Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6IQ22 (RAB12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-12
Gene names
Name:RAB12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Enzyme regulation

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. Ref.6

Subunit structure

May interact with RABIF.

Subcellular location

Recycling endosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Lysosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Golgi apparatus membrane By similarity.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Sequence caution

The sequence AAH71600.2 differs from that shown. Reason: Intron retention.

The sequence AAH98407.1 differs from that shown. Reason: Intron retention.

The sequence BC050338 differs from that shown. Reason: Frameshift at position 195.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 244244Ras-related protein Rab-12
PRO_0000271377

Regions

Nucleotide binding49 – 579GTP
Nucleotide binding97 – 1015GTP By similarity
Nucleotide binding155 – 1595GTP
Nucleotide binding187 – 1882GTP
Motif71 – 799Effector region By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9 Ref.10
Modified residue211Phosphoserine By similarity
Modified residue1061Phosphoserine By similarity
Lipidation2431S-geranylgeranyl cysteine By similarity
Lipidation2441S-geranylgeranyl cysteine By similarity

Secondary structure

.............................. 244
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6IQ22 [UniParc].

Last modified January 9, 2007. Version 3.
Checksum: B4DC65DD0DCB45C4

FASTA24427,248
        10         20         30         40         50         60 
MDPGAALQRR AGGGGGLGAG SPALSGGQGR RRKQPPRPAD FKLQVIIIGS RGVGKTSLME 

        70         80         90        100        110        120 
RFTDDTFCEA CKSTVGVDFK IKTVELRGKK IRLQIWDTAG QERFNSITSA YYRSAKGIIL 

       130        140        150        160        170        180 
VYDITKKETF DDLPKWMKMI DKYASEDAEL LLVGNKLDCE TDREITRQQG EKFAQQITGM 

       190        200        210        220        230        240 
RFCEASAKDN FNVDEIFLKL VDDILKKMPL DILRNELSNS ILSLQPEPEI PPELPPPRPH 


VRCC 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001020471.2. NM_001025300.2.
UniGeneHs.270074.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IL1X-ray2.10A36-208[»]
ProteinModelPortalQ6IQ22.
SMRQ6IQ22. Positions 38-208.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128387. 4 interactions.
STRING9606.ENSP00000331748.

PTM databases

PhosphoSiteQ6IQ22.

Polymorphism databases

DMDM122064944.

Proteomic databases

PaxDbQ6IQ22.
PRIDEQ6IQ22.

Protocols and materials databases

DNASU201475.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329286; ENSP00000331748; ENSG00000206418.
GeneID201475.
KEGGhsa:201475.
UCSCuc002knp.3. human.

Organism-specific databases

CTD201475.
GeneCardsGC18P008600.
HGNCHGNC:31332. RAB12.
HPAHPA040727.
neXtProtNX_Q6IQ22.
PharmGKBPA142671102.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidQ6IQ22.
KOK07907.
OMAPPRMRCC.
OrthoDBEOG769ZKM.
PhylomeDBQ6IQ22.
TreeFamTF314097.

Gene expression databases

BgeeQ6IQ22.
CleanExHS_RAB12.
GenevestigatorQ6IQ22.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAB12. human.
EvolutionaryTraceQ6IQ22.
GenomeRNAi201475.
NextBio90147.
PROQ6IQ22.

Entry information

Entry nameRAB12_HUMAN
AccessionPrimary (citable) accession number: Q6IQ22
Secondary accession number(s): A6NEF5, Q4KMQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: April 16, 2014
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM