M18BP_MOUSE
ID M18BP_MOUSE Reviewed; 998 AA.
AC Q80WQ8; Q571G6; Q8BPR7; Q8CBB5; Q8CG92;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Mis18-binding protein 1;
DE AltName: Full=Kinetochore-associated protein KNL-2 homolog;
GN Name=Mis18bp1; Synonyms=Kiaa1903, Knl2, M18bp1;
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 MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Bone, and Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Embryo, and 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 172-998 (ISOFORM 1).
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-516 AND THR-578, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Spleen, 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).
RN [5]
RP INTERACTION WITH FLNA.
RX PubMed=21228480; DOI=10.1271/bbb.100567;
RA Qiu H., Nomiyama R., Moriguchi K., Fukada T., Sugimoto K.;
RT "Identification of novel nuclear protein interactions with the N-terminal
RT part of filamin A.";
RL Biosci. Biotechnol. Biochem. 75:145-147(2011).
CC -!- FUNCTION: Required for recruitment of CENPA to centromeres and normal
CC chromosome segregation during mitosis. {ECO:0000250|UniProtKB:Q6P0N0}.
CC -!- SUBUNIT: Interacts with SP1. Interacts with MIS18A. Identified in a
CC complex containing MIS18A, OIP5/MIS18B, MIS18BP1, RBBP7 and RBBP4.
CC Interacts with KAT7/HBO1 (By similarity). Interacts (via N-terminus)
CC with FLNA (via N-terminus) (PubMed:21228480).
CC {ECO:0000250|UniProtKB:Q6P0N0, ECO:0000269|PubMed:21228480}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6P0N0}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:Q6P0N0}. Note=Associated
CC with centromeres in interphase cells, from late anaphase to the G1
CC phase. Not detected on centromeres during earlier phases of mitosis.
CC Associated with chromatin. {ECO:0000250|UniProtKB:Q6P0N0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80WQ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80WQ8-2; Sequence=VSP_037732, VSP_037733;
CC Name=3;
CC IsoId=Q80WQ8-3; Sequence=VSP_037731;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK036395; BAC29410.1; -; mRNA.
DR EMBL; AK053496; BAC35403.1; -; mRNA.
DR EMBL; AK162657; BAE37008.1; -; mRNA.
DR EMBL; BC042728; AAH42728.1; -; mRNA.
DR EMBL; BC052175; AAH52175.1; -; mRNA.
DR EMBL; AK220223; BAD90148.1; -; mRNA.
DR CCDS; CCDS25942.1; -. [Q80WQ8-1]
DR RefSeq; NP_766166.2; NM_172578.2. [Q80WQ8-1]
DR AlphaFoldDB; Q80WQ8; -.
DR SMR; Q80WQ8; -.
DR BioGRID; 229939; 9.
DR ComplexPortal; CPX-3273; Mis18 complex.
DR STRING; 10090.ENSMUSP00000052109; -.
DR iPTMnet; Q80WQ8; -.
DR PhosphoSitePlus; Q80WQ8; -.
DR EPD; Q80WQ8; -.
DR jPOST; Q80WQ8; -.
DR MaxQB; Q80WQ8; -.
DR PaxDb; Q80WQ8; -.
DR PeptideAtlas; Q80WQ8; -.
DR PRIDE; Q80WQ8; -.
DR ProteomicsDB; 295741; -. [Q80WQ8-1]
DR ProteomicsDB; 295742; -. [Q80WQ8-2]
DR ProteomicsDB; 295743; -. [Q80WQ8-3]
DR Antibodypedia; 12; 60 antibodies from 14 providers.
DR DNASU; 217653; -.
DR Ensembl; ENSMUST00000052201; ENSMUSP00000052109; ENSMUSG00000047534. [Q80WQ8-1]
DR Ensembl; ENSMUST00000222244; ENSMUSP00000152490; ENSMUSG00000047534. [Q80WQ8-2]
DR GeneID; 217653; -.
DR KEGG; mmu:217653; -.
DR UCSC; uc007nrg.2; mouse. [Q80WQ8-1]
DR UCSC; uc007nri.1; mouse. [Q80WQ8-3]
DR UCSC; uc011ymg.1; mouse. [Q80WQ8-2]
DR CTD; 55320; -.
DR MGI; MGI:2145099; Mis18bp1.
DR VEuPathDB; HostDB:ENSMUSG00000047534; -.
