NKAP_HUMAN
ID NKAP_HUMAN Reviewed; 415 AA.
AC Q8N5F7; Q6IPW6; Q96BQ2; Q9H638;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=NF-kappa-B-activating protein;
GN Name=NKAP;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=B-cell;
RX PubMed=14550261; DOI=10.1016/j.bbrc.2003.09.074;
RA Chen D., Li Z., Yang Q., Zhang J., Zhai Z., Shu H.-B.;
RT "Identification of a nuclear protein that promotes NF-kappaB activation.";
RL Biochem. Biophys. Res. Commun. 310:720-724(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, Placenta, and Testis;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
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 [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 FUNCTION, AND INTERACTION WITH CIR1 AND HDAC3.
RX PubMed=19409814; DOI=10.1016/j.immuni.2009.02.011;
RA Pajerowski A.G., Nguyen C., Aghajanian H., Shapiro M.J., Shapiro V.S.;
RT "NKAP is a transcriptional repressor of notch signaling and is required for
RT T cell development.";
RL Immunity 30:696-707(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-9; SER-50; SER-64;
RP SER-149; SER-157 AND THR-161, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-283 AND LYS-305, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [15]
RP INVOLVEMENT IN MRXSHD, AND VARIANT MRXSHD GLN-333.
RX PubMed=26358559; DOI=10.1002/ajmg.a.37378;
RA Hackmann K., Rump A., Haas S.A., Lemke J.R., Fryns J.P., Tzschach A.,
RA Wieczorek D., Albrecht B., Kuechler A., Ripperger T., Kobelt A., Oexle K.,
RA Tinschert S., Schrock E., Kalscheuer V.M., Di Donato N.;
RT "Tentative clinical diagnosis of Lujan-Fryns syndrome--A conglomeration of
RT different genetic entities?";
RL Am. J. Med. Genet. A 170A:94-102(2016).
RN [16]
RP INVOLVEMENT IN MRXSHD, VARIANTS MRXSHD CYS-330; HIS-330; GLN-333; THR-337
RP AND GLN-361, AND FUNCTION.
RX PubMed=31587868; DOI=10.1016/j.ajhg.2019.09.009;
RA Fiordaliso S.K., Iwata-Otsubo A., Ritter A.L., Quesnel-Vallieres M.,
RA Fujiki K., Nishi E., Hancarova M., Miyake N., Morton J.E.V., Lee S.,
RA Hackmann K., Bando M., Masuda K., Nakato R., Arakawa M., Bhoj E., Li D.,
RA Hakonarson H., Takeda R., Harr M., Keena B., Zackai E.H., Okamoto N.,
RA Mizuno S., Ko J.M., Valachova A., Prchalova D., Vlckova M., Pippucci T.,
RA Seiler C., Choi M., Matsumoto N., Di Donato N., Barash Y., Sedlacek Z.,
RA Shirahige K., Izumi K.;
RT "Missense mutations in NKAP cause a disorder of transcriptional regulation
RT characterized by Marfanoid habitus and cognitive impairment.";
RL Am. J. Hum. Genet. 105:987-995(2019).
CC -!- FUNCTION: Acts as a transcriptional repressor (PubMed:14550261,
CC PubMed:19409814, PubMed:31587868). Plays a role as a transcriptional
CC corepressor of the Notch-mediated signaling required for T-cell
CC development (PubMed:19409814). Also involved in the TNF and IL-1
CC induced NF-kappa-B activation. Associates with chromatin at the Notch-
CC regulated SKP2 promoter. {ECO:0000269|PubMed:14550261,
CC ECO:0000269|PubMed:19409814, ECO:0000269|PubMed:31587868}.
CC -!- SUBUNIT: Component of the Notch corepressor complex. Interacts with
CC CIR1 and HDAC3. {ECO:0000269|PubMed:19409814}.
