KRI1_HUMAN
ID KRI1_HUMAN Reviewed; 703 AA.
AC Q8N9T8; Q2M1R5; Q2M1R7; Q7L5J7; Q96G92; Q9BU50; Q9H6I1; Q9H978;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein KRI1 homolog;
GN Name=KRI1;
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], AND VARIANTS LYS-266; GLN-349 AND
RP PRO-703.
RC TISSUE=Teratocarcinoma, and Trachea;
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].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-703, AND VARIANTS ARG-138;
RP LYS-266; GLN-349 AND PRO-703.
RC TISSUE=Lung, and Ovary;
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-136 AND SER-171, AND
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-628 AND SER-639, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91; SER-93; SER-94; SER-95;
RP SER-97; SER-136; SER-141; SER-171; SER-280; SER-281 AND SER-639, 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-280, AND
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-171; SER-622;
RP SER-628 AND SER-639, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91; SER-95; SER-97; SER-136;
RP SER-171 AND SER-639, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-136; SER-163; SER-171;
RP SER-309 AND SER-628, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-171; SER-280;
RP SER-281 AND SER-628, VARIANT [LARGE SCALE ANALYSIS] LYS-266, AND
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).
CC -!- SIMILARITY: Belongs to the KRI1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14357.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15278.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04240.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AK023011; BAB14357.1; ALT_INIT; mRNA.
DR EMBL; AK025907; BAB15278.1; ALT_INIT; mRNA.
DR EMBL; AK093879; BAC04240.1; ALT_SEQ; mRNA.
DR EMBL; AC011461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002890; AAH02890.3; -; mRNA.
DR EMBL; BC009876; AAH09876.2; -; mRNA.
DR EMBL; BC112249; AAI12250.1; -; mRNA.
DR EMBL; BC112251; AAI12252.1; -; mRNA.
DR CCDS; CCDS12242.1; -.
DR RefSeq; NP_075384.3; NM_023008.3.
DR AlphaFoldDB; Q8N9T8; -.
DR SMR; Q8N9T8; -.
DR BioGRID; 122394; 215.
DR IntAct; Q8N9T8; 67.
DR MINT; Q8N9T8; -.
DR STRING; 9606.ENSP00000320917; -.
DR GlyGen; Q8N9T8; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8N9T8; -.
DR PhosphoSitePlus; Q8N9T8; -.
DR BioMuta; KRI1; -.
DR DMDM; 550544300; -.
DR EPD; Q8N9T8; -.
DR jPOST; Q8N9T8; -.
DR MassIVE; Q8N9T8; -.
DR MaxQB; Q8N9T8; -.
DR PaxDb; Q8N9T8; -.
DR PeptideAtlas; Q8N9T8; -.
DR PRIDE; Q8N9T8; -.
DR ProteomicsDB; 72582; -.
DR Antibodypedia; 53207; 91 antibodies from 18 providers.
DR DNASU; 65095; -.
DR Ensembl; ENST00000312962.12; ENSP00000320917.9; ENSG00000129347.21.
DR GeneID; 65095; -.
DR KEGG; hsa:65095; -.
DR MANE-Select; ENST00000312962.12; ENSP00000320917.9; NM_023008.5; NP_075384.4.
DR UCSC; uc002moy.2; human.
DR CTD; 65095; -.
DR DisGeNET; 65095; -.
DR GeneCards; KRI1; -.
DR HGNC; HGNC:25769; KRI1.
DR HPA; ENSG00000129347; Low tissue specificity.
DR neXtProt; NX_Q8N9T8; -.
DR OpenTargets; ENSG00000129347; -.
DR PharmGKB; PA162393682; -.
DR VEuPathDB; HostDB:ENSG00000129347; -.
DR eggNOG; KOG2409; Eukaryota.
DR GeneTree; ENSGT00390000005605; -.
DR HOGENOM; CLU_009647_0_1_1; -.
DR InParanoid; Q8N9T8; -.
DR OMA; QWRKETF; -.
DR OrthoDB; 572360at2759; -.
DR TreeFam; TF320278; -.
