PXK_HUMAN
ID PXK_HUMAN Reviewed; 578 AA.
AC Q7Z7A4; Q3BCH4; Q3BCH5; Q3BCH6; Q3BDW1; Q45L83; Q59EX3; Q6PK17; Q6ZN39;
AC Q96CA3; Q96R07; Q9NXB8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=PX domain-containing protein kinase-like protein;
DE AltName: Full=Modulator of Na,K-ATPase;
DE Short=MONaKA;
GN Name=PXK {ECO:0000312|HGNC:HGNC:23326};
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] {ECO:0000305, ECO:0000312|EMBL:AAZ38821.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain {ECO:0000269|PubMed:16135750};
RX PubMed=16135750; DOI=10.1523/jneurosci.0635-05.2005;
RA Mao H., Ferguson T.S., Cibulsky S.M., Holmqvist M., Ding C., Fei H.,
RA Levitan I.B.;
RT "MONaKA, a novel modulator of the plasma membrane Na,K-ATPase.";
RL J. Neurosci. 25:7934-7943(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAR98521.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 5; 6 AND 7), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-54; TYR-56 AND ARG-92, AND VARIANT
RP ARG-481.
RC TISSUE=Fetal brain {ECO:0000269|PubMed:16142408};
RX PubMed=16142408;
RA Zou X., Qiu G., Chen C., Wu M., Hu Y., Zheng H., Li X., Gu S., Ji C.,
RA Mao Y.;
RT "Expression pattern and subcellular localization of five splice isoforms of
RT human PXK.";
RL Int. J. Mol. Med. 16:701-707(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAK94455.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Hong W.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAK94455.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Shan Y.X., Yu L.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAK94455.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain {ECO:0000312|EMBL:BAD92925.1};
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305, ECO:0000312|EMBL:BAD18536.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Caudate nucleus {ECO:0000312|EMBL:BAD18536.1}, and
RC Hepatoma {ECO:0000312|EMBL:BAA91097.1};
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 [7] {ECO:0000305, ECO:0000312|EMBL:AAH14479.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-461 (ISOFORMS 1/2).
RC TISSUE=B-cell {ECO:0000312|EMBL:AAH14479.1}, and
RC Kidney {ECO:0000312|EMBL:AAH08943.1};
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 [8]
RP IDENTIFICATION BY 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-426 AND ARG-481.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Binds to and modulates brain Na,K-ATPase subunits ATP1B1 and
CC ATP1B3 and may thereby participate in the regulation of electrical
CC excitability and synaptic transmission. May not display kinase
CC activity. {ECO:0000250|UniProtKB:Q8BX57, ECO:0000303|PubMed:16142408}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16142408}. Cell
CC membrane {ECO:0000269|PubMed:16142408}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16142408}. Note=Also associates with the plasma
CC membrane. Isoform 3 is present throughout the cell.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1 {ECO:0000269|PubMed:16135750}; Synonyms=Long
CC {ECO:0000303|PubMed:16135750}, v1 {ECO:0000303|PubMed:16142408};
CC IsoId=Q7Z7A4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16135750}; Synonyms=Short
CC {ECO:0000303|PubMed:16135750};
CC IsoId=Q7Z7A4-2; Sequence=VSP_051912, VSP_051913;
CC Name=3 {ECO:0000269|PubMed:16142408}; Synonyms=v3
CC {ECO:0000303|PubMed:16142408};
CC IsoId=Q7Z7A4-3; Sequence=VSP_051907;
CC Name=4 {ECO:0000305};
CC IsoId=Q7Z7A4-4; Sequence=VSP_051911;
CC Name=5 {ECO:0000269|PubMed:16142408}; Synonyms=v4
CC {ECO:0000303|PubMed:16142408};
CC IsoId=Q7Z7A4-5; Sequence=VSP_051908;
CC Name=6 {ECO:0000269|PubMed:16142408}; Synonyms=v2
CC {ECO:0000303|PubMed:16142408};
CC IsoId=Q7Z7A4-6; Sequence=VSP_051910;
CC Name=7 {ECO:0000269|PubMed:16142408}; Synonyms=v5
CC {ECO:0000303|PubMed:16142408};
CC IsoId=Q7Z7A4-7; Sequence=VSP_051909;
CC -!- TISSUE SPECIFICITY: Widely expressed in all tissues examined except in
CC heart. Isoform 1 is expressed in high levels in the brain, skeletal
CC muscle, spleen and testis. Isoform 7 expression has yet to be
CC demonstrated. {ECO:0000269|PubMed:16142408}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14479.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91097.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD18536.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD92925.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ124707; AAZ38821.1; -; mRNA.
