RAB6C_HUMAN
ID RAB6C_HUMAN Reviewed; 254 AA.
AC Q9H0N0; Q53RU3; Q6FIF7; Q9P128;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Ras-related protein Rab-6C;
DE AltName: Full=Rab6-like protein WTH3;
GN Name=RAB6C; Synonyms=WTH3;
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], AND VARIANT THR-159.
RX PubMed=12007787; DOI=10.1016/s0167-4889(02)00164-7;
RA Shan J., Yuan L., Budman D.R., Xu H.-P.;
RT "WTH3, a new member of the Rab6 gene family, and multidrug resistance.";
RL Biochim. Biophys. Acta 1589:112-123(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-159.
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-159.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-159.
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-175, AND VARIANT THR-159.
RX PubMed=11054569; DOI=10.1016/s0378-1119(00)00395-4;
RA Shan J., Mason J.M., Yuan L., Barcia M., Porti D., Calabro A., Budman D.,
RA Vinciguerra V., Xu H.-P.;
RT "Rab6c, a new member of the Rab gene family, is involved in drug resistance
RT in MCF7/AdrR cells.";
RL Gene 257:67-75(2000).
RN [8]
RP GTP-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=16103095; DOI=10.1158/0008-5472.can-05-0658;
RA Tian K., Jurukovski V., Yuan L., Shan J., Xu H.;
RT "WTH3, which encodes a small G protein, is differentially regulated in
RT multidrug-resistant and sensitive MCF7 cells.";
RL Cancer Res. 65:7421-7428(2005).
RN [9]
RP FUNCTION.
RX PubMed=17426708; DOI=10.1038/sj.bjc.6603724;
RA Tian K., Wang Y., Xu H.;
RT "WTH3 is a direct target of the p53 protein.";
RL Br. J. Cancer 96:1579-1586(2007).
RN [10]
RP FUNCTION.
RX PubMed=18992151; DOI=10.1186/1471-2407-8-327;
RA Tian K., Wang Y., Huang Y., Sun B., Li Y., Xu H.;
RT "Methylation of WTH3, a possible drug resistant gene, inhibits p53
RT regulated expression.";
RL BMC Cancer 8:327-327(2008).
RN [11]
RP RETROGENE, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ALA-25 AND ILE-45.
RX PubMed=20064528; DOI=10.1016/j.jmb.2010.01.009;
RA Young J., Menetrey J., Goud B.;
RT "RAB6C is a retrogene that encodes a centrosomal protein involved in cell
RT cycle progression.";
RL J. Mol. Biol. 397:69-88(2010).
RN [12]
RP AMPYLATION AT TYR-82.
RX PubMed=21822290; DOI=10.1038/nature10335;
RA Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.;
RT "Modulation of Rab GTPase function by a protein phosphocholine
RT transferase.";
RL Nature 477:103-106(2011).
CC -!- FUNCTION: May be involved in the regulation of centrosome duplication
CC and cell cycle progression. {ECO:0000269|PubMed:17426708,
CC ECO:0000269|PubMed:18992151, ECO:0000269|PubMed:20064528}.
CC -!- INTERACTION:
CC Q9H0N0; Q92870-2: APBB2; NbExp=3; IntAct=EBI-2856714, EBI-21535880;
CC Q9H0N0; D3DTS7: PMP22; NbExp=3; IntAct=EBI-2856714, EBI-25882629;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16103095}. Cytoplasm
CC {ECO:0000269|PubMed:16103095}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:20064528}.
CC -!- TISSUE SPECIFICITY: Highest levels are found in fetal and adult brain,
CC prostate, testis and spinal cord. Undetectable expression in adrenal
CC gland, skeletal muscle, bone marrow, fetal, and adult liver, heart,
CC salivary gland, and trachea. Detected in the HEK293, HEK293T, LNCaP,
CC MCF-7, T-47D and EVSA-T cell lines (at protein level).
CC {ECO:0000269|PubMed:20064528}.
CC -!- MISCELLANEOUS: Primate-specific retrogene derived from isoform 2 of
CC RAB6A transcript.
CC -!- MISCELLANEOUS: Previously reported to exhibit GTP-binding affinity
CC comparable to that of RAB6A (PubMed:16103095). In contrast
CC (PubMed:20064528) concludes that RAB6C is an inefficient GTP-binding.
CC {ECO:0000305|PubMed:16103095, ECO:0000305|PubMed:20064528}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF309646; AAN39685.1; -; mRNA.
DR EMBL; AL136727; CAB66661.1; -; mRNA.
DR EMBL; CR533469; CAG38500.1; -; mRNA.
DR EMBL; AC079776; AAY15045.1; -; Genomic_DNA.
DR EMBL; CH471103; EAW95362.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11700.1; -; Genomic_DNA.
