DIP2B_MOUSE
ID DIP2B_MOUSE Reviewed; 1574 AA.
AC Q3UH60; Q8C1W5; Q8CDG9; Q8CHA2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Disco-interacting protein 2 homolog B;
DE Short=DIP2 homolog B;
GN Name=Dip2b; Synonyms=Kiaa1463;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Testis;
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 MRNA] OF 614-1574.
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [3]
RP IDENTIFICATION BY 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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-152 AND SER-202, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [6]
RP FUNCTION, INTERACTION WITH ALPHA-TUBULIN, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=32153366; DOI=10.3389/fncel.2020.00029;
RA Xing Z.K., Zhang L.Q., Zhang Y., Sun X., Sun X.L., Yu H.L., Zheng Y.W.,
RA He Z.X., Zhu X.J.;
RT "DIP2B Interacts With alpha-Tubulin to Regulate Axon Outgrowth.";
RL Front. Cell. Neurosci. 14:29-29(2020).
CC -!- FUNCTION: Negatively regulates axonal outgrowth and is essential for
CC normal synaptic transmission (PubMed:32153366). Not required for
CC regulation of axon polarity (PubMed:32153366). Promotes acetylation of
CC alpha-tubulin (PubMed:32153366). {ECO:0000269|PubMed:32153366}.
CC -!- SUBUNIT: Interacts with alpha-tubulin. {ECO:0000269|PubMed:32153366}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC {ECO:0000269|PubMed:32153366}. Cell projection, axon
CC {ECO:0000269|PubMed:32153366}. Perikaryon
CC {ECO:0000269|PubMed:32153366}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UH60-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UH60-2; Sequence=VSP_031278, VSP_031279;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and spinal cord (at
CC protein level) (PubMed:32153366). In brain, expression is detected in
CC the main olfactory bulb, cortex, lateral ventricle, cornu ammonis 1,
CC cornu ammonis 3, dentate gyrus, striatum, cerebellar cortex and medial
CC habenula (PubMed:32153366). Expressed primarily in neurons including
CC excitatory pyramidal neurons and inhibitory interneurons
CC (PubMed:32153366). {ECO:0000269|PubMed:32153366}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expression initiates at 15.5 dpc in
CC both the neocortex and hippocampus. {ECO:0000269|PubMed:32153366}.
CC -!- DISRUPTION PHENOTYPE: Excessive axonal outgrowth and branching with
CC decreased dendritic outgrowth (PubMed:32153366). Reduced acetylation of
CC alpha-tubulin (PubMed:32153366). {ECO:0000269|PubMed:32153366}.
CC -!- SIMILARITY: Belongs to the DIP2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41112.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK030064; BAC26764.1; -; mRNA.
DR EMBL; AK090139; BAC41112.1; ALT_INIT; mRNA.
DR EMBL; AK147562; BAE27997.1; -; mRNA.
DR EMBL; AB093297; BAC41479.1; -; mRNA.
DR CCDS; CCDS49731.1; -. [Q3UH60-1]
DR RefSeq; NP_001152833.1; NM_001159361.1. [Q3UH60-1]
DR AlphaFoldDB; Q3UH60; -.
DR SMR; Q3UH60; -.
DR BioGRID; 232113; 15.
DR IntAct; Q3UH60; 4.
DR MINT; Q3UH60; -.
DR STRING; 10090.ENSMUSP00000097777; -.
DR iPTMnet; Q3UH60; -.
DR PhosphoSitePlus; Q3UH60; -.
DR EPD; Q3UH60; -.
DR jPOST; Q3UH60; -.
DR MaxQB; Q3UH60; -.
DR PaxDb; Q3UH60; -.
DR PeptideAtlas; Q3UH60; -.
DR PRIDE; Q3UH60; -.
DR ProteomicsDB; 279415; -. [Q3UH60-1]
DR ProteomicsDB; 279416; -. [Q3UH60-2]
DR Antibodypedia; 55127; 39 antibodies from 14 providers.
DR DNASU; 239667; -.
DR Ensembl; ENSMUST00000100203; ENSMUSP00000097777; ENSMUSG00000023026. [Q3UH60-1]
DR GeneID; 239667; -.
DR KEGG; mmu:239667; -.
DR UCSC; uc007xqq.2; mouse. [Q3UH60-1]
DR CTD; 57609; -.
DR MGI; MGI:2145977; Dip2b.
DR VEuPathDB; HostDB:ENSMUSG00000023026; -.
DR eggNOG; KOG3628; Eukaryota.
DR GeneTree; ENSGT00950000182997; -.
DR InParanoid; Q3UH60; -.
DR OMA; VPVCTAT; -.
DR OrthoDB; 539697at2759; -.
DR PhylomeDB; Q3UH60; -.
DR TreeFam; TF312871; -.
DR BioGRID-ORCS; 239667; 1 hit in 57 CRISPR screens.
DR ChiTaRS; Dip2b; mouse.
DR PRO; PR:Q3UH60; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q3UH60; protein.
DR Bgee; ENSMUSG00000023026; Expressed in floor plate of midbrain and 257 other tissues.
