S39A7_HUMAN
ID S39A7_HUMAN Reviewed; 469 AA.
AC Q92504; B0UXF6; Q5STP8; Q9UIQ0;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Zinc transporter SLC39A7;
DE AltName: Full=Histidine-rich membrane protein Ke4 {ECO:0000303|PubMed:14525538};
DE AltName: Full=Really interesting new gene 5 protein;
DE AltName: Full=Solute carrier family 39 member 7;
DE AltName: Full=Zrt-, Irt-like protein 7 {ECO:0000303|PubMed:15705588};
DE Short=ZIP7 {ECO:0000303|PubMed:15705588};
GN Name=SLC39A7; Synonyms=HKE4 {ECO:0000303|PubMed:14525538}, RING5;
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], AND VARIANT GLY-280.
RC TISSUE=Kidney;
RX PubMed=8812499; DOI=10.1006/geno.1996.0405;
RA Ando A., Kikuti Y.Y., Shigenari A., Kawata H., Okamoto N., Shiina T.,
RA Chen L., Ikemura T., Abe K., Kimura M., Inoko H.;
RT "cDNA cloning of the human homologues of the mouse Ke4 and Ke6 genes at the
RT centromeric end of the human MHC region.";
RL Genomics 35:600-602(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-280.
RA Vergara A., Lana I., Corella A., de Miguel C., Migliaccio M., Encio I.;
RT "Molecular cloning and characterization of the human KE4 gene and 5'
RT flanking region.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14525538; DOI=10.1042/bj20031183;
RA Taylor K.M., Morgan H.E., Johnson A., Nicholson R.I.;
RT "Structure-function analysis of HKE4, a member of the new LIV-1 subfamily
RT of zinc transporters.";
RL Biochem. J. 377:131-139(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15705588; DOI=10.1074/jbc.m412188200;
RA Huang L., Kirschke C.P., Zhang Y., Yu Y.Y.;
RT "The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc
RT homeostasis of the Golgi apparatus.";
RL J. Biol. Chem. 280:15456-15463(2005).
RN [8]
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-276, AND
RP IDENTIFICATION BY 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 FUNCTION, PHOSPHORYLATION AT SER-275 AND SER-276, AND MUTAGENESIS OF
RP SER-275 AND SER-276.
RX PubMed=22317921; DOI=10.1126/scisignal.2002585;
RA Taylor K.M., Hiscox S., Nicholson R.I., Hogstrand C., Kille P.;
RT "Protein kinase CK2 triggers cytosolic zinc signaling pathways by
RT phosphorylation of zinc channel ZIP7.";
RL Sci. Signal. 5:RA11-RA11(2012).
RN [11]
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).
RN [12]
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 [13]
RP METHYLATION.
RX PubMed=33563959; DOI=10.1038/s41467-020-20670-7;
RA Davydova E., Shimazu T., Schuhmacher M.K., Jakobsson M.E.,
RA Willemen H.L.D.M., Liu T., Moen A., Ho A.Y.Y., Malecki J., Schroer L.,
RA Pinto R., Suzuki T., Groensberg I.A., Sohtome Y., Akakabe M., Weirich S.,
RA Kikuchi M., Olsen J.V., Dohmae N., Umehara T., Sodeoka M., Siino V.,
RA McDonough M.A., Eijkelkamp N., Schofield C.J., Jeltsch A., Shinkai Y.,
RA Falnes P.O.;
RT "The methyltransferase METTL9 mediates pervasive 1-methylhistidine
RT modification in mammalian proteomes.";
RL Nat. Commun. 12:891-891(2021).
CC -!- FUNCTION: Zinc transporter, that transports Zn(2+) from the endoplasmic
CC reticulum/Golgi apparatus to the cytosol. Transport is stimulated by
CC growth factors, such as EGF, and Ca(2+), as well as by exogenous
CC Zn(2+). {ECO:0000269|PubMed:14525538, ECO:0000269|PubMed:15705588,
CC ECO:0000269|PubMed:22317921}.
