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P61224

- RAP1B_HUMAN

UniProt

P61224 - RAP1B_HUMAN

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Protein

Ras-related protein Rap-1b

Gene

RAP1B

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

Functioni

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.3 Publications

Enzyme regulationi

Activated by binding to the GTPase-activating protein RAP1GAP. Activated by guanine nucleotide-exchange factor (GEF) EPAC2 in a cAMP-dependent manner.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 189GTP
Nucleotide bindingi57 – 615GTP
Nucleotide bindingi116 – 1194GTP
Nucleotide bindingi147 – 1493GTP

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTPase activity Source: UniProtKB
  3. GTP binding Source: UniProtKB
  4. protein complex binding Source: MGI

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cell proliferation Source: Ensembl
  3. cellular response to cAMP Source: UniProtKB
  4. energy reserve metabolic process Source: Reactome
  5. establishment of endothelial barrier Source: UniProtKB
  6. negative regulation of calcium ion-dependent exocytosis Source: Ensembl
  7. negative regulation of synaptic vesicle exocytosis Source: Ensembl
  8. platelet activation Source: Reactome
  9. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  10. Rap protein signal transduction Source: UniProtKB
  11. regulation of cell junction assembly Source: UniProtKB
  12. regulation of establishment of cell polarity Source: UniProtKB
  13. regulation of insulin secretion Source: Reactome
  14. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_23898. Rap1 signalling.
SignaLinkiP61224.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rap-1b
Alternative name(s):
GTP-binding protein smg p21B
Gene namesi
Name:RAP1B
ORF Names:OK/SW-cl.11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9857. RAP1B.

Subcellular locationi

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.

GO - Cellular componenti

  1. cell-cell junction Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. intracellular Source: LIFEdb
  5. lipid particle Source: UniProtKB
  6. membrane Source: UniProtKB
  7. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121G → V: Constitutively activated.
Mutagenesisi25 – 251Q → A: Impairs interaction with KRIT1.
Mutagenesisi32 – 321Y → A: 25-fold reduction in RAP1GAP-stimulated GTPase activity. 1 Publication
Mutagenesisi32 – 321Y → F: 2-fold reduction in RAP1GAP-stimulated GTPase activity. 1 Publication
Mutagenesisi37 – 371E → A: Strong reduction in nucleotide exchange with EPAC2. 1 Publication
Mutagenesisi38 – 381D → A: Impairs interaction with KRIT1.
Mutagenesisi63 – 631Q → E: Abolishes complex formation with RAP1GAP. Loss GTPase activity. 1 Publication
Mutagenesisi64 – 641F → A: Abolishes complex formation with RAP1GAP. Loss GTPase activity. 1 Publication
Mutagenesisi179 – 1791S → A: Abolishes phosphorylation by PKA. 1 Publication

Organism-specific databases

PharmGKBiPA34219.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 181181Ras-related protein Rap-1bPRO_0000030209Add
BLAST
Propeptidei182 – 1843Removed in mature formPRO_0000030210

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391ADP-ribosylserine; by botulinum toxin1 Publication
Modified residuei179 – 1791Phosphoserine; by PKA1 Publication
Modified residuei181 – 1811Cysteine methyl ester1 Publication
Lipidationi181 – 1811S-geranylgeranyl cysteine1 Publication

Keywords - PTMi

ADP-ribosylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP61224.
PaxDbiP61224.
PRIDEiP61224.

2D gel databases

OGPiP09526.

PTM databases

PhosphoSiteiP61224.

Expressioni

Gene expression databases

BgeeiP61224.
CleanExiHS_RAP1B.
ExpressionAtlasiP61224. baseline.
GenevestigatoriP61224.

Interactioni

Subunit structurei

Heterodimer with RAP1GAP. Interacts with EPAC2, SGSM1, SGSM2 and SGSM3. Interacts with KRIT1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RALGDSQ129672EBI-358143,EBI-365861
RAP1GAPP477363EBI-358143,EBI-722307
UBCP0CG482EBI-358143,EBI-3390054

Protein-protein interaction databases

BioGridi111843. 36 interactions.
DIPiDIP-35407N.
IntActiP61224. 31 interactions.
MINTiMINT-1133272.
STRINGi9606.ENSP00000250559.