DR ExpressionAtlas; Q3UH60; baseline and differential.
DR Genevisible; Q3UH60; MM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:2000758; P:positive regulation of peptidyl-lysine acetylation; IMP:UniProtKB.
DR CDD; cd05905; Dip2; 2.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.12780; -; 2.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR037337; Dip2-like_dom.
DR InterPro; IPR010506; DMAP1-bd.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF06464; DMAP_binding; 1.
DR SMART; SM01137; DMAP_binding; 1.
DR PROSITE; PS51912; DMAP1_BIND; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Neurogenesis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1574
FT /note="Disco-interacting protein 2 homolog B"
FT /id="PRO_0000318737"
FT DOMAIN 12..130
FT /note="DMAP1-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01260"
FT REGION 31..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P265"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P265"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P265"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P265"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P265"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P265"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P265"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P265"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P265"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P265"
FT VAR_SEQ 1..233
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031278"
FT VAR_SEQ 234..263
FT /note="PANIDLPPSGIVKGMHKGSNRSSLMDTADG -> MVGFHRRCCELTVEKRSS
FT TREEGAWVAFPC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031279"
FT CONFLICT 303..304
FT /note="GI -> V (in Ref. 1; BAC26764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1574 AA; 171126 MW; 915CE0332029FE45 CRC64;
MAERGLEPSP AAVAALPPEV RAQLAELELE LSEGDITQKG YEKKRSKLLS PYSPQTQETD
SIGQKERNQT PAPTAAQTSA PSKYHRSRSG GARDERYRSD IHTEAVQAAL AKHKEQKMAL
PMPTKRRSTF VQSPADACTP PDTSSASEDE GSLRRQAALS AALQQSLQNA ESWINRSIQG
SSTSSSASST LSHGEVKGTS GSLADVFANT RIENVSAPPD VTATTSSSSS SLRPANIDLP
PSGIVKGMHK GSNRSSLMDT ADGVPVNSRV STKIQQLLNT LKRPKRPPLK EFFVDDSEEI
VEGIPQPDPN QPKPEGRQMT PVKGEPLGVI CNWPPALESA LQRWGSTQAK CPCLTGLDVT
GKPVYTLTYG KLWSRSLKLA YTLLNKLGTK NEPVLKPGDR VALVYPNNDP VMFMVAFYGC
LLAEVIPVPI EVPLTRKDAG GQQIGFLLGS CGIALALTSE ICLKGLPKTQ NGEIVQFKGW
PRLKWVVTDS KYLSKPPKDW QPHISPAGTE PAYIEYKTSK EGSVMGVTVS RLAMLSQCQA
LSQACNYSEG ETVVNVLDFK KDAGLWHGMF ANVMNKMHTI SVPYSVMKTC PLSWVQRVHA
HKAKVALVKC RDLHWAMMAH RDQRDVSLSS LRMLIVTDGA NPWSVSSCDA FLSLFQSHGL
KPEAICPCAT SAEAMTVAIR RPGVPGAPLP GRAILSMNGL SYGVIRVNTE DKNSALTVQD
VGHVMPGGMM CIVKPDGLPQ LCRTDEIGEI CVSSRTGGMM YFGLAGVTKN TFEVIPVTSS
GSPVGDVPFI RSGLLGFVGP GSLVFVVGKM DGLLMVSGRR HNADDIVATG LAVESIKTVY
RGRIAVFSVS VFYDERIVVV AEQRPDASEE DSFQWMSRVL QAIDSIHQVG VYCLALVPAN
TLPKTPLGGI HISQTKQLFL EGSLHPCNIL MCPHTCVTNL PKPRQKQPGV GPASVMVGNL
VAGKRIAQAA GRDLGQIEEN DLVRKHQFLA EILQWRAQAT PDHVLFMLLN AKGTTVCTAS
CLQLHKRAER IASVLGDKGH LNAGDNVVLL YPPGIELIAA FYGCLYAGCI PVTVRPPHAQ
NLTATLPTVR MVVDVSKAAC VLTTQTLMRL LKSREAAAAV DVKTWPAIID TDDLPRKRLP
QLYKPPTPEM LAYLDFSVST TGMLTGVKMS HSAVNALCRA IKLQCELYSS RQIAICLDPY
CGLGFALWCL CSVYSGHQSV LIPPMELENN LFLWLATVNQ YKIRDTFCSY SVMELCTKGL
GNQVEVLKTR GINLSCIRTC VVVAEERPRV SLQQSFSKLF KDIGLSPRAV STTFGSRVNV
AICLQGTSGP DPTTVYVDLK SLRHDRVRLV ERGAPQSLLL SESGKILPGV KVVIVNPETK
GPVGDSHLGE IWVNSPHTAS GYYTIYDSET LQADHFNTRL SFGDAAQTLW ARTGYLGFVR
RTELTAATGE RHDALYVVGA LDETLELRGL RYHPIDIETS VSRVHRSIAE CAVFTWTNLL
VVVVELCGSE QEALDLVPLV TNVVLEEHYL IVGVVVVVDP GVVPINSRGE KQRMHLRDSF
LADQLDPIYV AYNM
