Ras-related protein Rab-31 - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-31
Alternative name(s):
Rab-22B

Gene names

Name:	RAB31
Synonyms:	RAB22B

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	194 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential.
Tissue specificity	Highest expression in placenta and brain with lower levels in heart and lung. Not detected in liver, skeletal muscle, kidney or pancreas. Ref.2
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

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Ontologies

Keywords
Cellular component	Cell membrane Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Phosphoprotein Prenylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein transport Inferred from electronic annotation. Source: InterPro small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 194

194

Ras-related protein Rab-31

PRO_0000121232

Regions

Nucleotide binding

12 – 19

8

GTP By similarity

Nucleotide binding

60 – 64

5

GTP By similarity

Nucleotide binding

118 – 121

4

GTP By similarity

Motif

34 – 42

9

Effector region By similarity

Amino acid modifications

Modified residue

35

1

Phosphoserine Ref.10 Ref.11

Lipidation

193

1

S-geranylgeranyl cysteine By similarity

Lipidation

194

1

S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis

64

1

Q → L: No change in GTPase activity. Ref.2

Sequence conflict

189

1

A → S in AAC50773. Ref.1

Secondary structure

1

.

194

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q13636-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 19825648A9C214B9
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FASTA

194

21,569

        10         20         30         40         50         60 
MAIRELKVCL LGDTGVGKSS IVCRFVQDHF DHNISPTIGA SFMTKTVPCG NELHKFLIWD 

        70         80         90        100        110        120 
TAGQERFHSL APMYYRGSAA AVIVYDITKQ DSFYTLKKWV KELKEHGPEN IVMAIAGNKC 

       130        140        150        160        170        180 
DLSDIREVPL KDAKEYAESI GAIVVETSAK NAINIEELFQ GISRQIPPLD PHENGNNGTI 

       190 
KVEKPTMQAS RRCC

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of two novel rab genes from human melanocytes." Chen D., Guo J., Miki T., Tachibana M., Gahl W.A. Gene 174:129-134(1996) [PubMed: 8863739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Melanocyte.
[2]	"Molecular cloning, bacterial expression and properties of Rab31 and Rab32." Bao X., Faris A.E., Jang E.K., Haslam R.J. Eur. J. Biochem. 269:259-271(2002) [PubMed: 11784320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, MUTAGENESIS OF GLN-64. Tissue: Platelet.
[3]	"Small GTPase Rab22B is expressed in intestinal epithelial Caco-2 cells." Opdam F.J.M., van den Vorstenbosch R., Booltink E., Fransen J.A.M. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"A novel gene expressed in human pheochromocytoma." Peng Y., Gu Y., Tu Y., Xu S., Han Z., Fu G., Chen Z. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pheochromocytoma.
[5]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Puhl H.L. III, Ikeda S.R., Aronstam R.S. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]	"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: Lung.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"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-35, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

U57091 mRNA. Translation: AAC50773.1.
U59877 mRNA. Translation: AAB02832.1.
AF234995 mRNA. Translation: AAG13847.1.
AF183421 mRNA. Translation: AAG09690.1. Different initiation.
AF498957 mRNA. Translation: AAM21105.1.
AK314809 mRNA. Translation: BAG37334.1.
BT020027 mRNA. Translation: AAV38830.1.
BT020028 mRNA. Translation: AAV38831.1.
CR407659 mRNA. Translation: CAG28587.1.
BC001148 mRNA. Translation: AAH01148.1. Different initiation.

IPI

IPI00014376.

PIR

JC4961.

RefSeq

NP_006859.2.

UniGene

Hs.714730
Hs.99528

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FG5	X-ray	2.80	A	2-174	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13636. 1 interaction.

PTM databases

PhosphoSite

Q13636.

Proteomic databases

PRIDE

Q13636.

Genome annotation databases

Ensembl

ENSG00000168461. Homo sapiens. [Contig view]

GeneID

11031.

KEGG

hsa:11031.

Organism-specific databases

GeneCards

GC18P009701.

H-InvDB

HIX0014328.

HGNC

HGNC:9771. RAB31.

MIM

605694. gene.

PharmGKB

PA34122.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q13636.

Gene expression databases

ArrayExpress

Q13636.

Bgee

Q13636.

CleanEx

HS_RAB31.

GermOnline

ENSG00000168461. Homo sapiens.

Family and domain databases

InterPro

IPR003579. GTPase_Rab.
IPR015594. Rab22-like.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
[Graphical view]

PANTHER

PTHR11708:SF190. Rab22_like. 1 hit.

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 Resources

NextBio

41922.

SOURCE

Search...

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Entry information

Entry name

RAB31_HUMAN

Accession

Primary (citable) accession number: Q13636
Secondary accession number(s): B2RBT7, Q15770, Q9HC00

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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