DR PathwayCommons; Q8N9T8; -.
DR SignaLink; Q8N9T8; -.
DR BioGRID-ORCS; 65095; 405 hits in 622 CRISPR screens.
DR ChiTaRS; KRI1; human.
DR GenomeRNAi; 65095; -.
DR Pharos; Q8N9T8; Tdark.
DR PRO; PR:Q8N9T8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8N9T8; protein.
DR Bgee; ENSG00000129347; Expressed in sural nerve and 181 other tissues.
DR ExpressionAtlas; Q8N9T8; baseline and differential.
DR Genevisible; Q8N9T8; HS.
DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR InterPro; IPR018034; Kri1.
DR InterPro; IPR024626; Kri1-like_C.
DR PANTHER; PTHR14490; PTHR14490; 1.
DR Pfam; PF05178; Kri1; 1.
DR Pfam; PF12936; Kri1_C; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..703
FT /note="Protein KRI1 homolog"
FT /id="PRO_0000298976"
FT REGION 27..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..266
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..432
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VARIANT 138
FT /note="G -> R (in dbSNP:rs12984043)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034751"
FT VARIANT 179
FT /note="E -> A (in dbSNP:rs11545166)"
FT /id="VAR_034752"
FT VARIANT 266
FT /note="E -> K (in dbSNP:rs3745249)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:24275569"
FT /id="VAR_034753"
FT VARIANT 309
FT /note="S -> L (in dbSNP:rs34743532)"
FT /id="VAR_034754"
FT VARIANT 336
FT /note="R -> W (in dbSNP:rs33999611)"
FT /id="VAR_034755"
FT VARIANT 349
FT /note="E -> Q (in dbSNP:rs3826709)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_034756"
FT VARIANT 445
FT /note="L -> P (in dbSNP:rs1982074)"
FT /id="VAR_034757"
FT VARIANT 703
FT /note="S -> P (in dbSNP:rs3087689)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_034758"
FT CONFLICT 165
FT /note="R -> W (in Ref. 1; BAC04240)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="E -> G (in Ref. 1; BAB14357)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="D -> G (in Ref. 1; BAB14357)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="S -> N (in Ref. 1; BAC04240)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="K -> E (in Ref. 1; BAC04240)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="K -> E (in Ref. 1; BAB15278)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="E -> G (in Ref. 1; BAB15278)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 703 AA; 82598 MW; 0C34E54AB1250141 CRC64;
MPEPRGSSQL RVNAAFAARY NRYREREELQ RLKDRYGDRD SSSDSSSESD SSDERVEFDP
QQERDFYKTL SLLKKKDPRI YQKDATFYNR TASSSDSEED PEALEKQKKV RPMYLKDYER
KVILEKAGKY VDEENSDGET SNHRLQETSS QSYVEEQKQL KESFRAFVED SEDEDGAGEG
GSSLLQKRAK TRQEKAQEEA DYIEWLKGQK EIRNPDSLKE LTHLKEYWND PELDEGERFL
RDYILNKRYE EEEEEEEDEE EMEEEEGVHG PPVQLAVDDS SDEGELFLKK QEDFEQKYNF
RFEEPDSASV KTYPRSIASS VRRKDERRKE KREETRERKK REKAKKQEEL KQLKNLKRKE
ILAKLEKLRK VTGNEMLGLE EGDLEDDFDP AQHDQLMQKC FGDEYYGAVE EEKPQFEEEE
GLEDDWNWDT WDGPEQEGDW SQQELHCEDP NFNMDADYDP SQPRKKKREA PLTGKKKRKS
PFAAAVGQEK PVFEPGDKTF EEYLDEYYRL DYEDIIDDLP CRFKYRTVVP CDFGLSTEEI
LAADDKELNR WCSLKKTCMY RSEQEELRDK RAYSQKAQNS WKKRQVFKSL CREEAETPAE
ATGKPQRDEA GPQRQLPALD GSLMGPESPP AQEEEAPVSP HKKPAPQKRR RAKKARLLGP
TVMLGGCEFS RQRLQAFGLN PKRLHFRQLG RQRRKQQGPK NSS