DR EMBL; DQ124708; AAZ38822.1; -; mRNA.
DR EMBL; AY437879; AAR98521.1; -; mRNA.
DR EMBL; AY847222; AAX73354.1; -; mRNA.
DR EMBL; AY847220; AAX73352.1; -; mRNA.
DR EMBL; AY847221; AAX73353.1; -; mRNA.
DR EMBL; AF399753; AAK94455.1; -; mRNA.
DR EMBL; AY274811; AAP42076.1; -; mRNA.
DR EMBL; AB209688; BAD92925.1; ALT_FRAME; mRNA.
DR EMBL; AK000342; BAA91097.1; ALT_FRAME; mRNA.
DR EMBL; AK131385; BAD18536.1; ALT_FRAME; mRNA.
DR EMBL; BC008943; AAH08943.1; -; mRNA.
DR EMBL; BC014479; AAH14479.1; ALT_SEQ; mRNA.
DR CCDS; CCDS2889.1; -. [Q7Z7A4-1]
DR CCDS; CCDS74952.1; -. [Q7Z7A4-2]
DR RefSeq; NP_001276024.1; NM_001289095.1.
DR RefSeq; NP_001276025.1; NM_001289096.1. [Q7Z7A4-6]
DR RefSeq; NP_001276027.1; NM_001289098.1. [Q7Z7A4-2]
DR RefSeq; NP_001276028.1; NM_001289099.1. [Q7Z7A4-7]
DR RefSeq; NP_001276029.1; NM_001289100.1.
DR RefSeq; NP_001276030.1; NM_001289101.1. [Q7Z7A4-5]
DR RefSeq; NP_060241.2; NM_017771.4. [Q7Z7A4-1]
DR RefSeq; XP_016862160.1; XM_017006671.1.
DR RefSeq; XP_016862164.1; XM_017006675.1.
DR RefSeq; XP_016862175.1; XM_017006686.1.
DR AlphaFoldDB; Q7Z7A4; -.
DR SMR; Q7Z7A4; -.
DR BioGRID; 120245; 31.
DR IntAct; Q7Z7A4; 16.
DR STRING; 9606.ENSP00000348472; -.
DR GlyGen; Q7Z7A4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z7A4; -.
DR PhosphoSitePlus; Q7Z7A4; -.
DR BioMuta; PXK; -.
DR DMDM; 74759261; -.
DR EPD; Q7Z7A4; -.
DR jPOST; Q7Z7A4; -.
DR MassIVE; Q7Z7A4; -.
DR MaxQB; Q7Z7A4; -.
DR PaxDb; Q7Z7A4; -.
DR PeptideAtlas; Q7Z7A4; -.
DR PRIDE; Q7Z7A4; -.
DR ProteomicsDB; 69499; -. [Q7Z7A4-1]
DR ProteomicsDB; 69500; -. [Q7Z7A4-2]
DR ProteomicsDB; 69501; -. [Q7Z7A4-3]
DR ProteomicsDB; 69502; -. [Q7Z7A4-4]
DR ProteomicsDB; 69503; -. [Q7Z7A4-5]
DR ProteomicsDB; 69504; -. [Q7Z7A4-6]
DR ProteomicsDB; 69505; -. [Q7Z7A4-7]
DR Antibodypedia; 15176; 175 antibodies from 26 providers.
DR DNASU; 54899; -.
DR Ensembl; ENST00000356151.7; ENSP00000348472.2; ENSG00000168297.16. [Q7Z7A4-1]
DR Ensembl; ENST00000383716.7; ENSP00000373222.4; ENSG00000168297.16. [Q7Z7A4-2]
DR Ensembl; ENST00000484288.5; ENSP00000417915.1; ENSG00000168297.16. [Q7Z7A4-2]
DR GeneID; 54899; -.
DR KEGG; hsa:54899; -.
DR MANE-Select; ENST00000356151.7; ENSP00000348472.2; NM_017771.5; NP_060241.2.
DR UCSC; uc003djx.2; human. [Q7Z7A4-1]
DR CTD; 54899; -.
DR DisGeNET; 54899; -.
DR GeneCards; PXK; -.
DR HGNC; HGNC:23326; PXK.
DR HPA; ENSG00000168297; Tissue enriched (brain).
DR MalaCards; PXK; -.
DR MIM; 611450; gene.
DR neXtProt; NX_Q7Z7A4; -.
DR OpenTargets; ENSG00000168297; -.
DR Orphanet; 536; Systemic lupus erythematosus.
DR PharmGKB; PA134899496; -.
DR VEuPathDB; HostDB:ENSG00000168297; -.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00390000017669; -.
DR HOGENOM; CLU_036868_0_0_1; -.
