Q13636 (RAB31_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-31

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

Gene names

Name:	RAB31
Synonyms:	RAB22B

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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	194 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. Required for the integrity and for normal function of the Golgi apparatus and the trans-Golgi network. Plays a role in insulin-stimulated translocation of GLUT4 to the cell membrane. Plays a role in M6PR transport from the trans-Golgi network to endosomes. Plays a role in the internalization of EGFR from the cell membrane into endosomes. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Ref.12 Ref.13 Ref.15 Ref.17 Ref.18
Subunit structure	Interacts with OCRL. Interacts with NGFR By similarity. Interacts (in GDP-bound form) with RIN3 and GAPVD1, which function as guanine exchange factors (GEF). Interacts (in GTP-bound form) with EEA1. Interacts with EGFR. Ref.13 Ref.15 Ref.17
Subcellular location	Golgi apparatus › trans-Golgi network. Golgi apparatus › trans-Golgi network membrane; Lipid-anchor; Cytoplasmic side Probable. Early endosome. Cytoplasmic vesicle › phagosome. Cytoplasmic vesicle › phagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Rapidly recruited to phagosomes containing S.aureus or M.tuberculosis. Ref.12 Ref.13 Ref.15 Ref.17 Ref.18
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.
Sequence caution	The sequence AAG09690.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAH01148.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Endosome 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	Golgi to plasma membrane protein transport Inferred from mutant phenotype Ref.12. Source: UniProtKB cellular response to insulin stimulus Inferred from mutant phenotype Ref.13. Source: UniProtKB phagosome maturation Inferred from mutant phenotype Ref.18. Source: UniProtKB receptor internalization Inferred from mutant phenotype Ref.15. Source: UniProtKB regulated secretory pathway Inferred from mutant phenotype Ref.13. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell early endosome Inferred from direct assay Ref.13. Source: UniProtKB phagocytic vesicle Inferred from direct assay Ref.18. Source: UniProtKB phagocytic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell trans-Golgi network membrane Inferred from direct assay Ref.12. Source: UniProtKB
Molecular_function	GDP binding Inferred from direct assay Ref.13. Source: UniProtKB GTP binding Inferred from direct assay Ref.13. Source: UniProtKB GTPase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

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

Nucleotide binding

60 – 64

5

GTP

Nucleotide binding

118 – 121

4

GTP

Motif

34 – 42

9

Effector region By similarity

Amino acid modifications

Modified residue

35

1

Phosphoserine Ref.14

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

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194

Helix Strand Turn

Details...

Beta strand

4 – 12

9

Helix

18 – 27

10

Beta strand

38 – 48

11

Beta strand

50 – 61

12

Helix

65 – 71

7

Helix

72 – 75

4

Beta strand

79 – 86

8

Helix

91 – 106

16

Beta strand

112 – 118

7

Helix

120 – 125

6

Helix

130 – 138

9

Turn

139 – 141

3

Beta strand

143 – 146

4

Turn

149 – 152

4

Helix

155 – 164

10

Sequences

	Sequence		Length	Mass (Da)
	Q13636 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 19825648A9C214B9	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

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] [Europe PMC] [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] [Europe PMC] [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. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [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]	"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].
[10]	"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: Lung.
[11]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"Rab22B's role in trans-Golgi network membrane dynamics." Ng E.L., Wang Y., Tang B.L. Biochem. Biophys. Res. Commun. 361:751-757(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]	"Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates Glut4 trafficking in adipocytes." Lodhi I.J., Chiang S.-H., Chang L., Vollenweider D., Watson R.T., Inoue M., Pessin J.E., Saltiel A.R. Cell Metab. 5:59-72(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH GAPVD1 AND EEA1, SUBCELLULAR LOCATION.
[14]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Rab22B is expressed in the CNS astroglia lineage and plays a role in epidermal growth factor receptor trafficking in A431 cells." Ng E.L., Ng J.J., Liang F., Tang B.L. J. Cell. Physiol. 221:716-728(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EGFR AND EEA1.
[16]	"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].
[17]	"Characterization of RIN3 as a guanine nucleotide exchange factor for the Rab5 subfamily GTPase Rab31." Kajiho H., Sakurai K., Minoda T., Yoshikawa M., Nakagawa S., Fukushima S., Kontani K., Katada T. J. Biol. Chem. 286:24364-24373(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RIN3.
[18]	"Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes." Seto S., Tsujimura K., Koide Y. Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[19]	"Crystal structure of human RAB31 in complex with a GTP analogue." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-174 IN COMPLEX WITH GTP ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
AC006238 Genomic DNA. No translation available.
AP000902 Genomic DNA. No translation available.
BC001148 mRNA. Translation: AAH01148.1. Different initiation.

PIR

JC4961.

RefSeq

NP_006859.2. NM_006868.3.

UniGene

Hs.744887.
Hs.99528.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q13636.

SMR

Q13636. Positions 3-167.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

116221. 18 interactions.

IntAct

Q13636. 3 interactions.

MINT

MINT-1404598.

STRING

9606.ENSP00000304565.

PTM databases

PhosphoSite

Q13636.

Polymorphism databases

DMDM

2500069.

Proteomic databases

PaxDb

Q13636.

PRIDE

Q13636.

Protocols and materials databases

DNASU

11031.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000578921; ENSP00000461945; ENSG00000168461.

GeneID

11031.

KEGG

hsa:11031.

UCSC

uc002kog.2. human.

Organism-specific databases

CTD

11031.

GeneCards

GC18P009701.

HGNC

HGNC:9771. RAB31.

HPA

HPA019717.

MIM

605694. gene.

neXtProt

NX_Q13636.

PharmGKB

PA34122.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOVERGEN

HBG009351.

InParanoid

Q13636.

KO

K07891.

OMA

KQIPPLE.

OrthoDB

EOG77DJ7M.

PhylomeDB

Q13636.

TreeFam

TF331262.

Gene expression databases

ArrayExpress

Q13636.

Bgee

Q13636.

CleanEx

HS_RAB31.

Genevestigator

Q13636.

Family and domain databases

InterPro

IPR027417. P-loop_NTPase.
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]

SUPFAM

SSF52540. SSF52540. 1 hit.

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51419. RAB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RAB31. human.

EvolutionaryTrace

Q13636.

GeneWiki

RAB31.

GenomeRNAi

11031.

NextBio

41922.

PRO

Q13636.

SOURCE

Search...

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:	February 19, 2014
This is version 131 of the entry and version 1 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.