Q9H0U4 (RAB1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-1B

Gene names

Name:

RAB1B

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	201 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein transport. Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Ref.7
Subunit structure	Interacts with MICAL1, MICAL2 and MICAL3. Interacts with GDI1; the interaction requires the GDP-bound state. Interacts with CHM/REP1; the interaction requires the GDP-bound form and is necessary for prenylation by GGTase II. Ref.6 Ref.7 Ref.8 Ref.9
Subcellular location	Membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm. Note: Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments. In the GDP-form, colocalizes with GDI in the cytoplasm By similarity. Ref.8
Post-translational modification	Prenylated; by GGTase II, only after interaction of the substrate with Rab escort protein 1 (REP1). AMPylation at Tyr-77 occurs in the switch 2 region and leads to moderate inactivation of the GTPase activity. It appears to prolong the lifetime of the GTP state of RAB1B by restricting access of GTPase effectors to switch 2 and blocking effector-stimulated GTP hydrolysis, thereby rendering RAB1B constitutively active.
Miscellaneous	Rab-1B binds GTP and GDP and possesses intrinsic GTPase activity By similarity.
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Methylation Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing 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 apparatus Inferred from direct assay. Source: LIFEdb 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 – 201

201

Ras-related protein Rab-1B

PRO_0000121061

Regions

Nucleotide binding

15 – 22

8

GTP By similarity

Nucleotide binding

63 – 67

5

GTP By similarity

Nucleotide binding

121 – 124

4

GTP By similarity

Region

64 – 83

20

Switch 2 region; required for interaction with REP1/CHM

Motif

37 – 45

9

Effector region By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.5 Ref.13

Modified residue

77

1

O-AMP-tyrosine; by Legionella DrrA

Modified residue

201

1

Cysteine methyl ester Potential

Lipidation

200

1

S-geranylgeranyl cysteine Ref.6 Ref.8

Lipidation

201

1

S-geranylgeranyl cysteine Ref.6 Ref.8

Experimental info

Mutagenesis

67

1

Q → L: No effect on GDI1 binding. Reduces, in vitro, but not, in vivo prenylation. No effect on interaction with REP1/CHM Much lower GDP/GTP ratio. Ref.6 Ref.7

Mutagenesis

73

1

I → N: Abolishes interaction with REP1/CHM. No prenylation. Much lower GDP/GTP ratio. Ref.7

Mutagenesis

77

1

Y → F: Abolishes AMPylation by Legionella DrrA. Ref.12

Mutagenesis

78

1

Y → D: Abolishes interaction with REP1/CHM and GDI1. No prenylation. Much lower GDP/GTP ratio. No membrane association. Ref.7 Ref.8

Mutagenesis

81

1

A → D: Abolishes interaction with REP1/CHM. No prenylation. Lowers GDP/GTP ratio by half. Ref.7

Mutagenesis

103

1

L → R: No effect on prenylation. Ref.7

Mutagenesis

110

1

A → D: No effect on prenylation. Ref.7

Mutagenesis

137

1

K → E: No effect on prenylation. Ref.7

Mutagenesis

144

1

G → N: No effect on prenylation. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

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201

Helix Strand Turn

Details...

Beta strand

6 – 14

9

Helix

22 – 30

9

Beta strand

44 – 51

8

Beta strand

56 – 63

8

Helix

68 – 70

3

Helix

71 – 75

5

Beta strand

85 – 87

3

Helix

93 – 97

5

Helix

99 – 109

11

Beta strand

117 – 119

3

Turn

126 – 128

3

Helix

133 – 142

10

Turn

152 – 154

3

Helix

158 – 171

14

Sequences

	Sequence		Length	Mass (Da)
	Q9H0U4 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 9812FF4DAC34B2BE	FASTA	201	22,171
	10 20 30 40 50 60 MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI ELDGKTIKLQ 70 80 90 100 110 120 IWDTAGQERF RTITSSYYRG AHGIIVVYDV TDQESYANVK QWLQEIDRYA SENVNKLLVG 130 140 150 160 170 180 NKSDLTTKKV VDNTTAKEFA DSLGIPFLET SAKNATNVEQ AFMTMAAEIK KRMGPGAASG 190 200 GERPNLKIDS TPVKPAGGGC C

