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Q15286 (RAB35_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-35
Alternative name(s):
GTP-binding protein RAY
Ras-related protein Rab-1C
Gene names
Name:RAB35
Synonyms:RAB1C, RAY
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length201 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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Ref.9 Ref.15

Enzyme regulation

Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP). That Rab is activated by the guanine exchange factors DENND1A, DENND1B and DENND1C. Ref.11

Subunit structure

Interacts with DENND1A and DENND1B; in a nucleotide-dependent manner. Interacts with DENND1C; weak interaction which is nucleotide-independent. Interacts (GTP-bound form) with ACAP2 and MICALL1; the interaction is direct and probably recruits ACAP2 and MICALL1 to membranes. Interacts with EHD1; the interaction is indirect through MICALL1 and probably recruits EHD1 to membranes. Ref.11 Ref.13 Ref.14 Ref.15

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Membraneclathrin-coated pit. Cytoplasmic vesicleclathrin-coated vesicle. Endosome. Melanosome. Note: Present on sorting endosomes and recycling endosome tubules. Tends to be enriched in PIP2-positive cell membrane domains. During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis. Identified in stage I to stage IV melanosomes. Ref.9 Ref.10 Ref.15

Post-translational modification

AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the switch 2 region and leads to moderate inactivation of the GTPase activity. It appears to prolong the lifetime of the GTP state of RAB1B by restricting access of GTPase effectors to switch 2 and blocking effector-stimulated GTP hydrolysis, thereby rendering RAB35 constitutively active.

Phosphocholinated by L.pneumophila AnkX. Both GDP-bound and GTP-bound forms can be phosphocholinated. Phosphocholination inhibits the GEF activity of DENND1A.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell membrane
Coated pit
Cytoplasmic vesicle
Endosome
Membrane
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Traceable author statement Ref.1. Source: GOC

antigen processing and presentation

Inferred from mutant phenotype PubMed 19717423. Source: UniProt

cellular response to nerve growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cytokinesis

Inferred from mutant phenotype Ref.9. Source: UniProtKB

endosomal transport

Inferred from mutant phenotype Ref.9Ref.15. Source: UniProtKB

neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization

Inferred from mutant phenotype Ref.9. Source: UniProtKB

protein localization to endosome

Inferred from mutant phenotype Ref.15. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell projection membrane

Inferred from direct assay Ref.9. Source: UniProtKB

clathrin-coated endocytic vesicle

Inferred from direct assay Ref.9. Source: UniProtKB

coated pit

Inferred from direct assay Ref.9. Source: UniProtKB

endosome membrane

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

intercellular bridge

Inferred from direct assay Ref.9. Source: UniProtKB

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionGDP binding

Inferred from direct assay PubMed 20937701. Source: UniProtKB

GTP binding

Inferred from direct assay PubMed 20937701. Source: UniProtKB

GTPase activity

Traceable author statement Ref.1. Source: ProtInc

phosphatidylinositol-4,5-bisphosphate binding

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MICALL1Q8N3F82EBI-722275,EBI-1056885

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15286-1)

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 2 (identifier: Q15286-2)

The sequence of this isoform differs from the canonical sequence as follows:
     118-201: VGNKNDDPER...KNSKRKKRCC → DVQLHHGAGPPSKERQPGKTAAATTERCGEAHEEQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Ras-related protein Rab-35
PRO_0000121245

Regions

Nucleotide binding15 – 228GTP By similarity
Nucleotide binding63 – 675GTP By similarity
Nucleotide binding120 – 1234GTP By similarity
Motif37 – 459Effector region By similarity

Amino acid modifications

Modified residue751O-(2-cholinephosphoryl)serine; by Legionella AnkX Probable
Modified residue771O-AMP-tyrosine; by Legionella DrrA Probable
Lipidation2001S-geranylgeranyl cysteine By similarity
Lipidation2011S-geranylgeranyl cysteine By similarity

Natural variations

Alternative sequence118 – 20184VGNKN…KKRCC → DVQLHHGAGPPSKERQPGKT AAATTERCGEAHEEQ in isoform 2.
VSP_042918

Experimental info

Mutagenesis221S → N: Destabilization of the intercellular bridge during cytokinesis. Strong reduction in fast recycling. Ref.9
Mutagenesis671Q → L: Loss of GTPase activity. Increased fast recycling. Ref.9

Secondary structure

.............................. 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 31EB15D6D42E076E

FASTA20123,025
        10         20         30         40         50         60 
MARDYDHLFK LLIIGDSGVG KSSLLLRFAD NTFSGSYITT IGVDFKIRTV EINGEKVKLQ 

        70         80         90        100        110        120 
IWDTAGQERF RTITSTYYRG THGVIVVYDV TSAESFVNVK RWLHEINQNC DDVCRILVGN 

       130        140        150        160        170        180 
KNDDPERKVV ETEDAYKFAG QMGIQLFETS AKENVNVEEM FNCITELVLR AKKDNLAKQQ 

       190        200 
QQQQNDVVKL TKNSKRKKRC C 

« Hide

Isoform 2 [UniParc].