CC -!- INTERACTION:
CC Q8N5F7; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-721539, EBI-541426;
CC Q8N5F7; Q9UJV9: DDX41; NbExp=3; IntAct=EBI-721539, EBI-1046350;
CC Q8N5F7; Q14562: DHX8; NbExp=2; IntAct=EBI-721539, EBI-2511477;
CC Q8N5F7; O43395: PRPF3; NbExp=2; IntAct=EBI-721539, EBI-744322;
CC Q8N5F7; O75400: PRPF40A; NbExp=2; IntAct=EBI-721539, EBI-473291;
CC Q8N5F7; Q9Y388: RBMX2; NbExp=2; IntAct=EBI-721539, EBI-7704044;
CC Q8N5F7; Q01081: U2AF1; NbExp=2; IntAct=EBI-721539, EBI-632461;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14550261}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic,
CC Hackman-Di Donato type (MRXSHD) [MIM:301039]: An X-linked recessive
CC disorder characterized by impaired intellectual development, global
CC developmental delay, hypotonia, joint contractures, behavioral
CC abnormalities, Marfanoid habitus, scoliosis, and mildly dysmorphic
CC facies. {ECO:0000269|PubMed:26358559, ECO:0000269|PubMed:31587868}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the NKAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH71686.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AY388958; AAQ90402.1; -; mRNA.
DR EMBL; AK026279; BAB15428.1; -; mRNA.
DR EMBL; BC015354; AAH15354.1; -; mRNA.
DR EMBL; BC032442; AAH32442.1; -; mRNA.
DR EMBL; BC071686; AAH71686.1; ALT_SEQ; mRNA.
DR CCDS; CCDS14592.1; -.
DR RefSeq; NP_078804.2; NM_024528.3.
DR PDB; 6QDV; EM; 3.30 A; Z=329-358.
DR PDBsum; 6QDV; -.
DR AlphaFoldDB; Q8N5F7; -.
DR SMR; Q8N5F7; -.
DR BioGRID; 122723; 110.
DR IntAct; Q8N5F7; 75.
DR MINT; Q8N5F7; -.
DR STRING; 9606.ENSP00000360464; -.
DR GlyGen; Q8N5F7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N5F7; -.
DR PhosphoSitePlus; Q8N5F7; -.
DR BioMuta; NKAP; -.
DR DMDM; 74728990; -.
DR EPD; Q8N5F7; -.
DR jPOST; Q8N5F7; -.
DR MassIVE; Q8N5F7; -.
DR MaxQB; Q8N5F7; -.
DR PaxDb; Q8N5F7; -.
DR PeptideAtlas; Q8N5F7; -.
DR PRIDE; Q8N5F7; -.
DR ProteomicsDB; 72046; -.
DR Antibodypedia; 364; 138 antibodies from 25 providers.
DR DNASU; 79576; -.
DR Ensembl; ENST00000371410.5; ENSP00000360464.3; ENSG00000101882.10.
DR GeneID; 79576; -.
DR KEGG; hsa:79576; -.
DR MANE-Select; ENST00000371410.5; ENSP00000360464.3; NM_024528.4; NP_078804.2.
DR UCSC; uc004esh.4; human.
DR CTD; 79576; -.
DR DisGeNET; 79576; -.
DR GeneCards; NKAP; -.
DR HGNC; HGNC:29873; NKAP.
DR HPA; ENSG00000101882; Low tissue specificity.
DR MalaCards; NKAP; -.
DR MIM; 300766; gene.
DR MIM; 301039; phenotype.
DR neXtProt; NX_Q8N5F7; -.
DR OpenTargets; ENSG00000101882; -.
DR PharmGKB; PA162397584; -.
DR VEuPathDB; HostDB:ENSG00000101882; -.
DR eggNOG; KOG2812; Eukaryota.
DR GeneTree; ENSGT00940000160787; -.
DR HOGENOM; CLU_032439_1_0_1; -.
DR InParanoid; Q8N5F7; -.
DR OMA; VERWPND; -.
DR OrthoDB; 1561377at2759; -.
DR PhylomeDB; Q8N5F7; -.
