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P61019

- RAB2A_HUMAN

UniProt

P61019 - RAB2A_HUMAN

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Protein
Ras-related protein Rab-2A
Gene
RAB2A, RAB2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Required for protein transport from the endoplasmic reticulum to the Golgi complex.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 219GTP
Nucleotide bindingi61 – 655GTP By similarity
Nucleotide bindingi119 – 1224GTP
Nucleotide bindingi149 – 1513GTP

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTP binding Source: UniProtKB
  3. GTPase activity Source: UniProtKB

GO - Biological processi

  1. ER to Golgi vesicle-mediated transport Source: ProtInc
  2. GTP catabolic process Source: GOC
  3. mitotic cell cycle Source: Reactome
  4. protein transport Source: UniProtKB-KW
  5. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-2A
Gene namesi
Name:RAB2A
Synonyms:RAB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:9763. RAB2A.

Subcellular locationi

Endoplasmic reticulum-Golgi intermediate compartment membrane; Lipid-anchor. Melanosome. Endoplasmic reticulum membrane; Lipid-anchor Reviewed prediction. Golgi apparatus membrane; Lipid-anchor Reviewed prediction
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.1 Publication

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProt
  5. lysosomal membrane Source: UniProtKB
  6. melanosome Source: UniProtKB-SubCell
  7. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162400618.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 212211Ras-related protein Rab-2A
PRO_0000121066Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Lipidationi211 – 2111S-geranylgeranyl cysteine1 Publication
Lipidationi212 – 2121S-geranylgeranyl cysteine1 Publication

Keywords - PTMi

Acetylation, Lipoprotein, Prenylation

Proteomic databases

MaxQBiP61019.
PaxDbiP61019.
PRIDEiP61019.

PTM databases

PhosphoSiteiP61019.

Expressioni

Gene expression databases

ArrayExpressiP61019.
BgeeiP61019.
CleanExiHS_RAB2A.
GenevestigatoriP61019.

Organism-specific databases

HPAiCAB018781.

Interactioni

Subunit structurei

Interacts with PRKCI.1 Publication

Protein-protein interaction databases

BioGridi111800. 22 interactions.
DIPiDIP-316N.
IntActiP61019. 14 interactions.
MINTiMINT-5001132.
STRINGi9606.ENSP00000262646.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1411
Helixi19 – 2810
Beta strandi43 – 508
Beta strandi53 – 619
Turni66 – 694
Helixi73 – 764
Beta strandi79 – 879
Helixi91 – 955
Helixi97 – 10711
Beta strandi113 – 1197
Helixi124 – 1263
Helixi131 – 14111
Beta strandi144 – 1485
Turni150 – 1523
Helixi156 – 16914

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z0AX-ray2.12A/B/C/D2-170[»]
ProteinModelPortaliP61019.
SMRiP61019. Positions 2-170.

Miscellaneous databases

EvolutionaryTraceiP61019.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 1918Required for interaction with PRKCI
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi35 – 439Effector region By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
KOiK07877.
OMAiHPTTNST.
OrthoDBiEOG7QK0CV.
PhylomeDBiP61019.
TreeFamiTF300032.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P61019-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMITI    50
DGKQIKLQIW DTAGQESFRS ITRSYYRGAA GALLVYDITR RDTFNHLTTW 100
LEDARQHSNS NMVIMLIGNK SDLESRREVK KEEGEAFARE HGLIFMETSA 150
KTASNVEEAF INTAKEIYEK IQEGVFDINN EANGIKIGPQ HAATNATHAG 200
NQGGQQAGGG CC 212
Length:212
Mass (Da):23,546
Last modified:April 26, 2004 - v1
Checksum:iF8731E3F8FB399A3
GO
Isoform 2 (identifier: P61019-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     16-39: Missing.

Note: No experimental confirmation available.

