KLF1_HUMAN
ID KLF1_HUMAN Reviewed; 362 AA.
AC Q13351; Q6PIJ5; Q92899;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Krueppel-like factor 1;
DE AltName: Full=Erythroid krueppel-like transcription factor;
DE Short=EKLF;
GN Name=KLF1; Synonyms=EKLF;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=8924208; DOI=10.1089/dna.1996.15.347;
RA Bieker J.J.;
RT "Isolation, genomic structure, and expression of human erythroid Kruppel-
RT like factor (EKLF).";
RL DNA Cell Biol. 15:347-352(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9119377; DOI=10.1006/geno.1996.4472;
RA van Ree J.H., Roskrow M.A., Becher A.M., McNall R., Valentine V.A.,
RA Jane S.M., Cunningham J.M.;
RT "The human erythroid-specific transcription factor EKLF localizes to
RT chromosome 19p13.12-p13.13.";
RL Genomics 39:393-395(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-102.
RC TISSUE=Lung;
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 ACETYLATION, AND INTERACTION WITH CBP; EP300 AND PCAF.
RX PubMed=9707565; DOI=10.1073/pnas.95.17.9855;
RA Zhang W., Bieker J.J.;
RT "Acetylation and modulation of erythroid Krueppel-like factor (EKLF)
RT activity by interaction with histone acetyltransferases.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9855-9860(1998).
RN [6]
RP ROLE IN ERYTHROPOIESIS, FUNCTION AS TRANSCRIPTIONAL ACTIVATOR OF CD44 AND
RP AQP1, SUBCELLULAR LOCATION, VARIANT PRO-102, VARIANT CDAN4 LYS-325, AND
RP CHARACTERIZATION OF VARIANT CDAN4 LYS-325.
RX PubMed=21055716; DOI=10.1016/j.ajhg.2010.10.010;
RA Arnaud L., Saison C., Helias V., Lucien N., Steschenko D., Giarratana M.C.,
RA Prehu C., Foliguet B., Montout L., de Brevern A.G., Francina A.,
RA Ripoche P., Fenneteau O., Da Costa L., Peyrard T., Coghlan G., Illum N.,
RA Birgens H., Tamary H., Iolascon A., Delaunay J., Tchernia G., Cartron J.P.;
RT "A dominant mutation in the gene encoding the erythroid transcription
RT factor KLF1 causes a congenital dyserythropoietic anemia.";
RL Am. J. Hum. Genet. 87:721-727(2010).
RN [7]
RP FUNCTION AS REGULATOR OF FETAL-TO-ADULT GLOBIN SWITCHING, AND POLYMORPHISM.
RX PubMed=20676099; DOI=10.1038/ng.630;
RA Borg J., Papadopoulos P., Georgitsi M., Gutierrez L., Grech G., Fanis P.,
RA Phylactides M., Verkerk A.J., van der Spek P.J., Scerri C.A., Cassar W.,
RA Galdies R., van Ijcken W., Ozgur Z., Gillemans N., Hou J., Bugeja M.,
RA Grosveld F.G., von Lindern M., Felice A.E., Patrinos G.P., Philipsen S.;
RT "Haploinsufficiency for the erythroid transcription factor KLF1 causes
RT hereditary persistence of fetal hemoglobin.";
RL Nat. Genet. 42:801-805(2010).
RN [8]
RP 9AATAD MOTIF.
RX PubMed=31375868; DOI=10.1007/s00018-019-03251-w;
RA Piskacek M., Havelka M., Jendruchova K., Knight A., Keegan L.P.;
RT "The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with
RT valines and intron reservoirs.";
RL Cell. Mol. Life Sci. 77:1793-1810(2020).
RN [9]
RP STRUCTURE BY NMR OF 51-90 IN COMPLEX WITH YEAST TFB1, FUNCTION, AND
RP INTERACTION WITH TFB1; CREBBP AND EP300.
RX PubMed=21670263; DOI=10.1073/pnas.1017029108;
RA Mas C., Lussier-Price M., Soni S., Morse T., Arseneault G., Di Lello P.,
RA Lafrance-Vanasse J., Bieker J.J., Omichinski J.G.;
RT "Structural and functional characterization of an atypical activation
RT domain in erythroid Kruppel-like factor (EKLF).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10484-10489(2011).