CC -!- INTERACTION:
CC Q92504; Q13520: AQP6; NbExp=3; IntAct=EBI-1051105, EBI-13059134;
CC Q92504; Q13323: BIK; NbExp=3; IntAct=EBI-1051105, EBI-700794;
CC Q92504; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-1051105, EBI-713677;
CC Q92504; P68400: CSNK2A1; NbExp=4; IntAct=EBI-1051105, EBI-347804;
CC Q92504; P48165: GJA8; NbExp=3; IntAct=EBI-1051105, EBI-17458373;
CC Q92504; Q9H3M0: KCNF1; NbExp=3; IntAct=EBI-1051105, EBI-6918743;
CC Q92504; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-1051105, EBI-11749135;
CC Q92504; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-1051105, EBI-11987425;
CC Q92504; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-1051105, EBI-1044640;
CC Q92504; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-1051105, EBI-11962058;
CC Q92504; Q5T751: LCE1C; NbExp=3; IntAct=EBI-1051105, EBI-12224199;
CC Q92504; Q5T754: LCE1F; NbExp=3; IntAct=EBI-1051105, EBI-11958008;
CC Q92504; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-1051105, EBI-11973993;
CC Q92504; Q5TA82: LCE2D; NbExp=3; IntAct=EBI-1051105, EBI-10246750;
CC Q92504; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-1051105, EBI-10246358;
CC Q92504; Q5TCM9: LCE5A; NbExp=3; IntAct=EBI-1051105, EBI-11955689;
CC Q92504; Q5T871: LELP1; NbExp=3; IntAct=EBI-1051105, EBI-18115868;
CC Q92504; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-1051105, EBI-3918154;
CC Q92504; Q6UXX9-2: RSPO2; NbExp=3; IntAct=EBI-1051105, EBI-12009390;
CC Q92504; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-1051105, EBI-18037857;
CC Q92504; O95436-2: SLC34A2; NbExp=3; IntAct=EBI-1051105, EBI-12811757;
CC Q92504; P49901: SMCP; NbExp=3; IntAct=EBI-1051105, EBI-750494;
CC Q92504; O43610: SPRY3; NbExp=3; IntAct=EBI-1051105, EBI-12290641;
CC Q92504; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-1051105, EBI-8638294;
CC Q92504; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-1051105, EBI-1044859;
CC Q92504; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-1051105, EBI-13356252;
CC Q92504; Q8WWY7: WFDC12; NbExp=3; IntAct=EBI-1051105, EBI-11958577;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14525538}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:15705588}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14525538,
CC ECO:0000269|PubMed:15705588}.
CC -!- INDUCTION: Down-regulated by Zn(+2). {ECO:0000269|PubMed:15705588}.
CC -!- PTM: Rapidly phosphorylated by CK2 following Zn(2+) treatment. This
CC phosphorylation is required for efficient cytosolic Zn(2+) release.
CC {ECO:0000269|PubMed:22317921}.
CC -!- PTM: Methylation at some His residue by METTL9 leads to reduced zinc-
CC binding. {ECO:0000269|PubMed:33563959}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC KE4/Catsup subfamily. {ECO:0000305}.
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DR EMBL; D82060; BAA11528.1; -; mRNA.
DR EMBL; AF117221; AAD12305.1; -; Genomic_DNA.
DR EMBL; AL031228; CAA20238.1; -; Genomic_DNA.
DR EMBL; AL645940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR936877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR354565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03680.1; -; Genomic_DNA.
DR EMBL; BC000645; AAH00645.1; -; mRNA.
DR CCDS; CCDS43453.1; -.
DR RefSeq; NP_001070984.1; NM_001077516.1.
DR RefSeq; NP_001275706.1; NM_001288777.1.
DR RefSeq; NP_008910.2; NM_006979.2.
DR AlphaFoldDB; Q92504; -.
DR SMR; Q92504; -.
DR BioGRID; 113652; 183.
DR IntAct; Q92504; 56.
DR MINT; Q92504; -.
DR STRING; 9606.ENSP00000363809; -.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR TCDB; 2.A.5.4.3; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR iPTMnet; Q92504; -.
DR PhosphoSitePlus; Q92504; -.
DR SwissPalm; Q92504; -.
DR BioMuta; SLC39A7; -.
DR DMDM; 12643344; -.
DR EPD; Q92504; -.
DR jPOST; Q92504; -.
DR MassIVE; Q92504; -.
DR MaxQB; Q92504; -.
DR PaxDb; Q92504; -.
DR PeptideAtlas; Q92504; -.
DR PRIDE; Q92504; -.
DR ProteomicsDB; 75275; -.
DR Antibodypedia; 28954; 258 antibodies from 33 providers.
DR DNASU; 7922; -.
DR Ensembl; ENST00000374675.7; ENSP00000363807.3; ENSG00000112473.18.
DR Ensembl; ENST00000374677.8; ENSP00000363809.3; ENSG00000112473.18.
DR Ensembl; ENST00000383213.8; ENSP00000372700.4; ENSG00000206288.13.
DR Ensembl; ENST00000383214.8; ENSP00000372701.4; ENSG00000206288.13.
DR Ensembl; ENST00000416369.6; ENSP00000403583.2; ENSG00000229802.11.
DR Ensembl; ENST00000418477.6; ENSP00000416439.2; ENSG00000226614.11.
DR Ensembl; ENST00000423043.6; ENSP00000389623.2; ENSG00000226614.11.
DR Ensembl; ENST00000431735.6; ENSP00000410656.2; ENSG00000224399.11.
DR Ensembl; ENST00000441854.6; ENSP00000391735.2; ENSG00000229802.11.
DR Ensembl; ENST00000441953.6; ENSP00000413027.2; ENSG00000224399.11.
DR Ensembl; ENST00000443773.6; ENSP00000407093.2; ENSG00000227402.11.