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a novel human cDNA homology to rat ras-related rab1B cDNA." Zhao Y., Yu L., Xin Y.R., Zhang M., Chen S.Y., Zhao S.Y. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta and Synovium.
[4]	"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: Pancreas.
[5]	Bienvenut W.V. Submitted (JUN-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-21; 28-46; 59-69; 80-100 AND 138-170, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[6]	"Prenylation of a Rab1B mutant with altered GTPase activity is impaired in cell-free systems but not in intact mammalian cells." Wilson A.L., Sheridan K.M., Erdman R.A., Maltese W.A. Biochem. J. 318:1007-1014(1996) [PubMed: 8836150] [Abstract] Cited for: ISOPRENYLATION AT CYS-200 AND CYS-201, INTERACTION WITH GDI1, MUTAGENESIS OF GLN-67.
[7]	"The putative 'switch 2' domain of the Ras-related GTPase, Rab1B, plays an essential role in the interaction with Rab escort protein." Overmeyer J.H., Wilson A.L., Erdman R.A., Maltese W.A. Mol. Biol. Cell 9:223-235(1998) [PubMed: 9437002] [Abstract] Cited for: INTERACTION WITH CHM, FUNCTION, MUTAGENESIS OF GLN-67; ILE-73; TYR-78; ALA-81; LEU-103; ALA-110; LYS-137 AND GLY-144.
[8]	"Membrane targeting of a Rab GTPase that fails to associate with Rab escort protein (REP) or guanine nucleotide dissociation inhibitor (GDI)." Overmeyer J.H., Wilson A.L., Maltese W.A. J. Biol. Chem. 276:20379-20386(2001) [PubMed: 11389151] [Abstract] Cited for: SUBCELLULAR LOCATION, ISOPRENYLATION, INTERACTION WITH GDI1 AND CHM, MUTAGENESIS OF TYR-78.
[9]	"The MICAL proteins and rab1: a possible link to the cytoskeleton?" Fischer J., Weide T., Barnekow A. Biochem. Biophys. Res. Commun. 328:415-423(2005) [PubMed: 15694364] [Abstract] Cited for: INTERACTION WITH MICAL1; MICAL2 AND MICAL3.
[10]	"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].
[11]	"RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity." Schoebel S., Oesterlin L.K., Blankenfeldt W., Goody R.S., Itzen A. Mol. Cell 36:1060-1072(2009) [PubMed: 20064470] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 3-174 IN COMPLEX WITH L.PNEUMOPHILA DRRA GEF DOMAIN.
[12]	"The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b." Muller M.P., Peters H., Blumer J., Blankenfeldt W., Goody R.S., Itzen A. Science 329:946-949(2010) [PubMed: 20651120] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3-174 IN COMPLEX WITH L.PNEUMOPHILA DRRA, AMPYLATION AT TYR-77, MASS SPECTROMETRY, MUTAGENESIS OF TYR-77.
[13]	"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. Tissue: Embryonic kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF092437 mRNA. Translation: AAP97212.1.
AL136635 mRNA. Translation: CAB66570.1.
AK292086 mRNA. Translation: BAF84775.1.
AK315333 mRNA. Translation: BAG37733.1.
BC071169 mRNA. Translation: AAH71169.1.

IPI

IPI00008964.

RefSeq

NP_112243.1. NM_030981.2.

UniGene

Hs.300816.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3JZA	X-ray	1.80	A	3-174	[»]
3NKV	X-ray	1.70	A/B	3-174	[»]

ProteinModelPortal

Q9H0U4.

SMR

Q9H0U4. Positions 4-173.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H0U4. 3 interactions.

MINT

MINT-1343701.

STRING

Q9H0U4.

PTM databases

PhosphoSite

Q9H0U4.

Polymorphism databases

DMDM

23396834.

Proteomic databases

PeptideAtlas

Q9H0U4.

PRIDE

Q9H0U4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000311481; ENSP00000310226; ENSG00000174903.
ENST00000394080; ENSP00000377642; ENSG00000174903.

GeneID

81876.

KEGG

hsa:81876.

UCSC

uc001ohf.1. human.

Organism-specific databases

CTD

81876.

GeneCards

GC11P066036.

H-InvDB

HIX0009826.

HGNC

HGNC:18370. RAB1B.

HPA

CAB010225.

MIM

612565. gene.

neXtProt

NX_Q9H0U4.

PharmGKB

PA34108.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00550000074219.

HOGENOM

HBG745225.

HOVERGEN

HBG009351.

InParanoid

Q9H0U4.

OMA

VESYIST.

OrthoDB

EOG48D0WM.

PhylomeDB

Q9H0U4.

Gene expression databases

ArrayExpress

Q9H0U4.

Bgee

Q9H0U4.

CleanEx

HS_RAB1B.

Genevestigator

Q9H0U4.

GermOnline

ENSG00000174903. Homo sapiens.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]

KO

K07875.

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

72222.

SOURCE

Search...

Entry information

Entry name

RAB1B_HUMAN

Accession

Primary (citable) accession number: Q9H0U4
Secondary accession number(s): A8K7S1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 106 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.