POP1_HUMAN
ID POP1_HUMAN Reviewed; 1024 AA.
AC Q99575; A8K5W9; Q15037;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Ribonucleases P/MRP protein subunit POP1;
DE Short=hPOP1;
GN Name=POP1; Synonyms=KIAA0061;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-126, FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=8918471; DOI=10.1002/j.1460-2075.1996.tb00980.x;
RA Lygerou Z., Pluk H., Van Venrooij W.J., Seraphin B.;
RT "hPop1: an autoantigenic protein subunit shared by the human RNase P and
RT RNase MRP ribonucleoproteins.";
RL EMBO J. 15:5936-5948(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 122-1024.
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [5]
RP IDENTIFICATION BY 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 [6]
RP IDENTIFICATION IN RNASE P AND MRP COMPLEXES, AND SUBUNIT.
RX PubMed=16723659; DOI=10.1261/rna.2293906;
RA Welting T.J., Kikkert B.J., van Venrooij W.J., Pruijn G.J.;
RT "Differential association of protein subunits with the human RNase MRP and
RT RNase P complexes.";
RL RNA 12:1373-1382(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 AND SER-730, AND
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INVOLVEMENT IN ANXD2, AND VARIANT ANXD2 GLU-583.
RX PubMed=21455487; DOI=10.1371/journal.pgen.1002027;
RA Glazov E.A., Zankl A., Donskoi M., Kenna T.J., Thomas G.P., Clark G.R.,
RA Duncan E.L., Brown M.A.;
RT "Whole-exome re-sequencing in a family quartet identifies POP1 mutations as
RT the cause of a novel skeletal dysplasia.";
RL PLoS Genet. 7:E1002027-E1002027(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-730, AND
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-584 AND SER-730, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [16]
RP INVOLVEMENT IN ANXD2, AND VARIANT ANXD2 SER-582.
RX PubMed=27380734; DOI=10.1002/ajmg.a.37839;
RA Elalaoui S.C., Laarabi F.Z., Mansouri M., Mrani N.A., Nishimura G.,
RA Sefiani A.;
RT "Further evidence of POP1 mutations as the cause of anauxetic dysplasia.";
RL Am. J. Med. Genet. A 170:2462-2465(2016).
RN [17]
RP FUNCTION, AND SUBUNIT.
RX PubMed=28115465; DOI=10.1101/gad.286963.116;
RA Goldfarb K.C., Cech T.R.;
RT "Targeted CRISPR disruption reveals a role for RNase MRP RNA in human
RT preribosomal RNA processing.";
RL Genes Dev. 31:59-71(2017).
RN [18] {ECO:0007744|PDB:6AHR, ECO:0007744|PDB:6AHU}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.66 ANGSTROMS) OF RNASE P HOLOENZYME IN
RP COMPLEX WITH TRNA, FUNCTION, AND SUBUNIT.
RX PubMed=30454648; DOI=10.1016/j.cell.2018.10.003;
RA Wu J., Niu S., Tan M., Huang C., Li M., Song Y., Wang Q., Chen J., Shi S.,
RA Lan P., Lei M.;
RT "Cryo-EM Structure of the Human Ribonuclease P Holoenzyme.";
RL Cell 175:1393-1404.e11(2018).
RN [19]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-675.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [20]
RP VARIANTS ANXD2 TYR-511 AND SER-582.
RX PubMed=28067412; DOI=10.1111/cge.12964;
RA Barraza-Garcia J., Rivera-Pedroza C.I., Hisado-Oliva A.,
RA Belinchon-Martinez A., Sentchordi-Montane L., Duncan E.L., Clark G.R.,
RA Del Pozo A., Ibanez-Garikano K., Offiah A., Prieto-Matos P.,
RA Cormier-Daire V., Heath K.E.;
RT "Broadening the phenotypic spectrum of POP1-skeletal dysplasias:
RT identification of POP1 mutations in a mild and severe skeletal dysplasia.";
RL Clin. Genet. 92:91-98(2017).
CC -!- FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that
CC generates mature tRNA molecules by cleaving their 5'-ends
CC (PubMed:8918471, PubMed:30454648). Also a component of the MRP
CC ribonuclease complex, which cleaves pre-rRNA sequences
CC (PubMed:28115465). {ECO:0000269|PubMed:28115465,
CC ECO:0000269|PubMed:30454648, ECO:0000269|PubMed:8918471}.