DR eggNOG; ENOG502QRUS; Eukaryota.
DR GeneTree; ENSGT00390000007395; -.
DR HOGENOM; CLU_009019_1_0_1; -.
DR InParanoid; Q80WQ8; -.
DR OMA; MCHSNCQ; -.
DR OrthoDB; 815579at2759; -.
DR PhylomeDB; Q80WQ8; -.
DR TreeFam; TF106401; -.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR BioGRID-ORCS; 217653; 22 hits in 77 CRISPR screens.
DR ChiTaRS; Mis18bp1; mouse.
DR PRO; PR:Q80WQ8; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q80WQ8; protein.
DR Bgee; ENSMUSG00000047534; Expressed in metanephric ureteric bud and 173 other tissues.
DR ExpressionAtlas; Q80WQ8; baseline and differential.
DR Genevisible; Q80WQ8; MM.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR039110; KNL2-like.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR015216; SANTA.
DR PANTHER; PTHR16124; PTHR16124; 1.
DR Pfam; PF09133; SANTA; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW DNA-binding; Isopeptide bond; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..998
FT /note="Mis18-binding protein 1"
FT /id="PRO_0000379895"
FT DOMAIN 336..422
FT /note="SANTA"
FT DOMAIN 741..796
FT /note="SANT"
FT REGION 122..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT MOD_RES 516
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 578
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT MOD_RES 688
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT MOD_RES 955
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT CROSSLNK 707
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT CROSSLNK 765
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT CROSSLNK 821
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT CROSSLNK 828
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT CROSSLNK 847
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT CROSSLNK 948
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6P0N0"
FT VAR_SEQ 433..998
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037731"
FT VAR_SEQ 433..434
FT /note="AE -> EN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037732"
FT VAR_SEQ 435..998
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037733"
FT CONFLICT 226
FT /note="T -> I (in Ref. 3; BAD90148)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="T -> A (in Ref. 1; BAC29410)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 998 AA; 113956 MW; E0194CC994543C8F CRC64;
MIVTPLKHSG IHLSSGTLQR RNMPLDAVFI DSIPSGTLTP LKDLVKYQKS SLKVNGHKKN
QLLEIRTSNN KDLFQSTMLS EATLPNSSLD ISVIKPSMDR LRNEMIYESP GKIFQRMKAK
VQRDKQEQLT RSSSMLGSPQ GEHTKDFPPN TDKKAQLQQT YICEEKQTSV QSNDPSLGDP
PILNQEQKNV SASCISKKAL TRAQFGGQVL HSKESPVRIT VSKKNTFVLG GIDCTYEKFE
NTDVNTISSL CVPIKNHSQS ITSDNDVTTE RTAKEDITEP NEEMMSRRTI LQDPIKNTSK
IKRSSPRPNL TLSGRSQRKC TKLETVVKEV KKYQAVHLQE WMIKVINNNT AICVEGKLVD
MTDVYWHSNV IIERIKHNEL RTLSGNIYIL KGLIDSVSMK EAGYPCYLTR KFMFGFPHNW
KEHIDKFLEQ LRAEKKNKTR QETARVQEKQ KSKKKDAEDK ETYVLQKASI TYDLNDNSLE
RTEVPTDPLN SLEQPTSGKE RRHPLLSQKR AYVLITPLRN KKLIEQRCID YSLSIEGISD
FFKAKHQEES DSDIHGTPSS TSKSQETFEH RVGFEGNTKE DCNECDIITA RHIQIPCPKS
KQMLTNDFMK KNKLPSKLQK TENQIGVSQY CRSSSHLSSE ENEVEIKSRT RARNTKERLN
RERENTNHIT KDILLISETE GERACYITPK RPRSCYITPK RPRSSAKESH YKSAVSKDFL
TEGKASDRTS RQLLDHLPGL TDDEEWSEQE LQKLHCAFTS LPKHKPGFWS DVAMAVGSRT
ADECQKKYTE EPQGQGSRKH GSKKKQANKV QNGEKDSADA KTIKITAKVG TLKRKRQMRD
CLEHLAKDNH DDFFTATPLQ KQRIQLPSFQ YSQDDDFLLD MDRDPASPSS IITSPLRSTT
PQCQHFSPSM LAAIERNNCD RYVYQMQKNA KKYGKSNGGL VWGNIRKKTV KTDLSSPPPT
RKALFNKDLG KNTDISKYFI DDTESDEEEK DYYFSNSD