DR Ensembl; ENST00000456261.6; ENSP00000414145.2; ENSG00000227402.11.
DR GeneID; 7922; -.
DR KEGG; hsa:7922; -.
DR MANE-Select; ENST00000374677.8; ENSP00000363809.3; NM_006979.3; NP_008910.2.
DR UCSC; uc003odf.4; human.
DR CTD; 7922; -.
DR DisGeNET; 7922; -.
DR GeneCards; SLC39A7; -.
DR HGNC; HGNC:4927; SLC39A7.
DR HPA; ENSG00000112473; Low tissue specificity.
DR MIM; 601416; gene.
DR neXtProt; NX_Q92504; -.
DR OpenTargets; ENSG00000112473; -.
DR PharmGKB; PA29305; -.
DR VEuPathDB; HostDB:ENSG00000112473; -.
DR eggNOG; KOG2693; Eukaryota.
DR GeneTree; ENSGT00940000160076; -.
DR HOGENOM; CLU_015114_0_1_1; -.
DR InParanoid; Q92504; -.
DR OMA; IWLHSIG; -.
DR OrthoDB; 657777at2759; -.
DR PhylomeDB; Q92504; -.
DR TreeFam; TF318470; -.
DR PathwayCommons; Q92504; -.
DR Reactome; R-HSA-442380; Zinc influx into cells by the SLC39 gene family.
DR SignaLink; Q92504; -.
DR BioGRID-ORCS; 7922; 635 hits in 1082 CRISPR screens.
DR ChiTaRS; SLC39A7; human.
DR GeneWiki; SLC39A7; -.
DR GenomeRNAi; 7922; -.
DR Pharos; Q92504; Tbio.
DR PRO; PR:Q92504; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q92504; protein.
DR Bgee; ENSG00000112473; Expressed in stromal cell of endometrium and 95 other tissues.
DR ExpressionAtlas; Q92504; baseline and differential.
DR Genevisible; Q92504; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR003689; ZIP.
DR Pfam; PF02535; Zip; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Golgi apparatus; Ion transport; Membrane;
KW Methylation; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..469
FT /note="Zinc transporter SLC39A7"
FT /id="PRO_0000213688"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 42..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..259
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 275
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:22317921,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 276
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:22317921,
FT ECO:0007744|PubMed:20068231"
FT VARIANT 87
FT /note="D -> N (in dbSNP:rs34211188)"
FT /id="VAR_050034"
FT VARIANT 124
FT /note="G -> R (in dbSNP:rs35690712)"
FT /id="VAR_050035"
FT VARIANT 280
FT /note="E -> G (in dbSNP:rs1048778)"
FT /evidence="ECO:0000269|PubMed:8812499, ECO:0000269|Ref.2"
FT /id="VAR_050036"
FT MUTAGEN 275
FT /note="S->A: Loss of phosphorylation in response to Zn(2+)
FT treatment and of cytosolic Zn(2+) release; when associated
FT with A-276."
FT /evidence="ECO:0000269|PubMed:22317921"
FT MUTAGEN 276
FT /note="S->A: Loss of phosphorylation in response to Zn(2+)
FT treatment and of cytosolic Zn(2+) release; when associated
FT with A-275."
FT /evidence="ECO:0000269|PubMed:22317921"
FT CONFLICT 7
FT /note="A -> G (in Ref. 1; BAA11528 and 2; AAD12305)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="S -> T (in Ref. 1; BAA11528 and 2; AAD12305)"
FT /evidence="ECO:0000305"
FT CONFLICT 397..469
FT /note="CALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQS
FT LLEVLGLLGGVIMMVLIAHLE -> VPFSLKEEQWTVKLQVVQVLAGSCHLLQVALST
FT (in Ref. 1; BAA11528 and 2; AAD12305)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 50118 MW; 6504A1EF5AA6A5B9 CRC64;
MARGLGAPHW VAVGLLTWAT LGLLVAGLGG HDDLHDDLQE DFHGHSHRHS HEDFHHGHSH
AHGHGHTHES IWHGHTHDHD HGHSHEDLHH GHSHGYSHES LYHRGHGHDH EHSHGGYGES
GAPGIKQDLD AVTLWAYALG ATVLISAAPF FVLFLIPVES NSPRHRSLLQ ILLSFASGGL
LGDAFLHLIP HALEPHSHHT LEQPGHGHSH SGQGPILSVG LWVLSGIVAF LVVEKFVRHV
KGGHGHSHGH GHAHSHTRGS HGHGRQERST KEKQSSEEEE KETRGVQKRR GGSTVPKDGP
VRPQNAEEEK RGLDLRVSGY LNLAADLAHN FTDGLAIGAS FRGGRGLGIL TTMTVLLHEV
PHEVGDFAIL VQSGCSKKQA MRLQLLTAVG ALAGTACALL TEGGAVGSEI AGGAGPGWVL
PFTAGGFIYV ATVSVLPELL REASPLQSLL EVLGLLGGVI MMVLIAHLE
