NIPBL_MOUSE
ID NIPBL_MOUSE Reviewed; 2798 AA.
AC Q6KCD5; Q6KC78; Q7TNS4; Q8BKV4; Q8CES9; Q9CUC6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Nipped-B-like protein;
DE AltName: Full=Delangin homolog;
DE AltName: Full=SCC2 homolog;
GN Name=Nipbl; Synonyms=Scc2 {ECO:0000303|PubMed:28914604};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RX PubMed=15146185; DOI=10.1038/ng1363;
RA Tonkin E.T., Wang T.-J., Lisgo S., Bamshad M.J., Strachan T.;
RT "NIPBL, encoding a homolog of fungal Scc2-type sister chromatid cohesion
RT proteins and fly Nipped-B, is mutated in Cornelia de Lange syndrome.";
RL Nat. Genet. 36:636-641(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-325, AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF
RP 2575-2798 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 DEVELOPMENTAL STAGE.
RX PubMed=15146186; DOI=10.1038/ng1364;
RA Krantz I.D., McCallum J., DeScipio C., Kaur M., Gillis L.A., Yaeger D.,
RA Jukofsky L., Wasserman N., Bottani A., Morris C.A., Nowaczyk M.J.M.,
RA Toriello H., Bamshad M.J., Carey J.C., Rappaport E., Kawauchi S.,
RA Lander A.D., Calof A.L., Li H.-H., Devoto M., Jackson L.G.;
RT "Cornelia de Lange syndrome is caused by mutations in NIPBL, the human
RT homolog of Drosophila melanogaster Nipped-B.";
RL Nat. Genet. 36:631-635(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-2652; THR-2661 AND
RP SER-2666, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2661 AND SER-2666
RP (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2652, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; SER-256; SER-274;
RP SER-280; SER-284; SER-301; SER-306; SER-318; SER-1083; SER-1084; SER-1090;
RP SER-1144; SER-1146; SER-1148; TYR-1153; SER-1154; SER-2487; SER-2503;
RP SER-2505; SER-2507; SER-2652; THR-2661 AND SER-2666, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT THR-2661 AND SER-2666 (ISOFORM 2), AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23967866; DOI=10.1186/1747-1028-8-12;
RA Kuleszewicz K., Fu X., Kudo N.R.;
RT "Cohesin loading factor Nipbl localizes to chromosome axes during mammalian
RT meiotic prophase.";
RL Cell Div. 8:12-12(2013).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1076, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24287868; DOI=10.1007/s00412-013-0444-7;
RA Visnes T., Giordano F., Kuznetsova A., Suja J.A., Lander A.D., Calof A.L.,
RA Stroem L.;
RT "Localisation of the SMC loading complex Nipbl/Mau2 during mammalian
RT meiotic prophase I.";
RL Chromosoma 123:239-252(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE INTEGRATOR COMPLEX AND
RP ZNF609, AND DEVELOPMENTAL STAGE.
RX PubMed=28041881; DOI=10.1016/j.neuron.2016.11.047;
RA van den Berg D.L., Azzarelli R., Oishi K., Martynoga B., Urban N.,
RA Dekkers D.H., Demmers J.A., Guillemot F.;
RT "Nipbl interacts with Zfp609 and the Integrator complex to regulate
RT cortical neuron migration.";
RL Neuron 93:348-361(2017).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=28914604; DOI=10.7554/elife.30000;
RA Rhodes J., Mazza D., Nasmyth K., Uphoff S.;
RT "Scc2/Nipbl hops between chromosomal cohesin rings after loading.";
RL Elife 6:0-0(2017).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29094699; DOI=10.1038/nature24281;
RA Schwarzer W., Abdennur N., Goloborodko A., Pekowska A., Fudenberg G.,
RA Loe-Mie Y., Fonseca N.A., Huber W., Haering C.H., Mirny L., Spitz F.;
RT "Two independent modes of chromatin organization revealed by cohesin
RT removal.";
RL Nature 551:51-56(2017).
CC -!- FUNCTION: Plays an important role in the loading of the cohesin complex
CC on to DNA (PubMed:29094699). Forms a heterodimeric complex (also known
CC as cohesin loading complex) with MAU2/SCC4 which mediates the loading
CC of the cohesin complex onto chromatin. Plays a role in cohesin loading
CC at sites of DNA damage. Its recruitment to double-strand breaks (DSBs)
CC sites occurs in a CBX3-, RNF8- and RNF168-dependent manner whereas its
CC recruitment to UV irradiation-induced DNA damage sites occurs in a
CC ATM-, ATR-, RNF8- and RNF168-dependent manner (By similarity). Along
CC with ZNF609, promotes cortical neuron migration during brain
CC development by regulating the transcription of crucial genes in this
CC process. Preferentially binds promoters containing paused RNA
CC polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and
CC GABBR2 genes, among others (PubMed:28041881).
