Q9D1G1 (RAB1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-1B

Gene names

Name:

Rab1b

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	201 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein transport. Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments By similarity.
Subunit structure	Interacts with MICAL1, MICAL2 and MICAL3. Interacts with GDI1; the interaction requires the GDP-bound state. Interacts with CHM/REP1; the interaction requires the GDP-bound form and is necessary for prenylation by GGTase II By similarity.
Subcellular location	Membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm. Note: Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments. In the GDP-form, colocalizes with GDI in the cytoplasm By similarity.
Post-translational modification	Prenylated; by GGTase II, only after interaction of the substrate with Rab escort protein 1 (REP1) By similarity.
Miscellaneous	Rab-1B binds GTP and GDP and possesses intrinsic GTPase activity By similarity.
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Methylation Prenylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI
Molecular_function	GTP binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 201	201	Ras-related protein Rab-1B		PRO_0000121062
Regions
	Nucleotide binding	15 – 22	8	GTP By similarity
	Nucleotide binding	63 – 67	5	GTP By similarity
	Nucleotide binding	121 – 124	4	GTP By similarity
	Region	64 – 83	20	Switch 2 region; required for interaction with REP1/CHM By similarity
	Motif	37 – 45	9	Effector region By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	201	1	Cysteine methyl ester Potential
	Lipidation	200	1	S-geranylgeranyl cysteine By similarity
	Lipidation	201	1	S-geranylgeranyl cysteine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9D1G1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 870DFF52AEF4B2BE	FASTA	201	22,187
	10 20 30 40 50 60 MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI ELDGKTIKLQ 70 80 90 100 110 120 IWDTAGQERF RTITSSYYRG AHGIIVVYDV TDQESYANVK QWLQEIDRYA SENVNKLLVG 130 140 150 160 170 180 NKSDLTTKKV VDNTTAKEFA DSLGVPFLET SAKNATNVEQ AFMTMAAEIK KRMGPGAASG 190 200 GERPNLKIDS TPVKPASGGC C

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 and NOD. Tissue: Embryo and Spleen.
[2]	"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: Kidney.
[3]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 11-21; 59-69; 72-100; 109-122; 138-153 AND 173-187, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK003609 mRNA. Translation: BAB22888.1. AK156726 mRNA. Translation: BAE33821.1. BC016408 mRNA. Translation: AAH16408.1.
IPI	IPI00133706.
RefSeq	NP_083852.1. NM_029576.3.
UniGene	Mm.182563.
3D structure databases
ProteinModelPortal	Q9D1G1.
SMR	Q9D1G1. Positions 4-173.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4998063.
PTM databases
PhosphoSite	Q9D1G1.
Proteomic databases
PaxDb	Q9D1G1.
PRIDE	Q9D1G1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025804; ENSMUSP00000025804; ENSMUSG00000024870.
GeneID	76308.
KEGG	mmu:76308.
UCSC	uc008gcf.1. mouse.
Organism-specific databases
CTD	81876.
MGI	MGI:1923558. Rab1b.
Phylogenomic databases
eggNOG	COG1100.
GeneTree	ENSGT00700000104049.
HOGENOM	HOG000233968.
HOVERGEN	HBG009351.
InParanoid	Q9D1G1.
KO	K07875.
OMA	MIMASEI.
OrthoDB	EOG48D0WM.
Gene expression databases
ArrayExpress	Q9D1G1.
Bgee	Q9D1G1.
CleanEx	MM_RAB1B.
Genevestigator	Q9D1G1.
GermOnline	ENSMUSG00000024870. Mus musculus.
Family and domain databases
InterPro	IPR027417. P-loop_NTPase. IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003579. Small_GTPase_Rab_type. [Graphical view]
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00175. RAB. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51419. RAB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RAB1B. mouse.
NextBio	344943.
SOURCE	Search...

Entry information

Entry name

RAB1B_MOUSE

Accession

Primary (citable) accession number: Q9D1G1
Secondary accession number(s): Q3U0N1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	June 1, 2001
Last modified:	May 29, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program