RN [10]
RP VARIANTS BLOOD GROUP-IN(LU) TYR-299; LEU-328; HIS-328 AND GLY-331, AND
RP POLYMORPHISM.
RX PubMed=18487511; DOI=10.1182/blood-2008-03-145672;
RA Singleton B.K., Burton N.M., Green C., Brady R.L., Anstee D.J.;
RT "Mutations in EKLF/KLF1 form the molecular basis of the rare blood group
RT In(Lu) phenotype.";
RL Blood 112:2081-2088(2008).
RN [11]
RP VARIANTS LYS-5; PRO-298; ASP-299; ARG-334 AND TYR-341.
RX PubMed=24829204; DOI=10.1182/blood-2014-03-561779;
RA Liu D., Zhang X., Yu L., Cai R., Ma X., Zheng C., Zhou Y., Liu Q., Wei X.,
RA Lin L., Yan T., Huang J., Mohandas N., An X., Xu X.;
RT "KLF1 mutations are relatively more common in a thalassemia endemic region
RT and ameliorate the severity of beta-thalassemia.";
RL Blood 124:803-811(2014).
RN [12]
RP VARIANTS PRO-298 AND SER-338, CHARACTERIZATION OF VARIANTS PRO-298 AND
RP SER-338, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25585695; DOI=10.1038/ejhg.2014.291;
RA Huang J., Zhang X., Liu D., Wei X., Shang X., Xiong F., Yu L., Yin X.,
RA Xu X.;
RT "Compound heterozygosity for KLF1 mutations is associated with microcytic
RT hypochromic anemia and increased fetal hemoglobin.";
RL Eur. J. Hum. Genet. 23:1341-1348(2015).
RN [13]
RP VARIANT TRP-316.
RX PubMed=25690802; DOI=10.3109/03630269.2015.1008702;
RA Nitta T., Kawano F., Yamashiro Y., Takagi F., Murata T., Tanaka T.,
RA Ferania M., Adhiyanto C., Hattori Y.;
RT "A new Krueppel-like factor 1 mutation (c.947G > A or p.C316Y) in humans
RT causes beta-thalassemia minor.";
RL Hemoglobin 39:121-126(2015).
CC -!- FUNCTION: Transcription regulator of erythrocyte development that
CC probably serves as a general switch factor during erythropoiesis. Is a
CC dual regulator of fetal-to-adult globin switching. Binds to the CACCC
CC box in the beta-globin gene promoter and acts as a preferential
CC activator of this gene. Furthermore, it binds to the BCL11A promoter
CC and activates expression of BCL11A, which in turn represses the HBG1
CC and HBG2 genes. This dual activity ensures that, in most adults, fetal
CC hemoglobin levels are low. Able to activate CD44 and AQP1 promoters.
CC When sumoylated, acts as a transcriptional repressor by promoting
CC interaction with CDH2/MI2beta and also represses megakaryocytic
CC differentiation. {ECO:0000250|UniProtKB:P46099,
CC ECO:0000269|PubMed:25585695}.
CC -!- SUBUNIT: Interacts with PCAF; the interaction does not acetylate EKLF
CC and inhibits its transactivation activity (By similarity). Interacts
CC with CREBBP/CBP and EP300; the interactions enhance the transactivation
CC activity. Interacts with TFB1. {ECO:0000250,
CC ECO:0000269|PubMed:21670263, ECO:0000269|PubMed:9707565}.
