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Protein

Ras-related protein Rab-27B

Gene

RAB27B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 249GTP
Nucleotide bindingi74 – 785GTPBy similarity
Nucleotide bindingi133 – 1364GTP
Nucleotide bindingi163 – 1653GTP

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTPase activity Source: UniProtKB
  3. GTP binding Source: UniProtKB
  4. myosin V binding Source: UniProtKB
  5. protein domain specific binding Source: UniProtKB

GO - Biological processi

  1. GTP catabolic process Source: GO_Central
  2. intracellular protein transport Source: GO_Central
  3. melanosome transport Source: GO_Central
  4. multivesicular body sorting pathway Source: UniProtKB
  5. positive regulation of exocytosis Source: UniProtKB
  6. protein secretion Source: GO_Central
  7. Rab protein signal transduction Source: GO_Central
  8. vesicle docking involved in exocytosis Source: GO_Central
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-27B
Alternative name(s):
C25KG
Gene namesi
Name:RAB27B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:9767. RAB27B.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. extracellular vesicular exosome Source: UniProtKB
  3. Golgi stack Source: UniProtKB
  4. melanosome Source: UniProtKB
  5. multivesicular body membrane Source: UniProtKB
  6. secretory granule Source: GO_Central
  7. trans-Golgi network transport vesicle Source: UniProtKB
  8. zymogen granule membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34118.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 218217Ras-related protein Rab-27BPRO_0000121224Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Disulfide bondi123 ↔ 1881 Publication
Lipidationi216 – 2161S-geranylgeranyl cysteineBy similarity
Modified residuei218 – 2181Cysteine methyl esterBy similarity
Lipidationi218 – 2181S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiO00194.
PaxDbiO00194.
PRIDEiO00194.

2D gel databases

OGPiO00194.

PTM databases

PhosphoSiteiO00194.

Expressioni

Tissue specificityi

Expressed primarily in testis.

Gene expression databases

BgeeiO00194.
CleanExiHS_RAB27B.
ExpressionAtlasiO00194. baseline and differential.
GenevestigatoriO00194.

Organism-specific databases

HPAiCAB017712.
HPA019849.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi111812. 9 interactions.
DIPiDIP-48948N.
STRINGi9606.ENSP00000262094.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1610Combined sources
Helixi22 – 309Combined sources
Beta strandi37 – 5418Combined sources
Beta strandi65 – 7713Combined sources
Helixi78 – 8912Combined sources
Beta strandi94 – 1007Combined sources
Helixi104 – 11512Combined sources
Turni122 – 1243Combined sources
Beta strandi127 – 1337Combined sources
Helixi138 – 1403Combined sources
Helixi145 – 15410Combined sources
Beta strandi159 – 1624Combined sources
Turni164 – 1663Combined sources
Helixi170 – 18819Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F7SX-ray2.70A/B4-201[»]
ProteinModelPortaliO00194.
SMRiO00194. Positions 5-190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00194.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi38 – 469Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00770000120510.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiO00194.
KOiK07886.
OMAiQNVEKSV.
PhylomeDBiO00194.
TreeFamiTF312895.

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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O00194-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDGDYDYLI KLLALGDSGV GKTTFLYRYT DNKFNPKFIT TVGIDFREKR
60 70 80 90 100
VVYNAQGPNG SSGKAFKVHL QLWDTAGQER FRSLTTAFFR DAMGFLLMFD
110 120 130 140 150
LTSQQSFLNV RNWMSQLQAN AYCENPDIVL IGNKADLPDQ REVNERQARE
160 170 180 190 200
LADKYGIPYF ETSAATGQNV EKAVETLLDL IMKRMEQCVE KTQIPDTVNG
210
GNSGNLDGEK PPEKKCIC
Length:218
Mass (Da):24,608
Last modified:January 23, 2007 - v4
Checksum:i8ED640F0C15EDCD3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921A → T.
Corresponds to variant rs9966265 [ dbSNP | Ensembl ].
VAR_051714

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11958.1.
RefSeqiNP_004154.2. NM_004163.4.
XP_005266790.1. XM_005266733.1.
XP_005266791.1. XM_005266734.2.
UniGeneiHs.25318.

Genome annotation databases

EnsembliENST00000262094; ENSP00000262094; ENSG00000041353.
GeneIDi5874.
KEGGihsa:5874.
UCSCiuc002lfr.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11958.1.
RefSeqiNP_004154.2. NM_004163.4.
XP_005266790.1. XM_005266733.1.
XP_005266791.1. XM_005266734.2.
UniGeneiHs.25318.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F7SX-ray2.70A/B4-201[»]
ProteinModelPortaliO00194.
SMRiO00194. Positions 5-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111812. 9 interactions.
DIPiDIP-48948N.
STRINGi9606.ENSP00000262094.

PTM databases

PhosphoSiteiO00194.

2D gel databases

OGPiO00194.

Proteomic databases

MaxQBiO00194.
PaxDbiO00194.
PRIDEiO00194.

Protocols and materials databases

DNASUi5874.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262094; ENSP00000262094; ENSG00000041353.
GeneIDi5874.
KEGGihsa:5874.
UCSCiuc002lfr.3. human.

Organism-specific databases

CTDi5874.
GeneCardsiGC18P052385.
HGNCiHGNC:9767. RAB27B.
HPAiCAB017712.
HPA019849.
MIMi603869. gene.
neXtProtiNX_O00194.
PharmGKBiPA34118.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00770000120510.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiO00194.
KOiK07886.
OMAiQNVEKSV.
PhylomeDBiO00194.
TreeFamiTF312895.

Miscellaneous databases

EvolutionaryTraceiO00194.
GenomeRNAii5874.
NextBioi22822.
PROiO00194.
SOURCEiSearch...

Gene expression databases

BgeeiO00194.
CleanExiHS_RAB27B.
ExpressionAtlasiO00194. baseline and differential.
GenevestigatoriO00194.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiRB27B_HUMAN
AccessioniPrimary (citable) accession number: O00194
Secondary accession number(s): B2RAB0, Q9BZB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 144 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.