DJC27_HUMAN
ID DJC27_HUMAN Reviewed; 273 AA.
AC Q9NZQ0; Q5JV88; Q86Y24;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=DnaJ homolog subfamily C member 27;
DE AltName: Full=Rab and DnaJ domain-containing protein;
GN Name=DNAJC27; Synonyms=RABJS, RBJ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RA Chen T., Zhang W., Li N., Wan T., Zhang M., Chen G., Zhang Y., Cao X.;
RT "Identification of a unique Rab GTPase containing a J domain that interacts
RT with Hsc70.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP IDENTIFICATION, AND POSSIBLE LACK OF GTPASE ACTIVITY.
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 [6]
RP TISSUE SPECIFICITY.
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).
RN [7]
RP STRUCTURE BY NMR OF 197-273.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the dnaJ-like domain from human Ras-associated
RT protein RAP1.";
RL Submitted (OCT-2007) to the PDB data bank.
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:0000250|UniProtKB:Q8CFP6}.
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:0000250|UniProtKB:Q8CFP6}.
CC -!- INTERACTION:
CC Q9NZQ0; Q12800: TFCP2; NbExp=6; IntAct=EBI-10317544, EBI-717422;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8CFP6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NZQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZQ0-2; Sequence=VSP_033409, VSP_033410;
CC Name=3;
CC IsoId=Q9NZQ0-3; Sequence=VSP_033411, VSP_033412;
CC -!- TISSUE SPECIFICITY: Overexpressed in gastrointestinal cancers;
CC expression correlates with later tumor-node-metastasis stages of
CC colorectal cancers. {ECO:0000269|PubMed:24746703}.
CC -!- MISCELLANEOUS: DNAJC27/RBJ knockdown in several colorectal cancer cell
CC lines is correlated to inhibition of MEK/ERK activation, cell
CC proliferation, colony formation and in vivo tumor growth.
CC {ECO:0000269|PubMed:24746703}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF178983; AAF44347.1; -; mRNA.
DR EMBL; AY094594; AAM22521.1; -; mRNA.
DR EMBL; AL137731; CAI46214.1; -; mRNA.
DR EMBL; CH471053; EAX00736.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00735.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00737.1; -; Genomic_DNA.
DR EMBL; BC034049; AAH34049.1; -; mRNA.
DR EMBL; BK001284; DAA01323.1; -; mRNA.
DR CCDS; CCDS1716.1; -. [Q9NZQ0-1]
DR CCDS; CCDS74493.1; -. [Q9NZQ0-3]
DR RefSeq; NP_001185488.1; NM_001198559.1. [Q9NZQ0-3]
DR RefSeq; NP_057628.1; NM_016544.2. [Q9NZQ0-1]
DR PDB; 2YS8; NMR; -; A=197-273.
DR PDBsum; 2YS8; -.
DR AlphaFoldDB; Q9NZQ0; -.
DR SMR; Q9NZQ0; -.
DR BioGRID; 119429; 14.
DR IntAct; Q9NZQ0; 1.
DR STRING; 9606.ENSP00000264711; -.
DR iPTMnet; Q9NZQ0; -.
DR PhosphoSitePlus; Q9NZQ0; -.
DR BioMuta; DNAJC27; -.
DR DMDM; 74734733; -.
DR MassIVE; Q9NZQ0; -.
DR PaxDb; Q9NZQ0; -.
DR PeptideAtlas; Q9NZQ0; -.
DR PRIDE; Q9NZQ0; -.
DR ProteomicsDB; 83475; -. [Q9NZQ0-1]
DR ProteomicsDB; 83477; -. [Q9NZQ0-3]
DR Antibodypedia; 27605; 157 antibodies from 22 providers.
DR DNASU; 51277; -.
DR Ensembl; ENST00000264711.7; ENSP00000264711.2; ENSG00000115137.12. [Q9NZQ0-1]
DR Ensembl; ENST00000380809.7; ENSP00000370187.3; ENSG00000115137.12. [Q9NZQ0-2]
DR Ensembl; ENST00000534855.5; ENSP00000440086.2; ENSG00000115137.12. [Q9NZQ0-3]
DR GeneID; 51277; -.
DR KEGG; hsa:51277; -.
DR MANE-Select; ENST00000264711.7; ENSP00000264711.2; NM_016544.3; NP_057628.1.
DR UCSC; uc002rft.2; human. [Q9NZQ0-1]
DR CTD; 51277; -.
DR DisGeNET; 51277; -.
DR GeneCards; DNAJC27; -.
DR HGNC; HGNC:30290; DNAJC27.
DR HPA; ENSG00000115137; Tissue enhanced (testis).
DR MIM; 613527; gene.
DR neXtProt; NX_Q9NZQ0; -.
DR OpenTargets; ENSG00000115137; -.
DR PharmGKB; PA164718860; -.
DR VEuPathDB; HostDB:ENSG00000115137; -.
DR eggNOG; KOG0098; Eukaryota.
DR GeneTree; ENSGT00940000157133; -.
DR HOGENOM; CLU_041217_16_0_1; -.
DR InParanoid; Q9NZQ0; -.
DR OMA; MGNAETG; -.
DR OrthoDB; 1288652at2759; -.
DR PhylomeDB; Q9NZQ0; -.
DR TreeFam; TF328564; -.
DR PathwayCommons; Q9NZQ0; -.
DR SignaLink; Q9NZQ0; -.
DR BioGRID-ORCS; 51277; 11 hits in 1072 CRISPR screens.
DR EvolutionaryTrace; Q9NZQ0; -.
DR GenomeRNAi; 51277; -.
DR Pharos; Q9NZQ0; Tbio.
DR PRO; PR:Q9NZQ0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NZQ0; protein.
DR Bgee; ENSG00000115137; Expressed in endothelial cell and 187 other tissues.
DR Genevisible; Q9NZQ0; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0071701; P:regulation of MAPK export from nucleus; IEA:Ensembl.
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 3D-structure; Alternative splicing; GTP-binding; Nucleotide-binding;
KW Nucleus; Oncogene; Reference proteome.
FT CHAIN 1..273
FT /note="DnaJ homolog subfamily C member 27"
FT /id="PRO_0000332975"
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:0000250|UniProtKB:Q8CFP6"
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 VAR_SEQ 81..90
FT /note="VRNEFYKDTQ -> MRKLRRREVK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033409"
FT VAR_SEQ 91..273
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033410"
FT VAR_SEQ 177
FT /note="T -> G (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_033411"
FT VAR_SEQ 178..273
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_033412"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:2YS8"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:2YS8"
FT HELIX 230..244
FT /evidence="ECO:0007829|PDB:2YS8"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:2YS8"
FT HELIX 254..272
FT /evidence="ECO:0007829|PDB:2YS8"
SQ SEQUENCE 273 AA; 30855 MW; A3A0CE43EA6A2BCA CRC64;
MEANMPKRKE PGRSLRIKVI SMGNAEVGKS CIIKRYCEKR FVSKYLATIG IDYGVTKVHV
RDREIKVNIF DMAGHPFFYE VRNEFYKDTQ GVILVYDVGQ KDSFDALDAW LAEMKQELGP
HGNMENIIFV VCANKIDCTK HRCVDESEGR LWAESKGFLY FETSAQTGEG INEMFQTFYI
SIVDLCENGG KRPTTNSSAS FTKEQADAIR RIRNSKDSWD MLGVKPGASR DEVNKAYRKL
AVLLHPDKCV APGSEDAFKA VVNARTALLK NIK
