P61224 (RAP1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rap-1b

Alternative name(s):
GTP-binding protein smg p21B

Gene names

Name:	RAP1B
ORF Names:	OK/SW-cl.11

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	184 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.17 Ref.19
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.18
Subunit structure	Heterodimer with RAP1GAP. Interacts with EPAC2, SGSM1, SGSM2 and SGSM3. Interacts with KRIT1. Ref.16 Ref.18 Ref.19 Ref.20
Subcellular location	Cell membrane. Cytoplasm › cytosol. 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 component	Cell junction Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Nucleotide-binding
PTM	ADP-ribosylation Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Inferred from electronic annotation. Source: Compara energy reserve metabolic process Traceable author statement. Source: Reactome platelet activation Traceable author statement. Source: Reactome regulation of establishment of cell polarity Inferred from mutant phenotype Ref.17. Source: UniProtKB regulation of insulin secretion Traceable author statement. Source: Reactome small GTPase mediated signal transduction Inferred from electronic annotation. Source: Compara
Cellular_component	cell-cell junction Inferred from direct assay Ref.17. Source: UniProtKB cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell lipid particle Inferred from direct assay PubMed 14741744. Source: UniProtKB plasma membrane Traceable author statement. Source: Reactome
Molecular_function	GDP binding Inferred from direct assay Ref.18. Source: UniProtKB GTP binding Inferred from direct assay Ref.18. Source: UniProtKB GTPase activity Inferred from direct assay Ref.18. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 181

181

Ras-related protein Rap-1b

PRO_0000030209

Propeptide

182 – 184

3

Removed in mature form

PRO_0000030210

Regions

Nucleotide binding

10 – 18

9

GTP

Nucleotide binding

57 – 61

5

GTP

Nucleotide binding

116 – 119

4

GTP

Nucleotide binding

147 – 149

3

GTP

Region

25 – 67

43

Interaction with KRIT1

Motif

32 – 40

9

Effector region Probable

Amino acid modifications

Modified residue

39

1

ADP-ribosylserine; by botulinum toxin Probable

Modified residue

179

1

Phosphoserine; by PKA

Modified residue

181

1

Cysteine methyl ester

Lipidation

181

1

S-geranylgeranyl cysteine Ref.15

Natural variations

Alternative sequence

20 – 61

42

Missing in isoform 4.

VSP_045303

Alternative sequence

43 – 61

19

Missing in isoform 3.

VSP_045304

Alternative sequence

62 – 108

47

Missing in isoform 2.

VSP_045305

Experimental info

Mutagenesis

12

1

G → V: Constitutively activated.

Mutagenesis

25

1

Q → A: Impairs interaction with KRIT1.

Mutagenesis

32

1

Y → A: 25-fold reduction in RAP1GAP-stimulated GTPase activity. Ref.18

Mutagenesis

32

1

Y → F: 2-fold reduction in RAP1GAP-stimulated GTPase activity. Ref.18

Mutagenesis

37

1

E → A: Strong reduction in nucleotide exchange with EPAC2. Ref.19

Mutagenesis

38

1

D → A: Impairs interaction with KRIT1.

Mutagenesis

63

1

Q → E: Abolishes complex formation with RAP1GAP. Loss GTPase activity. Ref.18

Mutagenesis

64

1

F → A: Abolishes complex formation with RAP1GAP. Loss GTPase activity. Ref.18

Sequence conflict

8

1

V → F in AAH95467. Ref.11

Sequence conflict

16

1

K → N in AAH78173. Ref.11

Secondary structure

1

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184

Helix Strand Turn

Details...

