Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P61224 (RAP1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rap-1b
Alternative name(s):
GTP-binding protein smg p21B
Gene names
Name:RAP1B
ORF Names:OK/SW-cl.11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function. Ref.17 Ref.18 Ref.20

Enzyme regulation

Activated by binding to the GTPase-activating protein RAP1GAP. Activated by guanine nucleotide-exchange factor (GEF) EPAC2 in a cAMP-dependent manner. Ref.19

Subunit structure

Heterodimer with RAP1GAP. Interacts with EPAC2, SGSM1, SGSM2 and SGSM3. Interacts with KRIT1. Ref.16 Ref.19 Ref.20 Ref.21

Subcellular location

Cell membrane. Cytoplasmcytosol. Cell junction. Note: May shuttle between plasma membrane and cytosol. Presence of KRIT1 and CDH5 is required for its localization to the cell junction. Ref.12 Ref.17

Sequence similarities

Belongs to the small GTPase superfamily. Ras family.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   PTMADP-ribosylation
Lipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRap protein signal transduction

Inferred from mutant phenotype Ref.18. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular response to cAMP

Inferred from direct assay Ref.18. Source: UniProtKB

energy reserve metabolic process

Traceable author statement. Source: Reactome

establishment of endothelial barrier

Inferred from mutant phenotype Ref.18. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

regulation of cell junction assembly

Inferred from mutant phenotype Ref.18. Source: UniProtKB

regulation of establishment of cell polarity

Inferred from mutant phenotype Ref.17. Source: UniProtKB

regulation of insulin secretion

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcell-cell junction

Inferred from direct assay Ref.17. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 20458337. Source: UniProt

intracellular

Inferred from direct assay. Source: LIFEdb

lipid particle

Inferred from direct assay PubMed 14741744. Source: UniProtKB

membrane

Traceable author statement PubMed 2105724Ref.15. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionGDP binding

Inferred from direct assay Ref.19. Source: UniProtKB

GTP binding

Inferred from direct assay Ref.19. Source: UniProtKB

GTPase activity

Inferred from direct assay Ref.19. Source: UniProtKB

protein complex binding

Inferred from direct assay PubMed 23209302. Source: MGI

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P61224-1)

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: P61224-2)

The sequence of this isoform differs from the canonical sequence as follows:
     62-108: Missing.
Isoform 3 (identifier: P61224-3)

The sequence of this isoform differs from the canonical sequence as follows:
     43-61: Missing.
Isoform 4 (identifier: P61224-4)

The sequence of this isoform differs from the canonical sequence as follows:
     20-61: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 181181Ras-related protein Rap-1b
PRO_0000030209
Propeptide182 – 1843Removed in mature form
PRO_0000030210

Regions

Nucleotide binding10 – 189GTP
Nucleotide binding57 – 615GTP
Nucleotide binding116 – 1194GTP
Nucleotide binding147 – 1493GTP
Region25 – 6743Interaction with KRIT1
Motif32 – 409Effector region Probable

Amino acid modifications

Modified residue391ADP-ribosylserine; by botulinum toxin Probable
Modified residue1791Phosphoserine; by PKA
Modified residue1811Cysteine methyl ester
Lipidation1811S-geranylgeranyl cysteine Ref.15

Natural variations

Alternative sequence20 – 6142Missing in isoform 4.
VSP_045303
Alternative sequence43 – 6119Missing in isoform 3.
VSP_045304
Alternative sequence62 – 10847Missing in isoform 2.
VSP_045305

Experimental info

Mutagenesis121G → V: Constitutively activated.
Mutagenesis251Q → A: Impairs interaction with KRIT1.
Mutagenesis321Y → A: 25-fold reduction in RAP1GAP-stimulated GTPase activity. Ref.19
Mutagenesis321Y → F: 2-fold reduction in RAP1GAP-stimulated GTPase activity. Ref.19
Mutagenesis371E → A: Strong reduction in nucleotide exchange with EPAC2. Ref.20
Mutagenesis381D → A: Impairs interaction with KRIT1.
Mutagenesis631Q → E: Abolishes complex formation with RAP1GAP. Loss GTPase activity. Ref.19
Mutagenesis641F → A: Abolishes complex formation with RAP1GAP. Loss GTPase activity. Ref.19
Sequence conflict81V → F in AAH95467. Ref.11
Sequence conflict161K → N in AAH78173. Ref.11