CC -!- INTERACTION:
CC Q13351; Q07021: C1QBP; NbExp=3; IntAct=EBI-8284732, EBI-347528;
CC Q13351; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-8284732, EBI-10961624;
CC Q13351; Q92793: CREBBP; NbExp=2; IntAct=EBI-8284732, EBI-81215;
CC Q13351; Q92997: DVL3; NbExp=3; IntAct=EBI-8284732, EBI-739789;
CC Q13351; O95967: EFEMP2; NbExp=3; IntAct=EBI-8284732, EBI-743414;
CC Q13351; P32780: GTF2H1; NbExp=2; IntAct=EBI-8284732, EBI-715539;
CC Q13351; P13807: GYS1; NbExp=3; IntAct=EBI-8284732, EBI-740553;
CC Q13351; P52597: HNRNPF; NbExp=3; IntAct=EBI-8284732, EBI-352986;
CC Q13351; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-8284732, EBI-7060731;
CC Q13351; Q13064: MKRN3; NbExp=3; IntAct=EBI-8284732, EBI-2340269;
CC Q13351; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-8284732, EBI-11022007;
CC Q13351; Q15365: PCBP1; NbExp=3; IntAct=EBI-8284732, EBI-946095;
CC Q13351; P79522: PRR3; NbExp=3; IntAct=EBI-8284732, EBI-2803328;
CC Q13351; P98175: RBM10; NbExp=3; IntAct=EBI-8284732, EBI-721525;
CC Q13351; Q9BQ04: RBM4B; NbExp=3; IntAct=EBI-8284732, EBI-715531;
CC Q13351; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-8284732, EBI-11987469;
CC Q13351; P09234: SNRPC; NbExp=3; IntAct=EBI-8284732, EBI-766589;
CC Q13351; Q01085-2: TIAL1; NbExp=3; IntAct=EBI-8284732, EBI-11064654;
CC Q13351; Q08117-2: TLE5; NbExp=3; IntAct=EBI-8284732, EBI-11741437;
CC Q13351; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-8284732, EBI-2559305;
CC Q13351; P32776: TFB1; Xeno; NbExp=3; IntAct=EBI-8284732, EBI-19146;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21055716,
CC ECO:0000269|PubMed:25585695}. Note=Colocalizes with SUMO1 in nuclear
CC speckles. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expression restricted to adult bone marrow and
CC fetal liver. Not expressed in myeloid nor lymphoid cell lines.
CC {ECO:0000269|PubMed:8924208, ECO:0000269|PubMed:9119377}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:31375868}.
CC -!- PTM: Acetylated; can be acetylated on both Lys-274 and Lys-288.
CC Acetylation on Lys-274 (by CBP) appears to be the major site affecting
CC EKLF transactivation activity (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated; sumoylation, promoted by PIAS1, leads to repression of
CC megakaryocyte differentiation. Also promotes the interaction with the
CC CDH4 subunit of the NuRD repression complex (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated primarily on serine residues in the transactivation
CC domain. Phosphorylation on Thr-23 is critical for the transactivation
CC activity (By similarity). {ECO:0000250}.
CC -!- POLYMORPHISM: Genetic variations in KLF1 underlie the fetal hemoglobin
CC quantitative trait locus 6 (HBFQTL6) [MIM:613566]. Classic hereditary
CC persistence of fetal hemoglobin (HPFH) is characterized by a
CC substantial elevation of fetal hemoglobin (HbF) in adult red blood
CC cells. There are no other phenotypic or hematologic manifestations. In
CC healthy adults, fetal hemoglobin (HbF) is present at residual levels
CC (less than 0.06% of total hemoglobin) with over 20-fold variation. Ten
CC to fifteen percent of adults fall within the upper tail of the
CC distribution. {ECO:0000269|PubMed:20676099}.
CC -!- POLYMORPHISM: Genetic variations in KLF1 underlie the blood group-
CC Lutheran inhibitor (In(Lu)) phenotype [MIM:111150]; also known as
CC dominant Lu (a-b-) phenotype. In(Lu) is characterized phenotypically by
CC the apparent absence of the Lu antigen (BCAM) on red blood cells during
CC serologic tests: Lu(a-b-). {ECO:0000269|PubMed:18487511}.
CC -!- DISEASE: Anemia, congenital dyserythropoietic, 4 (CDAN4) [MIM:613673]:
CC A blood disorder characterized by ineffective erythropoiesis and
CC hemolysis resulting in anemia. Circulating erythroblasts and
CC erythroblasts in the bone marrow show various morphologic
CC abnormalities. Affected individuals with CDA4 also have increased
CC levels of fetal hemoglobin. {ECO:0000269|PubMed:21055716,
CC ECO:0000269|PubMed:25585695}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U37106; AAC50562.1; -; Genomic_DNA.
DR EMBL; U65404; AAC51108.1; -; mRNA.
DR EMBL; AD000092; AAB51173.1; -; Genomic_DNA.
DR EMBL; BC033580; AAH33580.1; -; mRNA.
DR CCDS; CCDS12285.1; -.
DR PIR; T45072; T45072.
DR RefSeq; NP_006554.1; NM_006563.4.
DR PDB; 2L2I; NMR; -; B=51-90.