Show »
Length:188
Mass (Da):20,847
Checksum:i5B13DD3486CC230F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei16 – 3924Missing in isoform 2.
VSP_042917Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti144 – 1441I → M in AAA60241. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12953 mRNA. Translation: CAA31411.1.
M28213 mRNA. Translation: AAA60241.1.
AF498930 mRNA. Translation: AAM21078.1.
BT019695 mRNA. Translation: AAV38501.1.
AK297576 mRNA. Translation: BAG59967.1.
AK312344 mRNA. Translation: BAG35265.1.
AC068389 Genomic DNA. No translation available.
AC079065 Genomic DNA. No translation available.
CH471068 Genomic DNA. Translation: EAW86827.1.
BC008929 mRNA. Translation: AAH08929.1.
CCDSiCCDS56537.1. [P61019-2]
CCDS6175.1. [P61019-1]
PIRiB34323.
RefSeqiNP_001229573.1. NM_001242644.1. [P61019-2]
NP_002856.1. NM_002865.2. [P61019-1]
UniGeneiHs.369017.

Genome annotation databases

EnsembliENST00000262646; ENSP00000262646; ENSG00000104388. [P61019-1]
ENST00000531289; ENSP00000431846; ENSG00000104388. [P61019-2]
GeneIDi5862.
KEGGihsa:5862.
UCSCiuc003xud.2. human. [P61019-1]
uc011lef.2. human. [P61019-2]

Polymorphism databases

DMDMi46577636.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12953 mRNA. Translation: CAA31411.1 .
M28213 mRNA. Translation: AAA60241.1 .
AF498930 mRNA. Translation: AAM21078.1 .
BT019695 mRNA. Translation: AAV38501.1 .
AK297576 mRNA. Translation: BAG59967.1 .
AK312344 mRNA. Translation: BAG35265.1 .
AC068389 Genomic DNA. No translation available.
AC079065 Genomic DNA. No translation available.
CH471068 Genomic DNA. Translation: EAW86827.1 .
BC008929 mRNA. Translation: AAH08929.1 .
CCDSi CCDS56537.1. [P61019-2 ]
CCDS6175.1. [P61019-1 ]
PIRi B34323.
RefSeqi NP_001229573.1. NM_001242644.1. [P61019-2 ]
NP_002856.1. NM_002865.2. [P61019-1 ]
UniGenei Hs.369017.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Z0A X-ray 2.12 A/B/C/D 2-170 [» ]
ProteinModelPortali P61019.
SMRi P61019. Positions 2-170.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111800. 22 interactions.
DIPi DIP-316N.
IntActi P61019. 14 interactions.
MINTi MINT-5001132.
STRINGi 9606.ENSP00000262646.

Chemistry

BindingDBi P61019.

PTM databases

PhosphoSitei P61019.

Polymorphism databases

DMDMi 46577636.

Proteomic databases

MaxQBi P61019.
PaxDbi P61019.
PRIDEi P61019.

Protocols and materials databases

DNASUi 5862.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262646 ; ENSP00000262646 ; ENSG00000104388 . [P61019-1 ]
ENST00000531289 ; ENSP00000431846 ; ENSG00000104388 . [P61019-2 ]
GeneIDi 5862.
KEGGi hsa:5862.
UCSCi uc003xud.2. human. [P61019-1 ]
uc011lef.2. human. [P61019-2 ]

Organism-specific databases

CTDi 5862.
GeneCardsi GC08P061429.
HGNCi HGNC:9763. RAB2A.
HPAi CAB018781.
MIMi 179509. gene.
neXtProti NX_P61019.
PharmGKBi PA162400618.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
KOi K07877.
OMAi HPTTNST.
OrthoDBi EOG7QK0CV.
PhylomeDBi P61019.
TreeFami TF300032.

Enzyme and pathway databases

Reactomei REACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.

Miscellaneous databases

ChiTaRSi RAB2A. human.
EvolutionaryTracei P61019.
GeneWikii RAB2A.
GenomeRNAii 5862.
NextBioi 22766.
PROi P61019.
SOURCEi Search...

Gene expression databases

ArrayExpressi P61019.
Bgeei P61019.
CleanExi HS_RAB2A.
Genevestigatori P61019.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00175. RAB. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51419. RAB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORM 1).
    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] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain and Brain cortex.
  6. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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: Skin.
  9. Cited for: ISOPRENYLATION AT CYS-211 AND CYS-212.
  10. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKCI.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  12. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 2-170 IN COMPLEX WITH GDP.

Entry informationi

Entry nameiRAB2A_HUMAN
AccessioniPrimary (citable) accession number: P61019
Secondary accession number(s): B2R5W8, B4DMQ5, P08886
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: September 3, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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