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Q9H0T7 (RAB17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-17
Gene names
Name:RAB17
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in transcytosis, the directed movement of endocytosed material through the cell and its exocytosis from the plasma membrane at the opposite side. Mainly observed in epithelial cells, transcytosis mediates for instance, the transcellular transport of immunoglobulins from the basolateral surface to the apical surface. Most probably controls membrane trafficking through apical recycling endosomes in a post-endocytic step of transcytosis. Required for melanosome transport and release from melanocytes, it also regulates dendrite and dendritic spine development By similarity. May also play a role in cell migration. Ref.8

Subcellular location

Recycling endosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Cell projectiondendrite By similarity. Note: May also localize at the basolateral and apical plasma membrane. In neurons, localizes to the cell body and dendritic shaft and spine By similarity.

Tissue specificity

Expressed in melanocytes (at protein level). Ref.7

Induction

Up-regulated by forskolin probably through the transcription factor MITF. Ref.7

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell projection
Endosome
Membrane
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytic recycling

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of melanosome localization

Inferred from sequence or structural similarity. Source: UniProtKB

filopodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor

Inferred from sequence or structural similarity. Source: UniProtKB

melanosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of dendrite development

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of filopodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of synapse assembly

Inferred from sequence or structural similarity. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

transcytosis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentapical plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

basolateral plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

intracellular

Inferred from direct assay. Source: LIFEdb

melanosome

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProtKB

recycling endosome

Inferred from sequence or structural similarity. Source: UniProtKB

recycling endosome membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGDP binding

Inferred from direct assay PubMed 20937701. Source: UniProtKB

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Ras-related protein Rab-17
PRO_0000121191

Regions

Nucleotide binding26 – 338GTP By similarity
Nucleotide binding73 – 775GTP By similarity
Nucleotide binding132 – 1354GTP By similarity
Motif47 – 559Effector region By similarity

Amino acid modifications

Lipidation2091S-geranylgeranyl cysteine By similarity
Lipidation2101S-geranylgeranyl cysteine By similarity

Natural variations

Natural variant191V → A. Ref.3
Corresponds to variant rs3751112 [ dbSNP | Ensembl ].
VAR_051711
Natural variant1841S → G.
Corresponds to variant rs34311889 [ dbSNP | Ensembl ].
VAR_051712
Natural variant1911L → P.
Corresponds to variant rs2280289 [ dbSNP | Ensembl ].
VAR_022102

Experimental info

Sequence conflict1571L → P in CAB66580. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9H0T7 [UniParc].

Last modified October 10, 2003. Version 2.
Checksum: 40E8CE5F445E5CF2

FASTA21223,491
        10         20         30         40         50         60 
MAQAHRTPQP RAAPSQPRVF KLVLLGSGSV GKSSLALRYV KNDFKSILPT VGCAFFTKVV 

        70         80         90        100        110        120 
DVGATSLKLE IWDTAGQEKY HSVCHLYFRG ANAALLVYDI TRKDSFLKAQ QWLKDLEEEL 

       130        140        150        160        170        180 
HPGEVLVMLV GNKTDLSQER EVTFQEGKEF ADSQKLLFME TSAKLNHQVS EVFNTVAQEL 

       190        200        210 
LQRSDEEGQA LRGDAAVALN KGPARQAKCC AH 

« Hide

References

« Hide 'large scale' references
[1]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-19.
[4]"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].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Colon and Placenta.
[7]"The recycling endosome protein Rab17 regulates melanocytic filopodia formation and melanosome trafficking."
Beaumont K.A., Hamilton N.A., Moores M.T., Brown D.L., Ohbayashi N., Cairncross O., Cook A.L., Smith A.G., Misaki R., Fukuda M., Taguchi T., Sturm R.A., Stow J.L.
Traffic 12:627-643(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION BY FORSKOLIN.
[8]"ERK2 drives tumour cell migration in three-dimensional microenvironments by suppressing expression of Rab17 and liprin-beta2."
von Thun A., Birtwistle M., Kalna G., Grindlay J., Strachan D., Kolch W., von Kriegsheim A., Norman J.C.
J. Cell Sci. 125:1465-1477(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL136645 mRNA. Translation: CAB66580.1.
AK022600 mRNA. Translation: BAB14121.1.
CR457282 mRNA. Translation: CAG33563.1.
AC104667 Genomic DNA. Translation: AAY24047.1.
CH471063 Genomic DNA. Translation: EAW71118.1.
BC000929 mRNA. Translation: AAH00929.1.
BC050426 mRNA. Translation: AAH50426.1.
CCDSCCDS2520.1.
RefSeqNP_071894.1. NM_022449.3.
UniGeneHs.44278.

3D structure databases

ProteinModelPortalQ9H0T7.
SMRQ9H0T7. Positions 17-208.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122128. 3 interactions.
IntActQ9H0T7. 2 interactions.
MINTMINT-1422334.
STRING9606.ENSP00000264601.

PTM databases

PhosphoSiteQ9H0T7.

Polymorphism databases

DMDM37999892.

Proteomic databases

MaxQBQ9H0T7.
PaxDbQ9H0T7.
PRIDEQ9H0T7.

Protocols and materials databases

DNASU64284.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264601; ENSP00000264601; ENSG00000124839.
GeneID64284.
KEGGhsa:64284.
UCSCuc002vwz.2. human.

Organism-specific databases

CTD64284.
GeneCardsGC02M238499.
HGNCHGNC:16523. RAB17.
HPAHPA035176.
MIM602206. gene.
neXtProtNX_Q9H0T7.
PharmGKBPA34105.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidQ9H0T7.
KOK07909.
OMASVCHLYY.
PhylomeDBQ9H0T7.
TreeFamTF300199.

Gene expression databases

ArrayExpressQ9H0T7.
BgeeQ9H0T7.
CleanExHS_RAB17.
GenevestigatorQ9H0T7.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRAB17.
GenomeRNAi64284.
NextBio66211.
PROQ9H0T7.
SOURCESearch...

Entry information

Entry nameRAB17_HUMAN
AccessionPrimary (citable) accession number: Q9H0T7
Secondary accession number(s): Q53QV6 expand/collapse secondary AC list , Q6IA73, Q9BVU1, Q9H9U9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 10, 2003
Last modified: July 9, 2014
This is version 129 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM