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Q15286

- RAB35_HUMAN

UniProt

Q15286 - RAB35_HUMAN

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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

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: UniProtKB
  3. GTP binding Source: UniProtKB
  4. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB

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: UniProtKB
  6. neuron projection development Source: UniProtKB
  7. plasma membrane to endosome transport Source: UniProtKB
  8. protein localization Source: UniProtKB
  9. protein localization to endosome Source: UniProtKB
  10. protein transport Source: UniProtKB-KW
  11. small GTPase mediated signal transduction Source: InterPro
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-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. mitochondrion Source: Ensembl
  8. plasma membrane Source: UniProtKB
Complete GO annotation...

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 DrrA1 Publication
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

BgeeiQ15286.
CleanExiHS_RAB35.
ExpressionAtlasiQ15286. baseline and differential.
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 – 148Combined sources
Helixi21 – 288Combined sources
Turni38 – 403Combined sources
Beta strandi41 – 5212Combined sources
Beta strandi55 – 6410Combined sources
Helixi67 – 693Combined sources
Helixi75 – 784Combined sources
Beta strandi82 – 898Combined sources
Helixi93 – 10917Combined sources
Beta strandi113 – 1208Combined sources
Helixi125 – 1273Combined sources
Helixi132 – 14211Combined sources
Beta strandi146 – 1483Combined sources
Turni151 – 1544Combined sources
Helixi157 – 17519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00740000115017.
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

        10         20         30         40         50
MARDYDHLFK LLIIGDSGVG KSSLLLRFAD NTFSGSYITT IGVDFKIRTV
60 70 80 90 100
EINGEKVKLQ IWDTAGQERF RTITSTYYRG THGVIVVYDV TSAESFVNVK
110 120 130 140 150
RWLHEINQNC DDVCRILVGN KNDDPERKVV ETEDAYKFAG QMGIQLFETS
160 170 180 190 200
AKENVNVEEM FNCITELVLR AKKDNLAKQQ QQQQNDVVKL TKNSKRKKRC

C
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00740000115017.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
InParanoidi Q15286.
KOi K07876.
OMAi NRILVGN.
OrthoDBi EOG7VB2H4.
PhylomeDBi Q15286.
TreeFami TF105954.

Miscellaneous databases

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

Gene expression databases

Bgeei Q15286.
CleanExi HS_RAB35.
ExpressionAtlasi Q15286. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 140 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