DJC27_MOUSE
ID DJC27_MOUSE Reviewed; 273 AA.
AC Q8CFP6; Q8BX00; Q923I0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=DnaJ homolog subfamily C member 27;
DE AltName: Full=Rab and DnaJ domain-containing protein;
GN Name=Dnajc27; Synonyms=Rabj, Rbj;
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 [MRNA].
RA Chen T., Zhang W., Cao X.;
RT "Novel Rab gene rabJ.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Eye;
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 IDENTIFICATION.
RX PubMed=14980719; DOI=10.1016/j.gene.2003.11.010;
RA Nepomuceno-Silva J.L., de Melo L.D., Mendonca S.M., Paixao J.C.,
RA Lopes U.G.;
RT "RJLs: a new family of Ras-related GTP-binding proteins.";
RL Gene 327:221-232(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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, SUBCELLULAR LOCATION, INTERACTION WITH MAPK1 AND MAP2K1, AND
RP MUTAGENESIS OF SER-30 AND HIS-75.
RX PubMed=24746703; DOI=10.1016/j.ccr.2014.03.009;
RA Chen T., Yang M., Yu Z., Tang S., Wang C., Zhu X., Guo J., Li N., Zhang W.,
RA Hou J., Liu H., Han C., Liu Q., Gu Y., Qian C., Wan T., Cui L., Zhu M.,
RA Zheng W., Cao X.;
RT "Small GTPase RBJ mediates nuclear entrapment of MEK1/MEK2 in tumor
RT progression.";
RL Cancer Cell 25:682-696(2014).
CC -!- FUNCTION: GTPase which can activate the MEK/ERK pathway and induce cell
CC transformation when overexpressed. May act as a nuclear scaffold for
CC MAPK1, probably by association with MAPK1 nuclear export signal leading
CC to enhanced ERK1/ERK2 signaling. {ECO:0000269|PubMed:24746703}.
CC -!- SUBUNIT: Interacts directly with MAPK1 (wild-type and kinase-deficient
CC forms). Interacts directly (in GTP-bound form) with MAP2K1 (wild-type
CC and kinase-deficient forms). {ECO:0000269|PubMed:24746703}.
CC -!- INTERACTION:
CC Q8CFP6; P31938: Map2k1; NbExp=3; IntAct=EBI-9548773, EBI-298860;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24746703}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AY035893; AAK62027.1; -; mRNA.
DR EMBL; AK049300; BAC33667.1; -; mRNA.
DR EMBL; BC042643; AAH42643.1; -; mRNA.
DR EMBL; BC051140; AAH51140.1; -; mRNA.
DR EMBL; BK001285; DAA01324.1; -; mRNA.
DR CCDS; CCDS25786.1; -.
DR RefSeq; NP_694722.2; NM_153082.4.
DR AlphaFoldDB; Q8CFP6; -.
DR SMR; Q8CFP6; -.
DR IntAct; Q8CFP6; 2.
DR STRING; 10090.ENSMUSP00000020986; -.
DR iPTMnet; Q8CFP6; -.
DR PhosphoSitePlus; Q8CFP6; -.
DR EPD; Q8CFP6; -.
DR MaxQB; Q8CFP6; -.
DR PaxDb; Q8CFP6; -.
DR PeptideAtlas; Q8CFP6; -.
DR PRIDE; Q8CFP6; -.
DR ProteomicsDB; 279673; -.
DR Antibodypedia; 27605; 157 antibodies from 22 providers.
DR DNASU; 217378; -.
DR Ensembl; ENSMUST00000020986; ENSMUSP00000020986; ENSMUSG00000020657.
DR Ensembl; ENSMUST00000049584; ENSMUSP00000106803; ENSMUSG00000020657.
DR Ensembl; ENSMUST00000219923; ENSMUSP00000151848; ENSMUSG00000020657.
DR GeneID; 217378; -.
DR KEGG; mmu:217378; -.
DR UCSC; uc007mxi.2; mouse.
DR CTD; 51277; -.
DR MGI; MGI:2443036; Dnajc27.
DR VEuPathDB; HostDB:ENSMUSG00000020657; -.
DR eggNOG; KOG0098; Eukaryota.
DR GeneTree; ENSGT00940000157133; -.
DR HOGENOM; CLU_041217_16_0_1; -.
DR InParanoid; Q8CFP6; -.
DR OMA; MGNAETG; -.
DR OrthoDB; 1288652at2759; -.
DR PhylomeDB; Q8CFP6; -.
DR TreeFam; TF328564; -.
DR BioGRID-ORCS; 217378; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Dnajc27; mouse.
DR PRO; PR:Q8CFP6; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8CFP6; protein.
DR Bgee; ENSMUSG00000020657; Expressed in spermatocyte and 183 other tissues.
DR Genevisible; Q8CFP6; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR GO; GO:0071701; P:regulation of MAPK export from nucleus; IDA:UniProtKB.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..273
FT /note="DnaJ homolog subfamily C member 27"
FT /id="PRO_0000332976"
FT DOMAIN 217..273
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 1..18
FT /note="Required for interaction with MAPK1"
FT /evidence="ECO:0000269|PubMed:24746703"
FT BINDING 23..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 71..75
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 134..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MUTAGEN 30
FT /note="S->N: Abolishes GTP binding."
FT /evidence="ECO:0000269|PubMed:24746703"
FT MUTAGEN 75
FT /note="H->L: Abolishes GTPase activity."
FT /evidence="ECO:0000269|PubMed:24746703"
FT MUTAGEN 75
FT /note="H->Q: Increases GTPase activity."
FT /evidence="ECO:0000269|PubMed:24746703"
FT CONFLICT 3..5
FT /note="TNV -> AYM (in Ref. 1; AAK62027)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="K -> E (in Ref. 1; AAK62027)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="S -> F (in Ref. 1; AAK62027)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="K -> E (in Ref. 1; AAK62027)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="T -> A (in Ref. 2; BAC33667)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="K -> KW (in Ref. 1; AAK62027)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 30831 MW; 805523789CECC329 CRC64;
METNVPKRKE PAKSLRIKVI SMGNAEVGKS CIIKRYCEKR FVSKYLATIG IDYGVTKVQV
RDREIKVNIF DMAGHPFFFE VRNEFYKDTQ GVILVYDVGQ KDSFDALDSW LAEMKQELGP
HGNMDNIVFV VCANKIDCSK HRCIDESEGR LWAESKGFLY FETSAQTGEG INEMFQTFYL
SIVDLCENGG KRPTASSSAS FTKEQADTIR RIRNSKDSWE MLGVRPGASR EEVNKAYRKL
AVLLHPDKCV APGSEDAFKA VVNARTALLK NIK