Beta strand

2 – 11

10

Helix

16 – 25

10

Turn

27 – 29

3

Beta strand

36 – 46

11

Beta strand

49 – 58

10

Beta strand

60 – 62

3

Helix

65 – 74

10

Beta strand

76 – 83

8

Helix

87 – 91

5

Helix

93 – 104

12

Beta strand

105 – 107

3

Beta strand

111 – 116

6

Helix

121 – 123

3

Helix

128 – 137

10

Beta strand

142 – 145

4

Turn

148 – 151

4

Helix

154 – 166

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2004. Version 1. Checksum: CE976895E5965224	FASTA	184	20,825
	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
	Isoform 2 [UniParc]. Checksum: A142020053FE1BC5	FASTA	137	15,356
	10 20 30 40 50 60 MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDAQQ CMLEILDTAG 70 80 90 100 110 120 TVPMILVGNK CDLEDERVVG KEQGQNLARQ WNNCAFLESS AKSKINVNEI FYDLVRQINR 130 KTPVPGKARK KSSCQLL
	Isoform 3 [UniParc]. Checksum: 5F70CFF192C43A4A	FASTA	165	18,778
	10 20 30 40 50 60 MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKEQFTAMRD LYMKNGQGFA 70 80 90 100 110 120 LVYSITAQST FNDLQDLREQ ILRVKDTDDV PMILVGNKCD LEDERVVGKE QGQNLARQWN 130 140 150 160 NCAFLESSAK SKINVNEIFY DLVRQINRKT PVPGKARKKS SCQLL
	Isoform 4 [UniParc]. Checksum: EA48A041F34E0074	FASTA	142	16,033
	10 20 30 40 50 60 MREYKLVVLG SGGVGKSALE QFTAMRDLYM KNGQGFALVY SITAQSTFND LQDLREQILR 70 80 90 100 110 120 VKDTDDVPMI LVGNKCDLED ERVVGKEQGQ NLARQWNNCA FLESSAKSKI NVNEIFYDLV 130 140 RQINRKTPVP GKARKKSSCQ LL

References

	« Hide 'large scale' referencesShow '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. , 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]	"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.
[19]	"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.
[20]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

SeattleSNPs

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.

IPI

IPI00015148.

PIR

TVHUR1. S01952.

RefSeq

NP_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.

UniGene

Hs.369920.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P61224.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35407N.

IntAct

P61224. 9 interactions.

MINT

MINT-1133272.

STRING

9606.ENSP00000250559.

PTM databases

PhosphoSite

P61224.

Polymorphism databases

DMDM

47117723.

2D gel databases

OGP

P09526.

Proteomic databases

PaxDb

P61224.

PRIDE

P61224.

Protocols and materials databases

DNASU

5908.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000250559; ENSP00000250559; ENSG00000127314.
ENST00000341355; ENSP00000441275; ENSG00000127314.
ENST00000393436; ENSP00000377085; ENSG00000127314.
ENST00000450214; ENSP00000399986; ENSG00000127314.
ENST00000537460; ENSP00000439966; ENSG00000127314.
ENST00000539091; ENSP00000444830; ENSG00000127314.
ENST00000540209; ENSP00000446318; ENSG00000127314.
ENST00000542145; ENSP00000440014; ENSG00000127314.

GeneID

5908.

KEGG

hsa:5908.

UCSC

uc001sub.3. human.

Organism-specific databases

CTD

5908.

GeneCards

GC12P069005.

H-InvDB

HIX0032084.

HGNC

HGNC:9857. RAP1B.

MIM

179530. gene.

neXtProt

NX_P61224.

PharmGKB

PA34219.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOVERGEN

HBG009351.

InParanoid

P61224.

KO

K07836.

OMA

RANVNEV.

OrthoDB

EOG45MN6H.

PhylomeDB

P61224.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.
ephbfwdpathway. EPHB forward signaling.
ifngpathway. IFN-gamma pathway.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
mapktrkpathway. Trk receptor signaling mediated by the MAPK pathway.

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P61224.

Bgee

P61224.

CleanEx

HS_RAP1B.

Genevestigator

P61224.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]

PANTHER

PTHR24070. PTHR24070. 1 hit.

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00173. RAS. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51421. RAS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RAP1B. human.

EvolutionaryTrace

P61224.

GenomeRNAi

5908.

NextBio

22980.

SOURCE

Search...

Entry information

Entry name

RAP1B_HUMAN

Accession

Primary (citable) accession number: P61224
Secondary accession number(s): B2R5Z2 , 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:	May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.