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Q9BZG1 (RAB34_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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-34
Alternative name(s):
Ras-related protein Rab-39
Ras-related protein Rah
Gene names
Name:RAB34
Synonyms:RAB39, RAH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length259 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein transport. Involved in the redistribution of lysosomes to the peri-Golgi region By similarity. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes. Ref.11

Subunit structure

Interacts with RILP. Ref.7

Subcellular location

Cytoplasm By similarity. Golgi apparatus By similarity. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Recruited to phagosomes containing S.aureus or M.tuberculosis. Ref.11

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Cytoplasmic vesicle
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Lipoprotein
Phosphoprotein
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to plasma membrane protein transport

Inferred from direct assay PubMed 17881736. Source: UniProt

antigen processing and presentation

Inferred from mutant phenotype PubMed 19717423. Source: UniProt

lysosome localization

Inferred from direct assay PubMed 17881736. Source: UniProt

phagosome maturation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

phagosome-lysosome fusion

Inferred from mutant phenotype Ref.11. Source: UniProtKB

protein localization to plasma membrane

Inferred from direct assay PubMed 17881736. Source: UniProt

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 16138900. Source: UniProt

Golgi cisterna

Inferred from direct assay PubMed 17881736. Source: UniProt

Golgi stack

Inferred from direct assay PubMed 17881736. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

perinuclear region of cytoplasm

Inferred from direct assay PubMed 16138900. Source: UniProt

phagocytic vesicle

Inferred from direct assay Ref.11. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

vesicle

Inferred from direct assay PubMed 17881736. Source: UniProt

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BZG1-1)

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: Q9BZG1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     164-171: Missing.
Isoform NARR (identifier: P0DI83-1)

The sequence of this isoform can be found in the external entry P0DI83.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform 4 (identifier: Q9BZG1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     51-72: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 259259Ras-related protein Rab-34
PRO_0000121243

Regions

Nucleotide binding59 – 668GTP By similarity
Nucleotide binding107 – 1115GTP By similarity
Nucleotide binding166 – 1694GTP By similarity
Motif81 – 899Effector region By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.12 Ref.13
Modified residue2411Phosphoserine Ref.8 Ref.10
Modified residue2441Phosphoserine Ref.10
Lipidation2571S-geranylgeranyl cysteine Potential
Lipidation2581S-geranylgeranyl cysteine Potential

Natural variations

Alternative sequence51 – 7222Missing in isoform 4.
VSP_044734
Alternative sequence164 – 1718Missing in isoform 2.
VSP_010142
Natural variant1971V → L.
Corresponds to variant rs12125 [ dbSNP | Ensembl ].
VAR_015097

Experimental info

Sequence conflict101D → Y in BAG65412. Ref.4
Sequence conflict551V → I in BAC11141. Ref.4

Sequences

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

Last modified June 1, 2001. Version 1.
Checksum: 6D38A6F090F9802D

FASTA25929,044
        10         20         30         40         50         60 
MNILAPVRRD RVLAELPQCL RKEAALHGHK DFHPRVTCAC QEHRTGTVGF KISKVIVVGD 

        70         80         90        100        110        120 
LSVGKTCLIN RFCKDTFDKN YKATIGVDFE MERFEVLGIP FSLQLWDTAG QERFKCIAST 

       130        140        150        160        170        180 
YYRGAQAIII VFNLNDVASL EHTKQWLADA LKENDPSSVL LFLVGSKKDL STPAQYALME 

       190        200        210        220        230        240 
KDALQVAQEM KAEYWAVSSL TGENVREFFF RVAALTFEAN VLAELEKSGA RRIGDVVRIN 

       250 
SDDSNLYLTA SKKKPTCCP 

« Hide

Isoform 2 [UniParc].

Checksum: 8022E7023BC5137B
Show »

FASTA25128,230
Isoform NARR [UniParc].

See P0DI83.

Isoform 4 [UniParc].

Checksum: 8AD7BEDE6338BB85
Show »

FASTA23726,673

References

« Hide 'large scale' references
[1]"Human Rab39 coding region (cDNA)."
Hong W.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Full-length sequencing of 100 cDNA clones from human adult skeletal muscle."
Stanchi F., Lanfranchi G.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Skeletal muscle.
[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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"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 4).
Tissue: Embryo, Mammary gland and Uterus.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
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: Brain and Pancreas.
[7]"A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34."
Wang T., Wong K.K., Hong W.
Mol. Biol. Cell 15:815-826(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RILP.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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].
[10]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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.
[12]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF322067 mRNA. Translation: AAK09397.1.
AJ277106 mRNA. Translation: CAC81760.1.
BT006702 mRNA. Translation: AAP35348.1.
AK027312 mRNA. Translation: BAB55034.1.
AK074689 mRNA. Translation: BAC11141.1.
AK304633 mRNA. Translation: BAG65412.1.
AC010761 Genomic DNA. No translation available.
BC016841 mRNA. Translation: AAH16841.1.
BC091510 mRNA. Translation: AAH91510.1.
RefSeqNP_001138414.1. NM_001144942.1.
NP_001243205.1. NM_001256276.1.
NP_001243206.1. NM_001256277.1.
NP_001243207.1. NM_001256278.1.
NP_114140.4. NM_031934.5.
UniGeneHs.301853.

3D structure databases

ProteinModelPortalQ9BZG1.
SMRQ9BZG1. Positions 54-213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123784. 3 interactions.
IntActQ9BZG1. 1 interaction.
MINTMINT-4538882.
STRING9606.ENSP00000410403.

PTM databases

PhosphoSiteQ9BZG1.

Polymorphism databases

DMDM20139693.

Proteomic databases

PaxDbQ9BZG1.
PRIDEQ9BZG1.

Protocols and materials databases

DNASU83871.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301043; ENSP00000301043; ENSG00000109113. [Q9BZG1-1]
ENST00000395243; ENSP00000378664; ENSG00000109113. [Q9BZG1-2]
ENST00000395245; ENSP00000378666; ENSG00000109113. [Q9BZG1-1]
ENST00000415040; ENSP00000410279; ENSG00000109113. [Q9BZG1-4]
ENST00000436730; ENSP00000404180; ENSG00000109113. [Q9BZG1-1]
ENST00000450529; ENSP00000391048; ENSG00000109113. [Q9BZG1-2]
GeneID83871.
KEGGhsa:83871.
UCSCuc002hce.2. human. [Q9BZG1-1]
uc002hcg.2. human. [Q9BZG1-2]

Organism-specific databases

CTD83871.
GeneCardsGC17M027041.
HGNCHGNC:16519. RAB34.
HPAHPA021366.
MIM610917. gene.
neXtProtNX_Q9BZG1.
PharmGKBPA34126.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233970.
HOVERGENHBG106693.
InParanoidQ9BZG1.
KOK07921.
PhylomeDBQ9BZG1.

Gene expression databases

ArrayExpressQ9BZG1.
BgeeQ9BZG1.
CleanExHS_RAB34.
HS_RAB39.
GenevestigatorQ9BZG1.

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

ChiTaRSRAB34. human.
GeneWikiRAB34.
GenomeRNAi83871.
NextBio72895.
PROQ9BZG1.
SOURCESearch...

Entry information

Entry nameRAB34_HUMAN
AccessionPrimary (citable) accession number: Q9BZG1
Secondary accession number(s): B4E3A0 expand/collapse secondary AC list , E9PEJ9, Q5BJE6, Q8NCJ8, Q96AR4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 126 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM