EVI2B_MOUSE
ID EVI2B_MOUSE Reviewed; 444 AA.
AC Q8VD58; Q3U1A3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protein EVI2B {ECO:0000250|UniProtKB:P34910};
DE AltName: Full=Ecotropic viral integration site 2B protein;
DE Short=EVI-2B {ECO:0000250|UniProtKB:P34910};
DE AltName: CD_antigen=CD361;
DE Flags: Precursor;
GN Name=Evi2b {ECO:0000312|MGI:MGI:1890682};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Diencephalon, Spleen, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-250 AND SER-295, AND
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; SER-272; SER-279 AND
RP SER-295, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
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 [7]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=28186500; DOI=10.1038/cdd.2017.6;
RA Zjablovskaja P., Kardosova M., Danek P., Angelisova P., Benoukraf T.,
RA Wurm A.A., Kalina T., Sian S., Balastik M., Delwel R., Brdicka T.,
RA Tenen D.G., Behre G., Fiore F., Malissen B., Horejsi V., Alberich-Jorda M.;
RT "EVI2B is a C/EBPalpha target gene required for granulocytic
RT differentiation and functionality of hematopoietic progenitors.";
RL Cell Death Differ. 24:705-716(2017).
CC -!- FUNCTION: Required for granulocyte differentiation and functionality of
CC hematopoietic progenitor cells through the control of cell cycle
CC progression and survival of hematopoietic progenitor cells.
CC {ECO:0000269|PubMed:28186500}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in myeloid and lymphoid progenitors and
CC increased in mature hematopoietic populations with the highest levels
CC in granulocytes. {ECO:0000269|PubMed:28186500}.
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DR EMBL; AK034440; BAC28709.1; -; mRNA.
DR EMBL; AK039968; BAE20560.1; -; mRNA.
DR EMBL; AK156127; BAE33597.1; -; mRNA.
DR EMBL; AK170476; BAE41820.1; -; mRNA.
DR EMBL; AK171686; BAE42611.1; -; mRNA.
DR EMBL; AL591174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017548; AAH17548.1; -; mRNA.
DR CCDS; CCDS25121.1; -.
DR RefSeq; NP_001070964.1; NM_001077496.1.
DR RefSeq; NP_666135.1; NM_146023.4.
DR AlphaFoldDB; Q8VD58; -.
DR SMR; Q8VD58; -.
DR GlyGen; Q8VD58; 4 sites.
DR iPTMnet; Q8VD58; -.
DR PhosphoSitePlus; Q8VD58; -.
DR EPD; Q8VD58; -.
DR jPOST; Q8VD58; -.
DR MaxQB; Q8VD58; -.
DR PaxDb; Q8VD58; -.
DR PeptideAtlas; Q8VD58; -.
DR PRIDE; Q8VD58; -.
DR ProteomicsDB; 275698; -.
DR Ensembl; ENSMUST00000170422; ENSMUSP00000128569; ENSMUSG00000070354.
DR Ensembl; ENSMUST00000179322; ENSMUSP00000136153; ENSMUSG00000093938.
DR GeneID; 101488212; -.
DR GeneID; 216984; -.
DR KEGG; mmu:101488212; -.
DR KEGG; mmu:216984; -.
DR UCSC; uc007kko.1; mouse.
DR CTD; 101488212; -.
DR CTD; 2124; -.
DR MGI; MGI:1890682; Evi2b.
DR VEuPathDB; HostDB:ENSMUSG00000070354; -.
DR VEuPathDB; HostDB:ENSMUSG00000093938; -.
DR eggNOG; ENOG502S3T8; Eukaryota.
DR GeneTree; ENSGT00390000009142; -.
DR HOGENOM; CLU_048893_0_0_1; -.
DR InParanoid; Q8VD58; -.
DR OMA; NNEIQCQ; -.
DR OrthoDB; 997203at2759; -.
DR PhylomeDB; Q8VD58; -.
DR TreeFam; TF336167; -.
DR BioGRID-ORCS; 101488212; 5 hits in 33 CRISPR screens.
DR BioGRID-ORCS; 216984; 3 hits in 39 CRISPR screens.
DR PRO; PR:Q8VD58; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VD58; protein.
DR Bgee; ENSMUSG00000070354; Expressed in granulocyte and 17 other tissues.
DR ExpressionAtlas; Q8VD58; baseline and differential.
DR Genevisible; Q8VD58; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0061515; P:myeloid cell development; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0030854; P:positive regulation of granulocyte differentiation; IMP:UniProtKB.
DR GO; GO:0045660; P:positive regulation of neutrophil differentiation; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:2000035; P:regulation of stem cell division; IMP:UniProtKB.
DR InterPro; IPR033239; EVI2B.
DR PANTHER; PTHR15384; PTHR15384; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..444
FT /note="Protein EVI2B"
FT /id="PRO_0000021214"
FT TOPO_DOM 24..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 104..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..189
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 250
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 444 AA; 47993 MW; 2BEBB2E4515489BF CRC64;
MEFKYLVFIV LCQYLDNTFF SETEAITTEQ QSLSTLITPS LYVTTDSQNT AGNALSQTTR
FKNISSGQQA SPAQITPEQA TPAVYVSSSP LTYNITRQAE SAVNNSLPQT SPSGFTLTNQ
PSPSTYNSTG QPPKHLVYTS TQQPPSPAPT SSGKPEVEST HNQPTKSTPT IYLQRDTPPP
PPPPLTSEPP SGKGTAHKNN HNAIAAILIG TIIISMLVAI LMIILWKYLR KPVLNDQNWA
GRSPFADGET PEMCMDNIRE SEASTKRASV VSLMTWKPSK STLLADDLEV KLFESSEHIN
DTSNLKTDNV EVQINGLSED SADGSTVGTA VSSDDADLAL PPPLLDLDEN LPNKPTVTVV
SPLPNDSINP QPSPDGLNQV CEEQHSKIQE PFPPPPDSFN VPLSAGDFIN NQESAHEAQC
QEFSTPDLHP DLTDSLPPPP TELL
