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P51157 (RAB28_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-28
Gene names
Name:RAB28
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Cytoplasmcytoskeletoncilium basal body. Note: Expressed in the basal body and ciliary rootlet of the photoreceptors By similarity.

Tissue specificity

Isoform S is detected in most tissues investigated: cortex, liver, kidney, skeletal muscle, adipose tissue, testis, urothelium, lung, bone marrow and retinal pigment epithelium (RPE). Isoform L 2 is widely and abundantly expressed all tissues. Isoform 3 is highly expressed in heart, lung, bone marrow, retina, brain, and RPE. Ref.8

Involvement in disease

Cone-rod dystrophy 18 (CORD18) [MIM:615374]: A form of cone-rod dystrophy, an inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform S (identifier: P51157-1)

Also known as: Rab28S;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform L (identifier: P51157-2)

Also known as: Rab28L;

The sequence of this isoform differs from the canonical sequence as follows:
     193-221: VVKADIVNYNQEPMSRTVNPPRSSMCAVQ → IVRAEIVKYPEEENQHTTSTQSRICSVQ
Isoform 3 (identifier: P51157-3)

The sequence of this isoform differs from the canonical sequence as follows:
     192-221: RVVKADIVNYNQEPMSRTVNPPRSSMCAVQ → GHFIIFISSTNRE
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 218217Ras-related protein Rab-28
PRO_0000121227
Propeptide219 – 2213Removed in mature form Probable
PRO_0000396721

Regions

Nucleotide binding19 – 279GTP
Nucleotide binding68 – 725GTP
Nucleotide binding129 – 1324GTP
Nucleotide binding159 – 1613GTP
Motif41 – 499Effector region By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.7
Modified residue81Phosphoserine Ref.7
Modified residue2181Cysteine methyl ester Probable
Lipidation2181S-farnesyl cysteine Ref.5

Natural variations

Alternative sequence192 – 22130RVVKA…MCAVQ → GHFIIFISSTNRE in isoform 3.
VSP_045807
Alternative sequence193 – 22129VVKAD…MCAVQ → IVRAEIVKYPEEENQHTTST QSRICSVQ in isoform L.
VSP_005530

Experimental info

Sequence conflict221A → T in CAA64364. Ref.1

Secondary structure

.................................. 221
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform S (Rab28S) [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 65AC9D6F10491916

FASTA22124,841
        10         20         30         40         50         60 
MSDSEEESQD RQLKIVVLGD GASGKTSLTT CFAQETFGKQ YKQTIGLDFF LRRITLPGNL 

        70         80         90        100        110        120 
NVTLQIWDIG GQTIGGKMLD KYIYGAQGVL LVYDITNYQS FENLEDWYTV VKKVSEESET 

       130        140        150        160        170        180 
QPLVALVGNK IDLEHMRTIK PEKHLRFCQE NGFSSHFVSA KTGDSVFLCF QKVAAEILGI 

       190        200        210        220 
KLNKAEIEQS QRVVKADIVN YNQEPMSRTV NPPRSSMCAV Q 

« Hide

Isoform L (Rab28L) [UniParc].

Checksum: 693F137237519E71
Show »

FASTA22024,853
Isoform 3 [UniParc].

Checksum: 3533DB9E6E6FD456
Show »

FASTA20422,971

References

« Hide 'large scale' references
[1]"Alternative mRNA splicing of the novel GTPase Rab28 generates isoforms with different C-termini."
Brauers A., Schuermann A., Massmann S., Muehl-Zuerbes P., Becker W., Kainulainen H., Lie C., Joost H.-G.
Eur. J. Biochem. 237:833-840(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS L AND S).
Tissue: Testis.
[2]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM L).
Tissue: Brain.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS S AND 3).
Tissue: Brain and Embryonic stem cell.
[5]"Towards complete sets of farnesylated and geranylgeranylated proteins."
Maurer-Stroh S., Koranda M., Benetka W., Schneider G., Sirota F.L., Eisenhaber F.
PLoS Comput. Biol. 3:634-648(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-218.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"Mutations in RAB28, encoding a farnesylated small GTPase, are associated with autosomal-recessive cone-rod dystrophy."
European Retinal Disease Consortium
Roosing S., Rohrschneider K., Beryozkin A., Sharon D., Weisschuh N., Staller J., Kohl S., Zelinger L., Peters T.A., Neveling K., Strom T.M., van den Born L.I., Hoyng C.B., Klaver C.C., Roepman R., Wissinger B., Banin E., Cremers F.P., den Hollander A.I.
Am. J. Hum. Genet. 93:110-117(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CORD18, TISSUE SPECIFICITY.
[9]"Large nucleotide-dependent conformational change in Rab28."
Lee S.H., Baek K., Dominguez R.
FEBS Lett. 582:4107-4111(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 11-184 IN COMPLEX WITH GTP AND GDP ANALOGS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X94703 mRNA. Translation: CAA64364.1.
AF498955 mRNA. Translation: AAM21103.1.
AC006226 Genomic DNA. No translation available.
AC006445 Genomic DNA. No translation available.
AC020729 Genomic DNA. No translation available.
BC035054 mRNA. Translation: AAH35054.1.
CX165950 mRNA. No translation available.
CCDSCCDS33961.1. [P51157-1]
CCDS3409.1. [P51157-2]
CCDS54741.1. [P51157-3]
PIRS65477.
S72399.
RefSeqNP_001017979.1. NM_001017979.2. [P51157-1]
NP_001153073.1. NM_001159601.1. [P51157-3]
NP_004240.2. NM_004249.3. [P51157-2]
XP_005248272.1. XM_005248215.2. [P51157-3]
UniGeneHs.656060.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HXSX-ray1.10A11-184[»]
3E5HX-ray1.50A11-184[»]
ProteinModelPortalP51157.
SMRP51157. Positions 8-184.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114765. 2 interactions.
STRING9606.ENSP00000328551.

PTM databases

PhosphoSiteP51157.

Polymorphism databases

DMDM85700393.

Proteomic databases

MaxQBP51157.
PaxDbP51157.
PRIDEP51157.

Protocols and materials databases

DNASU9364.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000288723; ENSP00000288723; ENSG00000157869. [P51157-2]
ENST00000330852; ENSP00000328551; ENSG00000157869. [P51157-1]
ENST00000338176; ENSP00000340079; ENSG00000157869. [P51157-3]
GeneID9364.
KEGGhsa:9364.
UCSCuc003gmt.2. human. [P51157-2]
uc003gmu.2. human. [P51157-1]

Organism-specific databases

CTD9364.
GeneCardsGC04M013369.
HGNCHGNC:9768. RAB28.
HPAHPA044575.
MIM612994. gene.
615374. phenotype.
neXtProtNX_P51157.
Orphanet1872. Cone rod dystrophy.
PharmGKBPA34119.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG101090.
InParanoidP51157.
KOK07915.
OMACFQRIAA.
PhylomeDBP51157.
TreeFamTF313852.

Gene expression databases

ArrayExpressP51157.
BgeeP51157.
CleanExHS_RAB28.
GenevestigatorP51157.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP51157.
GenomeRNAi9364.
NextBio35067.
PROP51157.
SOURCESearch...

Entry information

Entry nameRAB28_HUMAN
AccessionPrimary (citable) accession number: P51157
Secondary accession number(s): G8JLC5, Q8IYR8, Q8NI05
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 24, 2006
Last modified: July 9, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM