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P62834

- RAP1A_HUMAN

UniProt

P62834 - RAP1A_HUMAN

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Protein

Ras-related protein Rap-1A

Gene

RAP1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes. Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions.2 Publications

Enzyme regulationi

Activated by guanine nucleotide-exchange factors (GEF) EPAC and EPAC2 in a cAMP-dependent manner, and GFR.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178GTPBy similarity
Nucleotide bindingi57 – 615GTPBy similarity
Nucleotide bindingi116 – 1194GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: ProtInc
  2. GTP binding Source: UniProtKB-KW
  3. protein complex binding Source: UniProtKB
  4. protein transporter activity Source: UniProtKB
  5. Rap guanyl-nucleotide exchange factor activity Source: UniProtKB

GO - Biological processi

  1. activation of MAPKK activity Source: Reactome
  2. blood coagulation Source: Reactome
  3. cellular response to cAMP Source: UniProtKB
  4. cellular response to nerve growth factor stimulus Source: UniProtKB
  5. energy reserve metabolic process Source: Reactome
  6. establishment of endothelial barrier Source: UniProtKB
  7. negative regulation of synaptic vesicle exocytosis Source: Ensembl
  8. nerve growth factor signaling pathway Source: UniProtKB
  9. neurotrophin TRK receptor signaling pathway Source: Reactome
  10. platelet activation Source: Reactome
  11. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  12. positive regulation of neuron projection development Source: UniProtKB
  13. positive regulation of protein kinase activity Source: UniProtKB
  14. positive regulation of Rap GTPase activity Source: UniProtKB
  15. positive regulation of vasculogenesis Source: UniProtKB
  16. protein transport Source: UniProtKB
  17. Rap protein signal transduction Source: UniProtKB
  18. regulation of cell junction assembly Source: UniProtKB
  19. regulation of insulin secretion Source: Reactome
  20. signal transduction Source: ProtInc
  21. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Neurogenesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_12002. ARMS-mediated activation.
REACT_12076. Frs2-mediated activation.
REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_23898. Rap1 signalling.
SignaLinkiP62834.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rap-1A
Alternative name(s):
C21KG
G-22K
GTP-binding protein smg p21A
Ras-related protein Krev-1
Gene namesi
Name:RAP1A
Synonyms:KREV1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9855. RAP1A.

Subcellular locationi

Cell membrane 1 Publication; Lipid-anchor 1 Publication. Cytoplasm 1 Publication. Cytoplasmperinuclear region 1 Publication. Cell junction By similarity. Early endosome By similarity
Note: Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. Localized with RAPGEF2 at cell-cell junctions (By similarity). Colocalized with RAPGEF2 in the perinuclear region.By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. early endosome Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProt
  6. guanyl-nucleotide exchange factor complex Source: Ensembl
  7. late endosome Source: UniProtKB
  8. neuron projection Source: Ensembl
  9. perinuclear region of cytoplasm Source: UniProtKB
  10. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA34217.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 181181Ras-related protein Rap-1APRO_0000030199Add
BLAST
Propeptidei182 – 1843Removed in mature formPRO_0000030200

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei181 – 1811Cysteine methyl ester1 Publication
Lipidationi181 – 1811S-geranylgeranyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP62834.
PaxDbiP62834.
PRIDEiP62834.

2D gel databases

OGPiP62834.

PTM databases

PhosphoSiteiP62834.

Expressioni

Gene expression databases

BgeeiP62834.
CleanExiHS_RAP1A.
ExpressionAtlasiP62834. baseline and differential.
GenevestigatoriP62834.

Organism-specific databases

HPAiCAB018335.

Interactioni

Subunit structurei

Found in a complex, at least composed of ITGB1BP1, KRIT1 and RAP1A. Interacts (active GTP-bound form preferentially) with KRIT1 (via C-terminus FERM domain); the interaction does not induce the opening conformation of KRIT1. In its GTP-bound form interacts with PLCE1 and RADIL. Interacts with SGSM1, SGSM2 and SGSM3. Interacts (via GTP-bound active form) with RAPGEF2 (via Ras-associating domain).7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAF1P040492EBI-491414,EBI-365996
RASSF5Q8WWW0-23EBI-491414,EBI-960502
Rassf5Q5EBH12EBI-491414,EBI-960530From a different organism.

Protein-protein interaction databases

BioGridi111841. 43 interactions.
DIPiDIP-29106N.
IntActiP62834. 11 interactions.
MINTiMINT-1509313.
STRINGi9606.ENSP00000348786.

