Q6IQ22 (RAB12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-12

Gene names

Name:

RAB12

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Protein existence	Evidence 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.5
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.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Endosome Golgi apparatus Lysosome Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB endosome to lysosome transport Inferred from sequence or structural similarity. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from sequence or structural similarity. Source: UniProtKB recycling endosome membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	GDP binding Inferred from direct assay Ref.5. Source: UniProtKB GTP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 244

244

Ras-related protein Rab-12

PRO_0000271377

Regions

Nucleotide binding

49 – 57

9

GTP

Nucleotide binding

97 – 101

5

GTP By similarity

Nucleotide binding

155 – 159

5

GTP

Nucleotide binding

187 – 188

2

GTP

Motif

71 – 79

9

Effector region By similarity

Amino acid modifications

Modified residue

21

1

Phosphoserine By similarity

Modified residue

106

1

Phosphoserine By similarity

Lipidation

243

1

S-geranylgeranyl cysteine By similarity

Lipidation

244

1

S-geranylgeranyl cysteine By similarity

Secondary structure

1

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244

Helix Strand Turn

Details...

Beta strand

40 – 48

9

Helix

55 – 62

8

Beta strand

77 – 86

10

Beta strand

89 – 98

10

Helix

102 – 104

3

Helix

105 – 114

10

Beta strand

116 – 123

8

Helix

127 – 131

5

Helix

133 – 143

11

Beta strand

149 – 155

7

Helix

157 – 162

6

Helix

167 – 175

9

Beta strand

181 – 184

4

Turn

187 – 190

4

Helix

193 – 206

14

Sequences

	Sequence		Length	Mass (Da)
	Q6IQ22 [UniParc]. Last modified January 9, 2007. Version 3. Checksum: B4DC65DD0DCB45C4	FASTA	244	27,248
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.
[6]	"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].
[7]	"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.
[8]	"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.

IPI

IPI00419932.

RefSeq

NP_001020471.2. NM_001025300.2.

UniGene

Hs.270074.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IL1	X-ray	2.10	A	36-208	[»]

ProteinModelPortal

Q6IQ22.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000331748.

PTM databases

PhosphoSite

Q6IQ22.

Polymorphism databases

DMDM

122064944.

Proteomic databases

PaxDb

Q6IQ22.

PRIDE

Q6IQ22.

Protocols and materials databases

DNASU

201475.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000329286; ENSP00000331748; ENSG00000206418.

GeneID

201475.

KEGG

hsa:201475.

UCSC

uc002knp.3. human.

Organism-specific databases

CTD

201475.

GeneCards

GC18P008600.

HGNC

HGNC:31332. RAB12.

HPA

HPA040727.

neXtProt

NX_Q6IQ22.

PharmGKB

PA142671102.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233968.

HOVERGEN

HBG009351.

InParanoid

Q6IQ22.

KO

K07907.

OMA

CEVDREI.

OrthoDB

EOG45757M.

Gene expression databases

Bgee

Q6IQ22.

CleanEx

HS_RAB12.

Genevestigator

Q6IQ22.

Family and domain databases

InterPro

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]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51419. RAB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RAB12. human.

EvolutionaryTrace

Q6IQ22.

GenomeRNAi

201475.

NextBio

90147.

Entry information

Entry name

RAB12_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.