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Nucleobindin-1 (CALNUC)

 NUCB1_MOUSE             Reviewed;         459 AA.
Q02819; Q3TU42; Q9CWA1; Q9D8J4; Q9DBL3;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
02-NOV-2001, sequence version 2.
12-SEP-2018, entry version 161.
RecName: Full=Nucleobindin-1;
AltName: Full=CALNUC;
Flags: Precursor;
Name=Nucb1; Synonyms=Nuc, Nucb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1520323; DOI=10.1016/S0006-291X(05)81503-7;
Miura K., Titani K., Kurosawa Y., Kanai Y.;
"Molecular cloning of nucleobindin, a novel DNA-binding protein that
contains both a signal peptide and a leucine zipper structure.";
Biochem. Biophys. Res. Commun. 187:375-380(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Corpus striatum, Head, Kidney, Liver, Pancreas, and
Spinal cord;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION AT SER-85.
PubMed=15378723; DOI=10.1002/rcm.1604;
Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
"Phosphoproteome analysis of mouse liver using immobilized metal
affinity purification and linear ion trap mass spectrometry.";
Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
"Mitochondrial phosphoproteome revealed by an improved IMAC method and
MS/MS/MS.";
Mol. Cell. Proteomics 6:669-676(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-368 AND SER-456,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Major calcium-binding protein of the Golgi. May have a
role in calcium homeostasis (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with GNAI2 and GNAI3. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
{ECO:0000250|UniProtKB:Q63083}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q63083}; Lumenal side
{ECO:0000250|UniProtKB:Q63083}. Cytoplasm
{ECO:0000250|UniProtKB:Q63083}. Secreted
{ECO:0000250|UniProtKB:Q63083}. Note=A small fraction of the
protein may be cytoplasmic. In bone at least part of it is found
in the extracellular matrix and in the culture medium of calvaria
explants (By similarity). In lupus prone, but not in normal mice,
at least part of it is in the serum where it induces the formation
of autoantibodies including anti-DNA antibodies.
{ECO:0000250|UniProtKB:Q63083, ECO:0000305}.
-!- TISSUE SPECIFICITY: Lymphoid cells as well as other somatic cells,
such as liver and kidney cells.
-!- DOMAIN: The EF-hand domains are unfolded in the absence of Ca(2+)
and fold upon Ca(2+) addition. {ECO:0000250}.
-!- MISCELLANEOUS: Discovered as DNA-binding protein in the serum of
lupus-prone mice.
-!- SIMILARITY: Belongs to the nucleobindin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M96823; AAA39842.1; -; mRNA.
EMBL; AK002630; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK004886; BAB23644.1; -; mRNA.
EMBL; AK007976; BAB25383.1; -; mRNA.
EMBL; AK140710; BAE24451.1; -; mRNA.
EMBL; AK160981; BAE36129.1; -; mRNA.
EMBL; AK164088; BAE37619.1; -; mRNA.
EMBL; BC072554; AAH72554.1; -; mRNA.
CCDS; CCDS52247.1; -.
PIR; JC1224; JC1224.
RefSeq; NP_001157134.1; NM_001163662.1.
RefSeq; NP_032775.1; NM_008749.2.
RefSeq; XP_006540759.1; XM_006540696.2.
RefSeq; XP_017177513.1; XM_017322024.1.
UniGene; Mm.258923; -.
ProteinModelPortal; Q02819; -.
SMR; Q02819; -.
BioGrid; 201875; 6.
IntAct; Q02819; 8.
MINT; Q02819; -.
STRING; 10090.ENSMUSP00000033096; -.
iPTMnet; Q02819; -.
PhosphoSitePlus; Q02819; -.
EPD; Q02819; -.
MaxQB; Q02819; -.
PaxDb; Q02819; -.
PeptideAtlas; Q02819; -.
PRIDE; Q02819; -.
Ensembl; ENSMUST00000211765; ENSMUSP00000147383; ENSMUSG00000030824.
GeneID; 18220; -.
KEGG; mmu:18220; -.
UCSC; uc009gvm.2; mouse.
CTD; 4924; -.
MGI; MGI:97388; Nucb1.
eggNOG; KOG3866; Eukaryota.
eggNOG; ENOG410XW7D; LUCA.
GeneTree; ENSGT00390000001927; -.
HOGENOM; HOG000007216; -.
HOVERGEN; HBG052685; -.
InParanoid; Q02819; -.
KO; K20371; -.
OMA; AKMDAEQ; -.
OrthoDB; EOG091G0HG8; -.
PhylomeDB; Q02819; -.
TreeFam; TF323218; -.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
ChiTaRS; Srebf2; mouse.
PRO; PR:Q02819; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030824; Expressed in 288 organ(s), highest expression level in prostate gland.
CleanEx; MM_NUCB1; -.
ExpressionAtlas; Q02819; baseline and differential.
Genevisible; Q02819; MM.
GO; GO:0005801; C:cis-Golgi network; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
GO; GO:0005576; C:extracellular region; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0090498; C:extrinsic component of Golgi membrane; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0032580; C:Golgi cisterna membrane; ISO:MGI.
GO; GO:0005798; C:Golgi-associated vesicle; ISO:MGI.
GO; GO:0098547; C:lumenal side of Golgi membrane; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
GO; GO:1903533; P:regulation of protein targeting; ISO:MGI.
GO; GO:0072718; P:response to cisplatin; IEA:Ensembl.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13499; EF-hand_7; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 2.
1: Evidence at protein level;
Calcium; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Golgi apparatus; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Repeat; Secreted;
Signal.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 459 Nucleobindin-1.
/FTId=PRO_0000004163.
DOMAIN 239 274 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 291 326 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DNA_BIND 171 217 {ECO:0000255}.
CA_BIND 252 263 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 304 315 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
REGION 227 320 Binds to GNAI2 and GNAI3. {ECO:0000250}.
COILED 149 217 {ECO:0000255}.
COILED 340 407 {ECO:0000255}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:15378723}.
MOD_RES 147 147 Phosphothreonine.
{ECO:0000250|UniProtKB:Q02818}.
MOD_RES 368 368 Phosphoserine.
{ECO:0000244|PubMed:17208939,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 456 456 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 42 42 E -> D (in Ref. 2; BAB25383).
{ECO:0000305}.
CONFLICT 146 146 H -> E (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 151 151 R -> I (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 390 393 Missing (in Ref. 1; AAA39842).
{ECO:0000305}.
SEQUENCE 459 AA; 53409 MW; 1CC1102D216CC60B CRC64;
MPTSVPRGAP FLLLPPLLML SAVLAVPVDR AAPPQEDSQA TETPDTGLYY HRYLQEVINV
LETDGHFREK LQAANAEDIK SGKLSQELDF VSHNVRTKLD ELKRQEVSRL RMLLKAKMDA
KQEPNLQVDH MNLLKQFEHL DPQNQHTFEA RDLELLIQTA TRDLAQYDAA HHEEFKRYEM
LKEHERRRYL ESLGEEQRKE AERKLQEQQR RHREHPKVNV PGSQAQLKEV WEELDGLDPN
RFNPKTFFIL HDINSDGVLD EQELEALFTK ELEKVYDPKN EEDDMREMEE ERLRMREHVM
KNVDTNQDRL VTLEEFLAST QRKEFGDTGE GWKTVEMSPA YTEEELKRFE EELAAREAEL
NARAQRLSQE TEALGRSQDR LEAQKRELQQ AVLQMEQRKQ QLQEQSAPPS KPDGQLQFRA
DTDDAPVPAP AGDQKDVPAS EKKVPEQPPE LPQLDSQHL


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