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   24-JAN-2024, entry version 157.
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,
RC   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).
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       cohesin complex composed of SMC1A/B and SMC3 heterodimer, RAD21 and
CC       STAG1/SA1. NIPBL directly contacts all members of the complex, RAD21,
CC       SMC1A/B, SMC3 and STAG1 (By similarity). Interacts directly (via PxVxL
CC       motif) with CBX3 and CBX5 (By similarity). Interacts with ZNF609 (via
CC       N-terminus) (PubMed:28041881). Interacts with the multiprotein complex
CC       Integrator (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; 15.
DR   DIP; DIP-56622N; -.
DR   IntAct; Q6KCD5; 14.
DR   MINT; Q6KCD5; -.
DR   STRING; 10090.ENSMUSP00000059385; -.
DR   GlyGen; Q6KCD5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6KCD5; -.
DR   PhosphoSitePlus; Q6KCD5; -.
DR   EPD; Q6KCD5; -.
DR   jPOST; Q6KCD5; -.
DR   MaxQB; Q6KCD5; -.
DR   PaxDb; 10090-ENSMUSP00000059385; -.
DR   PeptideAtlas; Q6KCD5; -.
DR   ProteomicsDB; 253071; -. [Q6KCD5-1]
DR   ProteomicsDB; 253072; -. [Q6KCD5-2]
DR   ProteomicsDB; 253073; -. [Q6KCD5-3]
DR   ProteomicsDB; 253074; -. [Q6KCD5-4]
DR   Pumba; Q6KCD5; -.
DR   Antibodypedia; 10283; 218 antibodies from 34 providers.
DR   DNASU; 71175; -.
DR   Ensembl; ENSMUST00000052965.8; ENSMUSP00000059385.7; ENSMUSG00000022141.8. [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   AGR; MGI:1913976; -.
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; 1409889at2759; -.
DR   PhylomeDB; Q6KCD5; -.
DR   TreeFam; TF313121; -.
DR   Reactome; R-MMU-2470946; Cohesin Loading onto Chromatin.
DR   BioGRID-ORCS; 71175; 20 hits in 78 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 256 other cell types or tissues.
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:0061775; F:cohesin loader activity; IMP:GO_Central.
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:0003714; F:transcription corepressor activity; ISO:MGI.
DR   GO; GO:0007420; P:brain development; ISO:MGI.
DR   GO; GO:0071481; P:cellular response to X-ray; ISO:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR   GO; GO:0050890; P:cognition; ISO:MGI.
DR   GO; GO:0048589; P:developmental growth; ISO:MGI.
DR   GO; GO:0048565; P:digestive tract development; IBA:GO_Central.
DR   GO; GO:0006974; P:DNA damage response; ISO:MGI.
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:gallbladder 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:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0003151; P:outflow tract morphogenesis; 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; Leucine-rich Repeat Variant; 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:SF18; NIPPED-B-LIKE PROTEIN; 1.
DR   PANTHER; PTHR21704; NIPPED-B-LIKE PROTEIN DELANGIN SCC2-RELATED; 1.
DR   Pfam; PF12765; Cohesin_HEAT; 1.
DR   Pfam; PF12830; Nipped-B_C; 1.
DR   SUPFAM; SSF48371; ARM repeat; 2.
DR   Genevisible; Q6KCD5; MM.
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
//