Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ras-related protein Rab-9B

Gene

Rab9b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the transport of proteins between the endosomes and the trans Golgi network.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 229GTPBy similarity
Nucleotide bindingi62 – 665GTPBy similarity
Nucleotide bindingi124 – 1274GTPBy similarity
Nucleotide bindingi154 – 1563GTPBy similarity

GO - Molecular functioni

GO - Biological processi

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-9B
Gene namesi
Name:Rab9b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:2442454. Rab9b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Ras-related protein Rab-9BPRO_0000121143Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341PhosphoserineCombined sources
Lipidationi200 – 2001S-geranylgeranyl cysteineBy similarity
Lipidationi201 – 2011S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Phosphoprotein, Prenylation

Proteomic databases

EPDiQ8BHH2.
MaxQBiQ8BHH2.
PaxDbiQ8BHH2.
PRIDEiQ8BHH2.

PTM databases

iPTMnetiQ8BHH2.
PhosphoSiteiQ8BHH2.

Expressioni

Gene expression databases

BgeeiQ8BHH2.
CleanExiMM_RAB9B.
ExpressionAtlasiQ8BHH2. baseline and differential.
GenevisibleiQ8BHH2. MM.

Interactioni

Protein-protein interaction databases

DIPiDIP-61069N.
IntActiQ8BHH2. 10 interactions.
STRINGi10090.ENSMUSP00000049739.

Structurei

3D structure databases

ProteinModelPortaliQ8BHH2.
SMRiQ8BHH2. Positions 3-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi36 – 449Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiKOG0394. Eukaryota.
ENOG410XNZV. LUCA.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ8BHH2.
KOiK07900.
OMAiKEFMYYS.
OrthoDBiEOG7G4QG8.
PhylomeDBiQ8BHH2.
TreeFamiTF326442.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BHH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGKSLLLKV ILLGDGGVGK SSLMNRYVTN KFDSQAFHTI GVEFLNRDLE
60 70 80 90 100
VDGRFVTLQI WDTAGQERFK SLRTPFYRGA DCCLLTFSVD DRQSFENLGN
110 120 130 140 150
WQKEFIYYAD VKDPDHFPFV VLGNKVDKED RQVTTEEAQA WCMENGNYPY
160 170 180 190 200
LETSAKDDTN VTVAFEEAVR QVLAVEEQLE HCMLGHTIDL NSGSKASSSC

C
Length:201
Mass (Da):22,704
Last modified:March 1, 2003 - v1
Checksum:i1E28B18F8F8DDDFD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034442 mRNA. Translation: BAC28710.1.
AK049693 mRNA. Translation: BAC33876.1.
CCDSiCCDS30425.1.
RefSeqiNP_795945.1. NM_176971.2.
UniGeneiMm.44557.

Genome annotation databases

EnsembliENSMUST00000058814; ENSMUSP00000049739; ENSMUSG00000043463.
GeneIDi319642.
KEGGimmu:319642.
UCSCiuc009uje.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034442 mRNA. Translation: BAC28710.1.
AK049693 mRNA. Translation: BAC33876.1.
CCDSiCCDS30425.1.
RefSeqiNP_795945.1. NM_176971.2.
UniGeneiMm.44557.

3D structure databases

ProteinModelPortaliQ8BHH2.
SMRiQ8BHH2. Positions 3-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61069N.
IntActiQ8BHH2. 10 interactions.
STRINGi10090.ENSMUSP00000049739.

PTM databases

iPTMnetiQ8BHH2.
PhosphoSiteiQ8BHH2.

Proteomic databases

EPDiQ8BHH2.
MaxQBiQ8BHH2.
PaxDbiQ8BHH2.
PRIDEiQ8BHH2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058814; ENSMUSP00000049739; ENSMUSG00000043463.
GeneIDi319642.
KEGGimmu:319642.
UCSCiuc009uje.1. mouse.

Organism-specific databases

CTDi51209.
MGIiMGI:2442454. Rab9b.

Phylogenomic databases

eggNOGiKOG0394. Eukaryota.
ENOG410XNZV. LUCA.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ8BHH2.
KOiK07900.
OMAiKEFMYYS.
OrthoDBiEOG7G4QG8.
PhylomeDBiQ8BHH2.
TreeFamiTF326442.

Miscellaneous databases

PROiQ8BHH2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BHH2.
CleanExiMM_RAB9B.
ExpressionAtlasiQ8BHH2. baseline and differential.
GenevisibleiQ8BHH2. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Diencephalon and Spinal cord.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiRAB9B_MOUSE
AccessioniPrimary (citable) accession number: Q8BHH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.