Structurei

Secondary structure

1
184
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Helixi16 – 2510Combined sources
Turni27 – 293Combined sources
Beta strandi36 – 4611Combined sources
Beta strandi49 – 5810Combined sources
Beta strandi60 – 623Combined sources
Beta strandi63 – 653Combined sources
Helixi68 – 747Combined sources
Beta strandi76 – 838Combined sources
Helixi87 – 915Combined sources
Helixi93 – 10412Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi111 – 1166Combined sources
Helixi121 – 1233Combined sources
Helixi128 – 13710Combined sources
Beta strandi142 – 1454Combined sources
Turni148 – 1514Combined sources
Helixi154 – 16613Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4MGIX-ray2.80R1-167[»]
4MGKX-ray2.70R1-167[»]
4MGYX-ray2.60R1-167[»]
4MGZX-ray3.00R1-167[»]
4MH0X-ray2.40R1-167[»]
ProteinModelPortaliP61224.
SMRiP61224. Positions 1-167.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61224.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 6743Interaction with KRIT1Add
BLAST

Motif

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

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118778.
HOVERGENiHBG009351.
InParanoidiP61224.
KOiK07836.
OMAiRDSTHPR.
OrthoDBiEOG7QVM41.
PhylomeDBiP61224.
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]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P61224-1) [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

        10         20         30         40         50
MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDAQQ
60 70 80 90 100
CMLEILDTAG TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI
110 120 130 140 150
LRVKDTDDVP MILVGNKCDL EDERVVGKEQ GQNLARQWNN CAFLESSAKS
160 170 180
KINVNEIFYD LVRQINRKTP VPGKARKKSS CQLL
Length:184
Mass (Da):20,825
Last modified:May 10, 2004 - v1
Checksum:iCE976895E5965224
GO
Isoform 2 (identifier: P61224-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     62-108: Missing.

Show »
Length:137
Mass (Da):15,356
Checksum:iA142020053FE1BC5
GO
Isoform 3 (identifier: P61224-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-61: Missing.

Show »
Length:165
Mass (Da):18,778
Checksum:i5F70CFF192C43A4A
GO
Isoform 4 (identifier: P61224-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:142
Mass (Da):16,033
Checksum:iEA48A041F34E0074
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81V → F in AAH95467. (PubMed:15489334)Curated
Sequence conflicti16 – 161K → N in AAH78173. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei20 – 6142Missing in isoform 4. 1 PublicationVSP_045303Add
BLAST
Alternative sequencei43 – 6119Missing in isoform 3. 1 PublicationVSP_045304Add
BLAST
Alternative sequencei62 – 10847Missing in isoform 2. 1 PublicationVSP_045305Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS58252.1. [P61224-2]
CCDS58253.1. [P61224-3]
CCDS58254.1. [P61224-4]
CCDS8984.1. [P61224-1]
PIRiS01952. TVHUR1.
RefSeqiNP_001010942.1. NM_001010942.2. [P61224-1]
NP_001238846.1. NM_001251917.1. [P61224-4]
NP_001238847.1. NM_001251918.1. [P61224-4]
NP_001238850.1. NM_001251921.1. [P61224-3]
NP_001238851.1. NM_001251922.1. [P61224-2]
NP_056461.1. NM_015646.5. [P61224-1]
UniGeneiHs.369920.

Genome annotation databases

EnsembliENST00000250559; 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]
GeneIDi5908.
KEGGihsa:5908.
UCSCiuc001sub.3. human. [P61224-1]
uc010stf.2. human.
uc010stg.2. human.
uc010sti.2. human.

