Reviewed, UniProtKB/Swiss-Prot P62820 (RAB1A_HUMAN)

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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 CDC2 kinase during mitosis. Ref.8
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 Direct protein sequencing
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 Ref.1 Traceable author statement. 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 Ref.1 Traceable author statement. 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.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 205

204

Ras-related protein Rab-1A

PRO_0000121056

Regions

Nucleotide binding

18 – 25

8

GTP By similarity

Nucleotide binding

66 – 70

5

GTP By similarity

Nucleotide binding

124 – 127

4

GTP By similarity

Motif

40 – 48

9

Effector region By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.7

Modified residue

194

1

Phosphoserine; by CDC2 Probable

Lipidation

204

1

S-geranylgeranyl cysteine

Lipidation

205

1

S-geranylgeranyl cysteine

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 – 18

9

Helix

24 – 33

10

Beta strand

45 – 47

3

Beta strand

49 – 55

7

Beta strand

58 – 65

8

Beta strand

85 – 92

8

Helix

96 – 100

5

Helix

102 – 111

10

Beta strand

118 – 124

7

Turn

129 – 131

3

Helix

136 – 146

11

Beta strand

150 – 152

3

Turn

155 – 158

4

Helix

161 – 175

15

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: 2501306] [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: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Brain.
[3]	The German cDNA consortium Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases 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: 14702039] [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]	"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] (ISOFORM 1). Tissue: Placenta.
[7]	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.
[8]	"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: 1902553] [Abstract] Cited for: PHOSPHORYLATION BY CDC2.
[9]	"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: 7991565] [Abstract] Cited for: ISOPRENYLATION AT CYS-204 AND CYS-205, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
BC000905 mRNA. Translation: AAH00905.1.

IPI

IPI00005719.
IPI00185217.
IPI00334174.

PIR

TVHUYP. A34323.

RefSeq

NP_004152.1.
NP_056358.1.

UniGene

Hs.310645

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FOL	X-ray	2.63	A	6-176	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P62820. 15 interactions.

PTM databases

PhosphoSite

P62820.

2-D gel databases

PMMA-2DPAGE

P62820.

Proteomic databases

PRIDE

P62820.

Genome annotation databases

Ensembl

ENSG00000138069. Homo sapiens. [Contig view]

GeneID

5861.

KEGG

hsa:5861.

Organism-specific databases

GeneCards

GC02M065225.

H-InvDB

HIX0002108.

HGNC

HGNC:9758. RAB1A.

HPA

CAB005331.

MIM

179508. gene.

PharmGKB

PA34107.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P62820.

HOVERGEN

P62820.

Gene expression databases

ArrayExpress

P62820.

Bgee

P62820.

CleanEx

HS_RAB1A.

GermOnline

ENSG00000138069. Homo sapiens.

Family and domain databases

InterPro

IPR003579. GTPase_Rab.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
[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 Resources

NextBio

22762.

SOURCE

Search...

Entry information

Entry name

RAB1A_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 66 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)