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Nipped-B protein (SCC2 homolog)

 NIPB_DROME              Reviewed;        2077 AA.
Q7PLI2; A4UZ37; Q058T3; Q058T4; Q7PLI3; Q9XYM2;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
02-MAY-2006, sequence version 3.
12-SEP-2018, entry version 123.
RecName: Full=Nipped-B protein;
AltName: Full=SCC2 homolog;
Name=Nipped-B; ORFNames=CG17704;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10353901;
Rollins R.A., Morcillo P., Dorsett D.;
"Nipped-B, a Drosophila homologue of chromosomal adherins,
participates in activation by remote enhancers in the cut and
Ultrabithorax genes.";
Genetics 152:577-593(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1177-2077.
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H.,
Yu C., Celniker S.E.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=15060134; DOI=10.1128/MCB.24.8.3100-3111.2004;
Rollins R.A., Korom M., Aulner N., Martens A., Dorsett D.;
"Drosophila nipped-B protein supports sister chromatid cohesion and
opposes the stromalin/Scc3 cohesion factor to facilitate long-range
activation of the cut gene.";
Mol. Cell. Biol. 24:3100-3111(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1986; SER-1991; SER-2066
AND THR-2067, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Plays a structural role in chromatin. Involved in sister
chromatid cohesion, probably via an interaction with the cohesin
complex. Participates in the transcriptional activation mediated
by remote enhancers on genes such as cut and Ubx, possibly by
alleviating the cohesin-mediated blocking of enhancer-promoter
communication. {ECO:0000269|PubMed:15060134}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15060134}.
-!- TISSUE SPECIFICITY: Ubiquitous. Expressed in all interphase nuclei
in embryo, third instar imaginal disks, salivary glands and fat
tissues. {ECO:0000269|PubMed:15060134}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
{ECO:0000269|PubMed:15060134}.
-!- SIMILARITY: Belongs to the SCC2/Nipped-B family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABJ17067.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 2061.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF114160; AAD26161.2; -; mRNA.
EMBL; AE013599; EAA46003.3; -; Genomic_DNA.
EMBL; AE013599; EAA46004.3; -; Genomic_DNA.
EMBL; BT029134; ABJ17067.1; ALT_TERM; mRNA.
EMBL; BT029135; ABJ17068.1; -; mRNA.
RefSeq; NP_001036451.1; NM_001042986.3.
RefSeq; NP_001036452.1; NM_001042987.3.
UniGene; Dm.1465; -.
ProteinModelPortal; Q7PLI2; -.
BioGrid; 78261; 23.
DIP; DIP-29198N; -.
IntAct; Q7PLI2; 2.
STRING; 7227.FBpp0110411; -.
iPTMnet; Q7PLI2; -.
PaxDb; Q7PLI2; -.
PRIDE; Q7PLI2; -.
EnsemblMetazoa; FBtr0111118; FBpp0110410; FBgn0026401.
EnsemblMetazoa; FBtr0111119; FBpp0110411; FBgn0026401.
GeneID; 3355136; -.
KEGG; dme:Dmel_CG17704; -.
CTD; 3355136; -.
FlyBase; FBgn0026401; Nipped-B.
eggNOG; KOG1020; Eukaryota.
eggNOG; ENOG410XP32; LUCA.
GeneTree; ENSGT00390000010427; -.
InParanoid; Q7PLI2; -.
KO; K06672; -.
OrthoDB; EOG091G00DH; -.
PhylomeDB; Q7PLI2; -.
Reactome; R-DME-2470946; Cohesin Loading onto Chromatin.
GenomeRNAi; 3355136; -.
PRO; PR:Q7PLI2; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0026401; Expressed in 5 organ(s), highest expression level in head.
ExpressionAtlas; Q7PLI2; differential.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
GO; GO:0032116; C:SMC loading complex; ISS:UniProtKB.
GO; GO:0035327; C:transcriptionally active chromatin; IDA:FlyBase.
GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
GO; GO:0048854; P:brain morphogenesis; IMP:FlyBase.
GO; GO:0050802; P:circadian sleep/wake cycle, sleep; IMP:FlyBase.
GO; GO:0007612; P:learning; IMP:FlyBase.
GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; ISS:UniProtKB.
GO; GO:0061780; P:mitotic cohesin loading; IMP:FlyBase.
GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:UniProtKB.
GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
GO; GO:0045927; P:positive regulation of growth; IMP:FlyBase.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0007614; P:short-term memory; IMP:FlyBase.
GO; GO:0007130; P:synaptonemal complex assembly; IMP:FlyBase.
GO; GO:0070193; P:synaptonemal complex organization; IMP:FlyBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0071733; P:transcriptional activation by promoter-enhancer looping; IGI:FlyBase.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR026003; Cohesin_HEAT.
InterPro; IPR024986; Nipped-B_C.
InterPro; IPR033031; SCC2/Nipped-B.
PANTHER; PTHR21704; PTHR21704; 1.
Pfam; PF12765; Cohesin_HEAT; 1.
Pfam; PF12830; Nipped-B_C; 1.
SUPFAM; SSF48371; SSF48371; 3.
1: Evidence at protein level;
Activator; Cell cycle; Complete proteome; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation.
CHAIN 1 2077 Nipped-B protein.
/FTId=PRO_0000218599.
REPEAT 1128 1159 HEAT 1.
REPEAT 1167 1198 HEAT 2.
REPEAT 1200 1235 HEAT 3.
REPEAT 1240 1273 HEAT 4.
REPEAT 1538 1569 HEAT 5.
REPEAT 1647 1678 HEAT 6.
REPEAT 1684 1715 HEAT 7.
MOD_RES 1986 1986 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1991 1991 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 2066 2066 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 2067 2067 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 308 308 L -> F (in Ref. 1; AAD26161).
{ECO:0000305}.
CONFLICT 657 657 T -> N (in Ref. 1; AAD26161).
{ECO:0000305}.
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


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