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O00194 (RB27B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-27B
Alternative name(s):
C25KG
Gene names
Name:RAB27B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in targeting uroplakins to urothelial apical membranes By similarity.

Subunit structure

Interacts with SYTL2, SYTL4, MYRIP and MLPH. Interacts with RPH3A and RPH3A By similarity.

Subcellular location

Membrane; Lipid-anchor.

Tissue specificity

Expressed primarily in testis.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Disulfide bond
Lipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processmultivesicular body sorting pathway

Inferred from mutant phenotype PubMed 19966785. Source: UniProtKB

positive regulation of exocytosis

Inferred from mutant phenotype PubMed 19966785. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: InterPro

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi stack

Inferred from direct assay PubMed 19966785. Source: UniProtKB

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

multivesicular body membrane

Inferred from direct assay PubMed 19966785. Source: UniProtKB

trans-Golgi network transport vesicle

Inferred from direct assay PubMed 19966785. Source: UniProtKB

zymogen granule membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGDP binding

Inferred from direct assay PubMed 20937701. Source: UniProtKB

GTP binding

Inferred from sequence or structural similarity. Source: UniProtKB

GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 16880209. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 218217Ras-related protein Rab-27B
PRO_0000121224

Regions

Nucleotide binding16 – 249GTP
Nucleotide binding74 – 785GTP By similarity
Nucleotide binding133 – 1364GTP
Nucleotide binding163 – 1653GTP
Motif38 – 469Effector region By similarity

Amino acid modifications

Modified residue21N-acetylthreonine Ref.9
Modified residue2181Cysteine methyl ester By similarity
Lipidation2161S-geranylgeranyl cysteine By similarity
Lipidation2181S-geranylgeranyl cysteine By similarity
Disulfide bond123 ↔ 188 Ref.11

Natural variations

Natural variant921A → T.
Corresponds to variant rs9966265 [ dbSNP | Ensembl ].
VAR_051714

Secondary structure

............................ 218
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00194 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 8ED640F0C15EDCD3

FASTA21824,608
        10         20         30         40         50         60 
MTDGDYDYLI KLLALGDSGV GKTTFLYRYT DNKFNPKFIT TVGIDFREKR VVYNAQGPNG 

        70         80         90        100        110        120 
SSGKAFKVHL QLWDTAGQER FRSLTTAFFR DAMGFLLMFD LTSQQSFLNV RNWMSQLQAN 

       130        140        150        160        170        180 
AYCENPDIVL IGNKADLPDQ REVNERQARE LADKYGIPYF ETSAATGQNV EKAVETLLDL 

       190        200        210 
IMKRMEQCVE KTQIPDTVNG GNSGNLDGEK PPEKKCIC 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of rab27a and rab27b, novel human rab proteins shared by melanocytes and platelets."
Chen D., Guo J., Miki T., Tachibana M., Gahl W.A.
Biochem. Mol. Med. 60:27-37(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Melanocyte.
[2]Chen D., Gahl W.A.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 206.
[3]"Chromosomal mapping, gene structure and characterization of the human and murine RAB27B gene."
Ramalho J.S., Tolmachova T., Hume A.N., McGuigan A., Gregory-Evans C.Y., Huxley C., Seabra M.C.
BMC Genet. 2:2-2(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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].
Tissue: Brain.
[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].
Tissue: Amygdala.
[6]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].
[7]"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: Prostate.
[8]"Purification, identification, and characterization of two GTP-binding proteins with molecular weights of 25,000 and 21,000 in human platelet cytosol. One is the rap1/smg21/Krev-1 protein and the other is a novel GTP-binding protein."
Nagata K., Itoh H., Katada T., Takenaka K., Ui M., Kaziro Y., Nozawa Y.
J. Biol. Chem. 264:17000-17005(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Platelet.
[9]Bienvenut W.V., Claeys D.
Submitted (NOV-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-28; 38-47; 50-64; 68-80 AND 150-184, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[10]"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].
[11]"The crystal structure of human RAB27B."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 4-201 IN COMPLEX WITH GDP, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U57093 mRNA. Translation: AAC51194.2.
AF329499 mRNA. Translation: AAK11243.1.
AF498954 mRNA. Translation: AAM21102.1.
AK314115 mRNA. Translation: BAG36807.1.
CH471096 Genomic DNA. Translation: EAW63010.1.
BC027474 mRNA. Translation: AAH27474.1.
RefSeqNP_004154.2. NM_004163.4.
XP_005266790.1. XM_005266733.1.
XP_005266791.1. XM_005266734.2.
UniGeneHs.25318.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F7SX-ray2.70A/B4-201[»]
ProteinModelPortalO00194.
SMRO00194. Positions 5-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111812. 6 interactions.
DIPDIP-48948N.
STRING9606.ENSP00000262094.

PTM databases

PhosphoSiteO00194.

2D gel databases

OGPO00194.

Proteomic databases

PaxDbO00194.
PRIDEO00194.

Protocols and materials databases

DNASU5874.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262094; ENSP00000262094; ENSG00000041353.
GeneID5874.
KEGGhsa:5874.
UCSCuc002lfr.3. human.

Organism-specific databases

CTD5874.
GeneCardsGC18P052385.
HGNCHGNC:9767. RAB27B.
HPACAB017712.
HPA019849.
MIM603869. gene.
neXtProtNX_O00194.
PharmGKBPA34118.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidO00194.
KOK07886.
OMAQNVEKSV.
PhylomeDBO00194.
TreeFamTF312895.

Gene expression databases

ArrayExpressO00194.
BgeeO00194.
CleanExHS_RAB27B.
GenevestigatorO00194.

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

EvolutionaryTraceO00194.
GenomeRNAi5874.
NextBio22822.
PROO00194.
SOURCESearch...

Entry information

Entry nameRB27B_HUMAN
AccessionPrimary (citable) accession number: O00194
Secondary accession number(s): B2RAB0, Q9BZB6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 136 of the entry and version 4 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 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 18

Human chromosome 18: entries, gene names and cross-references to MIM