ID NIPB_DROME Reviewed; 2077 AA.
AC Q7PLI2; A4UZ37; Q058T3; Q058T4; Q7PLI3; Q9XYM2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 24-JAN-2024, entry version 151.
DE RecName: Full=Nipped-B protein;
DE AltName: Full=SCC2 homolog;
GN Name=Nipped-B; ORFNames=CG17704;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10353901; DOI=10.1093/genetics/152.2.577;
RA Rollins R.A., Morcillo P., Dorsett D.;
RT "Nipped-B, a Drosophila homologue of chromosomal adherins, participates in
RT activation by remote enhancers in the cut and Ultrabithorax genes.";
RL Genetics 152:577-593(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1177-2077.
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15060134; DOI=10.1128/mcb.24.8.3100-3111.2004;
RA Rollins R.A., Korom M., Aulner N., Martens A., Dorsett D.;
RT "Drosophila nipped-B protein supports sister chromatid cohesion and opposes
RT the stromalin/Scc3 cohesion factor to facilitate long-range activation of
RT the cut gene.";
RL Mol. Cell. Biol. 24:3100-3111(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1986; SER-1991; SER-2066 AND
RP THR-2067, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Plays a structural role in chromatin. Involved in sister
CC chromatid cohesion, probably via an interaction with the cohesin
CC complex. Participates in the transcriptional activation mediated by
CC remote enhancers on genes such as cut and Ubx, possibly by alleviating
CC the cohesin-mediated blocking of enhancer-promoter communication.
CC {ECO:0000269|PubMed:15060134}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15060134}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in all interphase nuclei in
CC embryo, third instar imaginal disks, salivary glands and fat tissues.
CC {ECO:0000269|PubMed:15060134}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:15060134}.
CC -!- SIMILARITY: Belongs to the SCC2/Nipped-B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABJ17067.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 2061.; 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; AF114160; AAD26161.2; -; mRNA.
DR EMBL; AE013599; EAA46003.3; -; Genomic_DNA.
DR EMBL; AE013599; EAA46004.3; -; Genomic_DNA.
DR EMBL; BT029134; ABJ17067.1; ALT_TERM; mRNA.
DR EMBL; BT029135; ABJ17068.1; -; mRNA.
DR RefSeq; NP_001036451.1; NM_001042986.3.
DR RefSeq; NP_001036452.1; NM_001042987.3.
DR AlphaFoldDB; Q7PLI2; -.
DR SMR; Q7PLI2; -.
DR BioGRID; 78261; 24.
DR DIP; DIP-29198N; -.
DR IntAct; Q7PLI2; 2.
DR STRING; 7227.FBpp0110411; -.
DR GlyGen; Q7PLI2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7PLI2; -.
DR PaxDb; 7227-FBpp0110411; -.
DR EnsemblMetazoa; FBtr0111118; FBpp0110410; FBgn0026401.
DR EnsemblMetazoa; FBtr0111119; FBpp0110411; FBgn0026401.
DR GeneID; 3355136; -.
DR KEGG; dme:Dmel_CG17704; -.
DR AGR; FB:FBgn0026401; -.
DR CTD; 3355136; -.
DR FlyBase; FBgn0026401; Nipped-B.
DR VEuPathDB; VectorBase:FBgn0026401; -.
DR eggNOG; KOG1020; Eukaryota.
DR GeneTree; ENSGT00390000010427; -.
DR InParanoid; Q7PLI2; -.
DR OMA; GSTDWPA; -.
DR OrthoDB; 1409889at2759; -.
DR PhylomeDB; Q7PLI2; -.
DR Reactome; R-DME-2470946; Cohesin Loading onto Chromatin.
DR SignaLink; Q7PLI2; -.
DR BioGRID-ORCS; 3355136; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 3355136; -.
DR PRO; PR:Q7PLI2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0026401; Expressed in midgut and 10 other cell types or tissues.
DR ExpressionAtlas; Q7PLI2; baseline and differential.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0090694; C:Scc2-Scc4 cohesin loading complex; IBA:GO_Central.
DR GO; GO:0032116; C:SMC loading complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0061775; F:cohesin loader activity; IMP:FlyBase.
DR GO; GO:0048854; P:brain morphogenesis; IMP:FlyBase.
DR GO; GO:0140588; P:chromatin looping; IGI:FlyBase.
DR GO; GO:0050802; P:circadian sleep/wake cycle, sleep; IMP:FlyBase.
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:0007612; P:learning; IMP:FlyBase.
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; IMP:UniProtKB.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
DR GO; GO:0045927; P:positive regulation of growth; IMP:FlyBase.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IBA:GO_Central.
DR GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:FlyBase.
DR GO; GO:0070193; P:synaptonemal complex organization; IMP:FlyBase.
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; 1.
PE 1: Evidence at protein level;
KW Activator; Cell cycle; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..2077
FT /note="Nipped-B protein"
FT /id="PRO_0000218599"
FT REPEAT 1128..1159
FT /note="HEAT 1"
FT REPEAT 1167..1198
FT /note="HEAT 2"
FT REPEAT 1200..1235
FT /note="HEAT 3"
FT REPEAT 1240..1273
FT /note="HEAT 4"
FT REPEAT 1538..1569
FT /note="HEAT 5"
FT REPEAT 1647..1678
FT /note="HEAT 6"
FT REPEAT 1684..1715
FT /note="HEAT 7"
FT REGION 1030..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2039..2077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1986
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1991
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2066
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2067
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 308
FT /note="L -> F (in Ref. 1; AAD26161)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="T -> N (in Ref. 1; AAD26161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2077 AA; 236729 MW; 1877419A0E5B68AC CRC64;
MGERDNPTVP VTTLAGLTST SDLLSELPVA DSLQSAASLN KSLLFHALVA NESSNLLSMR
NENLVRQLVT AIERTNSDNI ELIHCPVQDT ATNCSTYPEL LQGIYHFRPA VFNTSIKIHS
PDQHTANARL EAKKMQIDSY SIPECYASPT NLSISNEHQL QDAQACFNQL TSMTSKEILE
EFSQINFKEN ATEKDKIDVI ENSDLNVTKI LSQNTLKKKS NTPERSTVQS IQEQFFIQQQ
EANYNLKHDL NQVSTNVGQI QNISDTFPQE PSNFNLNSVN IPNMLYVQSP PFTESEPTQA
HHSSIEYLKK KKSQILDVSI LNRQQVLENT SLHIINKSST YQTNQNVSTT TSTSTSSSGK
SQVRVCINRL SIEDSRLMQQ SIKKFVQKSP ELARSMGLLQ ETCQQQHENL NIIPTSAEEC
VLESRASSTN NTVKIPIDTF STIKADEKRS AKRKLAISIG DIPPEQIFSK PKMRRVERIT
PLSNTKCVKE EVTRSQTYQQ FIRNMDHIIE ILDDSESPNF DSEDVDETIE CISSKLLNSM
STDVAKLKAK QALDSIPKNK LTLLINYAMR NVYLARNYFA GTEDEDEFVD DEVIEKLLNA
MDACLLICNI YSTVSDLQFL QEDNVSHIIK FTQFQLRETI FPLHDPVYTA KSIKRTTHRK
KIKSHQAQNR SMQLFYLKTV ELLKVFVTLF DKCVFVDTIV LPLSTLAIEP FFVDNIETLQ
FVCLELVTTI FRKERYDKIR NSILGDILTS IDRLPSSKKN LRPYKLTNNG GNIQMVTALV
LQLIQCATIL PDSLCDNGKF SNKPQEGNTF DEEGKKLLQP SQDLLVLQKY DVAVSIGGNF
LTTFLNKCKS RSNETDFRPL FENFIHDLLA TVNKPEWPAS ELLLSLLGTM LVRYVSDKGI
EQSIRLVSLD YLGIVAARLR KDTVESRCRV NIIDSMIQSI KLEQEKEGDV TSNNDQFDLE
PEEQRTDFLQ KILLDFLAVN AQEENLIWDY ARHFYLAQWY RDVIYQRRRI NDGKKGLAFR
KSKIRNNRRT NGDYLDTSDS GSCDESDTDT NKKRIHCVDS NDFELNINIY KALEARKQYF
INKIKPFSVF GEQNHSSNQH IKTYIDYNNA QLIAQYLATK RPFSQSFDGC LKKIILVVNE
PSIAVRTRAM KCLANIVEVD PLVLKRKDMQ MGVNQKFLDT AISVREAAVD LVGKFVLSNQ
DLIDQYYDML STRILDTGVS VRKRVIKILR DICLEYPDFS KIPEICVKMI RRVHDEEGIQ
KLVTEVFMKM WFTPCTKNDK IGIQRKINHI IDVVNTAHDT GTTWLEGLLM SIFKPRDNML
RSEGCVQEFI KKNSEPPMDI VIACQQLADG LVDRLIELED TDNSRMLGCI TTLHLLAKVR
PQLLVKHAIT IEPYLNIKCH SATAAKFICA VADILEKVVP LVNNASESFL ASLEEHLMLL
VVSRNQAEVT SCVSCLGALV NKITHNFKLI RDCFQKFYRV LDVSRSQVIQ GNNSVDNIYT
PSFRRSLFTI GILMRYFDFK SPIALGETND GLPVSICEDV FHCLMFFCRC TNQEIRKQAL
ISLGSFCVLN DGYLTRSELK NLYCEILSSI ANDAGFKIIC MRNIWIYLTE SEMFMHNKEK
EWEKQSKHED LKEMNDVSSG MASRIIQLYL EEILECFLNR DDTVRLWAVK VIQIVLRQGL
VHPVRMVPYL ICLSTDHRIE SAHRADALLK DIDKTYSGFV NMKVQFGLQL CFKLQKILQI
NNRGKLEIIR GYASRGPDNT TTALNDFLYT LLRTTKPQRR ALVQTVTKQF DDQKTSLQQM
LYIADNLAYF PYVVQDEPLY LIHQIDLLIS MAGTHLLATF KEHIKPSDKE GDVLEDDDDV
EDPEVLFNRL PEDLTEIIKC ITSAQACMLL LILKDHLKEM YAITDSKISR YSPSEQKLYE
KAVTRKSVND FNPKTTIDVI KKQMSQEKLS TDINFTLTKE EKLDLVVKYL DFKQLMLKLD
PDDGDSDADE SRDKTMLNIS ASSDGVAFSS SAKNSHSACD GYSLTVTDVV DVPMSHIAKA
SMLTSKPSGR KTNPVRTKKK RRKIDSTDDE TSDAEYA
//
