LOCUS       NP_060823               1132 aa            linear   PRI 12-JUN-2025
DEFINITION  mis18-binding protein 1 [Homo sapiens].
ACCESSION   NP_060823
VERSION     NP_060823.3
DBSOURCE    REFSEQ: accession NM_018353.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Thamkachy,R., Medina-Pritchard,B., Park,S.H., Chiodi,C.G., Zou,J.,
            de la Torre-Barranco,M., Shimanaka,K., Abad,M.A., Gallego
            Paramo,C., Feederle,R., Ruksenaite,E., Heun,P., Davies,O.R.,
            Rappsilber,J., Schneidman-Duhovny,D., Cho,U.S. and Jeyaprakash,A.A.
  TITLE     Structural basis for Mis18 complex assembly and its implications
            for centromere maintenance
  JOURNAL   EMBO Rep 25 (8), 3348-3372 (2024)
   PUBMED   38951710
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Cuijpers,S.A.G., Willemstein,E. and Vertegaal,A.C.O.
  TITLE     Converging Small Ubiquitin-like Modifier (SUMO) and Ubiquitin
            Signaling: Improved Methodology Identifies Co-modified Target
            Proteins
  JOURNAL   Mol Cell Proteomics 16 (12), 2281-2295 (2017)
   PUBMED   28951443
  REMARK    GeneRIF: Results confirm the regulation of MIS18BP1 via
            SUMO-ubiquitin crosstalk during mitosis.
REFERENCE   4  (residues 1 to 1132)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 1132)
  AUTHORS   Pan,D., Klare,K., Petrovic,A., Take,A., Walstein,K., Singh,P.,
            Rondelet,A., Bird,A.W. and Musacchio,A.
  TITLE     CDK-regulated dimerization of M18BP1 on a Mis18 hexamer is
            necessary for CENP-A loading
  JOURNAL   Elife 6, e23352 (2017)
   PUBMED   28059702
  REMARK    GeneRIF: The authors demonstrate that CDK1 controls Mis18 complex
            recruitment to centromeres by regulating oligomerization of M18BP1
            through the Mis18alpha:Mis18beta scaffold.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1132)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 1132)
  AUTHORS   Maddox,P.S., Hyndman,F., Monen,J., Oegema,K. and Desai,A.
  TITLE     Functional genomics identifies a Myb domain-containing protein
            family required for assembly of CENP-A chromatin
  JOURNAL   J Cell Biol 176 (6), 757-763 (2007)
   PUBMED   17339379
REFERENCE   8  (residues 1 to 1132)
  AUTHORS   Fujita,Y., Hayashi,T., Kiyomitsu,T., Toyoda,Y., Kokubu,A., Obuse,C.
            and Yanagida,M.
  TITLE     Priming of centromere for CENP-A recruitment by human hMis18alpha,
            hMis18beta, and M18BP1
  JOURNAL   Dev Cell 12 (1), 17-30 (2007)
   PUBMED   17199038
  REMARK    GeneRIF: Three human proteins essential for centromere/kinetochore
            structure and function, hMis18alpha, hMis18beta, and M18BP1, the
            complex of which is accumulated specifically at the telophase-G1
            centromere, are identified.[Mis18alpha, Mis18beta, M18BP1]
REFERENCE   9  (residues 1 to 1132)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 1132)
  AUTHORS   Gunther,M., Laithier,M. and Brison,O.
  TITLE     A set of proteins interacting with transcription factor Sp1
            identified in a two-hybrid screening
  JOURNAL   Mol Cell Biochem 210 (1-2), 131-142 (2000)
   PUBMED   10976766
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB067490.1, BC065544.1 and AW971491.1.
            
            On Feb 6, 2004 this sequence version replaced NP_060823.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC065544.1, SRR1660805.98110.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310806.9/ ENSP00000309790.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q21.2"
     Protein         1..1132
                     /product="mis18-binding protein 1"
                     /note="putative protein p243 which interacts with
                     transcription factor Sp1; kinetochore null 2 homolog;
                     kinetochore-associated protein KNL-2 homolog; P243;
                     hsKNL-2"
                     /calculated_mol_wt=128955
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Region          123..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Region          306..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Region          383..470
                     /region_name="SANTA"
                     /note="SANTA (SANT Associated); pfam09133"
                     /db_xref="CDD:462689"
     Region          482..518
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Region          765..798
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            773
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Region          879..925
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cd00167"
                     /db_xref="CDD:238096"
     Site            order(880,913..914,916..917,919..921,923..925)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     Region          923..957
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            1008
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            1086
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            1087
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            1089
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            1104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            1116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     CDS             1..1132
                     /gene="MIS18BP1"
                     /gene_synonym="C14orf106; HSA242977; KNL2; M18BP1"
                     /coded_by="NM_018353.5:260..3658"
                     /db_xref="CCDS:CCDS9684.1"
                     /db_xref="GeneID:55320"
                     /db_xref="HGNC:HGNC:20190"
                     /db_xref="MIM:618139"
ORIGIN      
        1 miatplkhsr iylppeassq rrnlpmdaif fdsipsgtlt pvkdlvkyqn sslklndhkk
       61 nqflkmttfn nknifqstml teattsnssl disaikpnkd glknkanyes pgkiflrmke
      121 kvlrdkqeqp srnssllepq ksgnnetftp nrvekkklqh tylceekenn ksfqsddssl
      181 rasvqgvple ssnndiflpv kqkiqcqqek kaplhnltye lptlnqeqen flavearnkt
      241 ltraqlakqi fhskesivat tkskkdtfvl esvdsadeqf qntnaetlst ncipikngsl
      301 lmvsdsertt egtsqqkvke gngktvpget glpgsmkdtc kivlatprlh itiprrskrn
      361 isklspprif qtvtnglkkn qvvqlqewmi ksinnntaic vegklidvtn iywhsnviie
      421 riehnklrti sgnvyilkgm idqismkeag ypnylirkfm fgfpenwkeh idnfleqlra
      481 geknrektkq kqktgrsvrd irksmkndar enqtdtaqra tttydfdcdn lelksnkhse
      541 spgatelnmc hsncqnkptl rfpddqvnnt iqngggddls nqeligkkey kmsskklkig
      601 ertneriiks qkqetteeld vsidiltsre qffsdeerky mainqkkayi lvtplksrkv
      661 ieqrcmrynl sagtikavtd fvipecqkks pisksmgtle ntfeghkskn kedcderdll
      721 tvnrkikisn lekeqmltsd fkkntrllpk lkkienqvam sfykhqsspd lsseesetek
      781 eikrkaevkk tkagntkeav vhlrkstrnt snipvilepe teesenefyi kqkkarpsvk
      841 etlqksgvrk efpiteavgs dktnrhplec lpgliqdkew nekelqklhc afaslpkhkp
      901 gfwsevaaav gsrspeecqr kymenprgkg sqkhvtkkkp anskgqngkr gdadqkqtik
      961 itakvgtlkr kqqmrefleq lpkddhddff sttplqhqri llpsfqdsed dddilpnmdk
     1021 npttpssvif plvktpqcqh vspgmlgsin rndcdkyvfr mqkyhksngg ivwgnikkkl
     1081 vetdfstptp rrktpfntdl gensgigklf tnavesldee ekdyyfsnsd sa
//
