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Q86YS6 (RAB43_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-43
Alternative name(s):
Ras-related protein Rab-41
Gene names
Name:RAB43
Synonyms:RAB41
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. The low intrinsic GTPase activity of RAB43 is activated by USP6NL. Involved in retrograde transport from the endocytic pathway to the Golgi apparatus. Involved in the transport of Shiga toxin from early and recycling endosomes to the trans-Golgi network. Required for the structural integrity of the Golgi complex. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Golgi apparatus. Golgi apparatustrans-Golgi network membrane; Lipid-anchor By similarity. Golgi apparatustrans-Golgi network. Note: Recruited to phagosomes containing S.aureus or M.tuberculosis. Ref.6 Ref.8 Ref.9

Tissue specificity

Widely expressed in brain, testis, lung, heart, ovary, colon, kidney, uterus and spleen but not in liver. Ref.1

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86YS6-1)

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: Q9ULR0-1)

Also known as: ISY1-RAB43;

The sequence of this isoform can be found in the external entry Q9ULR0.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Based on a readthrough transcript which may produce a ISY1-RAB43 fusion protein. No experimental confirmation available.
Isoform 3 (identifier: Q86YS6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     130-155: GNKSDLSELREVSLAEAQSLAEHYDI → EMQSCYVAQADLELLASSNPPASTSK
     156-212: Missing.
Note: Gene prediction based on EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Ras-related protein Rab-43
PRO_0000244615

Regions

Nucleotide binding25 – 328GTP
Nucleotide binding73 – 775GTP By similarity
Nucleotide binding131 – 1344GTP
Nucleotide binding163 – 1642GTP
Motif47 – 559Effector region By similarity

Amino acid modifications

Modified residue491Phosphoserine By similarity
Modified residue2121Cysteine methyl ester By similarity
Lipidation2101S-geranylgeranyl cysteine By similarity
Lipidation2121S-geranylgeranyl cysteine By similarity

Natural variations

Alternative sequence130 – 15526GNKSD…EHYDI → EMQSCYVAQADLELLASSNP PASTSK in isoform 3.
VSP_054030
Alternative sequence156 – 21257Missing in isoform 3.
VSP_054031

Experimental info

Mutagenesis321T → N: Abolishes activity. Disrupts Golgi structure. Ref.7 Ref.8

Secondary structure

.............................. 212
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 2003. Version 1.
Checksum: 087EE3802B7159C9

FASTA21223,339
        10         20         30         40         50         60 
MAGPGPGPGD PDEQYDFLFK LVLVGDASVG KTCVVQRFKT GAFSERQGST IGVDFTMKTL 

        70         80         90        100        110        120 
EIQGKRVKLQ IWDTAGQERF RTITQSYYRS ANGAILAYDI TKRSSFLSVP HWIEDVRKYA 

       130        140        150        160        170        180 
GSNIVQLLIG NKSDLSELRE VSLAEAQSLA EHYDILCAIE TSAKDSSNVE EAFLRVATEL 

       190        200        210 
IMRHGGPLFS EKSPDHIQLN SKDIGEGWGC GC 

« Hide

Isoform 2 (ISY1-RAB43) [UniParc].

See Q9ULR0.

Isoform 3 [UniParc].

Checksum: CC4EA3C8FD5E005D
Show »

FASTA15517,074

References

« Hide 'large scale' references
[1]"Isolation, expression pattern of a novel human RAB gene RAB41 and characterization of its intronless homolog RAB41P."
Guo J.H., Chen L., Chen S., Liu X., Saiyin H., Deng Q., Zhuang Y., Wan B., Yu L., Zhao S.Y.
DNA Seq. 14:431-435(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
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]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Eye.
[6]"Specific Rab GTPase-activating proteins define the Shiga toxin and epidermal growth factor uptake pathways."
Fuchs E., Haas A.K., Spooner R.A., Yoshimura S., Lord J.M., Barr F.A.
J. Cell Biol. 177:1133-1143(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells."
Haas A.K., Yoshimura S., Stephens D.J., Preisinger C., Fuchs E., Barr F.A.
J. Cell Sci. 120:2997-3010(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF THR-32.
[8]"Rab18 and Rab43 have key roles in ER-Golgi trafficking."
Dejgaard S.Y., Murshid A., Erman A., Kizilay O., Verbich D., Lodge R., Dejgaard K., Ly-Hartig T.B., Pepperkok R., Simpson J.C., Presley J.F.
J. Cell Sci. 121:2768-2781(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF THR-32, SUBCELLULAR LOCATION.
[9]"Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
Seto S., Tsujimura K., Koide Y.
Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"Crystal structure of human RAB43 in complex with GDP."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 9-190 IN COMPLEX WITH GDP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY166852 mRNA. Translation: AAO17291.1.
AK291014 mRNA. Translation: BAF83703.1.
AC108673 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79283.1.
BC062319 mRNA. Translation: AAH62319.1.
CCDSCCDS33850.1. [Q86YS6-1]
RefSeqNP_001191812.1. NM_001204883.1. [Q86YS6-1]
NP_001191813.1. NM_001204884.1. [Q86YS6-1]
NP_001191814.1. NM_001204885.1. [Q86YS6-1]
NP_001191815.1. NM_001204886.1. [Q86YS6-1]
NP_001191816.1. NM_001204887.1. [Q86YS6-2]
NP_940892.1. NM_198490.2. [Q86YS6-1]
UniGeneHs.381132.
Hs.512661.
Hs.546542.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HUPX-ray2.05A/B9-190[»]
ProteinModelPortalQ86YS6.
SMRQ86YS6. Positions 15-186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid130830. 2 interactions.
STRING9606.ENSP00000319781.

PTM databases

PhosphoSiteQ86YS6.

Polymorphism databases

DMDM74727944.

Proteomic databases

MaxQBQ86YS6.
PaxDbQ86YS6.
PRIDEQ86YS6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315150; ENSP00000319781; ENSG00000172780. [Q86YS6-1]
ENST00000393304; ENSP00000376981; ENSG00000172780. [Q86YS6-1]
ENST00000393305; ENSP00000376982; ENSG00000172780. [Q86YS6-1]
ENST00000393307; ENSP00000376984; ENSG00000172780. [Q86YS6-1]
ENST00000393308; ENSP00000376985; ENSG00000172780. [Q86YS6-1]
ENST00000476465; ENSP00000427632; ENSG00000172780.
GeneID339122.
KEGGhsa:339122.
UCSCuc003eln.2. human. [Q86YS6-1]

Organism-specific databases

CTD339122.
GeneCardsGC03M128806.
HGNCHGNC:19983. RAB43.
HPAHPA046840.
neXtProtNX_Q86YS6.
PharmGKBPA134968262.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidQ86YS6.
KOK07930.
OMAKTCIVQR.
OrthoDBEOG7NGQCK.
PhylomeDBQ86YS6.
TreeFamTF300097.

Gene expression databases

ArrayExpressQ86YS6.
BgeeQ86YS6.
CleanExHS_RAB41.
HS_RAB43.
GenevestigatorQ86YS6.

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

EvolutionaryTraceQ86YS6.
GenomeRNAi339122.
NextBio97235.
PROQ86YS6.

Entry information

Entry nameRAB43_HUMAN
AccessionPrimary (citable) accession number: Q86YS6
Secondary accession number(s): A8K4P9, E9PBQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 108 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

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM