NSL1_HUMAN
ID NSL1_HUMAN Reviewed; 281 AA.
AC Q96IY1; E7ETD5; Q5SY75; Q9H2M5; Q9NRN8; Q9Y415;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Kinetochore-associated protein NSL1 homolog;
GN Name=NSL1; Synonyms=C1orf48; ORFNames=DC31, DC8, MIS14;
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] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Li Y., Peng Y., Li N., Gu W., Han Z., Fu G., Chen Z.;
RT "Novel genes expressed in human dendritic cell.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-254.
RC TISSUE=Dendritic cell;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PHE-4 AND
RP VAL-254.
RC TISSUE=Urinary bladder;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-281 (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP INTERACTION WITH DSN1 AND MIS12, AND SUBCELLULAR LOCATION.
RX PubMed=15502821; DOI=10.1038/ncb1187;
RA Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y., Yanagida M.;
RT "A conserved Mis12 centromere complex is linked to heterochromatic HP1 and
RT outer kinetochore protein Zwint-1.";
RL Nat. Cell Biol. 6:1135-1141(2004).
RN [7]
RP FUNCTION, COMPONENT OF MIS12 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=16585270; DOI=10.1083/jcb.200509158;
RA Kline S.L., Cheeseman I.M., Hori T., Fukagawa T., Desai A.;
RT "The human Mis12 complex is required for kinetochore assembly and proper
RT chromosome segregation.";
RL J. Cell Biol. 173:9-17(2006).
RN [8]
RP INTERACTION WITH KNL1.
RX PubMed=17981135; DOI=10.1016/j.devcel.2007.09.005;
RA Kiyomitsu T., Obuse C., Yanagida M.;
RT "Human Blinkin/AF15q14 is required for chromosome alignment and the mitotic
RT checkpoint through direct interaction with Bub1 and BubR1.";
RL Dev. Cell 13:663-676(2007).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND IDENTIFICATION BY
RP 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Part of the MIS12 complex which is required for normal
CC chromosome alignment and segregation and kinetochore formation during
CC mitosis. {ECO:0000269|PubMed:16585270}.
CC -!- SUBUNIT: Component of the MIS12 complex composed of MIS12, DSN1,
CC NSL1/DC8 and PMF1. Interacts with KNL1. {ECO:0000269|PubMed:15502821,
CC ECO:0000269|PubMed:17981135}.
CC -!- INTERACTION:
CC Q96IY1; P45973: CBX5; NbExp=6; IntAct=EBI-2554690, EBI-78219;
CC Q96IY1; P37173: TGFBR2; NbExp=3; IntAct=EBI-2554690, EBI-296151;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15502821,
CC ECO:0000269|PubMed:16585270}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}.
CC Note=Associated with the kinetochore (PubMed:15502821,
CC PubMed:16585270).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96IY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96IY1-2; Sequence=VSP_045741;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF86877.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF201941; AAF86877.1; ALT_FRAME; mRNA.
DR EMBL; AF255793; AAG44640.1; -; mRNA.
DR EMBL; AC104333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007067; AAH07067.1; -; mRNA.
DR EMBL; AL050084; CAB43260.1; -; mRNA.
DR CCDS; CCDS1509.1; -. [Q96IY1-1]
DR CCDS; CCDS53474.1; -. [Q96IY1-2]
DR PIR; T08737; T08737.
DR RefSeq; NP_001036014.1; NM_001042549.1. [Q96IY1-2]
DR RefSeq; NP_056286.3; NM_015471.3. [Q96IY1-1]
DR PDB; 4NF9; X-ray; 2.80 A; C/D=256-281.
DR PDB; 5LSI; X-ray; 2.00 A; E=29-99.
DR PDB; 5LSJ; X-ray; 3.25 A; G/N=92-206.
DR PDB; 5LSK; X-ray; 3.50 A; N=1-206.
DR PDBsum; 4NF9; -.
DR PDBsum; 5LSI; -.
DR PDBsum; 5LSJ; -.
DR PDBsum; 5LSK; -.
DR AlphaFoldDB; Q96IY1; -.
DR SMR; Q96IY1; -.
DR BioGRID; 117433; 56.
DR ComplexPortal; CPX-5643; Kinetochore MIS12 complex.
DR CORUM; Q96IY1; -.
DR IntAct; Q96IY1; 26.
DR MINT; Q96IY1; -.
DR STRING; 9606.ENSP00000355944; -.
DR GlyGen; Q96IY1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96IY1; -.
DR PhosphoSitePlus; Q96IY1; -.
DR BioMuta; NSL1; -.
DR DMDM; 147744577; -.
DR EPD; Q96IY1; -.
DR jPOST; Q96IY1; -.
DR MassIVE; Q96IY1; -.
