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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subcellular location	Golgi apparatus membrane; Lipid-anchor 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	Golgi apparatus Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome 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 membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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 Ref.4 Ref.5

Modified residue

25

1

Phosphoserine Ref.4

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

56 – 62

7

Beta strand

78 – 85

8

Beta strand

90 – 97

8

Helix

102 – 104

3

Helix

105 – 114

10

Beta strand

119 – 121

3

Helix

127 – 131

5

Helix

133 – 143

11

Beta strand

151 – 153

3

Helix

157 – 162

6

Helix

172 – 175

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: 16177791] [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: 15489334] [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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-25, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"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.

SMR

Q6IQ22. Positions 38-208.

ModBase

Search...

Protein-protein interaction databases

STRING

Q6IQ22.

PTM databases

PhosphoSite

Q6IQ22.

Polymorphism databases

DMDM

122064944.

Proteomic databases

PRIDE

Q6IQ22.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000329286; ENSP00000331748; ENSG00000206418.

GeneID

201475.

KEGG

hsa:201475.

NMPDR

fig|9606.3.peg.14764.

UCSC

uc002knp.1. human.

Organism-specific databases

CTD

201475.

GeneCards

GC18P008600.

HGNC

HGNC:31332. RAB12.

HPA

HPA040727.

neXtProt

NX_Q6IQ22.

PharmGKB

PA142671102.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00550000074219.

HOGENOM

HBG745225.

HOVERGEN

HBG009351.

InParanoid

Q6IQ22.

OMA

CEVDREI.

OrthoDB

EOG45757M.

PhylomeDB

Q6IQ22.

Gene expression databases

ArrayExpress

Q6IQ22.

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]

KO

K07907.

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

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:	December 14, 2011
This is version 77 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.