Checksum: 711F975E26440998
Show »

FASTA15217,058

References

« Hide 'large scale' references
[1]"Molecular cloning of two small GTP-binding proteins from human skeletal muscle."
Zhu A.X., Zhao Y., Flier J.S.
Biochem. Biophys. Res. Commun. 205:1875-1882(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Muscle.
[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 1).
Tissue: Brain.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"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] (ISOFORMS 1 AND 2).
Tissue: Tongue and Uterus.
[6]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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].
[8]"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] (ISOFORM 1).
Tissue: Uterus.
[9]"Rab35 regulates an endocytic recycling pathway essential for the terminal steps of cytokinesis."
Kouranti I., Sachse M., Arouche N., Goud B., Echard A.
Curr. Biol. 16:1719-1725(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-22 AND GLN-67.
[10]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[11]"The connecdenn family, Rab35 guanine nucleotide exchange factors interfacing with the clathrin machinery."
Marat A.L., McPherson P.S.
J. Biol. Chem. 285:10627-10637(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH DENND1A; DENND1B AND DENND1C.
[12]"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].
[13]"Modulation of Rab GTPase function by a protein phosphocholine transferase."
Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.
Nature 477:103-106(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH L.PNEUMOPHILA ANKX AND DRRA, AMPYLATION AT TYR-77, PHOSPHORYLATION AT SER-75.
[14]"Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins."
Goody P.R., Heller K., Oesterlin L.K., Muller M.P., Itzen A., Goody R.S.
EMBO J. 31:1774-1784(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH L.PNEUMOPHILA ANKX AND DRRA, AMPYLATION, PHOSPHORYLATION AT SER-75.
[15]"MICAL-L1 is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a."
Rahajeng J., Giridharan S.S., Cai B., Naslavsky N., Caplan S.
Traffic 13:82-93(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOCYTOSIS, SUBCELLULAR LOCATION, INTERACTION WITH MICALL1.
[16]"Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate."
Wu X., Bradley M.J., Cai Y., Kummel D., De La Cruz E.M., Barr F.A., Reinisch K.M.
Proc. Natl. Acad. Sci. U.S.A. 108:18672-18677(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-180 IN COMPLEX WITH DENND1B.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79781 mRNA. Translation: CAA56177.1.
AF498960 mRNA. Translation: AAM21108.1.
BT020024 mRNA. Translation: AAV38827.1.
CR536486 mRNA. Translation: CAG38725.1.
CR541683 mRNA. Translation: CAG46484.1.
AK304620 mRNA. Translation: BAG65402.1.
AK312538 mRNA. Translation: BAG35437.1.
AC004812 Genomic DNA. Translation: AAC83182.1.
CH471054 Genomic DNA. Translation: EAW98163.1.
CH471054 Genomic DNA. Translation: EAW98164.1.
BC015931 mRNA. Translation: AAH15931.1.
PIRJC2488.
RefSeqNP_001161078.1. NM_001167606.1.
NP_006852.1. NM_006861.6.
UniGeneHs.524788.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TW8X-ray2.10B/D1-180[»]
ProteinModelPortalQ15286.
SMRQ15286. Positions 4-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116211. 14 interactions.
IntActQ15286. 16 interactions.
MINTMINT-1370578.
STRING9606.ENSP00000229340.

PTM databases

PhosphoSiteQ15286.

Polymorphism databases

DMDM3024525.

Proteomic databases

PaxDbQ15286.
PRIDEQ15286.

Protocols and materials databases

DNASU11021.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229340; ENSP00000229340; ENSG00000111737. [Q15286-1]
ENST00000534951; ENSP00000441883; ENSG00000111737. [Q15286-2]
GeneID11021.
KEGGhsa:11021.
UCSCuc001txm.2. human. [Q15286-1]
uc010szh.2. human. [Q15286-2]

Organism-specific databases

CTD11021.
GeneCardsGC12M120532.
HGNCHGNC:9774. RAB35.
HPAHPA054146.
MIM604199. gene.
neXtProtNX_Q15286.
PharmGKBPA34127.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidQ15286.
KOK07876.
OMANRILVGN.
OrthoDBEOG7VB2H4.
PhylomeDBQ15286.
TreeFamTF105954.

Gene expression databases

ArrayExpressQ15286.
BgeeQ15286.
CleanExHS_RAB35.
GenevestigatorQ15286.

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

GeneWikiRAB35.
GenomeRNAi11021.
NextBio41874.
PROQ15286.
SOURCESearch...

Entry information

Entry nameRAB35_HUMAN
AccessionPrimary (citable) accession number: Q15286
Secondary accession number(s): B2R6E0, B4E390
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 134 of the entry and version 1 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 12

Human chromosome 12: entries, gene names and cross-references to MIM