KNOP1_MOUSE
ID KNOP1_MOUSE Reviewed; 478 AA.
AC Q9Z2Q2; Q3TKK6; Q7TMJ4; Q8BJI0; Q9D7H7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Lysine-rich nucleolar protein 1;
DE AltName: Full=Testis-specific gene 118 protein;
GN Name=Knop1; Synonyms=Tsg118;
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 [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=10430019; DOI=10.1016/s0171-9335(99)80080-6;
RA Larsson M., Brundell E., Joergensen P.M., Staehl S., Hoeoeg C.;
RT "Characterization of a novel nucleolar protein that transiently associates
RT with the condensed chromosomes in mitotic cells.";
RL Eur. J. Cell Biol. 78:382-390(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP INTERACTION WITH ZNF106, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=15833274; DOI=10.1016/j.biocel.2005.01.013;
RA Grasberger H., Bell G.I.;
RT "Subcellular recruitment by TSG118 and TSPYL implicates a role for zinc
RT finger protein 106 in a novel developmental pathway.";
RL Int. J. Biochem. Cell Biol. 37:1421-1437(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-312, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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).
CC -!- SUBUNIT: Interacts with ZNF106. {ECO:0000269|PubMed:15833274}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10430019,
CC ECO:0000269|PubMed:15833274}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Z2Q2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z2Q2-2; Sequence=VSP_031834;
CC Name=3;
CC IsoId=Q9Z2Q2-3; Sequence=VSP_031835;
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:15833274}.
CC -!- INDUCTION: Down-regulated during myoblast differentiation.
CC {ECO:0000269|PubMed:15833274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD01984.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF034580; AAD01984.1; ALT_INIT; mRNA.
DR EMBL; AK009230; BAB26153.1; -; mRNA.
DR EMBL; AK083845; BAC39038.1; -; mRNA.
DR EMBL; AK166956; BAE39139.1; -; mRNA.
DR EMBL; BC055941; AAH55941.1; -; mRNA.
DR CCDS; CCDS52375.1; -. [Q9Z2Q2-2]
DR CCDS; CCDS52376.1; -. [Q9Z2Q2-3]
DR CCDS; CCDS52377.1; -. [Q9Z2Q2-2]
DR RefSeq; NP_001161690.1; NM_001168218.1.
DR RefSeq; NP_001161691.1; NM_001168219.1.
DR RefSeq; NP_001161692.1; NM_001168220.1. [Q9Z2Q2-2]
DR RefSeq; NP_075686.2; NM_023197.3.
DR AlphaFoldDB; Q9Z2Q2; -.
DR IntAct; Q9Z2Q2; 1.
DR iPTMnet; Q9Z2Q2; -.
DR PhosphoSitePlus; Q9Z2Q2; -.
DR EPD; Q9Z2Q2; -.
DR jPOST; Q9Z2Q2; -.
DR MaxQB; Q9Z2Q2; -.
DR PaxDb; Q9Z2Q2; -.
DR PRIDE; Q9Z2Q2; -.
DR ProteomicsDB; 264790; -. [Q9Z2Q2-1]
DR ProteomicsDB; 264791; -. [Q9Z2Q2-2]
DR ProteomicsDB; 264792; -. [Q9Z2Q2-3]
DR Antibodypedia; 52534; 18 antibodies from 7 providers.
DR Ensembl; ENSMUST00000106549; ENSMUSP00000102159; ENSMUSG00000030980. [Q9Z2Q2-2]
DR GeneID; 66356; -.
DR KEGG; mmu:66356; -.
DR UCSC; uc009jkq.2; mouse. [Q9Z2Q2-2]
DR CTD; 400506; -.
DR MGI; MGI:1913606; Knop1.
DR VEuPathDB; HostDB:ENSMUSG00000030980; -.
DR eggNOG; ENOG502S1WB; Eukaryota.
DR GeneTree; ENSGT00500000044955; -.
DR HOGENOM; CLU_048750_0_0_1; -.
DR InParanoid; Q9Z2Q2; -.
DR OrthoDB; 1055972at2759; -.
DR PhylomeDB; Q9Z2Q2; -.
DR BioGRID-ORCS; 66356; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Knop1; mouse.
DR PRO; PR:Q9Z2Q2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9Z2Q2; protein.
DR Bgee; ENSMUSG00000030980; Expressed in metanephric loop of Henle and 254 other tissues.
DR ExpressionAtlas; Q9Z2Q2; baseline and differential.
DR Genevisible; Q9Z2Q2; MM.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR InterPro; IPR028124; SMAP_dom.
DR Pfam; PF15477; SMAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..478
FT /note="Lysine-rich nucleolar protein 1"
FT /id="PRO_0000321939"
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..478
FT /note="Interaction with ZNF106"
FT /evidence="ECO:0000269|PubMed:15833274"
FT REGION 340..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT CROSSLNK 309
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT CROSSLNK 373
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT CROSSLNK 393
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT CROSSLNK 395
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT CROSSLNK 427
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT CROSSLNK 462
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q1ED39"
FT VAR_SEQ 149..308
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031834"
FT VAR_SEQ 151..333
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031835"
FT CONFLICT 70
FT /note="I -> M (in Ref. 1; AAD01984 and 3; AAH55941)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="M -> MK (in Ref. 3; BAE39139)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="S -> L (in Ref. 3; BAB26153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 53846 MW; 8E2D38A74061FFE1 CRC64;
MVSKTQKADL GPQLPEKKKK KKKKKRVVAN VSEPETQYSV LNSNDYFIDA SPPRATSPSN
NVDEVQIPEI SLSKRKKKKK SCSTHLEECL GAEPTRARQK KSPSPRRQAL EQSAEGLIRE
KKKKRRKSLS KAASQGSGLK TSPDPKHAKE VSKAGRKSKK QRKEKKVPDT EALPPQDAWL
YEAGDSLHSC LEGAEAEEQA ALGQKRKQGS PRDHNMKKKK KTHQEGDILL VNSRVSVENS
LKKGSKKSVK SEALEFVPID SPKAPGKKKV KSKKKVEQPV GEGLAVKRKK KKKKRKENGV
KEDPWQEEKE ESDTDLEVVL EKKGNMDETC IDQVRRKALQ EEIDRESGKT EASEPKKWTV
GLSVKTEASE PKKWTGTQFG QWDTAGFENE EQKLKFLKLM GGFKHLSPSF SRPPSMTIRS
NMALDKKSSE MLQQSLQQDY DRAMSWKYSH GAGLGFNSEA RKVFYIDRNA SKSIKLQD
