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P51157

- RAB28_HUMAN

UniProt

P51157 - RAB28_HUMAN

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Protein
Ras-related protein Rab-28
Gene
RAB28
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 279GTP
Nucleotide bindingi68 – 725GTP
Nucleotide bindingi129 – 1324GTP
Nucleotide bindingi159 – 1613GTP

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTP binding Source: UniProtKB
  3. GTPase activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-28
Gene namesi
Name:RAB28
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:9768. RAB28.

Subcellular locationi

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

GO - Cellular componenti

  1. ciliary basal body Source: UniProtKB
  2. ciliary rootlet Source: UniProtKB
  3. cytoplasm Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication

Keywords - Diseasei

Cone-rod dystrophy

Organism-specific databases

MIMi615374. phenotype.
Orphaneti1872. Cone rod dystrophy.
PharmGKBiPA34119.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 218217Ras-related protein Rab-28
PRO_0000121227Add
BLAST
Propeptidei219 – 2213Removed in mature form Inferred
PRO_0000396721

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei8 – 81Phosphoserine1 Publication
Modified residuei218 – 2181Cysteine methyl ester Inferred
Lipidationi218 – 2181S-farnesyl cysteine1 Publication

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP51157.
PaxDbiP51157.
PRIDEiP51157.

PTM databases

PhosphoSiteiP51157.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

ArrayExpressiP51157.
BgeeiP51157.
CleanExiHS_RAB28.
GenevestigatoriP51157.

Organism-specific databases

HPAiHPA044575.

Interactioni

Protein-protein interaction databases

BioGridi114765. 2 interactions.
STRINGi9606.ENSP00000328551.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 187
Helixi25 – 339
Helixi34 – 363
Helixi39 – 435
Turni44 – 463
Beta strandi47 – 5610
Turni57 – 593
Beta strandi60 – 689
Helixi71 – 755
Helixi79 – 835
Beta strandi87 – 948
Helixi98 – 1025
Helixi104 – 11815
Beta strandi123 – 1297
Helixi131 – 1366
Helixi141 – 15111
Beta strandi154 – 1585
Turni160 – 1623
Helixi166 – 17712

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HXSX-ray1.10A11-184[»]
3E5HX-ray1.50A11-184[»]
ProteinModelPortaliP51157.
SMRiP51157. Positions 8-184.

Miscellaneous databases

EvolutionaryTraceiP51157.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi41 – 499Effector region By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233968.
HOVERGENiHBG101090.
InParanoidiP51157.
KOiK07915.
OMAiCFQRIAA.
PhylomeDBiP51157.
TreeFamiTF313852.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform S (identifier: P51157-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSDSEEESQD RQLKIVVLGD GASGKTSLTT CFAQETFGKQ YKQTIGLDFF    50
LRRITLPGNL NVTLQIWDIG GQTIGGKMLD KYIYGAQGVL LVYDITNYQS 100
FENLEDWYTV VKKVSEESET QPLVALVGNK IDLEHMRTIK PEKHLRFCQE 150
NGFSSHFVSA KTGDSVFLCF QKVAAEILGI KLNKAEIEQS QRVVKADIVN 200
YNQEPMSRTV NPPRSSMCAV Q 221
Length:221
Mass (Da):24,841
Last modified:January 24, 2006 - v2
Checksum:i65AC9D6F10491916
GO
Isoform L (identifier: P51157-2) [UniParc]FASTAAdd to Basket

Also known as: Rab28L

The sequence of this isoform differs from the canonical sequence as follows:
     193-221: VVKADIVNYNQEPMSRTVNPPRSSMCAVQ → IVRAEIVKYPEEENQHTTSTQSRICSVQ

Show »
Length:220
Mass (Da):24,853
Checksum:i693F137237519E71
GO
Isoform 3 (identifier: P51157-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     192-221: RVVKADIVNYNQEPMSRTVNPPRSSMCAVQ → GHFIIFISSTNRE

Note: No experimental confirmation available.

Show »
Length:204
Mass (Da):22,971
Checksum:i3533DB9E6E6FD456
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei192 – 22130RVVKA…MCAVQ → GHFIIFISSTNRE in isoform 3.
VSP_045807Add
BLAST
Alternative sequencei193 – 22129VVKAD…MCAVQ → IVRAEIVKYPEEENQHTTST QSRICSVQ in isoform L.
VSP_005530Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221A → T in CAA64364. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS33961.1. [P51157-1]
CCDS3409.1. [P51157-2]
CCDS54741.1. [P51157-3]
PIRiS65477.
S72399.
RefSeqiNP_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]
UniGeneiHs.656060.

Genome annotation databases

EnsembliENST00000288723; ENSP00000288723; ENSG00000157869. [P51157-2]
ENST00000330852; ENSP00000328551; ENSG00000157869. [P51157-1]
ENST00000338176; ENSP00000340079; ENSG00000157869. [P51157-3]
GeneIDi9364.
KEGGihsa:9364.
UCSCiuc003gmt.2. human. [P51157-2]
uc003gmu.2. human. [P51157-1]

Polymorphism databases

DMDMi85700393.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS33961.1. [P51157-1 ]
CCDS3409.1. [P51157-2 ]
CCDS54741.1. [P51157-3 ]
PIRi S65477.
S72399.
RefSeqi NP_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 ]
UniGenei Hs.656060.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HXS X-ray 1.10 A 11-184 [» ]
3E5H X-ray 1.50 A 11-184 [» ]
ProteinModelPortali P51157.
SMRi P51157. Positions 8-184.
ModBasei Search...

Protein-protein interaction databases

BioGridi 114765. 2 interactions.
STRINGi 9606.ENSP00000328551.

PTM databases

PhosphoSitei P51157.

Polymorphism databases

DMDMi 85700393.

Proteomic databases

MaxQBi P51157.
PaxDbi P51157.
PRIDEi P51157.

Protocols and materials databases

DNASUi 9364.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000288723 ; ENSP00000288723 ; ENSG00000157869 . [P51157-2 ]
ENST00000330852 ; ENSP00000328551 ; ENSG00000157869 . [P51157-1 ]
ENST00000338176 ; ENSP00000340079 ; ENSG00000157869 . [P51157-3 ]
GeneIDi 9364.
KEGGi hsa:9364.
UCSCi uc003gmt.2. human. [P51157-2 ]
uc003gmu.2. human. [P51157-1 ]

Organism-specific databases

CTDi 9364.
GeneCardsi GC04M013369.
HGNCi HGNC:9768. RAB28.
HPAi HPA044575.
MIMi 612994. gene.
615374. phenotype.
neXtProti NX_P51157.
Orphaneti 1872. Cone rod dystrophy.
PharmGKBi PA34119.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
HOGENOMi HOG000233968.
HOVERGENi HBG101090.
InParanoidi P51157.
KOi K07915.
OMAi CFQRIAA.
PhylomeDBi P51157.
TreeFami TF313852.

Miscellaneous databases

EvolutionaryTracei P51157.
GenomeRNAii 9364.
NextBioi 35067.
PROi P51157.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51157.
Bgeei P51157.
CleanExi HS_RAB28.
Genevestigatori P51157.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51419. RAB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiRAB28_HUMAN
AccessioniPrimary (citable) accession number: P51157
Secondary accession number(s): G8JLC5, Q8IYR8, Q8NI05
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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