receptors to the cell membrane (By
CC similarity). Detected in basolateral and apical membranes of all
CC tubular epithelia. {ECO:0000250|UniProtKB:Q6XUX1,
CC ECO:0000269|PubMed:23862974}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6XUX3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6XUX3-2; Sequence=VSP_018034;
CC Name=3;
CC IsoId=Q6XUX3-3; Sequence=VSP_018031;
CC Name=4;
CC IsoId=Q6XUX3-4; Sequence=VSP_018030, VSP_018032, VSP_018033;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and
CC testis. Expressed in basolateral and apical membranes of all tubular
CC epithelia. Expressed in thin ascending limb of the loop of Henle and
CC the distal convoluted tubule. Expressed in all layers of transitional
CC ureteric epithelium and in the ureteric smooth-muscle cells. Weakly
CC expressed in heart, brain, placenta, kidney, pancreas, spleen, thymus,
CC prostate, uterus, small intestine, white blood cells, stomach, spinal
CC cord and adrenal gland. Is widely distributed in the CNS. Also detected
CC in several tumor cell lines. Expressed in the skin (PubMed:28157540).
CC {ECO:0000269|PubMed:15178406, ECO:0000269|PubMed:17123648,
CC ECO:0000269|PubMed:23862974, ECO:0000269|PubMed:28157540}.
CC -!- DISEASE: Congenital anomalies of the kidney and urinary tract 1
CC (CAKUT1) [MIM:610805]: A disorder encompassing a broad spectrum of
CC renal and urinary tract malformations that include renal agenesis,
CC kidney hypodysplasia, multicystic kidney dysplasia, duplex collecting
CC system, posterior urethral valves and ureter abnormalities. Congenital
CC anomalies of kidney and urinary tract are the commonest cause of
CC chronic kidney disease in children. {ECO:0000269|PubMed:23862974}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- DISEASE: Spastic paraplegia 23, autosomal recessive (SPG23)
CC [MIM:270750]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body. SPG23 is an autosomal
CC recessive form characterized by childhood-onset of gait difficulties
CC and pigmentary abnormalities, including premature graying of the hair
CC and vitiligo-like or hyperpigmented skin lesions.
CC {ECO:0000269|PubMed:28157540}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AY208850; AAP42418.1; -; mRNA.
DR EMBL; AY429674; AAS55390.1; -; mRNA.
DR EMBL; AF068286; AAF65505.1; -; mRNA.
DR EMBL; AC093422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048204; AAH48204.1; -; mRNA.
DR EMBL; BC053627; AAH53627.1; -; mRNA.
DR EMBL; BC060870; AAH60870.2; -; mRNA.
DR EMBL; BC072406; AAH72406.1; -; mRNA.
DR EMBL; BC117411; AAI17412.1; -; mRNA.
DR EMBL; BC143603; AAI43604.1; -; mRNA.
DR EMBL; AB007941; BAA32317.1; -; mRNA.
DR CCDS; CCDS1451.1; -. [Q6XUX3-1]
DR CCDS; CCDS1452.1; -. [Q6XUX3-2]
DR RefSeq; NP_056190.1; NM_015375.2. [Q6XUX3-1]
DR RefSeq; NP_955749.1; NM_199462.2. [Q6XUX3-2]
DR AlphaFoldDB; Q6XUX3; -.
DR SMR; Q6XUX3; -.
DR BioGRID; 117313; 66.
DR IntAct; Q6XUX3; 23.
DR STRING; 9606.ENSP00000356130; -.
DR BindingDB; Q6XUX3; -.
DR ChEMBL; CHEMBL1908386; -.
DR DrugCentral; Q6XUX3; -.
DR GlyGen; Q6XUX3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6XUX3; -.
DR PhosphoSitePlus; Q6XUX3; -.
DR BioMuta; DSTYK; -.
DR DMDM; 296434486; -.
DR EPD; Q6XUX3; -.
DR jPOST; Q6XUX3; -.
DR MassIVE; Q6XUX3; -.
DR MaxQB; Q6XUX3; -.
DR PaxDb; Q6XUX3; -.
DR PeptideAtlas; Q6XUX3; -.
DR PRIDE; Q6XUX3; -.
DR ProteomicsDB; 67816; -. [Q6XUX3-1]
DR ProteomicsDB; 67817; -. [Q6XUX3-2]
DR ProteomicsDB; 67818; -. [Q6XUX3-3]
DR ProteomicsDB; 67819; -. [Q6XUX3-4]
DR Antibodypedia; 34564; 186 antibodies from 26 providers.
DR DNASU; 25778; -.
DR Ensembl; ENST00000367161.7; ENSP00000356129.3; ENSG00000133059.17. [Q6XUX3-2]
DR Ensembl; ENST00000367162.8; ENSP00000356130.3; ENSG00000133059.17. [Q6XUX3-1]
DR Ensembl; ENST00000615388.1; ENSP00000478016.1; ENSG00000133059.17. [Q6XUX3-4]
DR GeneID; 25778; -.
DR KEGG; hsa:25778; -.
DR MANE-Select; ENST00000367162.8; ENSP00000356130.3; NM_015375.3; NP_056190.1.
DR UCSC; uc001hbw.4; human. [Q6XUX3-1]
DR CTD; 25778; -.
DR DisGeNET; 25778; -.
DR GeneCards; DSTYK; -.
DR HGNC; HGNC:29043; DSTYK.
DR HPA; ENSG00000133059; Low tissue specificity.
DR MalaCards; DSTYK; -.
DR MIM; 270750; phenotype.
DR MIM; 610805; phenotype.
DR MIM; 612666; gene.