DR MaxQB; Q96IY1; -.
DR PaxDb; Q96IY1; -.
DR PeptideAtlas; Q96IY1; -.
DR PRIDE; Q96IY1; -.
DR ProteomicsDB; 18182; -.
DR ProteomicsDB; 76867; -. [Q96IY1-1]
DR Antibodypedia; 34610; 107 antibodies from 21 providers.
DR DNASU; 25936; -.
DR Ensembl; ENST00000366977.8; ENSP00000355944.3; ENSG00000117697.15. [Q96IY1-1]
DR Ensembl; ENST00000626725.1; ENSP00000486783.1; ENSG00000117697.15. [Q96IY1-2]
DR GeneID; 25936; -.
DR KEGG; hsa:25936; -.
DR MANE-Select; ENST00000366977.8; ENSP00000355944.3; NM_015471.4; NP_056286.3.
DR UCSC; uc001hjn.4; human. [Q96IY1-1]
DR CTD; 25936; -.
DR DisGeNET; 25936; -.
DR GeneCards; NSL1; -.
DR HGNC; HGNC:24548; NSL1.
DR HPA; ENSG00000117697; Low tissue specificity.
DR MIM; 609174; gene.
DR neXtProt; NX_Q96IY1; -.
DR OpenTargets; ENSG00000117697; -.
DR PharmGKB; PA162398188; -.
DR VEuPathDB; HostDB:ENSG00000117697; -.
DR eggNOG; ENOG502S001; Eukaryota.
DR GeneTree; ENSGT00390000001374; -.
DR HOGENOM; CLU_086065_0_0_1; -.
DR InParanoid; Q96IY1; -.
DR OMA; LRDVQWT; -.
DR PhylomeDB; Q96IY1; -.
DR TreeFam; TF333388; -.
DR PathwayCommons; Q96IY1; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q96IY1; -.
DR SIGNOR; Q96IY1; -.
DR BioGRID-ORCS; 25936; 611 hits in 1093 CRISPR screens.
DR ChiTaRS; NSL1; human.
DR GeneWiki; NSL1; -.
DR GenomeRNAi; 25936; -.
DR Pharos; Q96IY1; Tbio.
DR PRO; PR:Q96IY1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96IY1; protein.
DR Bgee; ENSG00000117697; Expressed in secondary oocyte and 209 other tissues.
DR ExpressionAtlas; Q96IY1; baseline and differential.
DR Genevisible; Q96IY1; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IDA:WormBase.
DR GO; GO:0000444; C:MIS12/MIND type complex; IDA:UniProtKB.
DR GO; GO:0031617; C:NMS complex; IC:ComplexPortal.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR InterPro; IPR013950; Mis14/Nsl1.
DR PANTHER; PTHR31749; PTHR31749; 1.
DR Pfam; PF08641; Mis14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; Chromosome partition; Kinetochore; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..281
FT /note="Kinetochore-associated protein NSL1 homolog"
FT /id="PRO_0000089260"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 167..281
FT /note="APHMENLKCRGETVAKEISEAMKSLPALIEQGEGFSQVLRMQPVIHLQRIHQ
FT EVFSSCHRKPDAKPENFITQIETTPTETASRKTSDMVLKRKQTKDCPQRKWYPLRPKKI
FT NLDT -> VLNGNAFNFSPFNMMLAVDLSYMVFITSSPSYGKFEMQRGNSSKGDQ (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_045741"
FT VARIANT 4
FT /note="S -> F (in dbSNP:rs17856201)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_051243"
FT VARIANT 254
FT /note="M -> V (in dbSNP:rs15702)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_016005"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:5LSI"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:5LSI"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:5LSI"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5LSI"
FT HELIX 69..85
FT /evidence="ECO:0007829|PDB:5LSI"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5LSI"
FT HELIX 106..149
FT /evidence="ECO:0007829|PDB:5LSJ"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:5LSJ"
FT HELIX 170..200
FT /evidence="ECO:0007829|PDB:5LSJ"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:4NF9"
SQ SEQUENCE 281 AA; 32162 MW; F9FB4379BAFF2626 CRC64;
MAGSPELVVL DPPWDKELAA GTESQALVSA TPREDFRVRC TSKRAVTEML QLCGRFVQKL
GDALPEEIRE PALRDAQWTF ESAVQENISI NGQAWQEASD NCFMDSDIKV LEDQFDEIIV
DIATKRKQYP RKILECVIKT IKAKQEILKQ YHPVVHPLDL KYDPDPAPHM ENLKCRGETV
AKEISEAMKS LPALIEQGEG FSQVLRMQPV IHLQRIHQEV FSSCHRKPDA KPENFITQIE
TTPTETASRK TSDMVLKRKQ TKDCPQRKWY PLRPKKINLD T
