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   28-JAN-2026, entry version 184.
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_016544.3. [Q9NZQ0-1]
DR   PDB; 2YS8; NMR; -; A=197-273.
DR   PDBsum; 2YS8; -.
DR   AlphaFoldDB; Q9NZQ0; -.
DR   SMR; Q9NZQ0; -.
DR   BioGRID; 119429; 14.
DR   FunCoup; Q9NZQ0; 932.
DR   IntAct; Q9NZQ0; 6.
DR   STRING; 9606.ENSP00000264711; -.
DR   iPTMnet; Q9NZQ0; -.
DR   PhosphoSitePlus; Q9NZQ0; -.
DR   BioMuta; DNAJC27; -.
DR   DMDM; 74734733; -.
DR   MassIVE; Q9NZQ0; -.
DR   PaxDb; 9606-ENSP00000264711; -.
DR   PeptideAtlas; Q9NZQ0; -.
DR   ProteomicsDB; 83475; -. [Q9NZQ0-1]
DR   ProteomicsDB; 83477; -. [Q9NZQ0-3]
DR   Antibodypedia; 27605; 158 antibodies from 21 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   AGR; HGNC:30290; -.
DR   ClinPGx; PA164718860; -.
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   OpenTargets; ENSG00000115137; -.
DR   VEuPathDB; HostDB:ENSG00000115137; -.
DR   eggNOG; KOG0098; Eukaryota.
DR   GeneTree; ENSGT00940000157133; -.
DR   HOGENOM; CLU_041217_16_0_1; -.
DR   InParanoid; Q9NZQ0; -.
DR   OMA; NMENVVF; -.
DR   OrthoDB; 8830751at2759; -.
DR   PAN-GO; Q9NZQ0; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9NZQ0; -.
DR   PathwayCommons; Q9NZQ0; -.
DR   SignaLink; Q9NZQ0; -.
DR   Agora; ENSG00000115137; -.
DR   BioGRID-ORCS; 51277; 12 hits in 1151 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 188 other cell types or tissues.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-ARBA.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-ARBA.
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   CDD; cd06257; DnaJ; 1.
DR   CDD; cd04119; RJL; 1.
DR   FunFam; 3.40.50.300:FF:000697; DnaJ homolog subfamily C member 27; 1.
DR   FunFam; 1.10.287.110:FF:000019; dnaJ homolog subfamily C member 27; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47981; RAB FAMILY; 1.
DR   PANTHER; PTHR47981:SF20; RAS-RELATED PROTEIN RAB-7A; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Proteomics identification; 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
//