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Protein

Ras-related protein Rab-12

Gene

Rab12

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

Functioni

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). That Rab may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor. Involved in autophagy.By similarity2 Publications

Enzyme regulationi

Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP) (By similarity). That Rab is activated by DENND3, a guanine exchange factor.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 569GTPBy similarity
Nucleotide bindingi96 – 1005GTPBy similarity
Nucleotide bindingi154 – 1585GTPBy similarity
Nucleotide bindingi186 – 1872GTPBy similarity

GO - Molecular functioni

GO - Biological processi

  • autophagy Source: UniProtKB-KW
  • cellular protein catabolic process Source: UniProtKB
  • endosome to lysosome transport Source: UniProtKB
  • positive regulation of macroautophagy Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-12
Alternative name(s):
Rab-13
Gene namesi
Name:Rab12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:894284. Rab12.

Subcellular locationi

GO - Cellular componenti

  • autophagosome Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB-KW
  • Golgi membrane Source: UniProtKB-SubCell
  • lysosomal membrane Source: UniProtKB-SubCell
  • lysosome Source: UniProtKB
  • recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Golgi apparatus, Lysosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001Q → L: Probable constitutively active mutant unable to hydrolyze GTP; increases degradation of the transferrin receptor. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 243243Ras-related protein Rab-12PRO_0000121180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei15 – 151PhosphoserineCombined sources
Modified residuei20 – 201PhosphoserineCombined sources
Modified residuei24 – 241PhosphoserineCombined sources
Modified residuei105 – 1051PhosphoserineCombined sources
Lipidationi242 – 2421S-geranylgeranyl cysteineBy similarity
Lipidationi243 – 2431S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP35283.
PaxDbiP35283.
PRIDEiP35283.

PTM databases

iPTMnetiP35283.
PhosphoSiteiP35283.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiP35283.
CleanExiMM_RAB12.
ExpressionAtlasiP35283. baseline and differential.
GenevisibleiP35283. MM.

Interactioni

Subunit structurei

Interacts with RABIF and OPTN.1 Publication

Protein-protein interaction databases

IntActiP35283. 6 interactions.
MINTiMINT-7898918.
STRINGi10090.ENSMUSP00000128645.

Structurei

3D structure databases

ProteinModelPortaliP35283.
SMRiP35283. Positions 37-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi70 – 789Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiKOG0078. Eukaryota.
ENOG410XPUI. LUCA.
GeneTreeiENSGT00760000118937.
HOVERGENiHBG009351.
InParanoidiP35283.
KOiK07907.
PhylomeDBiP35283.

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.

P35283-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPSAALHRR PAGGSLGAVS PALSGGQARR RKQPPRPADF KLQVIIIGSR
60 70 80 90 100
GVGKTSLMER FTDDTFCEAC KSTVGVDFKI KTVELRGKKI RLQIWDTAGQ
110 120 130 140 150
ERFNSITSAY YRSAKGIILV YDITKKETFD DLPKWMKMID KYASEDAELL
160 170 180 190 200
LVGNKLDCET DREISRQQGE KFAQQITGMR FCEASAKDNF NVDEIFLKLV
210 220 230 240
DDILKKMPLD VLRNELSNSI LSLQPEPEIP PELPPPRPHV RCC
Length:243
Mass (Da):27,329
Last modified:January 9, 2007 - v3
Checksum:i34E4EDC67F710510
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831V → L in BAB28956 (PubMed:16141072).Curated
Sequence conflicti86 – 861R → T in BAB28956 (PubMed:16141072).Curated
Sequence conflicti184 – 1852AS → PD in BAB28956 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB232607 mRNA. Translation: BAF02869.1.
M79303 mRNA. Translation: AAK14827.1.
AK013690 mRNA. Translation: BAB28956.1.
CCDSiCCDS50169.1.
PIRiJH0643.
RefSeqiNP_077768.2. NM_024448.2.
UniGeneiMm.248313.

Genome annotation databases

EnsembliENSMUST00000167962; ENSMUSP00000128645; ENSMUSG00000023460.
GeneIDi19328.
KEGGimmu:19328.
UCSCiuc008djy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB232607 mRNA. Translation: BAF02869.1.
M79303 mRNA. Translation: AAK14827.1.
AK013690 mRNA. Translation: BAB28956.1.
CCDSiCCDS50169.1.
PIRiJH0643.
RefSeqiNP_077768.2. NM_024448.2.
UniGeneiMm.248313.

3D structure databases

ProteinModelPortaliP35283.
SMRiP35283. Positions 37-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP35283. 6 interactions.
MINTiMINT-7898918.
STRINGi10090.ENSMUSP00000128645.

PTM databases

iPTMnetiP35283.
PhosphoSiteiP35283.

Proteomic databases

MaxQBiP35283.
PaxDbiP35283.
PRIDEiP35283.

Protocols and materials databases

DNASUi19328.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000167962; ENSMUSP00000128645; ENSMUSG00000023460.
GeneIDi19328.
KEGGimmu:19328.
UCSCiuc008djy.1. mouse.

Organism-specific databases

CTDi201475.
MGIiMGI:894284. Rab12.

Phylogenomic databases

eggNOGiKOG0078. Eukaryota.
ENOG410XPUI. LUCA.
GeneTreeiENSGT00760000118937.
HOVERGENiHBG009351.
InParanoidiP35283.
KOiK07907.
PhylomeDBiP35283.

Miscellaneous databases

ChiTaRSiRab12. mouse.
NextBioi296297.
PROiP35283.
SOURCEiSearch...

Gene expression databases

BgeeiP35283.
CleanExiMM_RAB12.
ExpressionAtlasiP35283. baseline and differential.
GenevisibleiP35283. 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

« Hide 'large scale' publications
  1. "Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16) domain-containing proteins based on their Rab-binding activity."
    Itoh T., Satoh M., Kanno E., Fukuda M.
    Genes Cells 11:1023-1037(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The complexity of the Rab and Rho GTP-binding protein subfamilies revealed by a PCR cloning approach."
    Chavrier P., Simons K., Zerial M.
    Gene 112:261-264(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-101.
    Tissue: Kidney.
  3. "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] OF 83-243.
    Strain: C57BL/6J.
    Tissue: Hippocampus.
  4. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-20 AND SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-20; SER-24 AND SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen and Testis.
  8. "Small GTPase Rab12 regulates constitutive degradation of transferrin receptor."
    Matsui T., Itoh T., Fukuda M.
    Traffic 12:1432-1443(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLN-100, ENZYME REGULATION.
  9. "M98K-OPTN induces transferrin receptor degradation and RAB12-mediated autophagic death in retinal ganglion cells."
    Sirohi K., Chalasani M.L., Sudhakar C., Kumari A., Radha V., Swarup G.
    Autophagy 9:510-527(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH OPTN.

Entry informationi

Entry nameiRAB12_MOUSE
AccessioniPrimary (citable) accession number: P35283
Secondary accession number(s): Q0PD43, Q9CUW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 9, 2007
Last modified: May 11, 2016
This is version 138 of the entry and version 3 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.