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Protein

Ras-related protein Rab-12

Gene

RAB12

Organism
Homo sapiens (Human)
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. 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 similarity).By similarity

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 bindingi49 – 579GTP
Nucleotide bindingi97 – 1015GTPBy similarity
Nucleotide bindingi155 – 1595GTP
Nucleotide bindingi187 – 1882GTP

GO - Molecular functioni

  • GDP binding Source: UniProtKB
  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

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
Gene namesi
Name:RAB12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:31332. RAB12.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Golgi apparatus, Lysosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671102.

Polymorphism and mutation databases

BioMutaiRAB12.
DMDMi122064944.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 244244Ras-related protein Rab-12PRO_0000271377Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei21 – 211PhosphoserineBy similarity
Modified residuei106 – 1061PhosphoserineBy similarity
Lipidationi243 – 2431S-geranylgeranyl cysteineBy similarity
Lipidationi244 – 2441S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiQ6IQ22.
PaxDbiQ6IQ22.
PRIDEiQ6IQ22.

PTM databases

PhosphoSiteiQ6IQ22.

Expressioni

Gene expression databases

BgeeiQ6IQ22.
CleanExiHS_RAB12.
GenevestigatoriQ6IQ22.

Organism-specific databases

HPAiHPA040727.

Interactioni

Subunit structurei

Interacts with RABIF and OPTN.2 Publications

Protein-protein interaction databases

BioGridi128387. 6 interactions.
STRINGi9606.ENSP00000331748.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 489Combined sources
Helixi55 – 628Combined sources
Beta strandi77 – 8610Combined sources
Beta strandi89 – 9810Combined sources
Helixi102 – 1043Combined sources
Helixi105 – 11410Combined sources
Beta strandi116 – 1238Combined sources
Helixi127 – 1315Combined sources
Helixi133 – 14311Combined sources
Beta strandi149 – 1557Combined sources
Helixi157 – 1626Combined sources
Helixi167 – 1759Combined sources
Beta strandi181 – 1844Combined sources
Turni187 – 1904Combined sources
Helixi193 – 20614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IL1X-ray2.10A36-208[»]
ProteinModelPortaliQ6IQ22.
SMRiQ6IQ22. Positions 38-208.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6IQ22.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi71 – 799Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00790000123010.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ6IQ22.
KOiK07907.
OMAiYNVDEIF.
OrthoDBiEOG769ZKM.
PhylomeDBiQ6IQ22.
TreeFamiTF314097.

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.

Q6IQ22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPGAALQRR AGGGGGLGAG SPALSGGQGR RRKQPPRPAD FKLQVIIIGS
60 70 80 90 100
RGVGKTSLME RFTDDTFCEA CKSTVGVDFK IKTVELRGKK IRLQIWDTAG
110 120 130 140 150
QERFNSITSA YYRSAKGIIL VYDITKKETF DDLPKWMKMI DKYASEDAEL
160 170 180 190 200
LLVGNKLDCE TDREITRQQG EKFAQQITGM RFCEASAKDN FNVDEIFLKL
210 220 230 240
VDDILKKMPL DILRNELSNS ILSLQPEPEI PPELPPPRPH VRCC
Length:244
Mass (Da):27,248
Last modified:January 9, 2007 - v3
Checksum:iB4DC65DD0DCB45C4
GO

Sequence cautioni

The sequence AAH71600.2 differs from that shown.Intron retention.Curated
The sequence AAH98407.1 differs from that shown.Intron retention.Curated
The sequence BC050338 differs from that shown. Reason: Frameshift at position 195. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP001793 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01616.1.
BC050338 mRNA. No translation available.
BC071600 mRNA. Translation: AAH71600.2. Sequence problems.
BC098407 mRNA. Translation: AAH98407.1. Sequence problems.
CCDSiCCDS42410.1.
RefSeqiNP_001020471.2. NM_001025300.2.
UniGeneiHs.270074.

Genome annotation databases

EnsembliENST00000329286; ENSP00000331748; ENSG00000206418.
GeneIDi201475.
KEGGihsa:201475.
UCSCiuc002knp.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP001793 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01616.1.
BC050338 mRNA. No translation available.
BC071600 mRNA. Translation: AAH71600.2. Sequence problems.
BC098407 mRNA. Translation: AAH98407.1. Sequence problems.
CCDSiCCDS42410.1.
RefSeqiNP_001020471.2. NM_001025300.2.
UniGeneiHs.270074.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IL1X-ray2.10A36-208[»]
ProteinModelPortaliQ6IQ22.
SMRiQ6IQ22. Positions 38-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128387. 6 interactions.
STRINGi9606.ENSP00000331748.

PTM databases

PhosphoSiteiQ6IQ22.

Polymorphism and mutation databases

BioMutaiRAB12.
DMDMi122064944.

Proteomic databases

MaxQBiQ6IQ22.
PaxDbiQ6IQ22.
PRIDEiQ6IQ22.

Protocols and materials databases

DNASUi201475.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000329286; ENSP00000331748; ENSG00000206418.
GeneIDi201475.
KEGGihsa:201475.
UCSCiuc002knp.3. human.

Organism-specific databases

CTDi201475.
GeneCardsiGC18P008600.
HGNCiHGNC:31332. RAB12.
HPAiHPA040727.
neXtProtiNX_Q6IQ22.
PharmGKBiPA142671102.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00790000123010.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ6IQ22.
KOiK07907.
OMAiYNVDEIF.
OrthoDBiEOG769ZKM.
PhylomeDBiQ6IQ22.
TreeFamiTF314097.

Miscellaneous databases

ChiTaRSiRAB12. human.
EvolutionaryTraceiQ6IQ22.
GenomeRNAii201475.
NextBioi90147.
PROiQ6IQ22.

Gene expression databases

BgeeiQ6IQ22.
CleanExiHS_RAB12.
GenevestigatoriQ6IQ22.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Placenta.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors."
    Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.
    J. Cell Biol. 191:367-381(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Identification and characterisation of novel Mss4-binding Rab GTPases."
    Wixler V., Wixler L., Altenfeld A., Ludwig S., Goody R.S., Itzen A.
    Biol. Chem. 392:239-248(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RABIF.
  9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Crystal structure of a predicted human GTPase in complex with GDP."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 36-208 IN COMPLEX WITH MAGNESIUM AND GDP.

Entry informationi

Entry nameiRAB12_HUMAN
AccessioniPrimary (citable) accession number: Q6IQ22
Secondary accession number(s): A6NEF5, Q4KMQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: May 27, 2015
This is version 111 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.