Polymorphism databases

DMDMi47117723.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS58252.1. [P61224-2 ]
CCDS58253.1. [P61224-3 ]
CCDS58254.1. [P61224-4 ]
CCDS8984.1. [P61224-1 ]
PIRi S01952. TVHUR1.
RefSeqi NP_001010942.1. NM_001010942.2. [P61224-1 ]
NP_001238846.1. NM_001251917.1. [P61224-4 ]
NP_001238847.1. NM_001251918.1. [P61224-4 ]
NP_001238850.1. NM_001251921.1. [P61224-3 ]
NP_001238851.1. NM_001251922.1. [P61224-2 ]
NP_056461.1. NM_015646.5. [P61224-1 ]
UniGenei Hs.369920.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BRW X-ray 3.40 D 1-167 [» ]
3CF6 X-ray 2.20 R 1-167 [» ]
4DXA X-ray 1.95 A 1-167 [» ]
4HDO X-ray 1.67 B 1-167 [» ]
4HDQ X-ray 1.95 B 1-167 [» ]
4M8N X-ray 3.29 E/F/G/H 1-166 [» ]
4MGI X-ray 2.80 R 1-167 [» ]
4MGK X-ray 2.70 R 1-167 [» ]
4MGY X-ray 2.60 R 1-167 [» ]
4MGZ X-ray 3.00 R 1-167 [» ]
4MH0 X-ray 2.40 R 1-167 [» ]
ProteinModelPortali P61224.
SMRi P61224. Positions 1-167.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111843. 36 interactions.
DIPi DIP-35407N.
IntActi P61224. 31 interactions.
MINTi MINT-1133272.
STRINGi 9606.ENSP00000250559.

PTM databases

PhosphoSitei P61224.

Polymorphism databases

DMDMi 47117723.

2D gel databases

OGPi P09526.

Proteomic databases

MaxQBi P61224.
PaxDbi P61224.
PRIDEi P61224.

Protocols and materials databases

DNASUi 5908.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000250559 ; 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 ]
GeneIDi 5908.
KEGGi hsa:5908.
UCSCi uc001sub.3. human. [P61224-1 ]
uc010stf.2. human.
uc010stg.2. human.
uc010sti.2. human.

Organism-specific databases

CTDi 5908.
GeneCardsi GC12P069005.
H-InvDB HIX0032084.
HGNCi HGNC:9857. RAP1B.
MIMi 179530. gene.
neXtProti NX_P61224.
PharmGKBi PA34219.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00760000118778.
HOVERGENi HBG009351.
InParanoidi P61224.
KOi K07836.
OMAi RDSTHPR.
OrthoDBi EOG7QVM41.
PhylomeDBi P61224.
TreeFami TF313014.

Enzyme and pathway databases

Reactomei REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_23898. Rap1 signalling.
SignaLinki P61224.

Miscellaneous databases

ChiTaRSi RAP1B. human.
EvolutionaryTracei P61224.
GeneWikii RAP1B.
GenomeRNAii 5908.
NextBioi 22980.
PROi P61224.
SOURCEi Search...

Gene expression databases

Bgeei P61224.
CleanExi HS_RAP1B.
ExpressionAtlasi P61224. baseline.
Genevestigatori P61224.

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. "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. 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.
    , 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.
    , 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. 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, METHYLATION AT CYS-181.
    Tissue: Platelet.
  16. "Mutational analysis of the cAMP-dependent protein kinase-mediated phosphorylation site of Rap1b."
    Altschuler D., Lapetina E.G.
    J. Biol. Chem. 268:7527-7531(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-179 BY PKA, MUTAGENESIS OF SER-179.
  17. "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.
  18. "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.
  19. Cited for: FUNCTION.
  20. "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.
  21. "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.
  22. "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.

Entry informationi

Entry nameiRAP1B_HUMAN
AccessioniPrimary (citable) accession number: P61224
Secondary accession number(s): B2R5Z2
, B4DQI8, B4DW74, B4DW94, P09526, Q502X3, Q5TZR4, Q6DCA1, Q6LES0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: October 29, 2014
This is version 129 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 12
    Human chromosome 12: 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