Structurei

Secondary structure

1
184
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Helixi16 – 2510Combined sources
Beta strandi36 – 4611Combined sources
Beta strandi49 – 5810Combined sources
Helixi66 – 749Combined sources
Beta strandi76 – 838Combined sources
Helixi87 – 915Combined sources
Helixi93 – 10412Combined sources
Beta strandi111 – 1166Combined sources
Helixi121 – 1233Combined sources
Helixi128 – 13710Combined sources
Turni138 – 1403Combined sources
Beta strandi142 – 1454Combined sources
Turni148 – 1503Combined sources
Helixi154 – 16613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C1YX-ray1.90A1-167[»]
1GUAX-ray2.00A1-167[»]
3KUCX-ray1.92A1-167[»]
4KVGX-ray1.65A/C1-167[»]
ProteinModelPortaliP62834.
SMRiP62834. Positions 1-167.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62834.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi32 – 409Effector regionCurated

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00770000120468.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP62834.
KOiK04353.
OMAiKPKKSLC.
OrthoDBiEOG7QVM41.
PhylomeDBiP62834.
TreeFamiTF313014.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62834-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDCQQ
60 70 80 90 100
CMLEILDTAG TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI
110 120 130 140 150
LRVKDTEDVP MILVGNKCDL EDERVVGKEQ GQNLARQWCN CAFLESSAKS
160 170 180
KINVNEIFYD LVRQINRKTP VEKKKPKKKS CLLL
Length:184
Mass (Da):20,987
Last modified:August 16, 2004 - v1
Checksum:i42C39290C98E0A92
GO

Sequence cautioni

The sequence CAB55685.2 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12533 mRNA. Translation: CAA31051.1.
M22995 mRNA. Translation: AAA36150.1.
AF493912 mRNA. Translation: AAM12626.1.
AL049557 Genomic DNA. Translation: CAB55685.2. Sequence problems.
BC014086 mRNA. Translation: AAH14086.1.
CCDSiCCDS840.1.
PIRiA32342.
RefSeqiNP_001010935.1. NM_001010935.2.
NP_001278825.1. NM_001291896.1.
NP_002875.1. NM_002884.3.
UniGeneiHs.190334.
Hs.586618.

Genome annotation databases

EnsembliENST00000356415; ENSP00000348786; ENSG00000116473.
ENST00000369709; ENSP00000358723; ENSG00000116473.
GeneIDi5906.
KEGGihsa:5906.
UCSCiuc001ebi.3. human.

Polymorphism databases

DMDMi51338607.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12533 mRNA. Translation: CAA31051.1 .
M22995 mRNA. Translation: AAA36150.1 .
AF493912 mRNA. Translation: AAM12626.1 .
AL049557 Genomic DNA. Translation: CAB55685.2 . Sequence problems.
BC014086 mRNA. Translation: AAH14086.1 .
CCDSi CCDS840.1.
PIRi A32342.
RefSeqi NP_001010935.1. NM_001010935.2.
NP_001278825.1. NM_001291896.1.
NP_002875.1. NM_002884.3.
UniGenei Hs.190334.
Hs.586618.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C1Y X-ray 1.90 A 1-167 [» ]
1GUA X-ray 2.00 A 1-167 [» ]
3KUC X-ray 1.92 A 1-167 [» ]
4KVG X-ray 1.65 A/C 1-167 [» ]
ProteinModelPortali P62834.
SMRi P62834. Positions 1-167.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111841. 43 interactions.
DIPi DIP-29106N.
IntActi P62834. 11 interactions.
MINTi MINT-1509313.
STRINGi 9606.ENSP00000348786.

Chemistry

BindingDBi P62834.
ChEMBLi CHEMBL1255139.

PTM databases

PhosphoSitei P62834.

Polymorphism databases

DMDMi 51338607.

2D gel databases

OGPi P62834.

Proteomic databases

MaxQBi P62834.
PaxDbi P62834.
PRIDEi P62834.

Protocols and materials databases

DNASUi 5906.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356415 ; ENSP00000348786 ; ENSG00000116473 .
ENST00000369709 ; ENSP00000358723 ; ENSG00000116473 .
GeneIDi 5906.
KEGGi hsa:5906.
UCSCi uc001ebi.3. human.

Organism-specific databases

CTDi 5906.
GeneCardsi GC01P112084.
HGNCi HGNC:9855. RAP1A.
HPAi CAB018335.
MIMi 179520. gene.
neXtProti NX_P62834.
PharmGKBi PA34217.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00770000120468.
HOGENOMi HOG000233973.
HOVERGENi HBG009351.
InParanoidi P62834.
KOi K04353.
OMAi KPKKSLC.
OrthoDBi EOG7QVM41.
PhylomeDBi P62834.
TreeFami TF313014.

Enzyme and pathway databases

Reactomei REACT_12002. ARMS-mediated activation.
REACT_12076. Frs2-mediated activation.
REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_23898. Rap1 signalling.
SignaLinki P62834.