CC {ECO:0000250|UniProtKB:Q6KC79, ECO:0000269|PubMed:28041881,
CC ECO:0000269|PubMed:29094699}.
CC -!- SUBUNIT: Heterodimerizes with MAU2/SCC4 to form the cohesin loading
CC complex (By similarity). The NIPBL-MAU2 heterodimer interacts with the
CC SMC1A-SMC3 heterodimer and with the cohesin complex composed of SMC1A,
CC SMC3, RAD21 and STAG1. Interacts directly (via PxVxL motif) with CBX3
CC and CBX5 (By similarity). Interacts with ZNF609 (via N-terminus)
CC (PubMed:28041881). Interacts with the multiprotein complex Integrator
CC (PubMed:28041881). {ECO:0000250|UniProtKB:Q6KC79,
CC ECO:0000269|PubMed:28041881}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23967866,
CC ECO:0000269|PubMed:24287868, ECO:0000269|PubMed:28041881,
CC ECO:0000269|PubMed:28914604}. Chromosome {ECO:0000269|PubMed:23967866,
CC ECO:0000269|PubMed:24287868}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6KCD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6KCD5-2; Sequence=VSP_011098, VSP_011099;
CC Name=3;
CC IsoId=Q6KCD5-3; Sequence=VSP_011094;
CC Name=4;
CC IsoId=Q6KCD5-4; Sequence=VSP_011095, VSP_011096, VSP_011097;
CC -!- TISSUE SPECIFICITY: Spermatocytes and oocytes (at protein level).
CC {ECO:0000269|PubMed:23967866, ECO:0000269|PubMed:24287868}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed at 9.5 and 10.5 dpc, with notable
CC accumulations in limb bud, branchial arch and craniofacial mesenchyme.
CC These regions are involved in patterning of the skeleton and soft
CC tissues of the limbs, jaw and face. Expressed in the developing brain,
CC with enrichment in the ventricular zone at 14.5 dpc (PubMed:28041881).
CC {ECO:0000269|PubMed:15146186, ECO:0000269|PubMed:28041881}.
CC -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
CC required for interaction with chromoshadow domains. This motif requires
CC additional residues -7, -6, +4 and +5 of the central Val which contact
CC the chromoshadow domain. {ECO:0000250|UniProtKB:Q6KC79}.
CC -!- DOMAIN: The C-terminal region containing HEAT repeats and Pro-Xaa-Val-
CC Xaa-Leu (PxVxL) motif are involved in the recruitment of NIPBL to sites
CC of DNA damage. {ECO:0000250|UniProtKB:Q6KC79}.
CC -!- DISRUPTION PHENOTYPE: Deletion of NIPBL in mouse liver leads to strong
CC depletion of chromatin-bound cohesin and marked reorganization of
CC chromosomal folding. Cells retain transcriptionally active (type A) and
CC transcriptionally inactive (type B) compartments, but lose
CC topologically associating domains (TADs) patterns and TAD-associated
CC peaks of contact enrichment across the whole genome. The
CC compartmentalization of chromatin in cells lacking NIPBL is enhanced
CC around 1.8-fold compared with controls. {ECO:0000269|PubMed:29094699}.
CC -!- SIMILARITY: Belongs to the SCC2/Nipped-B family. {ECO:0000305}.
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DR EMBL; AJ627033; CAF25291.1; -; mRNA.
DR EMBL; AJ640138; CAG26692.1; -; mRNA.
DR EMBL; AK014915; BAC25453.1; -; mRNA.
DR EMBL; AK016861; BAB30471.1; -; mRNA.
DR EMBL; AK049588; BAC33829.1; -; mRNA.
DR EMBL; BC055787; AAH55787.1; -; mRNA.
DR CCDS; CCDS37035.1; -. [Q6KCD5-1]
DR RefSeq; NP_081983.2; NM_027707.3. [Q6KCD5-1]
DR RefSeq; NP_957684.1; NM_201232.2. [Q6KCD5-2]
DR RefSeq; XP_006520057.1; XM_006519994.3. [Q6KCD5-1]
DR RefSeq; XP_006520058.1; XM_006519995.2. [Q6KCD5-1]
DR RefSeq; XP_017172234.1; XM_017316745.1.
DR SMR; Q6KCD5; -.
DR BioGRID; 214531; 13.
DR DIP; DIP-56622N; -.
DR IntAct; Q6KCD5; 13.
DR STRING; 10090.ENSMUSP00000059385; -.
DR iPTMnet; Q6KCD5; -.
DR PhosphoSitePlus; Q6KCD5; -.
DR EPD; Q6KCD5; -.
DR jPOST; Q6KCD5; -.
DR MaxQB; Q6KCD5; -.
DR PaxDb; Q6KCD5; -.
DR PeptideAtlas; Q6KCD5; -.
DR PRIDE; Q6KCD5; -.
DR ProteomicsDB; 253071; -. [Q6KCD5-1]
DR ProteomicsDB; 253072; -. [Q6KCD5-2]
DR ProteomicsDB; 253073; -. [Q6KCD5-3]
DR ProteomicsDB; 253074; -. [Q6KCD5-4]
DR Antibodypedia; 10283; 195 antibodies from 34 providers.
DR DNASU; 71175; -.
DR Ensembl; ENSMUST00000052965; ENSMUSP00000059385; ENSMUSG00000022141. [Q6KCD5-1]
DR GeneID; 71175; -.
DR KEGG; mmu:71175; -.
DR UCSC; uc007veq.2; mouse. [Q6KCD5-1]
DR UCSC; uc007ver.2; mouse. [Q6KCD5-2]
DR UCSC; uc007vev.1; mouse. [Q6KCD5-4]
DR CTD; 25836; -.
DR MGI; MGI:1913976; Nipbl.
DR VEuPathDB; HostDB:ENSMUSG00000022141; -.
DR eggNOG; KOG1020; Eukaryota.
DR GeneTree; ENSGT00390000010427; -.
DR HOGENOM; CLU_000763_0_0_1; -.
DR InParanoid; Q6KCD5; -.
DR OMA; KQNENRM; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q6KCD5; -.
DR TreeFam; TF313121; -.
DR Reactome; R-MMU-2470946; Cohesin Loading onto Chromatin.
DR BioGRID-ORCS; 71175; 18 hits in 73 CRISPR screens.
DR ChiTaRS; Nipbl; mouse.
DR PRO; PR:Q6KCD5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q6KCD5; protein.
DR Bgee; ENSMUSG00000022141; Expressed in rostral migratory stream and 252 other tissues.
DR Genevisible; Q6KCD5; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0032039; C:integrator complex; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090694; C:Scc2-Scc4 cohesin loading complex; ISS:UniProtKB.
DR GO; GO:0032116; C:SMC loading complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0070087; F:chromo shadow domain binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0036033; F:mediator complex binding; IDA:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:ARUK-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0071481; P:cellular response to X-ray; ISO:MGI.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0071921; P:cohesin loading; IMP:UniProtKB.
DR GO; GO:0048589; P:developmental growth; ISO:MGI.
DR GO; GO:0048565; P:digestive tract development; IBA:GO_Central.
DR GO; GO:0042471; P:ear morphogenesis; ISO:MGI.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:MGI.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; ISO:MGI.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; ISO:MGI.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:MGI.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; IBA:GO_Central.
DR GO; GO:0035261; P:external genitalia morphogenesis; ISO:MGI.
DR GO; GO:0048592; P:eye morphogenesis; ISO:MGI.
DR GO; GO:0060325; P:face morphogenesis; ISO:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
DR GO; GO:0035136; P:forelimb morphogenesis; ISO:MGI.
DR GO; GO:0061010; P:gall bladder development; ISO:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; ISO:MGI.
DR GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0061780; P:mitotic cohesin loading; IEA:InterPro.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISO:MGI.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:2001224; P:positive regulation of neuron migration; IMP:UniProtKB.
DR GO; GO:0045778; P:positive regulation of ossification; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0048638; P:regulation of developmental growth; ISO:MGI.
DR GO; GO:0045995; P:regulation of embryonic development; ISO:MGI.
DR GO; GO:0042634; P:regulation of hair cycle; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0061038; P:uterus morphogenesis; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026003; Cohesin_HEAT.
DR InterPro; IPR024986; Nipped-B_C.
DR InterPro; IPR033031; Scc2/Nipped-B.
DR PANTHER; PTHR21704; PTHR21704; 2.
DR Pfam; PF12765; Cohesin_HEAT; 1.
DR Pfam; PF12830; Nipped-B_C; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Cell cycle; Chromosome;
KW Developmental protein; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..2798
FT /note="Nipped-B-like protein"
FT /id="PRO_0000218597"
FT REPEAT 1761..1799
FT /note="HEAT 1"
FT REPEAT 1837..1875
FT /note="HEAT 2"
FT REPEAT 1939..1978
FT /note="HEAT 3"
FT REPEAT 2221..2261
FT /note="HEAT 4"
FT REPEAT 2307..2345
FT /note="HEAT 5"
FT REGION 128..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2467..2514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2645..2690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 990..1003
FT /note="PxVxL motif"
FT /evidence="ECO:0000250|UniProtKB:Q6KC79"
FT COMPBIAS 128..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1084
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2670..2687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC79"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC79"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC79"
FT MOD_RES 713
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC79"
FT MOD_RES 746
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC79"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC79"
FT MOD_RES 1076
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1084
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1153
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC79"
FT MOD_RES 1191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC79"
FT MOD_RES 2487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC79"
FT MOD_RES 2646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC79"
FT MOD_RES 2652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 2661
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..2694
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011094"
FT VAR_SEQ 1..263
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011095"
FT VAR_SEQ 499..556
FT /note="DKPLKKRKQDSYPQEAGGATGGNRPASQETGSTGNGSRPALMVSIDLHQAGR
FT VDSQAS -> GKGPLSLLLQHLATCVLIPTSLLRYEFHSLAEASISDLIIQYHRLSNLN
FT YITLFELLY (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011096"
FT VAR_SEQ 557..2798
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011097"
FT VAR_SEQ 2678..2691
FT /note="SLRRSKRNSDSTEL -> VRRRRSQRISQRIT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15146185,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011098"
FT VAR_SEQ 2692..2798
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15146185,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011099"
FT CONFLICT 2577
FT /note="K -> I (in Ref. 2; BAC25453)"
FT /evidence="ECO:0000305"
FT MOD_RES Q6KCD5-2:2661
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES Q6KCD5-2:2666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 2798 AA; 315450 MW; BC23B6E2C949C9B3 CRC64;
MNGDMPHVPI TTLAGIASLT DLLNQLPLPS PLPATTTKSL LFNSRIAEEV NCLLACRDDN
LVSQLVHSLN QVSTDHIELK DNLGSDDPEG DIPVLLQAVL ARSPNVFREK SMQNRYVQSG
MMMSQYKLSQ NSMHSSPASS NYQQTTISHS PSSRFVPPQT SSGNRFMPQQ NSPVPSPYAP
QSPAGYMPYS HPSSYTTHPQ MQQASVSSPI VAGGLRNIHD NKVSGPLSGN SANHHADNPR
HGSSDDYLHM VHRLSSDDGD SSTMRNAASF PLRSPQPVCS PAGSDGTPKG SRPPLILQSQ
SLPCSSPRDV PPDILLDSPE RKQKKQKKIK LGKDEKDQNE KAAMYDIISS PTKDSTKLTL
RLSRVRSSDM DQQDDMLSGM ENSNVSENDI PFNVQYPGQT SKTPITPQDV NRPLNAAQCL
SQQEQTAFLP ANQVPVLQQN TSVATKQPQT SVVQNQQQVS QQGPIYDEVE LDALAEIERI
ERESAIERER FSKEVQDKDK PLKKRKQDSY PQEAGGATGG NRPASQETGS TGNGSRPALM
VSIDLHQAGR VDSQASITQD SDSIKKPEET KQCNDAPISV LQEDIVGSLK SIPENHPETP
KKKSDPELSK SEMKQNESRL SESKPNENQL GESKSNESKL ETKTETPTEE LKQNENKTTE
SKQSESAVVE PKQNENRPCD TKPNDNKQNN TRSENTKARP ETPKQKAESR PETPKQKSEG
RPETPKQKGD GRPETPKQKS EGRPETPKQK GEGRPETPKH RHENRRDSGK PSTEKKPDVS
KHKQDIKSDS PRLKSERAEA LKQRPDGRWE SLRRDHDSKQ KSDDRGESER HRGDQSRVRR
PETLRSSSRN DHSTKSDGSK TEKLERKHRH ESGDSRDRPS GEQKSRPDSP RVKQGDTNKS
RPGFKSPNSK DDKRTEGNRS KVDSNKAHTD NKAEFPSYLL GGRSGALKNF VIPKIKRDKD
GNITQETKKM DMKGEQKDKV EKMGLVEDLN KGAKPVVVLQ KLSLDDVQKL IKDREEKSRS
SLKSIKNKPS KSNKGSIDQS VLKELPPELL AEIESTMPLC ERVKMNKRKR STVNEKPKYA
EISSDEDNDS DEAFESSRKR HKKDDDKAWE YEERDRRSSG DHRRSGHSHD GRRSSGGGRY
RNRSPSDSDM EDYSPPPSLS EVARKMKKKE KQKKRKAYEP KLTPEEMMDS STFKRFTASI
ENILDNLEDM DFTAFGDDDE IPQELLLGKH QLNELGSESA KIKAMGIMDK LSTDKTVKVL
NILEKNIQDG SKLSTLLNHN NDTEEEERLW RDLIMERVTK SADACLTTIN IMTSPNMPKA
VYIEDVIERV IQYTKFHLQN TLYPQYDPVY RVDPHGGGLL SSKAKRAKCS THKQRVIVML
YNKVCDIVSS LSELLEIQLL TDTTILQVSS MGITPFFVEN VSELQLCAIK LVTAVFSRYE
KHRQLILEEI FTSLARLPTS KRSLRNFRLN SSDVDGEPMY IQMVTALVLQ LIQCVVHLPS
SEKDPNSEED SNKKVDQDVV ITNSYETAMR TAQNFLSIFL KKCGSKQGEE DYRPLFENFV
QDLLSTVNKP EWPAAELLLS LLGRLLVHQF SNKSTEMALR VASLDYLGTV AARLRKDAVT
SKMDQGSIER ILKQVSGGED EIQQLQKALL DYLDENTETD PSLVFSRKFY IAQWFRDTTL
ETEKAMKSQK DEESSDATHH AKELETTGQI MHRAENRKKF LRSIIKTTPS QFSTLKMNSD
TVDYDDACLI VRYLASMRPF AQSFDIYLTQ ILRVLGENAI AVRTKAMKCL SEVVAVDPSI
LARLDMQRGV HGRLMDNSTS VREAAVELLG RFVLCRPQLA EQYYDMLIER ILDTGISVRK
RVIKILRDIC IEQPTFPKIT EMCVKMIRRV NDEEGIKKLV NETFQKLWFT PTPHNDKEAM
TRKILNITDV VAACRDTGYD WFEQLLQNLL KSEEDSSYKP VKKACTQLVD NLVEHILKYE
ESLADSDNKG VNSGRLVACI TTLFLFSKIR PQLMVKHAMT MQPYLTTKCS TQNDFMVICN
VAKILELVVP LMEHPSETFL ATIEEDLMKL IIKYGMTVVQ HCVSCLGAVV NKVTQNFKFV
WACFNRYYGA ISKLKSQHQE DPNNTSLLTN KPALLRSLFT VGALCRHFDF DLEDFKGNSK
VNIKDKVLEL LMYFTKHSDE EVQTKAIIGL GFAFIQHPSL MFEQEVKNLY NSILSDKNSS
VNLKIQVLKN LQTYLQEEDT RMQQADRDWK KVAKQEDLKE MGDVSSGMSS SIMQLYLKQV
LEAFFHTQSS VRHFALNVIA LTLNQGLIHP VQCVPYLIAM GTDPEPAMRN KADQQLVEID
KKYAGFIHMK AVAGMKMSYQ VQQAINTCLK DPVRGFRQDE SSSALCSHLY SMIRGNRQHR
RAFLISLLNL FDDTAKTEVT MLLYIADNLA CFPYQTQEEP LFIMHHIDIT LSVSGSNLLQ
SFKESMVKDK RKERKTSPAK ENESSESEEE VSRPRKSRKR VDSESDSDSE DDINSVMKCL
PENSAPLIEF ANVSQGILLL LMLKQHLKNL CGFSDSKIQK YSPSESAKVY DKAINRKTGV
HFHPKQTLDF LRSDMANSKL TEDVKRSIVR QYLDFKLLME HLDPDEEEEE GEVSASTNAR
NKAITSLLGG GSPKNNTAAD TEDEESDGED RGGGTSGSLR RSKRNSDSTE LAAQMNESVD
VMDVIAICCP KYKDRPQIAR VVQRTSSGVS VQWMAGSYSG SWTEAKRRDG RKLVPWVDTI
KESDIIYKKI ALTSANKLTN KVVQTLRSLY AAKDGTSS