CC -!- SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins
CC (PubMed:8918471, PubMed:16723659). RNase P consists of a catalytic RNA
CC moiety and 10 different protein chains; POP1, POP4, POP5, POP7, RPP14,
CC RPP21, RPP25, RPP30, RPP38 and RPP40 (PubMed:16723659,
CC PubMed:30454648). Within the RNase P complex, POP1, POP7 and RPP25 form
CC the 'finger' subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form
CC the 'palm' subcomplex, and RPP21, POP4 and RPP38 form the 'wrist'
CC subcomplex. All subunits of the RNase P complex interact with the
CC catalytic RNA (PubMed:30454648). Several subunits of RNase P are also
CC part of the RNase MRP complex. RNase MRP consists of a catalytic RNA
CC moiety and about 8 protein subunits; POP1, POP7, RPP25, RPP30, RPP38,
CC RPP40 and possibly also POP4 and POP5 (PubMed:16723659,
CC PubMed:28115465). {ECO:0000269|PubMed:16723659,
CC ECO:0000269|PubMed:28115465, ECO:0000269|PubMed:30454648,
CC ECO:0000269|PubMed:8918471}.
CC -!- INTERACTION:
CC Q99575; O95707: POP4; NbExp=3; IntAct=EBI-366741, EBI-366477;
CC Q99575; Q9BUL9: RPP25; NbExp=2; IntAct=EBI-366741, EBI-366570;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:8918471}.
CC -!- DISEASE: Anauxetic dysplasia 2 (ANXD2) [MIM:617396]: An autosomal
CC recessive spondyloepimetaphyseal dysplasia characterized by severe
CC short stature of prenatal onset, very short adult height (less than 1
CC meter), hypodontia, midface hypoplasia, and mild intellectual
CC disability. {ECO:0000269|PubMed:21455487, ECO:0000269|PubMed:27380734,
CC ECO:0000269|PubMed:28067412}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AK291434; BAF84123.1; -; mRNA.
DR EMBL; CH471060; EAW91776.1; -; Genomic_DNA.
DR EMBL; X99302; CAA67684.1; -; mRNA.
DR EMBL; D31765; BAA06543.1; -; mRNA.
DR CCDS; CCDS6277.1; -.
DR RefSeq; NP_001139332.1; NM_001145860.1.
DR RefSeq; NP_001139333.1; NM_001145861.1.
DR RefSeq; NP_055844.2; NM_015029.2.
DR PDB; 6AHR; EM; 3.92 A; B=1-1024.
DR PDB; 6AHU; EM; 3.66 A; B=1-1024.
DR PDBsum; 6AHR; -.
DR PDBsum; 6AHU; -.
DR AlphaFoldDB; Q99575; -.
DR SMR; Q99575; -.
DR BioGRID; 116140; 249.
DR CORUM; Q99575; -.
DR IntAct; Q99575; 73.
DR MINT; Q99575; -.
DR STRING; 9606.ENSP00000385787; -.
DR iPTMnet; Q99575; -.
DR MetOSite; Q99575; -.
DR PhosphoSitePlus; Q99575; -.
DR SwissPalm; Q99575; -.
DR BioMuta; POP1; -.
DR DMDM; 13124451; -.
DR EPD; Q99575; -.
DR jPOST; Q99575; -.
DR MassIVE; Q99575; -.
DR MaxQB; Q99575; -.
DR PaxDb; Q99575; -.
DR PeptideAtlas; Q99575; -.
DR PRIDE; Q99575; -.
DR ProteomicsDB; 78334; -.
DR Antibodypedia; 26061; 93 antibodies from 17 providers.
DR DNASU; 10940; -.
DR Ensembl; ENST00000349693.3; ENSP00000339529.3; ENSG00000104356.11.
DR Ensembl; ENST00000401707.7; ENSP00000385787.2; ENSG00000104356.11.
DR GeneID; 10940; -.
DR KEGG; hsa:10940; -.
DR MANE-Select; ENST00000401707.7; ENSP00000385787.2; NM_001145860.2; NP_001139332.1.
DR UCSC; uc003yij.5; human.
DR CTD; 10940; -.
DR DisGeNET; 10940; -.
DR GeneCards; POP1; -.
DR HGNC; HGNC:30129; POP1.
DR HPA; ENSG00000104356; Low tissue specificity.
DR MalaCards; POP1; -.
DR MIM; 602486; gene.
DR MIM; 617396; phenotype.
DR neXtProt; NX_Q99575; -.
DR OpenTargets; ENSG00000104356; -.
DR Orphanet; 93347; Anauxetic dysplasia.
DR PharmGKB; PA134907403; -.
DR VEuPathDB; HostDB:ENSG00000104356; -.
DR eggNOG; KOG3322; Eukaryota.
DR GeneTree; ENSGT00390000017478; -.
DR HOGENOM; CLU_007205_1_2_1; -.
DR InParanoid; Q99575; -.
DR OMA; KALSPMC; -.
DR OrthoDB; 543991at2759; -.
DR PhylomeDB; Q99575; -.
DR TreeFam; TF314236; -.
DR BRENDA; 3.1.26.5; 2681.
DR PathwayCommons; Q99575; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR SignaLink; Q99575; -.
DR BioGRID-ORCS; 10940; 691 hits in 1083 CRISPR screens.
DR ChiTaRS; POP1; human.