DR PDB; 2MBH; NMR; -; B=2-40.
DR PDB; 2N23; NMR; -; B=22-40.
DR PDBsum; 2L2I; -.
DR PDBsum; 2MBH; -.
DR PDBsum; 2N23; -.
DR AlphaFoldDB; Q13351; -.
DR BMRB; Q13351; -.
DR SMR; Q13351; -.
DR BioGRID; 115904; 35.
DR DIP; DIP-43776N; -.
DR IntAct; Q13351; 23.
DR MINT; Q13351; -.
DR STRING; 9606.ENSP00000264834; -.
DR ChEMBL; CHEMBL3407313; -.
DR iPTMnet; Q13351; -.
DR PhosphoSitePlus; Q13351; -.
DR BioMuta; KLF1; -.
DR DMDM; 2501699; -.
DR jPOST; Q13351; -.
DR MassIVE; Q13351; -.
DR MaxQB; Q13351; -.
DR PaxDb; Q13351; -.
DR PeptideAtlas; Q13351; -.
DR PRIDE; Q13351; -.
DR ProteomicsDB; 59335; -.
DR Antibodypedia; 13415; 413 antibodies from 38 providers.
DR DNASU; 10661; -.
DR Ensembl; ENST00000264834.6; ENSP00000264834.3; ENSG00000105610.6.
DR GeneID; 10661; -.
DR KEGG; hsa:10661; -.
DR MANE-Select; ENST00000264834.6; ENSP00000264834.3; NM_006563.5; NP_006554.1.
DR UCSC; uc002mvo.4; human.
DR CTD; 10661; -.
DR DisGeNET; 10661; -.
DR GeneCards; KLF1; -.
DR HGNC; HGNC:6345; KLF1.
DR HPA; ENSG00000105610; Tissue enriched (bone).
DR MalaCards; KLF1; -.
DR MIM; 111150; phenotype.
DR MIM; 600599; gene.
DR MIM; 613566; phenotype.
DR MIM; 613673; phenotype.
DR neXtProt; NX_Q13351; -.
DR OpenTargets; ENSG00000105610; -.
DR Orphanet; 293825; Congenital dyserythropoietic anemia type IV.
DR Orphanet; 46532; Hereditary persistence of fetal hemoglobin-beta-thalassemia syndrome.
DR Orphanet; 251380; Hereditary persistence of fetal hemoglobin-sickle cell disease syndrome.
DR PharmGKB; PA30131; -.
DR VEuPathDB; HostDB:ENSG00000105610; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161856; -.
DR HOGENOM; CLU_063878_0_0_1; -.
DR InParanoid; Q13351; -.
DR OMA; FPDTQED; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q13351; -.
DR TreeFam; TF350556; -.
DR PathwayCommons; Q13351; -.
DR SignaLink; Q13351; -.
DR SIGNOR; Q13351; -.
DR BioGRID-ORCS; 10661; 44 hits in 1105 CRISPR screens.
DR EvolutionaryTrace; Q13351; -.
DR GenomeRNAi; 10661; -.
DR Pharos; Q13351; Tbio.
DR PRO; PR:Q13351; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q13351; protein.
DR Bgee; ENSG00000105610; Expressed in trabecular bone tissue and 62 other tissues.
DR Genevisible; Q13351; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR DisProt; DP01640; -.
DR IDEAL; IID00468; -.
DR InterPro; IPR031786; EKLF_TAD1.
DR InterPro; IPR031784; EKLF_TAD2.
DR InterPro; IPR031785; KLF1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23235:SF63; PTHR23235:SF63; 1.
DR Pfam; PF16832; EKLF_TAD1; 1.