DR TreeFam; TF315333; -.
DR PathwayCommons; Q8N5F7; -.
DR SignaLink; Q8N5F7; -.
DR BioGRID-ORCS; 79576; 375 hits in 709 CRISPR screens.
DR ChiTaRS; NKAP; human.
DR GeneWiki; NKAP; -.
DR GenomeRNAi; 79576; -.
DR Pharos; Q8N5F7; Tbio.
DR PRO; PR:Q8N5F7; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8N5F7; protein.
DR Bgee; ENSG00000101882; Expressed in calcaneal tendon and 172 other tissues.
DR ExpressionAtlas; Q8N5F7; baseline and differential.
DR Genevisible; Q8N5F7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030851; P:granulocyte differentiation; IEA:Ensembl.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR InterPro; IPR040466; NKAP.
DR InterPro; IPR009269; NKAP_C.
DR PANTHER; PTHR13087; PTHR13087; 1.
DR Pfam; PF06047; Nkap_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; Intellectual disability;
KW Isopeptide bond; Notch signaling pathway; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..415
FT /note="NF-kappa-B-activating protein"
FT /id="PRO_0000259645"
FT REGION 1..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..272
FT /note="Necessary for interaction with CIR1"
FT /evidence="ECO:0000269|PubMed:19409814"
FT REGION 273..415
FT /note="Necessary for interaction with HDAC3 and
FT transcriptional repression"
FT /evidence="ECO:0000269|PubMed:19409814"
FT COMPBIAS 25..44
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..206
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..257
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 115
FT /note="P -> H (in dbSNP:rs34728541)"
FT /id="VAR_053799"
FT VARIANT 330
FT /note="R -> C (in MRXSHD; dbSNP:rs1603379781)"
FT /evidence="ECO:0000269|PubMed:31587868"
FT /id="VAR_083895"
FT VARIANT 330
FT /note="R -> H (in MRXSHD; dbSNP:rs1603379780)"
FT /evidence="ECO:0000269|PubMed:31587868"
FT /id="VAR_083896"
FT VARIANT 333
FT /note="R -> Q (in MRXSHD; unknown pathological
FT significance; dbSNP:rs1603379779)"
FT /evidence="ECO:0000269|PubMed:26358559,
FT ECO:0000269|PubMed:31587868"
FT /id="VAR_083897"
FT VARIANT 337
FT /note="I -> T (in MRXSHD; dbSNP:rs1603379772)"
FT /evidence="ECO:0000269|PubMed:31587868"
FT /id="VAR_083898"
FT VARIANT 361
FT /note="R -> Q (in MRXSHD; unknown pathological
FT significance; dbSNP:rs1603379318)"
FT /evidence="ECO:0000269|PubMed:31587868"
FT /id="VAR_083899"
FT CONFLICT 57
FT /note="T -> A (in Ref. 2; BAB15428)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="D -> Y (in Ref. 3; AAH15354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47138 MW; 44BD1DE20F7ED35A CRC64;
MAPVSGSRSP DREASGSGGR RRSSSKSPKP SKSARSPRGR RSRSHSCSRS GDRNGLTHQL
GGLSQGSRNQ SYRSRSRSRS RERPSAPRGI PFASASSSVY YGSYSRPYGS DKPWPSLLDK
EREESLRQKR LSERERIGEL GAPEVWGLSP KNPEPDSDEH TPVEDEEPKK STTSASTSEE
EKKKKSSRSK ERSKKRRKKK SSKRKHKKYS EDSDSDSDSE TDSSDEDNKR RAKKAKKKEK
KKKHRSKKYK KKRSKKSRKE SSDSSSKESQ EEFLENPWKD RTKAEEPSDL IGPEAPKTLT
SQDDKPLNYG HALLPGEGAA MAEYVKAGKR IPRRGEIGLT SEEIASFECS GYVMSGSRHR
RMEAVRLRKE NQIYSADEKR ALASFNQEER RKRENKILAS FREMVYRKTK GKDDK