DR GeneWiki; POP1_(gene); -.
DR GenomeRNAi; 10940; -.
DR Pharos; Q99575; Tbio.
DR PRO; PR:Q99575; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q99575; protein.
DR Bgee; ENSG00000104356; Expressed in cortical plate and 108 other tissues.
DR ExpressionAtlas; Q99575; baseline and differential.
DR Genevisible; Q99575; HS.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; IDA:UniProtKB.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000172; C:ribonuclease MRP complex; IDA:UniProtKB.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR GO; GO:0033204; F:ribonuclease P RNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
DR GO; GO:0016078; P:tRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR InterPro; IPR039182; Pop1.
DR InterPro; IPR009723; Pop1_N.
DR InterPro; IPR012590; POPLD_dom.
DR PANTHER; PTHR22731; PTHR22731; 1.
DR Pfam; PF06978; POP1; 2.
DR Pfam; PF08170; POPLD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Dwarfism; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; tRNA processing.
FT CHAIN 1..1024
FT /note="Ribonucleases P/MRP protein subunit POP1"
FT /id="PRO_0000058513"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VARIANT 127
FT /note="S -> L (in dbSNP:rs3824145)"
FT /id="VAR_057746"
FT VARIANT 460
FT /note="E -> A (in dbSNP:rs2306131)"
FT /id="VAR_057747"
FT VARIANT 511
FT /note="D -> Y (in ANXD2; dbSNP:rs1060505025)"
FT /evidence="ECO:0000269|PubMed:28067412"
FT /id="VAR_078770"
FT VARIANT 522
FT /note="K -> N (in dbSNP:rs17184326)"
FT /id="VAR_057748"
FT VARIANT 582
FT /note="P -> S (in ANXD2; dbSNP:rs1060505023)"
FT /evidence="ECO:0000269|PubMed:27380734,
FT ECO:0000269|PubMed:28067412"
FT /id="VAR_078771"
FT VARIANT 583
FT /note="G -> E (in ANXD2; dbSNP:rs374828868)"
FT /evidence="ECO:0000269|PubMed:21455487"
FT /id="VAR_067755"
FT VARIANT 675
FT /note="E -> Q (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036232"
FT VARIANT 994
FT /note="L -> V (in dbSNP:rs17856355)"
FT /id="VAR_057749"
SQ SEQUENCE 1024 AA; 114709 MW; A1DB872F3B940C02 CRC64;
MSNAKERKHA KKMRNQPTNV TLSSGFVADR GVKHHSGGEK PFQAQKQEPH PGTSRQRQTR
VNPHSLPDPE VNEQSSSKGM FRKKGGWKAG PEGTSQEIPK YITASTFAQA RAAEISAMLK
AVTQKSSNSL VFQTLPRHMR RRAMSHNVKR LPRRLQEIAQ KEAEKAVHQK KEHSKNKCHK
ARRCHMNRTL EFNRRQKKNI WLETHIWHAK RFHMVKKWGY CLGERPTVKS HRACYRAMTN
RCLLQDLSYY CCLELKGKEE EILKALSGMC NIDTGLTFAA VHCLSGKRQG SLVLYRVNKY
PREMLGPVTF IWKSQRTPGD PSESRQLWIW LHPTLKQDIL EEIKAACQCV EPIKSAVCIA
DPLPTPSQEK SQTELPDEKI GKKRKRKDDG ENAKPIKKII GDGTRDPCLP YSWISPTTGI
IISDLTMEMN RFRLIGPLSH SILTEAIKAA SVHTVGEDTE ETPHRWWIET CKKPDSVSLH
CRQEAIFELL GGITSPAEIP AGTILGLTVG DPRINLPQKK SKALPNPEKC QDNEKVRQLL
LEGVPVECTH SFIWNQDICK SVTENKISDQ DLNRMRSELL VPGSQLILGP HESKIPILLI
QQPGKVTGED RLGWGSGWDV LLPKGWGMAF WIPFIYRGVR VGGLKESAVH SQYKRSPNVP
GDFPDCPAGM LFAEEQAKNL LEKYKRRPPA KRPNYVKLGT LAPFCCPWEQ LTQDWESRVQ
AYEEPSVASS PNGKESDLRR SEVPCAPMPK KTHQPSDEVG TSIEHPREAE EVMDAGCQES
AGPERITDQE ASENHVAATG SHLCVLRSRK LLKQLSAWCG PSSEDSRGGR RAPGRGQQGL
TREACLSILG HFPRALVWVS LSLLSKGSPE PHTMICVPAK EDFLQLHEDW HYCGPQESKH
SDPFRSKILK QKEKKKREKR QKPGRASSDG PAGEEPVAGQ EALTLGLWSG PLPRVTLHCS
RTLLGFVTQG DFSMAVGCGE ALGFVSLTGL LDMLSSQPAA QRGLVLLRPP ASLQYRFARI
AIEV