DR Pfam; PF16833; EKLF_TAD2; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Congenital dyserythropoietic anemia;
KW Disease variant; DNA-binding; Hereditary hemolytic anemia; Isopeptide bond;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..362
FT /note="Krueppel-like factor 1"
FT /id="PRO_0000047160"
FT ZN_FING 279..303
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 309..333
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 339..361
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 71..79
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:31375868"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P46099, ECO:0000305"
FT MOD_RES 184
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P46099"
FT MOD_RES 274
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46099"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46099"
FT CROSSLNK 54
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VARIANT 5
FT /note="E -> K (in dbSNP:rs483352842)"
FT /evidence="ECO:0000269|PubMed:24829204"
FT /id="VAR_074272"
FT VARIANT 102
FT /note="S -> P (in dbSNP:rs2072597)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:21055716"
FT /id="VAR_043981"
FT VARIANT 182
FT /note="F -> L (in dbSNP:rs2072596)"
FT /id="VAR_043982"
FT VARIANT 298
FT /note="A -> P (found in a patient with autosomal recessive
FT microcytic hypochromic anemia and increased fetal
FT hemoglobin; unknown pathological significance; no effect on
FT protein abundance; no effect on protein localization;
FT decreased transcriptional activity; dbSNP:rs387907598)"
FT /evidence="ECO:0000269|PubMed:24829204,
FT ECO:0000269|PubMed:25585695"
FT /id="VAR_072737"
FT VARIANT 299
FT /note="H -> D (in dbSNP:rs137852688)"
FT /evidence="ECO:0000269|PubMed:24829204"
FT /id="VAR_074273"
FT VARIANT 299
FT /note="H -> Y (in blood group-In(Lu); dbSNP:rs137852688)"
FT /evidence="ECO:0000269|PubMed:18487511"
FT /id="VAR_058108"
FT VARIANT 316
FT /note="C -> W"
FT /evidence="ECO:0000269|PubMed:25690802"
FT /id="VAR_074274"
FT VARIANT 325
FT /note="E -> K (in CDAN4; has a dominant-negative effect on
FT the transcriptional activation of CD44 and AQP1 promoters;
FT dbSNP:rs267607201)"
FT /evidence="ECO:0000269|PubMed:21055716"
FT /id="VAR_064901"
FT VARIANT 328
FT /note="R -> H (in blood group-In(Lu); dbSNP:rs140252918)"
FT /evidence="ECO:0000269|PubMed:18487511"
FT /id="VAR_058109"
FT VARIANT 328
FT /note="R -> L (in blood group-In(Lu))"
FT /evidence="ECO:0000269|PubMed:18487511"
FT /id="VAR_058110"
FT VARIANT 331
FT /note="R -> G (in blood group-In(Lu))"
FT /evidence="ECO:0000269|PubMed:18487511"
FT /id="VAR_058111"
FT VARIANT 334
FT /note="T -> R (in dbSNP:rs483352841)"
FT /evidence="ECO:0000269|PubMed:24829204"
FT /id="VAR_074275"
FT VARIANT 338
FT /note="P -> S (found in a patient with autosomal recessive
FT microcytic hypochromic anemia and increased fetal
FT hemoglobin; with microcytic hypochromic anemia; no effect
FT on protein abundance; no effect on protein localization;
FT decreased transcriptional activity; dbSNP:rs387907599)"
FT /evidence="ECO:0000269|PubMed:25585695"
FT /id="VAR_072738"
FT VARIANT 341
FT /note="C -> Y (in dbSNP:rs483352839)"
FT /evidence="ECO:0000269|PubMed:24829204"
FT /id="VAR_074276"
FT CONFLICT 163
FT /note="A -> G (in Ref. 2; AAC51108)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="P -> A (in Ref. 2; AAC51108)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="R -> G (in Ref. 2; AAC51108)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="A -> E (in Ref. 2; AAC51108)"
FT /evidence="ECO:0000305"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:2MBH"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:2L2I"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:2L2I"
SQ SEQUENCE 362 AA; 38221 MW; 6E9A48A2B6A37C76 CRC64;
MATAETALPS ISTLTALGPF PDTQDDFLKW WRSEEAQDMG PGPPDPTEPP LHVKSEDQPG
EEEDDERGAD ATWDLDLLLT NFSGPEPGGA PQTCALAPSE ASGAQYPPPP ETLGAYAGGP
GLVAGLLGSE DHSGWVRPAL RARAPDAFVG PALAPAPAPE PKALALQPVY PGPGAGSSGG
YFPRTGLSVP AASGAPYGLL SGYPAMYPAP QYQGHFQLFR GLQGPAPGPA TSPSFLSCLG
PGTVGTGLGG TAEDPGVIAE TAPSKRGRRS WARKRQAAHT CAHPGCGKSY TKSSHLKAHL
RTHTGEKPYA CTWEGCGWRF ARSDELTRHY RKHTGQRPFR CQLCPRAFSR SDHLALHMKR
HL