DR InParanoid; Q7Z7A4; -.
DR OMA; NKDYWTV; -.
DR OrthoDB; 995721at2759; -.
DR PhylomeDB; Q7Z7A4; -.
DR TreeFam; TF324116; -.
DR PathwayCommons; Q7Z7A4; -.
DR SignaLink; Q7Z7A4; -.
DR BioGRID-ORCS; 54899; 11 hits in 1089 CRISPR screens.
DR ChiTaRS; PXK; human.
DR GenomeRNAi; 54899; -.
DR Pharos; Q7Z7A4; Tbio.
DR PRO; PR:Q7Z7A4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q7Z7A4; protein.
DR Bgee; ENSG00000168297; Expressed in corpus callosum and 178 other tissues.
DR ExpressionAtlas; Q7Z7A4; baseline and differential.
DR Genevisible; Q7Z7A4; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; NAS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; ISS:UniProtKB.
DR GO; GO:0043271; P:negative regulation of ion transport; ISS:UniProtKB.
DR CDD; cd06871; PX_MONaKA; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037903; MONaKA_PX.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR003124; WH2_dom.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Reference proteome.
FT CHAIN 1..578
FT /note="PX domain-containing protein kinase-like protein"
FT /id="PRO_0000086592"
FT DOMAIN 14..126
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 88..481
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 548..567
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 437..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..226
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16142408"
FT /id="VSP_051907"
FT VAR_SEQ 1..137
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16142408"
FT /id="VSP_051908"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16142408"
FT /id="VSP_051909"
FT VAR_SEQ 35..67
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16142408"
FT /id="VSP_051910"
FT VAR_SEQ 35..51
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_051911"
FT VAR_SEQ 510..515
FT /note="GISALP -> VEHAPF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16135750, ECO:0000303|Ref.3,
FT ECO:0000303|Ref.5"
FT /id="VSP_051912"
FT VAR_SEQ 516..578
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16135750, ECO:0000303|Ref.3,
FT ECO:0000303|Ref.5"
FT /id="VSP_051913"
FT VARIANT 426
FT /note="I -> V (in dbSNP:rs55973253)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041362"
FT VARIANT 481
FT /note="K -> R (in dbSNP:rs56384862)"
FT /evidence="ECO:0000269|PubMed:16142408,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_041363"
FT VARIANT 525
FT /note="A -> V (in dbSNP:rs34579268)"
FT /id="VAR_033911"
FT VARIANT 535
FT /note="A -> V (in dbSNP:rs34579268)"
FT /id="VAR_033912"
FT MUTAGEN 54
FT /note="R->Q: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:16142408"
FT MUTAGEN 56
FT /note="Y->A: Results in redistribution of protein from
FT cytoplasm throughout entire cell."
FT /evidence="ECO:0000269|PubMed:16142408"
FT MUTAGEN 92
FT /note="R->L: Results in redistribution of protein from
FT cytoplasm throughout entire cell."
FT /evidence="ECO:0000269|PubMed:16142408"
FT CONFLICT 42
FT /note="R -> G (in Ref. 3; AAK94455 and 6; BAA91097)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="R -> K (in Ref. 2; AAR98521)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="Missing (in Ref. 6; BAD18536)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 64950 MW; 73523CFC3731FFC8 CRC64;
MAFMEKPPAG KVLLDDTVPL TAAIEASQSL QSHTEYIIRV QRGISVENSW QIVRRYSDFD
LLNNSLQIAG LSLPLPPKKL IGNMDREFIA ERQKGLQNYL NVITTNHILS NCELVKKFLD
PNNYSANYTE IALQQVSMFF RSEPKWEVVE PLKDIGWRIR KKYFLMKIKN QPKERLVLSW
ADLGPDKYLS DKDFQCLIKL LPSCLHPYIY RVTFATANES SALLIRMFNE KGTLKDLIYK
AKPKDPFLKK YCNPKKIQGL ELQQIKTYGR QILEVLKFLH DKGFPYGHLH ASNVMLDGDT
CRLLDLENSL LGLPSFYRSY FSQFRKINTL ESVDVHCFGH LLYEMTYGRP PDSVPVDSFP
PAPSMAVVAV LESTLSCEAC KNGMPTISRL LQMPLFSDVL LTTSEKPQFK IPTKLKEALR
IAKECIEKRL IEEQKQIHQH RRLTRAQSHH GSEEERKKRK ILARKKSKRS ALENSEEHSA
KYSNSNNSAG SGASSPLTSP SSPTPPSTSG ISALPPPPPP PPPPAAPLPP ASTEAPAQLS
SQAVNGMSRG ALLSSIQNFQ KGTLRKAKTC DHSAPKIG