DR EMBL; BC120999; AAI21000.1; -; mRNA.
DR EMBL; AF124200; AAF28422.1; -; Genomic_DNA.
DR CCDS; CCDS46408.1; -.
DR RefSeq; NP_115520.2; NM_032144.2.
DR AlphaFoldDB; Q9H0N0; -.
DR SMR; Q9H0N0; -.
DR BioGRID; 123878; 10.
DR IntAct; Q9H0N0; 8.
DR MINT; Q9H0N0; -.
DR STRING; 9606.ENSP00000387307; -.
DR iPTMnet; Q9H0N0; -.
DR PhosphoSitePlus; Q9H0N0; -.
DR BioMuta; RAB6C; -.
DR DMDM; 166214970; -.
DR EPD; Q9H0N0; -.
DR jPOST; Q9H0N0; -.
DR MassIVE; Q9H0N0; -.
DR MaxQB; Q9H0N0; -.
DR PaxDb; Q9H0N0; -.
DR PeptideAtlas; Q9H0N0; -.
DR PRIDE; Q9H0N0; -.
DR ProteomicsDB; 80303; -.
DR TopDownProteomics; Q9H0N0; -.
DR Antibodypedia; 58076; 141 antibodies from 22 providers.
DR DNASU; 84084; -.
DR Ensembl; ENST00000410061.4; ENSP00000387307.2; ENSG00000222014.6.
DR GeneID; 84084; -.
DR KEGG; hsa:84084; -.
DR MANE-Select; ENST00000410061.4; ENSP00000387307.2; NM_032144.3; NP_115520.2.
DR UCSC; uc002tpx.2; human.
DR CTD; 84084; -.
DR DisGeNET; 84084; -.
DR GeneCards; RAB6C; -.
DR HGNC; HGNC:16525; RAB6C.
DR HPA; ENSG00000222014; Tissue enhanced (brain, breast, parathyroid gland).
DR MIM; 612909; gene.
DR neXtProt; NX_Q9H0N0; -.
DR OpenTargets; ENSG00000222014; -.
DR PharmGKB; PA34148; -.
DR VEuPathDB; HostDB:ENSG00000222014; -.
DR eggNOG; KOG0094; Eukaryota.
DR GeneTree; ENSGT00940000168192; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; Q9H0N0; -.
DR OrthoDB; 1277051at2759; -.
DR PhylomeDB; Q9H0N0; -.
DR TreeFam; TF300803; -.
DR PathwayCommons; Q9H0N0; -.
DR SignaLink; Q9H0N0; -.
DR SIGNOR; Q9H0N0; -.
DR BioGRID-ORCS; 84084; 41 hits in 1030 CRISPR screens.
DR ChiTaRS; RAB6C; human.
DR GeneWiki; RAB6C; -.
DR GenomeRNAi; 84084; -.
DR Pharos; Q9H0N0; Tbio.
DR PRO; PR:Q9H0N0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H0N0; protein.
DR Bgee; ENSG00000222014; Expressed in endometrium and 62 other tissues.
DR Genevisible; Q9H0N0; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
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; IDA:UniProtKB.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:GO_Central.
DR GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; GTP-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..254
FT /note="Ras-related protein Rab-6C"
FT /id="PRO_0000121117"
FT REGION 1..174
FT /note="Required for centrosome localization"
FT MOTIF 42..50
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 82
FT /note="O-AMP-tyrosine; by Legionella DrrA"
FT /evidence="ECO:0000269|PubMed:21822290"
FT VARIANT 159
FT /note="A -> T (in dbSNP:rs4662674)"
FT /evidence="ECO:0000269|PubMed:11054569,
FT ECO:0000269|PubMed:11230166, ECO:0000269|PubMed:12007787,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_038161"
FT MUTAGEN 25
FT /note="A->G: No GTP binding. No GTP binding; when
FT associated with T-45."
FT /evidence="ECO:0000269|PubMed:20064528"
FT MUTAGEN 45
FT /note="I->T: No GTP binding; when associated with G-25."
FT /evidence="ECO:0000269|PubMed:20064528"
SQ SEQUENCE 254 AA; 28355 MW; 72A4D8DED771F754 CRC64;
MSAGGDFGNP LRKFKLVFLG EQSVAKTSLI TRFRYDSFDN TYQAIIGIDF LSKTMYLEDG
TIGLRLWDTA GQERLRSLIP RYIRDSAAAV VVYDITNVNS FQQTTKWIDD VRTERGSDVI
ITLVGNRTDL ADKRQVSVEE GERKAKGLNV TFIETRAKAG YNVKQLFRRV AAALPGMEST
QDGSREDMSD IKLEKPQEQT VSEGGCSCYS PMSSSTLPQK PPYSFIDCSV NIGLNLFPSL
ITFCNSSLLP VSWR
