KRI1_MOUSE
ID KRI1_MOUSE Reviewed; 704 AA.
AC Q8VDQ9;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 3.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Protein KRI1 homolog;
GN Name=Kri1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-704.
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-177; SER-178 AND
RP SER-182, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-177; SER-178 AND
RP SER-182, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SIMILARITY: Belongs to the KRI1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21438.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH21438.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown at the N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC122525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021438; AAH21438.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; Q8VDQ9; -.
DR SMR; Q8VDQ9; -.
DR STRING; 10090.ENSMUSP00000039688; -.
DR iPTMnet; Q8VDQ9; -.
DR PhosphoSitePlus; Q8VDQ9; -.
DR EPD; Q8VDQ9; -.
DR jPOST; Q8VDQ9; -.
DR MaxQB; Q8VDQ9; -.
DR PaxDb; Q8VDQ9; -.
DR PeptideAtlas; Q8VDQ9; -.
DR PRIDE; Q8VDQ9; -.
DR ProteomicsDB; 263463; -.
DR MGI; MGI:2384899; Kri1.
DR eggNOG; KOG2409; Eukaryota.
DR InParanoid; Q8VDQ9; -.
DR ChiTaRS; Kri1; mouse.
DR PRO; PR:Q8VDQ9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VDQ9; protein.
DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
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..704
FT /note="Protein KRI1 homolog"
FT /id="PRO_0000298977"
FT REGION 29..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..270
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..704
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
SQ SEQUENCE 704 AA; 82057 MW; 8C7D2E5703137C2F CRC64;
MPEPRASGCL KVNAAFAARY SRYREREELQ RLKDRYGDPD VGGDSSSESD SSDEHVEFDP
QQERDFYRTL SLLKKKDPRI YQKDATFYQR TAEASSSESE EEPPAALGKQ EKQQKQQPMY
LKDYERKVIL EKGGKYVDED NSDGETVDHR LQETSTKSYV EEQKQLKESF RAFVEDSSDE
DSAGEGGSGL LQKHTKSREE KAQEEVDYLE WLKGQKDMDS SESLKELTHL KEYWNNPGLD
EGEQFLRDYI LNKRYEEEEE EEEEEEEEGA PGPPVQLAVD DSSDEGELFL KKQEDFEHKY
NFRFEEPDSA SVKTYPRSIA SSVRRKDERR KEKREETRER KKREKARKQE ELKQLKNLKR
KEILAKLEKL RQATGNETLG LEEQDLEADF DPAQHDQLMQ KCFGDAFYGT AEEEKPQFEE
EDGLEDDWNW DMWGGPEQDG AWSQQELHCE DPDFNMDADY DPSQPRKKLR EAPTSGKRKR
KSPFAAAVGQ EKPMFDPGDK TFEEYLDEYY RLDYEDIIDD LPCRFKYRTV VPCDFGLSTE
EILSADDKEL NRWCSLKKTC MYRSEQEEMQ EQRVYSQKAQ NMWKKRQIFK SLCQEEMEMS
TEATGKSQSK ASPQVQLPTP NGADQRTPQA ETLVSKEEGL AHTSCPEKPA SQKQKSKKAR
LLGPTVTLGG HKFSRQRLQA FGLNPKRLHF RQLGRQRKKQ QSHS
