P62820 (RAB1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-1A

Alternative name(s):
YPT1-related protein

Gene names

Name:	RAB1A
Synonyms:	RAB1

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	205 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably required for transit of protein from the ER through Golgi compartment. Binds GTP and GDP and possesses intrinsic GTPase activity.
Subunit structure	May interact with YIPF5 By similarity.
Subcellular location	Golgi apparatus. Endoplasmic reticulum.
Post-translational modification	Phosphorylated by CDK1 kinase during mitosis. Ref.10 Ref.14 Ref.15 Phosphocholinated at Ser-79 by L.pneumophila AnkX, leading to displace GDP dissociation inhibitors (GDI). Both GDP-bound and GTP-bound forms can be phosphocholinated. Dephosphocholinated by L.pneumophila Lem3, restoring accessibility to L.pneumophila GTPase effector LepB.
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Endoplasmic reticulum Golgi apparatus
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Phosphoprotein 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 vesicle-mediated transport Traceable author statement Ref.1. Source: ProtInc
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P62820-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P62820-2)

The sequence of this isoform differs from the canonical sequence as follows:
     33-96: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: P62820-3)

The sequence of this isoform differs from the canonical sequence as follows:
     65-140: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

Chain

2 – 205

204

Ras-related protein Rab-1A

PRO_0000121056

Regions

Nucleotide binding

18 – 26

9

GTP

Nucleotide binding

66 – 70

5

GTP By similarity

Nucleotide binding

124 – 127

4

GTP

Nucleotide binding

154 – 156

3

GTP

Motif

40 – 48

9

Effector region By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.9

Modified residue

79

1

O-(2-cholinephosphoryl)serine; by Legionella AnkX

Modified residue

194

1

Phosphoserine; by CDK1 Probable

Lipidation

204

1

S-geranylgeranyl cysteine Ref.11

Lipidation

205

1

S-geranylgeranyl cysteine Ref.11

Natural variations

Alternative sequence

33 – 96

64

Missing in isoform 2.

VSP_005525

Alternative sequence

65 – 140

76

Missing in isoform 3.

VSP_005526

Secondary structure

1

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205

Helix Strand Turn

Details...

Beta strand

10 – 17

8

Helix

24 – 28

5

Beta strand

30 – 32

3

Helix

39 – 44

6

Beta strand

47 – 55

9

Beta strand

58 – 65

8

Helix

70 – 72

3

Helix

78 – 80

3

Turn

81 – 83

3

Beta strand

85 – 92

8

Helix

96 – 112

17

Beta strand

117 – 125

9

Helix

129 – 131

3

Helix

136 – 145

10

Beta strand

150 – 154

5

Turn

155 – 157

3

Helix

159 – 175

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: B2A8F4E3B0FB17D6	FASTA	205	22,678
	10 20 30 40 50 60 MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI RTIELDGKTI 70 80 90 100 110 120 KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQESFN NVKQWLQEID RYASENVNKL 130 140 150 160 170 180 LVGNKCDLTT KKVVDYTTAK EFADSLGIPF LETSAKNATN VEQSFMTMAA EIKKRMGPGA 190 200 TAGGAEKSNV KIQSTPVKQS GGGCC
	Isoform 2 [UniParc] [UniParc]. Checksum: 620F588CA34B3A77	FASTA	141	15,331
	10 20 30 40 50 60 MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FAESFNNVKQ WLQEIDRYAS ENVNKLLVGN 70 80 90 100 110 120 KCDLTTKKVV DYTTAKEFAD SLGIPFLETS AKNATNVEQS FMTMAAEIKK RMGPGATAGG 130 140 AEKSNVKIQS TPVKQSGGGC C
	Isoform 3 [UniParc] [UniParc]. Checksum: 8325012BF5161AFE	FASTA	129	13,903
	10 20 30 40 50 60 MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI RTIELDGKTI 70 80 90 100 110 120 KLQIEFADSL GIPFLETSAK NATNVEQSFM TMAAEIKKRM GPGATAGGAE KSNVKIQSTP VKQSGGGCC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion." Zahraoui A., Touchot N., Chardin P., Tavitian A. J. Biol. Chem. 264:12394-12401(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Brain.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Colon.
[4]	"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] (ISOFORM 2).
[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] (ISOFORM 1). Tissue: Brain.
[6]	"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 (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[7]	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].
[8]	"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] (ISOFORM 1). Tissue: Placenta.
[9]	Bienvenut W.V., Claeys D. Submitted (NOV-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-30; 52-58; 62-72; 75-111; 176-187 AND 192-198, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Platelet.
[10]	"Phosphorylation of two small GTP-binding proteins of the Rab family by p34cdc2." Bailly E., McCaffrey M., Touchot N., Zahraoui A., Goud B., Bornens M. Nature 350:715-718(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY CDK1.
[11]	"Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A." Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A. Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994) [PubMed] [Europe PMC] [Abstract] Cited for: ISOPRENYLATION AT CYS-204 AND CYS-205, MASS SPECTROMETRY.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[13]	"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].
[14]	"Modulation of Rab GTPase function by a protein phosphocholine transferase." Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R. Nature 477:103-106(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH L.PNEUMOPHILA ANKX, CHOLINEPHOSPHORYLATION AT SER-79.
[15]	"Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination." Tan Y., Arnold R.J., Luo Z.Q. Proc. Natl. Acad. Sci. U.S.A. 108:21212-21217(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH L.PNEUMOPHILA LEM3, DECHOLINEPHOSPHORYLATION AT SER-79.
[16]	"Crystal structure of human RAB1A in complex with GDP." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 6-177 IN COMPLEX WITH GDP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M28209 mRNA. Translation: AAA60240.1.
AL050268 mRNA. Translation: CAB43369.1.
BX571747 mRNA. Translation: CAE11872.1.
AK055927 mRNA. Translation: BAB71048.1.
AF498929 mRNA. Translation: AAM21077.1.
CR533479 mRNA. Translation: CAG38510.1.
CH471053 Genomic DNA. Translation: EAW99921.1.
BC000905 mRNA. Translation: AAH00905.1.

IPI

IPI00005719.
IPI00185217.
IPI00334174.

PIR

TVHUYP. A34323.

RefSeq

NP_004152.1. NM_004161.4.
NP_056358.1. NM_015543.1.

UniGene

Hs.310645.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FOL	X-ray	2.63	A	6-176	[»]
2WWX	X-ray	1.50	A	4-178	[»]
3L0I	X-ray	2.85	B/D	1-177	[»]
3SFV	X-ray	1.73	A	1-176	[»]
3TKL	X-ray	2.18	A	1-191	[»]
4FMB	X-ray	3.20	B/D/F	6-176	[»]
4FMC	X-ray	2.80	B/D	6-176	[»]
			F	14-130	[»]
4FMD	X-ray	3.05	B/D	6-176	[»]
			F	13-176	[»]
4FME	X-ray	4.10	B/E	6-176	[»]

ProteinModelPortal

P62820.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1063N.

IntAct

P62820. 24 interactions.

MINT

MINT-1343792.

STRING

9606.ENSP00000387286.

PTM databases

PhosphoSite

P62820.

Polymorphism databases

DMDM

51338603.

Proteomic databases

PaxDb

P62820.

PRIDE

P62820.

Protocols and materials databases

DNASU

5861.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000398529; ENSP00000381540; ENSG00000138069.
ENST00000409784; ENSP00000387286; ENSG00000138069.
ENST00000409892; ENSP00000386451; ENSG00000138069.

GeneID

5861.

KEGG

hsa:5861.

UCSC

uc002sdm.3. human.
uc002sdn.3. human.
uc002sdo.3. human.

Organism-specific databases

CTD

5861.

GeneCards

GC02M065297.

HGNC

HGNC:9758. RAB1A.

HPA

CAB005331.

MIM

179508. gene.

neXtProt

NX_P62820.

PharmGKB

PA34107.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233968.

HOVERGEN

HBG009351.

KO

K07874.

OMA

NRVGPPS.

OrthoDB

EOG48D0WM.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpress

P62820.

Bgee

P62820.

CleanEx

HS_RAB1A.

Genevestigator

P62820.

GermOnline

ENSG00000138069. Homo sapiens.

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

RAB1A. human.

EvolutionaryTrace

P62820.

GenomeRNAi

5861.

NextBio

22762.

SOURCE

Search...

Entry information

Entry name

RAB1A_HUMAN

Accession

Primary (citable) accession number: P62820
Secondary accession number(s): P11476 , Q6FIE7, Q96N61, Q9Y3T2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 105 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.