RAB28_HUMAN
ID RAB28_HUMAN Reviewed; 221 AA.
AC P51157; G8JLC5; Q8IYR8; Q8NI05;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Ras-related protein Rab-28;
DE Flags: Precursor;
GN Name=RAB28;
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 L AND S).
RC TISSUE=Testis;
RX PubMed=8647132; DOI=10.1111/j.1432-1033.1996.0833p.x;
RA Brauers A., Schuermann A., Massmann S., Muehl-Zuerbes P., Becker W.,
RA Kainulainen H., Lie C., Joost H.-G.;
RT "Alternative mRNA splicing of the novel GTPase Rab28 generates isoforms
RT with different C-termini.";
RL Eur. J. Biochem. 237:833-840(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM L).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS S AND 3).
RC TISSUE=Brain, and Embryonic stem cell;
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 ISOPRENYLATION AT CYS-218.
RX PubMed=17411337; DOI=10.1371/journal.pcbi.0030066;
RA Maurer-Stroh S., Koranda M., Benetka W., Schneider G., Sirota F.L.,
RA Eisenhaber F.;
RT "Towards complete sets of farnesylated and geranylgeranylated proteins.";
RL PLoS Comput. Biol. 3:634-648(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-8, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP INVOLVEMENT IN CORD18, AND TISSUE SPECIFICITY.
RX PubMed=23746546; DOI=10.1016/j.ajhg.2013.05.005;
RG European Retinal Disease Consortium;
RA Roosing S., Rohrschneider K., Beryozkin A., Sharon D., Weisschuh N.,
RA Staller J., Kohl S., Zelinger L., Peters T.A., Neveling K., Strom T.M.,
RA van den Born L.I., Hoyng C.B., Klaver C.C., Roepman R., Wissinger B.,
RA Banin E., Cremers F.P., den Hollander A.I.;
RT "Mutations in RAB28, encoding a farnesylated small GTPase, are associated
RT with autosomal-recessive cone-rod dystrophy.";
RL Am. J. Hum. Genet. 93:110-117(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 11-184 IN COMPLEX WITH GTP AND GDP
RP ANALOGS.
RX PubMed=19026641; DOI=10.1016/j.febslet.2008.11.008;
RA Lee S.H., Baek K., Dominguez R.;
RT "Large nucleotide-dependent conformational change in Rab28.";
RL FEBS Lett. 582:4107-4111(2008).
CC -!- INTERACTION:
CC P51157; Q4G176: ACSF3; NbExp=3; IntAct=EBI-11898753, EBI-10714818;
CC P51157; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-11898753, EBI-742388;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton,
CC cilium basal body. Note=Expressed in the basal body and ciliary rootlet
CC of the photoreceptors. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=S; Synonyms=Rab28S;
CC IsoId=P51157-1; Sequence=Displayed;
CC Name=L; Synonyms=Rab28L;
CC IsoId=P51157-2; Sequence=VSP_005530;
CC Name=3;
CC IsoId=P51157-3; Sequence=VSP_045807;
CC -!- TISSUE SPECIFICITY: Isoform S is detected in most tissues investigated:
CC cortex, liver, kidney, skeletal muscle, adipose tissue, testis,
CC urothelium, lung, bone marrow and retinal pigment epithelium (RPE).
CC Isoform L 2 is widely and abundantly expressed all tissues. Isoform 3
CC is highly expressed in heart, lung, bone marrow, retina, brain, and
CC RPE. {ECO:0000269|PubMed:23746546}.
CC -!- DISEASE: Cone-rod dystrophy 18 (CORD18) [MIM:615374]: A form of cone-
CC rod dystrophy, an inherited retinal dystrophy characterized by retinal
CC pigment deposits visible on fundus examination, predominantly in the
CC macular region, and initial loss of cone photoreceptors followed by rod
CC degeneration. This leads to decreased visual acuity and sensitivity in
CC the central visual field, followed by loss of peripheral vision. Severe
CC loss of vision occurs earlier than in retinitis pigmentosa, due to cone
CC photoreceptors degenerating at a higher rate than rod photoreceptors.
CC {ECO:0000269|PubMed:23746546}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X94703; CAA64364.1; -; mRNA.
DR EMBL; AF498955; AAM21103.1; -; mRNA.
DR EMBL; AC006226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035054; AAH35054.1; -; mRNA.
DR EMBL; CX165950; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS33961.1; -. [P51157-1]
DR CCDS; CCDS3409.1; -. [P51157-2]
DR CCDS; CCDS54741.1; -. [P51157-3]
DR PIR; S65477; S65477.
DR PIR; S72399; S72399.
DR RefSeq; NP_001017979.1; NM_001017979.2. [P51157-1]
DR RefSeq; NP_001153073.1; NM_001159601.1. [P51157-3]
DR RefSeq; NP_004240.2; NM_004249.3. [P51157-2]
DR PDB; 2HXS; X-ray; 1.10 A; A=11-184.
DR PDB; 3E5H; X-ray; 1.50 A; A=11-184.
DR PDBsum; 2HXS; -.
DR PDBsum; 3E5H; -.
DR AlphaFoldDB; P51157; -.
DR SMR; P51157; -.
