Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q15286

- RAB35_HUMAN

UniProt

Q15286 - RAB35_HUMAN

Protein

Ras-related protein Rab-35

Gene

RAB35

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 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.2 Publications

    Enzyme regulationi

    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.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 228GTPBy similarity
    Nucleotide bindingi63 – 675GTPBy similarity
    Nucleotide bindingi120 – 1234GTPBy similarity

    GO - Molecular functioni

    1. GDP binding Source: UniProtKB
    2. GTPase activity Source: ProtInc
    3. GTP binding Source: UniProtKB
    4. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
    5. protein binding Source: IntAct

    GO - Biological processi

    1. antigen processing and presentation Source: UniProt
    2. cellular response to nerve growth factor stimulus Source: UniProtKB
    3. cytokinesis Source: UniProtKB
    4. endosomal transport Source: UniProtKB
    5. GTP catabolic process Source: GOC
    6. neuron projection development Source: UniProtKB
    7. protein localization Source: UniProtKB
    8. protein localization to endosome Source: UniProtKB
    9. protein transport Source: UniProtKB-KW
    10. small GTPase mediated signal transduction Source: InterPro

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-35
    Alternative name(s):
    GTP-binding protein RAY
    Ras-related protein Rab-1C
    Gene namesi
    Name:RAB35
    Synonyms:RAB1C, RAY
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9774. RAB35.

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. 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.

    GO - Cellular componenti

    1. cell projection membrane Source: UniProtKB
    2. clathrin-coated endocytic vesicle Source: UniProtKB
    3. coated pit Source: UniProtKB
    4. endosome membrane Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. intercellular bridge Source: UniProtKB
    7. melanosome Source: UniProtKB-SubCell
    8. mitochondrion Source: Ensembl
    9. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Coated pit, Cytoplasmic vesicle, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi22 – 221S → N: Destabilization of the intercellular bridge during cytokinesis. Strong reduction in fast recycling. 1 Publication
    Mutagenesisi67 – 671Q → L: Loss of GTPase activity. Increased fast recycling. 1 Publication

    Organism-specific databases

    PharmGKBiPA34127.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 201201Ras-related protein Rab-35PRO_0000121245Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751O-(2-cholinephosphoryl)serine; by Legionella AnkX2 Publications
    Modified residuei77 – 771O-AMP-tyrosine; by Legionella DrrA2 Publications
    Lipidationi200 – 2001S-geranylgeranyl cysteineBy similarity
    Lipidationi201 – 2011S-geranylgeranyl cysteineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Lipoprotein, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiQ15286.
    PaxDbiQ15286.
    PRIDEiQ15286.

    PTM databases

    PhosphoSiteiQ15286.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15286.
    BgeeiQ15286.
    CleanExiHS_RAB35.
    GenevestigatoriQ15286.

    Organism-specific databases

    HPAiHPA054146.

    Interactioni

    Subunit structurei

    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.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MICALL1Q8N3F82EBI-722275,EBI-1056885

    Protein-protein interaction databases

    BioGridi116211. 17 interactions.
    IntActiQ15286. 16 interactions.
    MINTiMINT-1370578.
    STRINGi9606.ENSP00000229340.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 148
    Helixi21 – 288
    Turni38 – 403
    Beta strandi41 – 5212
    Beta strandi55 – 6410
    Helixi67 – 693
    Helixi75 – 784
    Beta strandi82 – 898
    Helixi93 – 10917
    Beta strandi113 – 1208
    Helixi125 – 1273
    Helixi132 – 14211
    Beta strandi146 – 1483
    Turni151 – 1544
    Helixi157 – 17519

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3TW8X-ray2.10B/D1-180[»]
    ProteinModelPortaliQ15286.
    SMRiQ15286. Positions 4-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi37 – 459Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233968.
    HOVERGENiHBG009351.
    InParanoidiQ15286.
    KOiK07876.
    OMAiNRILVGN.
    OrthoDBiEOG7VB2H4.
    PhylomeDBiQ15286.
    TreeFamiTF105954.

    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. Align

    Isoform 1 (identifier: Q15286-1) [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

    MARDYDHLFK LLIIGDSGVG KSSLLLRFAD NTFSGSYITT IGVDFKIRTV    50
    EINGEKVKLQ IWDTAGQERF RTITSTYYRG THGVIVVYDV TSAESFVNVK 100
    RWLHEINQNC DDVCRILVGN KNDDPERKVV ETEDAYKFAG QMGIQLFETS 150
    AKENVNVEEM FNCITELVLR AKKDNLAKQQ QQQQNDVVKL TKNSKRKKRC 200
    C 201
    Length:201
    Mass (Da):23,025
    Last modified:November 1, 1996 - v1
    Checksum:i31EB15D6D42E076E
    GO
    Isoform 2 (identifier: Q15286-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         118-201: VGNKNDDPER...KNSKRKKRCC → DVQLHHGAGPPSKERQPGKTAAATTERCGEAHEEQ

    Note: No experimental confirmation available.

    Show »
    Length:152
    Mass (Da):17,058
    Checksum:i711F975E26440998
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei118 – 20184VGNKN…KKRCC → DVQLHHGAGPPSKERQPGKT AAATTERCGEAHEEQ in isoform 2. 1 PublicationVSP_042918Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS41846.1. [Q15286-1]
    CCDS53836.1. [Q15286-2]
    PIRiJC2488.
    RefSeqiNP_001161078.1. NM_001167606.1. [Q15286-2]
    NP_006852.1. NM_006861.6. [Q15286-1]
    UniGeneiHs.524788.

    Genome annotation databases

    EnsembliENST00000229340; ENSP00000229340; ENSG00000111737. [Q15286-1]
    ENST00000534951; ENSP00000441883; ENSG00000111737. [Q15286-2]
    GeneIDi11021.
    KEGGihsa:11021.
    UCSCiuc001txm.2. human. [Q15286-1]
    uc010szh.2. human. [Q15286-2]

    Polymorphism databases

    DMDMi3024525.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS41846.1. [Q15286-1 ]
    CCDS53836.1. [Q15286-2 ]
    PIRi JC2488.
    RefSeqi NP_001161078.1. NM_001167606.1. [Q15286-2 ]
    NP_006852.1. NM_006861.6. [Q15286-1 ]
    UniGenei Hs.524788.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3TW8 X-ray 2.10 B/D 1-180 [» ]
    ProteinModelPortali Q15286.
    SMRi Q15286. Positions 4-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116211. 17 interactions.
    IntActi Q15286. 16 interactions.
    MINTi MINT-1370578.
    STRINGi 9606.ENSP00000229340.

    PTM databases

    PhosphoSitei Q15286.

    Polymorphism databases

    DMDMi 3024525.

    Proteomic databases

    MaxQBi Q15286.
    PaxDbi Q15286.
    PRIDEi Q15286.

    Protocols and materials databases

    DNASUi 11021.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229340 ; ENSP00000229340 ; ENSG00000111737 . [Q15286-1 ]
    ENST00000534951 ; ENSP00000441883 ; ENSG00000111737 . [Q15286-2 ]
    GeneIDi 11021.
    KEGGi hsa:11021.
    UCSCi uc001txm.2. human. [Q15286-1 ]
    uc010szh.2. human. [Q15286-2 ]

    Organism-specific databases

    CTDi 11021.
    GeneCardsi GC12M120532.
    HGNCi HGNC:9774. RAB35.
    HPAi HPA054146.
    MIMi 604199. gene.
    neXtProti NX_Q15286.
    PharmGKBi PA34127.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi Q15286.
    KOi K07876.
    OMAi NRILVGN.
    OrthoDBi EOG7VB2H4.
    PhylomeDBi Q15286.
    TreeFami TF105954.

    Miscellaneous databases

    GeneWikii RAB35.
    GenomeRNAii 11021.
    NextBioi 41874.
    PROi Q15286.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15286.
    Bgeei Q15286.
    CleanExi HS_RAB35.
    Genevestigatori Q15286.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00175. RAB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51419. RAB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiRAB35_HUMAN
    AccessioniPrimary (citable) accession number: Q15286
    Secondary accession number(s): B2R6E0, B4E390
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 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 12
      Human chromosome 12: 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