P61019 (RAB2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-2A

Gene names

Name:	RAB2A
Synonyms:	RAB2

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	212 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	Required for protein transport from the endoplasmic reticulum to the Golgi complex.
Subunit structure	Interacts with PRKCI. Ref.9
Subcellular location	Endoplasmic reticulum-Golgi intermediate compartment membrane; Lipid-anchor. Melanosome. Endoplasmic reticulum membrane; Lipid-anchor Potential. Golgi apparatus membrane; Lipid-anchor Potential. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.10
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 Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ER to Golgi vesicle-mediated transport Traceable author statement. Source: ProtInc protein transport Inferred from electronic annotation. Source: UniProtKB-KW small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum-Golgi intermediate compartment membrane Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GDP binding Inferred from direct assay Ref.13. Source: UniProtKB GTP binding Inferred from direct assay Ref.13. Source: UniProtKB GTPase activity Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 212

211

Ras-related protein Rab-2A

PRO_0000121066

Regions

Nucleotide binding

13 – 21

9

GTP

Nucleotide binding

61 – 65

5

GTP By similarity

Nucleotide binding

119 – 122

4

GTP

Nucleotide binding

149 – 151

3

GTP

Region

2 – 19

18

Required for interaction with PRKCI

Motif

35 – 43

9

Effector region By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.11

Lipidation

211

1

S-geranylgeranyl cysteine Ref.8

Lipidation

212

1

S-geranylgeranyl cysteine Ref.8

Experimental info

Sequence conflict

144

1

I → M in AAA60241. Ref.2

Secondary structure

1

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212

Helix Strand Turn

Details...

Beta strand

4 – 14

11

Helix

19 – 28

10

Beta strand

43 – 50

8

Beta strand

53 – 61

9

Turn

66 – 69

4

Helix

73 – 76

4

Beta strand

79 – 87

9

Helix

91 – 95

5

Helix

97 – 107

11

Beta strand

113 – 119

7

Helix

124 – 126

3

Helix

131 – 141

11

Beta strand

144 – 148

5

Turn

150 – 152

3

Helix

156 – 169

14

Sequences

	Sequence		Length	Mass (Da)
	P61019 [UniParc]. Last modified April 26, 2004. Version 1. Checksum: F8731E3F8FB399A3	FASTA	212	23,546
	10 20 30 40 50 60 MAYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMITI DGKQIKLQIW 70 80 90 100 110 120 DTAGQESFRS ITRSYYRGAA GALLVYDITR RDTFNHLTTW LEDARQHSNS NMVIMLIGNK 130 140 150 160 170 180 SDLESRREVK KEEGEAFARE HGLIFMETSA KTASNVEEAF INTAKEIYEK IQEGVFDINN 190 200 210 EANGIKIGPQ HAATNATHAG NQGGQQAGGG CC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a new YPT1-related human cDNA which belongs to the ras gene superfamily." Tachibana K., Umezawa A., Kato S., Takano T. Nucleic Acids Res. 16:10368-10368(1988) [PubMed: 3057444] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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].
[3]	"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.
[4]	"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 (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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: Brain cortex.
[6]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: Skin.
[8]	"Isoprenoid modification of rab proteins terminating in CC or CXC motifs." Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R., Sinensky M., Balch W.E., Buss J.E., Der C.J. Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991) [PubMed: 1648736] [Abstract] Cited for: ISOPRENYLATION AT CYS-211 AND CYS-212.
[9]	"Rab2 interacts directly with atypical protein kinase C (aPKC) iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-phosphate dehydrogenase phosphorylation." Tisdale E.J. J. Biol. Chem. 278:52524-52530(2003) [PubMed: 14570876] [Abstract] Cited for: INTERACTION WITH PRKCI.
[10]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[11]	"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 ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"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].
[13]	"Structural basis of family-wide Rab GTPase recognition by rabenosyn-5." Eathiraj S., Pan X., Ritacco C., Lambright D.G. Nature 436:415-419(2005) [PubMed: 16034420] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 2-170 IN COMPLEX WITH GDP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X12953 mRNA. Translation: CAA31411.1.
M28213 mRNA. Translation: AAA60241.1.
AF498930 mRNA. Translation: AAM21078.1.
BT019695 mRNA. Translation: AAV38501.1.
AK312344 mRNA. Translation: BAG35265.1.
CH471068 Genomic DNA. Translation: EAW86827.1.
BC008929 mRNA. Translation: AAH08929.1.

IPI

IPI00031169.

PIR

B34323.

RefSeq

NP_002856.1. NM_002865.2.

UniGene

Hs.369017.
Hs.670775.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z0A	X-ray	2.12	A/B/C/D	2-170	[»]

ProteinModelPortal

P61019.

SMR

P61019. Positions 2-170.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-316N.

IntAct

P61019. 8 interactions.

MINT

MINT-5001132.

STRING

P61019.

PTM databases

PhosphoSite

P61019.

Polymorphism databases

DMDM

46577636.

Proteomic databases

PRIDE

P61019.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262646; ENSP00000262646; ENSG00000104388.

GeneID

5862.

KEGG

hsa:5862.

UCSC

uc003xud.1. human.

Organism-specific databases

CTD

5862.

GeneCards

GC08P061429.

H-InvDB

HIX0007531.

HGNC

HGNC:9763. RAB2A.

HPA

CAB018781.

MIM

179509. gene.

neXtProt

NX_P61019.

PharmGKB

PA162400618.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00600000084220.

HOVERGEN

HBG009351.

OrthoDB

EOG41G354.

PhylomeDB

P61019.

Gene expression databases

ArrayExpress

P61019.

Bgee

P61019.

CleanEx

HS_RAB2A.

Genevestigator

P61019.

GermOnline

ENSG00000104388. Homo sapiens.

Family and domain databases

InterPro

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

KO

K07877.

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

22766.

SOURCE

Search...

Entry information

Entry name

RAB2A_HUMAN

Accession

Primary (citable) accession number: P61019
Secondary accession number(s): B2R5W8, P08886

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	April 26, 2004
Last modified:	January 25, 2012
This is version 87 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.