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P51157

- RAB28_HUMAN

UniProt

P51157 - RAB28_HUMAN

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
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (24 Jan 2006)
      Previous versions | rss
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    Functioni

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 279GTP1 Publication
    Nucleotide bindingi68 – 725GTP1 Publication
    Nucleotide bindingi129 – 1324GTP1 Publication
    Nucleotide bindingi159 – 1613GTP1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

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

    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 Curated; Lipid-anchor Curated; Cytoplasmic side Curated. 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

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    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-28PRO_0000121227Add
    BLAST
    Propeptidei219 – 2213Removed in mature formCuratedPRO_0000396721

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei8 – 81Phosphoserine1 Publication
    Modified residuei218 – 2181Cysteine methyl esterCurated
    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

    1
    221
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51157.

    Family & Domainsi

    Motif

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

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221A → T in CAA64364. (PubMed:8647132)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei192 – 22130RVVKA…MCAVQ → GHFIIFISSTNRE in isoform 3. 1 PublicationVSP_045807Add
    BLAST
    Alternative sequencei193 – 22129VVKAD…MCAVQ → IVRAEIVKYPEEENQHTTST QSRICSVQ in isoform L. 2 PublicationsVSP_005530Add
    BLAST

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 138 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