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NIPB_DROME
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   03-AUG-2022, entry version 144.
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};
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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   iPTMnet; Q7PLI2; -.
DR   PaxDb; Q7PLI2; -.
DR   PRIDE; Q7PLI2; -.
DR   EnsemblMetazoa; FBtr0111118; FBpp0110410; FBgn0026401.
DR   EnsemblMetazoa; FBtr0111119; FBpp0110411; FBgn0026401.
DR   GeneID; 3355136; -.
DR   KEGG; dme:Dmel_CG17704; -.
DR   CTD; 3355136; -.
DR   FlyBase; FBgn0026401; Nipped-B.
DR   VEuPathDB; VectorBase:FBgn0026401; -.
DR   eggNOG; KOG1020; Eukaryota.
DR   GeneTree; ENSGT00390000010427; -.
DR   InParanoid; Q7PLI2; -.
DR   OrthoDB; 608077at2759; -.
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 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: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; IMP:FlyBase.
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:0010628; P:positive regulation of gene expression; IMP:FlyBase.
DR   GO; GO:0045927; P:positive regulation of growth; IMP:FlyBase.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; PTHR21704; 2.
DR   Pfam; PF12765; Cohesin_HEAT; 1.
DR   Pfam; PF12830; Nipped-B_C; 1.
DR   SUPFAM; SSF48371; SSF48371; 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
 
 
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