DR neXtProt; NX_Q6XUX3; -.
DR OpenTargets; ENSG00000133059; -.
DR Orphanet; 101003; Autosomal recessive spastic paraplegia type 23.
DR Orphanet; 93100; Renal agenesis, unilateral.
DR PharmGKB; PA164718861; -.
DR VEuPathDB; HostDB:ENSG00000133059; -.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00840000129948; -.
DR HOGENOM; CLU_014116_0_0_1; -.
DR InParanoid; Q6XUX3; -.
DR OMA; KSCIHLI; -.
DR OrthoDB; 254886at2759; -.
DR PhylomeDB; Q6XUX3; -.
DR TreeFam; TF331821; -.
DR PathwayCommons; Q6XUX3; -.
DR SignaLink; Q6XUX3; -.
DR BioGRID-ORCS; 25778; 24 hits in 1115 CRISPR screens.
DR ChiTaRS; DSTYK; human.
DR GeneWiki; RIPK5; -.
DR GenomeRNAi; 25778; -.
DR Pharos; Q6XUX3; Tchem.
DR PRO; PR:Q6XUX3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6XUX3; protein.
DR Bgee; ENSG00000133059; Expressed in lateral nuclear group of thalamus and 213 other tissues.
DR Genevisible; Q6XUX3; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell junction; Cell membrane;
KW Coiled coil; Cytoplasm; Disease variant; Hereditary spastic paraplegia;
KW Kinase; Membrane; Neurodegeneration; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..929
FT /note="Dual serine/threonine and tyrosine protein kinase"
FT /id="PRO_0000233118"
FT DOMAIN 652..906
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 189..215
FT /evidence="ECO:0000255"
FT COILED 395..431
FT /evidence="ECO:0000255"
FT ACT_SITE 777
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 658..666
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 681
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..539
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_018030"
FT VAR_SEQ 451..792
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018031"
FT VAR_SEQ 703..718
FT /note="SLPKHERLVDLHGSVI -> WVLASFISMRKIQRRI (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_018032"
FT VAR_SEQ 719..929
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_018033"
FT VAR_SEQ 824..868
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018034"
FT VARIANT 29
FT /note="R -> Q (in CAKUT1; unknown pathological
FT significance; dbSNP:rs200780796)"
FT /evidence="ECO:0000269|PubMed:23862974"
FT /id="VAR_071324"
FT VARIANT 200
FT /note="D -> G (in CAKUT1)"
FT /evidence="ECO:0000269|PubMed:23862974"
FT /id="VAR_071325"
FT VARIANT 432
FT /note="L -> V (in dbSNP:rs35845538)"
FT /id="VAR_057101"
FT VARIANT 843
FT /note="S -> L (in CAKUT1; dbSNP:rs778586547)"
FT /evidence="ECO:0000269|PubMed:23862974"
FT /id="VAR_071326"
FT MUTAGEN 681
FT /note="K->Q: No change."
FT /evidence="ECO:0000269|PubMed:15178406"
FT CONFLICT 247
FT /note="V -> A (in Ref. 4; AAH72406)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="G -> R (in Ref. 4; AAH60870)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="C -> R (in Ref. 1; AAP42418/AAS55390, 2; AAF65505,
FT 4; AAH53627/AAH72406/AAI17412/AAI43604 and 5; BAA32317)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 929 AA; 105206 MW; 8DDAAC289DE21EE7 CRC64;
MEGDGVPWGS EPVSGPGPGG GGMIRELCRG FGRYRRYLGR LRQNLRETQK FFRDIKCSHN
HTCLSSLTGG GGAERGPAGD VAETGLQAGQ LSCISFPPKE EKYLQQIVDC LPCILILGQD
CNVKCQLLNL LLGVQVLPTT KLGSEESCKL RRLRFTYGTQ TRVSLALPGQ YELVHTLVAH
QGNWETIPEE DLEVQENNED AAHVLAELEV TMHHALLQEV DVVVAPCQGL RPTVDVLGDL
VNDFLPVITY ALHKDELSER DEQELQEIRK YFSFPVFFFK VPKLGSEIID SSTRRMESER
SPLYRQLIDL GYLSSSHWNC GAPGQDTKAQ SMLVEQSEKL RHLSTFSHQV LQTRLVDAAK
ALNLVHCHCL DIFINQAFDM QRDLQITPKR LEYTRKKENE LYESLMNIAN RKQEEMKDMI
VETLNTMKEE LLDDATNMEF KDVIVPENGE PVGTREIKCC IRQIQELIIS RLNQAVANKL
ISSVDYLRES FVGTLERCLQ SLEKSQDVSV HITSNYLKQI LNAAYHVEVT FHSGSSVTRM
LWEQIKQIIQ RITWVSPPAI TLEWKRKVAQ EAIESLSASK LAKSICSQFR TRLNSSHEAF
AASLRQLEAG HSGRLEKTED LWLRVRKDHA PRLARLSLES CSLQDVLLHR KPKLGQELGR
GQYGVVYLCD NWGGHFPCAL KSVVPPDEKH WNDLALEFHY MRSLPKHERL VDLHGSVIDY
NYGGGSSIAV LLIMERLHRD LYTGLKAGLT LETRLQIALD VVEGIRFLHS QGLVHRDIKL
KNVLLDKQNR AKITDLGFCK PEAMMSGSIV GTPIHMAPEL FTGKYDNSVD VYAFGILFWY
ICSGSVKLPE AFERCASKDH LWNNVRRGAR PERLPVFDEE CWQLMEACWD GDPLKRPLLG
IVQPMLQGIM NRLCKSNSEQ PNRGLDDST