Secondary structure

................................... 184
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2004. Version 1.
Checksum: CE976895E5965224

FASTA18420,825
        10         20         30         40         50         60 
MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDAQQ CMLEILDTAG 

        70         80         90        100        110        120 
TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MILVGNKCDL 

       130        140        150        160        170        180 
EDERVVGKEQ GQNLARQWNN CAFLESSAKS KINVNEIFYD LVRQINRKTP VPGKARKKSS 


CQLL 

« Hide

Isoform 2 [UniParc].

Checksum: A142020053FE1BC5
Show »

FASTA13715,356
Isoform 3 [UniParc].

Checksum: 5F70CFF192C43A4A
Show »

FASTA16518,778
Isoform 4 [UniParc].

Checksum: EA48A041F34E0074
Show »

FASTA14216,033

References

« Hide 'large scale' references
[1]"Nucleotide sequence of a human cDNA encoding a ras-related protein (rap1B)."
Pizon V., Lerosey I., Chardin P., Tavitian A.
Nucleic Acids Res. 16:7719-7719(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"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: Uterus.
[3]"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon adenocarcinoma.
[4]"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] (ISOFORM 1).
Tissue: Brain.
[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. expand/collapse author list , 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; 2; 3 AND 4).
Tissue: Amygdala.
[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 1).
[7]"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]SeattleSNPs variation discovery resource
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]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. expand/collapse author list , 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].
[11]"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: Chondrosarcoma, Placenta and Testis.
[12]"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, SUBCELLULAR LOCATION, ADP-RIBOSYLATION AT SER-39.
[13]"Rap1-B is phosphorylated by protein kinase A in intact human platelets."
Siess W., Winegar D.A., Lapetina E.G.
Biochem. Biophys. Res. Commun. 170:944-950(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 146-180, PHOSPHORYLATION.
[14]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 168-176.
Tissue: Platelet.
[15]"Posttranslationally processed structure of the human platelet protein smg p21B: evidence for geranylgeranylation and carboxyl methylation of the C-terminal cysteine."
Kawata M., Farnsworth C.C., Yoshida Y., Gelb M.H., Glomset J.A., Takai Y.
Proc. Natl. Acad. Sci. U.S.A. 87:8960-8964(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-181.
Tissue: Platelet.
[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]"CCM1 regulates vascular-lumen organization by inducing endothelial polarity."
Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G., Chapon F., Dejana E.
J. Cell Sci. 123:1073-1080(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]"Epac1 and PDZ-GEF cooperate in Rap1 mediated endothelial junction control."
Pannekoek W.J., van Dijk J.J., Chan O.Y., Huveneers S., Linnemann J.R., Spanjaard E., Brouwer P.M., van der Meer A.J., Zwartkruis F.J., Rehmann H., de Rooij J., Bos J.L.
Cell. Signal. 23:2056-2064(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues."
Scrima A., Thomas C., Deaconescu D., Wittinghofer A.
EMBO J. 27:1145-1153(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-167 IN COMPLEX WITH GTP ANALOG AND RAP1GAP, SUBUNIT, ENZYME REGULATION, MUTAGENESIS OF TYR-32; GLN-63 AND PHE-64.
[20]"Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B."
Rehmann H., Arias-Palomo E., Hadders M.A., Schwede F., Llorca O., Bos J.L.
Nature 455:124-127(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-167 IN COMPLEX WITH EPAC2, FUNCTION, SUBUNIT, MUTAGENESIS OF GLU-37.
[21]"Structural basis for small G protein effector interaction of Ras-related protein 1 (Rap1) and adaptor protein Krev interaction trapped 1 (KRIT1)."
Li X., Zhang R., Draheim K.M., Liu W., Calderwood D.A., Boggon T.J.
J. Biol. Chem. 287:22317-22327(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-167 OF MUTANT VAL-12 IN COMPLEX WITH KRIT1; GTP ANALOG AND MAGNESIUM, INTERACTION WITH KRIT1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X08004 mRNA. Translation: CAB46488.1.
AL080212 mRNA. Translation: CAB45777.1.
AB062128 mRNA. Translation: BAB93460.1.
AF493913 mRNA. Translation: AAM12627.1.
AK298818 mRNA. Translation: BAG60950.1.
AK301401 mRNA. Translation: BAG62936.1.
AK301428 mRNA. Translation: BAG62956.1.
AK312371 mRNA. Translation: BAG35289.1.
CR407689 mRNA. Translation: CAG28617.1.
BT020093 mRNA. Translation: AAV38896.1.
EF581377 Genomic DNA. Translation: ABQ52130.1.
AC015550 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97189.1.
BC000176 mRNA. Translation: AAH00176.1.
BC078173 mRNA. Translation: AAH78173.1.
BC095467 mRNA. Translation: AAH95467.1.
PIRTVHUR1. S01952.
RefSeqNP_001010942.1. NM_001010942.2.
NP_001238846.1. NM_001251917.1.
NP_001238847.1. NM_001251918.1.
NP_001238850.1. NM_001251921.1.
NP_001238851.1. NM_001251922.1.
NP_056461.1. NM_015646.5.
UniGeneHs.369920.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BRWX-ray3.40D1-167[»]
3CF6X-ray2.20R1-167[»]
4DXAX-ray1.95A1-167[»]
4HDOX-ray1.67B1-167[»]
4HDQX-ray1.95B1-167[»]
4M8NX-ray3.29E/F/G/H1-166[»]
ProteinModelPortalP61224.
SMRP61224. Positions 1-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111843. 31 interactions.
DIPDIP-35407N.
IntActP61224. 30 interactions.
MINTMINT-1133272.
STRING9606.ENSP00000250559.

