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Protein

Ras-related protein Rab-17

Gene

RAB17

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 338GTPBy similarity
Nucleotide bindingi73 – 775GTPBy similarity
Nucleotide bindingi132 – 1354GTPBy similarity

GO - Molecular functioni

  • GDP binding Source: UniProtKB
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-17
Gene namesi
Name:RAB17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:16523. RAB17.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Endosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34105.

Polymorphism and mutation databases

BioMutaiRAB17.
DMDMi37999892.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Ras-related protein Rab-17PRO_0000121191Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi209 – 2091S-geranylgeranyl cysteineBy similarity
Lipidationi210 – 2101S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Prenylation

Proteomic databases

MaxQBiQ9H0T7.
PaxDbiQ9H0T7.
PRIDEiQ9H0T7.

PTM databases

PhosphoSiteiQ9H0T7.

Expressioni

Tissue specificityi

Expressed in melanocytes (at protein level).1 Publication

Inductioni

Up-regulated by forskolin probably through the transcription factor MITF.1 Publication

Gene expression databases

BgeeiQ9H0T7.
CleanExiHS_RAB17.
ExpressionAtlasiQ9H0T7. baseline and differential.
GenevisibleiQ9H0T7. HS.

Organism-specific databases

HPAiHPA035176.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
C11orf49Q9H6J73EBI-721615,EBI-721300
FAM9BQ8IZU03EBI-721615,EBI-10175124
MAGEA1P433553EBI-721615,EBI-740978

Protein-protein interaction databases

BioGridi122128. 11 interactions.
IntActiQ9H0T7. 5 interactions.
MINTiMINT-1422334.
STRINGi9606.ENSP00000264601.

Structurei

3D structure databases

ProteinModelPortaliQ9H0T7.
SMRiQ9H0T7. Positions 17-208.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi47 – 559Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119101.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9H0T7.
KOiK07909.
OMAiSAKLNYQ.
PhylomeDBiQ9H0T7.
TreeFamiTF300199.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H0T7-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MAQAHRTPQP RAAPSQPRVF KLVLLGSGSV GKSSLALRYV KNDFKSILPT
60 70 80 90 100
VGCAFFTKVV DVGATSLKLE IWDTAGQEKY HSVCHLYFRG ANAALLVYDI
110 120 130 140 150
TRKDSFLKAQ QWLKDLEEEL HPGEVLVMLV GNKTDLSQER EVTFQEGKEF
160 170 180 190 200
ADSQKLLFME TSAKLNHQVS EVFNTVAQEL LQRSDEEGQA LRGDAAVALN
210
KGPARQAKCC AH
Length:212
Mass (Da):23,491
Last modified:October 10, 2003 - v2
Checksum:i40E8CE5F445E5CF2
GO
Isoform 2 (identifier: Q9H0T7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-127: Missing.

Note: No experimental confirmation available.
Show »
Length:85
Mass (Da):9,394
Checksum:i5C22A7948C107A54
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571L → P in CAB66580 (PubMed:11230166).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191V → A.1 Publication
Corresponds to variant rs3751112 [ dbSNP | Ensembl ].
VAR_051711
Natural varianti184 – 1841S → G.
Corresponds to variant rs34311889 [ dbSNP | Ensembl ].
VAR_051712
Natural varianti191 – 1911L → P.
Corresponds to variant rs2280289 [ dbSNP | Ensembl ].
VAR_022102

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 127127Missing in isoform 2. 1 PublicationVSP_056400Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CH471063 Genomic DNA. Translation: EAW71119.1.
BC000929 mRNA. Translation: AAH00929.1.
BC050426 mRNA. Translation: AAH50426.1.
BC007907 mRNA. Translation: AAH07907.1.
BC009827 mRNA. Translation: AAH09827.1.
CCDSiCCDS2520.1. [Q9H0T7-1]
RefSeqiNP_071894.1. NM_022449.3. [Q9H0T7-1]
UniGeneiHs.44278.

Genome annotation databases

EnsembliENST00000264601; ENSP00000264601; ENSG00000124839.
ENST00000409822; ENSP00000386589; ENSG00000124839. [Q9H0T7-2]
GeneIDi64284.
KEGGihsa:64284.
UCSCiuc002vwz.2. human. [Q9H0T7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CH471063 Genomic DNA. Translation: EAW71119.1.
BC000929 mRNA. Translation: AAH00929.1.
BC050426 mRNA. Translation: AAH50426.1.
BC007907 mRNA. Translation: AAH07907.1.
BC009827 mRNA. Translation: AAH09827.1.
CCDSiCCDS2520.1. [Q9H0T7-1]
RefSeqiNP_071894.1. NM_022449.3. [Q9H0T7-1]
UniGeneiHs.44278.

3D structure databases

ProteinModelPortaliQ9H0T7.
SMRiQ9H0T7. Positions 17-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122128. 11 interactions.
IntActiQ9H0T7. 5 interactions.
MINTiMINT-1422334.
STRINGi9606.ENSP00000264601.

PTM databases

PhosphoSiteiQ9H0T7.

Polymorphism and mutation databases

BioMutaiRAB17.
DMDMi37999892.

Proteomic databases

MaxQBiQ9H0T7.
PaxDbiQ9H0T7.
PRIDEiQ9H0T7.

Protocols and materials databases

DNASUi64284.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264601; ENSP00000264601; ENSG00000124839.
ENST00000409822; ENSP00000386589; ENSG00000124839. [Q9H0T7-2]
GeneIDi64284.
KEGGihsa:64284.
UCSCiuc002vwz.2. human. [Q9H0T7-1]

Organism-specific databases

CTDi64284.
GeneCardsiGC02M238499.
HGNCiHGNC:16523. RAB17.
HPAiHPA035176.
MIMi602206. gene.
neXtProtiNX_Q9H0T7.
PharmGKBiPA34105.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119101.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9H0T7.
KOiK07909.
OMAiSAKLNYQ.
PhylomeDBiQ9H0T7.
TreeFamiTF300199.

Miscellaneous databases

GeneWikiiRAB17.
GenomeRNAii64284.
NextBioi66211.
PROiQ9H0T7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H0T7.
CleanExiHS_RAB17.
ExpressionAtlasiQ9H0T7. baseline and differential.
GenevisibleiQ9H0T7. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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.
    , 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] (ISOFORM 1).
  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] (ISOFORM 1), 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.
    , 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. 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] (ISOFORMS 1 AND 2).
    Tissue: Colon, Eye, Ovary 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.
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRAB17_HUMAN
AccessioniPrimary (citable) accession number: Q9H0T7
Secondary accession number(s): Q53QV6
, Q6IA73, Q6PJZ0, Q9BVU1, Q9H9U9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 10, 2003
Last modified: July 22, 2015
This is version 140 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.