Miscellaneous databases

ChiTaRSi RAP1A. human.
EvolutionaryTracei P62834.
GeneWikii RAP1A.
GenomeRNAii 5906.
NextBioi 22972.
PROi P62834.
SOURCEi Search...

Gene expression databases

Bgeei P62834.
CleanExi HS_RAP1A.
ExpressionAtlasi P62834. baseline and differential.
Genevestigatori P62834.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view ]
PANTHERi PTHR24070. PTHR24070. 1 hit.
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00173. RAS. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51421. RAS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region."
    Pizon V., Chardin P., Lerosey I., Olofsson B., Tavitian A.
    Oncogene 3:201-204(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Pizon V.
    Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 3.
  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 (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Skin.
  6. "Purification, identification, and characterization of two GTP-binding proteins with molecular weights of 25,000 and 21,000 in human platelet cytosol. One is the rap1/smg21/Krev-1 protein and the other is a novel GTP-binding protein."
    Nagata K., Itoh H., Katada T., Takenaka K., Ui M., Kaziro Y., Nozawa Y.
    J. Biol. Chem. 264:17000-17005(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Platelet.
  7. "Purification and characterization of the 22,000-dalton GTP-binding protein substrate for ADP-ribosylation by botulinum toxin, G22K."
    Bokoch G.M., Parkos C.A., Mumby S.M.
    J. Biol. Chem. 263:16744-16749(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-35.
  8. "Identification of a platelet Mr 22,000 GTP-binding protein as the novel smg-21 gene product having the same putative effector domain as the ras gene products."
    Ohmori T., Kikuchi A., Yamamoto K., Kawata M., Kondo J., Takai Y.
    Biochem. Biophys. Res. Commun. 157:670-676(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-5; 17-24; 32-42 AND 152-168.
  9. "The COOH-terminal domain of the Rap1A (Krev-1) protein is isoprenylated and supports transformation by an H-Ras:Rap1A chimeric protein."
    Buss J.E., Quilliam L.A., Kato K., Casey P.J., Solski P.A., Wong G., Clark R., McCormick F., Bokoch G.M., Der C.J.
    Mol. Cell. Biol. 11:1523-1530(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-181, METHYLATION AT CYS-181.
  10. "RA-GEF, a novel Rap1A guanine nucleotide exchange factor containing a Ras/Rap1A-associating domain, is conserved between nematode and humans."
    Liao Y., Kariya K., Hu C.-D., Shibatohge M., Goshima M., Okada T., Watari Y., Gao X., Jin T.-G., Yamawaki-Kataoka Y., Kataoka T.
    J. Biol. Chem. 274:37815-37820(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAPGEF2.
  11. "Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras."
    Song C., Hu C.-D., Masago M., Kariya K., Yamawaki-Kataoka Y., Shibatohge M., Wu D., Satoh T., Kataoka T.
    J. Biol. Chem. 276:2752-2757(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLCE1.
  12. "RA-GEF-1, a guanine nucleotide exchange factor for Rap1, is activated by translocation induced by association with Rap1*GTP and enhances Rap1-dependent B-Raf activation."
    Liao Y., Satoh T., Gao X., Jin T.G., Hu C.D., Kataoka T.
    J. Biol. Chem. 276:28478-28483(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAPGEF2, SUBCELLULAR LOCATION.
  13. "Differential roles of Ras and Rap1 in growth factor-dependent activation of phospholipase C epsilon."
    Song C., Satoh T., Edamatsu H., Wu D., Tadano M., Gao X., Kataoka T.
    Oncogene 21:8105-8113(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLCE1.
  14. "Krit 1 interactions with microtubules and membranes are regulated by Rap1 and integrin cytoplasmic domain associated protein-1."
    Beraud-Dufour S., Gautier R., Albiges-Rizo C., Chardin P., Faurobert E.
    FEBS J. 274:5518-5532(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH ITGB1BP1 AND KRIT1, INTERACTION WITH KRIT1.
  15. Cited for: INTERACTION WITH RADIL.
  16. "Identification of three novel proteins (SGSM1, 2, 3) which modulate small G protein (RAP and RAB)-mediated signaling pathway."
    Yang H., Sasaki T., Minoshima S., Shimizu N.
    Genomics 90:249-260(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGSM1; SGSM2 AND SGSM3.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: FUNCTION.
  19. "The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue."
    Nassar N., Horn G., Herrmann C., Scherer A., McCormick F., Wittinghofer A.
    Nature 375:554-560(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-167.
  20. "Ras/Rap effector specificity determined by charge reversal."
    Nassar N., Horn G., Herrmann C., Block C., Janknecht R., Wittinghofer A.
    Nat. Struct. Biol. 3:723-729(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-167.

Entry informationi

Entry nameiRAP1A_HUMAN
AccessioniPrimary (citable) accession number: P62834
Secondary accession number(s): P10113
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: November 26, 2014
This is version 126 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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