DR BioGRID; 114765; 23.
DR IntAct; P51157; 7.
DR STRING; 9606.ENSP00000328551; -.
DR iPTMnet; P51157; -.
DR PhosphoSitePlus; P51157; -.
DR BioMuta; RAB28; -.
DR DMDM; 85700393; -.
DR EPD; P51157; -.
DR jPOST; P51157; -.
DR MassIVE; P51157; -.
DR MaxQB; P51157; -.
DR PaxDb; P51157; -.
DR PeptideAtlas; P51157; -.
DR PRIDE; P51157; -.
DR ProteomicsDB; 34185; -.
DR ProteomicsDB; 56287; -. [P51157-1]
DR ProteomicsDB; 56288; -. [P51157-2]
DR Antibodypedia; 22919; 125 antibodies from 27 providers.
DR DNASU; 9364; -.
DR Ensembl; ENST00000288723.9; ENSP00000288723.4; ENSG00000157869.16. [P51157-2]
DR Ensembl; ENST00000330852.10; ENSP00000328551.5; ENSG00000157869.16. [P51157-1]
DR Ensembl; ENST00000338176.8; ENSP00000340079.4; ENSG00000157869.16. [P51157-3]
DR GeneID; 9364; -.
DR KEGG; hsa:9364; -.
DR MANE-Select; ENST00000330852.10; ENSP00000328551.5; NM_001017979.3; NP_001017979.1.
DR UCSC; uc003gmt.3; human. [P51157-1]
DR CTD; 9364; -.
DR DisGeNET; 9364; -.
DR GeneCards; RAB28; -.
DR HGNC; HGNC:9768; RAB28.
DR HPA; ENSG00000157869; Low tissue specificity.
DR MalaCards; RAB28; -.
DR MIM; 612994; gene.
DR MIM; 615374; phenotype.
DR neXtProt; NX_P51157; -.
DR OpenTargets; ENSG00000157869; -.
DR Orphanet; 1872; Cone rod dystrophy.
DR PharmGKB; PA34119; -.
DR VEuPathDB; HostDB:ENSG00000157869; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000161833; -.
DR HOGENOM; CLU_041217_10_4_1; -.
DR InParanoid; P51157; -.
DR OMA; YIYGSHA; -.
DR OrthoDB; 1144210at2759; -.
DR PhylomeDB; P51157; -.
DR TreeFam; TF313852; -.
DR PathwayCommons; P51157; -.
DR SignaLink; P51157; -.
DR BioGRID-ORCS; 9364; 52 hits in 1079 CRISPR screens.
DR ChiTaRS; RAB28; human.
DR EvolutionaryTrace; P51157; -.
DR GenomeRNAi; 9364; -.
DR Pharos; P51157; Tbio.
DR PRO; PR:P51157; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P51157; protein.
DR Bgee; ENSG00000157869; Expressed in tibia and 194 other tissues.
DR ExpressionAtlas; P51157; baseline and differential.
DR Genevisible; P51157; HS.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0035253; C:ciliary rootlet; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
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 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Cell projection; Cone-rod dystrophy; Cytoplasm; Cytoskeleton; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Phosphoprotein;
KW Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CHAIN 2..218
FT /note="Ras-related protein Rab-28"
FT /id="PRO_0000121227"
FT PROPEP 219..221
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396721"
FT MOTIF 41..49
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 19..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:19026641"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:19026641"
FT BINDING 129..132
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:19026641"
FT BINDING 159..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:19026641"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 218
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 218
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:17411337"
FT VAR_SEQ 192..221
FT /note="RVVKADIVNYNQEPMSRTVNPPRSSMCAVQ -> GHFIIFISSTNRE (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045807"
FT VAR_SEQ 193..221
FT /note="VVKADIVNYNQEPMSRTVNPPRSSMCAVQ -> IVRAEIVKYPEEENQHTTS
FT TQSRICSVQ (in isoform L)"
FT /evidence="ECO:0000303|PubMed:8647132, ECO:0000303|Ref.2"
FT /id="VSP_005530"
FT CONFLICT 22
FT /note="A -> T (in Ref. 1; CAA64364)"
FT /evidence="ECO:0000305"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:2HXS"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:2HXS"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:2HXS"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:2HXS"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2HXS"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:2HXS"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2HXS"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:2HXS"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:3E5H"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:2HXS"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:2HXS"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:2HXS"
FT HELIX 104..118
FT /evidence="ECO:0007829|PDB:2HXS"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:2HXS"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:2HXS"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:2HXS"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:2HXS"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:2HXS"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:2HXS"
SQ SEQUENCE 221 AA; 24841 MW; 65AC9D6F10491916 CRC64;
MSDSEEESQD RQLKIVVLGD GASGKTSLTT CFAQETFGKQ YKQTIGLDFF LRRITLPGNL
NVTLQIWDIG GQTIGGKMLD KYIYGAQGVL LVYDITNYQS FENLEDWYTV VKKVSEESET
QPLVALVGNK IDLEHMRTIK PEKHLRFCQE NGFSSHFVSA KTGDSVFLCF QKVAAEILGI
KLNKAEIEQS QRVVKADIVN YNQEPMSRTV NPPRSSMCAV Q