PTM databases

PhosphoSiteP61224.

Polymorphism databases

DMDM47117723.

2D gel databases

OGPP09526.

Proteomic databases

PaxDbP61224.
PRIDEP61224.

Protocols and materials databases

DNASU5908.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250559; ENSP00000250559; ENSG00000127314. [P61224-1]
ENST00000341355; ENSP00000441275; ENSG00000127314. [P61224-1]
ENST00000393436; ENSP00000377085; ENSG00000127314. [P61224-1]
ENST00000450214; ENSP00000399986; ENSG00000127314. [P61224-4]
ENST00000537460; ENSP00000439966; ENSG00000127314. [P61224-1]
ENST00000539091; ENSP00000444830; ENSG00000127314. [P61224-4]
ENST00000540209; ENSP00000446318; ENSG00000127314. [P61224-3]
ENST00000542145; ENSP00000440014; ENSG00000127314. [P61224-2]
GeneID5908.
KEGGhsa:5908.
UCSCuc001sub.3. human. [P61224-1]
uc010stf.2. human.
uc010stg.2. human.
uc010sti.2. human.

Organism-specific databases

CTD5908.
GeneCardsGC12P069005.
H-InvDBHIX0032084.
HGNCHGNC:9857. RAP1B.
MIM179530. gene.
neXtProtNX_P61224.
PharmGKBPA34219.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOVERGENHBG009351.
InParanoidP61224.
KOK07836.
OMARDSTHPR.
OrthoDBEOG7QVM41.
PhylomeDBP61224.
TreeFamTF313014.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP61224.

Gene expression databases

BgeeP61224.
CleanExHS_RAP1B.
GenevestigatorP61224.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERPTHR24070. PTHR24070. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAP1B. human.
EvolutionaryTraceP61224.
GeneWikiRAP1B.
GenomeRNAi5908.
NextBio22980.
PROP61224.
SOURCESearch...

Entry information

Entry nameRAP1B_HUMAN
AccessionPrimary (citable) accession number: P61224
Secondary accession number(s): B2R5Z2 expand/collapse secondary AC list , B4DQI8, B4DW74, B4DW94, P09526, Q502X3, Q5TZR4, Q6DCA1, Q6LES0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM