KNOP1_HUMAN
ID KNOP1_HUMAN Reviewed; 458 AA.
AC Q1ED39; O43328; Q5FWF3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Lysine-rich nucleolar protein 1;
DE AltName: Full=Protein FAM191A;
DE AltName: Full=Testis-specific gene 118 protein;
GN Name=KNOP1; Synonyms=C16orf88, FAM191A, TSG118;
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 GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic stem cell, and Lymph;
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-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-50; SER-265; THR-308
RP AND THR-310, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-111, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-111; SER-132; SER-265
RP AND THR-310, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP 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).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-430, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-275 AND LYS-407, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-373, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-101; LYS-130; LYS-249;
RP LYS-275; LYS-287; LYS-305; LYS-319; LYS-353; LYS-373; LYS-375; LYS-407 AND
RP LYS-442, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- SUBUNIT: Interacts with ZNF106. {ECO:0000250}.
CC -!- INTERACTION:
CC Q1ED39; Q96CW1: AP2M1; NbExp=3; IntAct=EBI-9977982, EBI-297683;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC05805.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH89430.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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; AC002550; AAC05805.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC089430; AAH89430.1; ALT_SEQ; mRNA.
DR EMBL; BC117562; AAI17563.1; -; mRNA.
DR CCDS; CCDS42127.1; -.
DR RefSeq; NP_001013009.2; NM_001012991.2.
DR RefSeq; NP_001335457.1; NM_001348528.1.
DR RefSeq; NP_001335458.1; NM_001348529.1.
DR RefSeq; NP_001335459.1; NM_001348530.1.
DR RefSeq; NP_001335460.1; NM_001348531.1.
DR AlphaFoldDB; Q1ED39; -.
DR BioGRID; 134613; 263.
DR IntAct; Q1ED39; 69.
DR STRING; 9606.ENSP00000219837; -.
DR GlyGen; Q1ED39; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q1ED39; -.
DR PhosphoSitePlus; Q1ED39; -.
DR BioMuta; KNOP1; -.
DR DMDM; 121940661; -.
DR EPD; Q1ED39; -.
DR jPOST; Q1ED39; -.
DR MassIVE; Q1ED39; -.
DR MaxQB; Q1ED39; -.
DR PaxDb; Q1ED39; -.
DR PeptideAtlas; Q1ED39; -.
DR PRIDE; Q1ED39; -.
DR ProteomicsDB; 61208; -.
DR Antibodypedia; 52534; 18 antibodies from 7 providers.
DR DNASU; 400506; -.
DR Ensembl; ENST00000219837.12; ENSP00000219837.7; ENSG00000103550.14.
DR GeneID; 400506; -.
DR KEGG; hsa:400506; -.
DR MANE-Select; ENST00000219837.12; ENSP00000219837.7; NM_001012991.3; NP_001013009.2.
DR UCSC; uc002dgq.4; human.
DR CTD; 400506; -.
DR DisGeNET; 400506; -.
DR GeneCards; KNOP1; -.
DR HGNC; HGNC:34404; KNOP1.
DR HPA; ENSG00000103550; Low tissue specificity.
DR neXtProt; NX_Q1ED39; -.
DR OpenTargets; ENSG00000103550; -.
DR PharmGKB; PA162378471; -.
DR VEuPathDB; HostDB:ENSG00000103550; -.
DR eggNOG; ENOG502S1WB; Eukaryota.
DR GeneTree; ENSGT00500000044955; -.
DR HOGENOM; CLU_048750_0_0_1; -.
DR InParanoid; Q1ED39; -.
DR OMA; NMDEACI; -.
DR OrthoDB; 1055972at2759; -.
DR PhylomeDB; Q1ED39; -.
DR TreeFam; TF336149; -.
DR PathwayCommons; Q1ED39; -.
DR SignaLink; Q1ED39; -.
DR BioGRID-ORCS; 400506; 10 hits in 1068 CRISPR screens.
DR ChiTaRS; KNOP1; human.
DR GenomeRNAi; 400506; -.
DR Pharos; Q1ED39; Tdark.
DR PRO; PR:Q1ED39; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q1ED39; protein.
DR Bgee; ENSG00000103550; Expressed in sural nerve and 190 other tissues.
DR ExpressionAtlas; Q1ED39; baseline and differential.
DR Genevisible; Q1ED39; HS.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR InterPro; IPR028124; SMAP_dom.
DR Pfam; PF15477; SMAP; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..458
FT /note="Lysine-rich nucleolar protein 1"
FT /id="PRO_0000321938"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..458
FT /note="Interaction with ZNF106"
FT /evidence="ECO:0000250"
FT REGION 336..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17693683,
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 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 308
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 310
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 430
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 319
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 373
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 375
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 407
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 442
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 28
FT /note="R -> Q (in dbSNP:rs11640454)"
FT /id="VAR_061716"
FT VARIANT 266
FT /note="A -> V (in dbSNP:rs2074036)"
FT /id="VAR_039387"
FT VARIANT 276
FT /note="V -> A (in dbSNP:rs28424569)"
FT /id="VAR_061717"
SQ SEQUENCE 458 AA; 51589 MW; F3935374029D61D9 CRC64;
MITKTHKVDL GLPEKKKKKK VVKEPETRYS VLNNDDYFAD VSPLRATSPS KSVAHGQAPE
MPLVKKKKKK KKGVSTLCEE HVEPETTLPA RRTEKSPSLR KQVFGHLEFL SGEKKNKKSP
LAMSHASGVK TSPDPRQGEE ETRVGKKLKK HKKEKKGAQD PTAFSVQDPW FCEAREARDV
GDTCSVGKKD EEQAALGQKR KRKSPREHNG KVKKKKKIHQ EGDALPGHSK PSRSMESSPR
KGSKKKPVKV EAPEYIPISD DPKASAKKKM KSKKKVEQPV IEEPALKRKK KKKRKESGVA
GDPWKEETDT DLEVVLEKKG NMDEAHIDQV RRKALQEEID RESGKTEASE TRKWTGTQFG
QWDTAGFENE DQKLKFLRLM GGFKNLSPSF SRPASTIARP NMALGKKAAD SLQQNLQRDY
DRAMSWKYSR GAGLGFSTAP NKIFYIDRNA SKSVKLED
