RAP1GAP

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RAP1GAP

Protein RAP1GAP PDB 1srq.png

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1SRQ, 3BRW

Identifiers

RAP1GAP, RAP1GA1, RAP1GAP1, RAP1GAPII, RAPGAP, RAP1 GTPase activating protein

External IDs

OMIM: 600278 MGI: 109338 HomoloGene: 2163 GeneCards: RAP1GAP

Gene location (Human)

Chr.	Chromosome 1 (human)^[1]

Band	1p36.12	Start	21,596,215 bp^[1]
Band	1p36.12	End	21,669,363 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 4 (mouse)^[2]

Band	4 D3\|4 70.02 cM	Start	137,664,726 bp^[2]
Band	4 D3\|4 70.02 cM	End	137,729,861 bp^[2]

RNA expression pattern

Top expressed in
putamen nucleus accumbens renal cortex thyroid gland renal medulla caudate nucleus fundus body of stomach
More reference expression data


More reference expression data

Gene ontology
Molecular function	protein homodimerization activity GO:0005083 GTPase regulator activity GO:0001948 protein binding GO:0006184 GTPase activity GO:0005097, GO:0005099, GO:0005100 GTPase activator activity
Cellular component	Golgi apparatus membrane Golgi membrane cytosol
Biological process	negative regulation of microvillus assembly GO:0043087, GO:0032313, GO:0032319, GO:0032314, GO:0043088 regulation of GTPase activity GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity regulation of small GTPase mediated signal transduction signal transduction axon guidance
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse


5909


110351

Ensembl


ENSG00000076864


ENSMUSG00000041351


P47736


A2ALS5

RefSeq (mRNA)

NM_001145657 NM_001145658 NM_002885 NM_001330383 NM_001350524
NM_001350525 NM_001350526 NM_001350527 NM_001350528


NM_001081155 NM_001256218 NM_029563 NM_001331215

RefSeq (protein)

NP_001139129 NP_001139130 NP_001317312 NP_002876 NP_001337453
NP_001337454 NP_001337455 NP_001337456 NP_001337457

NP_001074624 NP_001243147 NP_001318144 NP_083839 NP_001366162
NP_001366163 NP_001366164 NP_001366165

Location (UCSC)

Chr 1: 21.6 – 21.67 Mb

Chr 4: 137.66 – 137.73 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

Rap1 GTPase-activating protein 1 is an enzyme that in humans is encoded by the RAP1GAP gene.^[5]^[6]

Interactions[]

RAP1GAP has been shown to interact with MLLT4.^[7]

References[]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000076864 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000041351 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Rubinfeld B, Munemitsu S, Clark R, Conroy L, Watt K, Crosier WJ, McCormick F, Polakis P (June 1991). "Molecular cloning of a GTPase activating protein specific for the Krev-1 protein p21rap1". Cell. 65 (6): 1033–42. doi:10.1016/0092-8674(91)90555-D. PMID 1904317. S2CID 45725280.
^ "Entrez Gene: RAP1GAP RAP1 GTPase activating protein".
^ Su L, Hattori M, Moriyama M, Murata N, Harazaki M, Kaibuchi K, Minato N (April 2003). "AF-6 controls integrin-mediated cell adhesion by regulating Rap1 activation through the specific recruitment of Rap1GTP and SPA-1". The Journal of Biological Chemistry. 278 (17): 15232–8. doi:10.1074/jbc.M211888200. PMID 12590145.

Further reading[]

Hattori M, Minato N (October 2003). "Rap1 GTPase: functions, regulation, and malignancy". Journal of Biochemistry. 134 (4): 479–84. doi:10.1093/jb/mvg180. PMID 14607972.
Rubinfeld B, Crosier WJ, Albert I, Conroy L, Clark R, McCormick F, Polakis P (October 1992). "Localization of the rap1GAP catalytic domain and sites of phosphorylation by mutational analysis". Molecular and Cellular Biology. 12 (10): 4634–42. doi:10.1128/mcb.12.10.4634. PMC 360390. PMID 1406653.
Weiss J, Rubinfeld B, Polakis PG, McCormick F, Cavenee WK, Arden KC (1994). "The RAP1GA1 locus for human Rap1-GTPase activating protein 1 maps to chromosome 1p36.1-->p35". Cytogenetics and Cell Genetics. 66 (1): 18–21. doi:10.1159/000133655. PMID 8275700.
Peterson SN, Trabalzini L, Brtva TR, Fischer T, Altschuler DL, Martelli P, Lapetina EG, Der CJ, White GC (November 1996). "Identification of a novel RalGDS-related protein as a candidate effector for Ras and Rap1". The Journal of Biological Chemistry. 271 (47): 29903–8. doi:10.1074/jbc.271.47.29903. PMID 8939933.
Kurachi H, Wada Y, Tsukamoto N, Maeda M, Kubota H, Hattori M, Iwai K, Minato N (October 1997). "Human SPA-1 gene product selectively expressed in lymphoid tissues is a specific GTPase-activating protein for Rap1 and Rap2. Segregate expression profiles from a rap1GAP gene product". The Journal of Biological Chemistry. 272 (44): 28081–8. doi:10.1074/jbc.272.44.28081. PMID 9346962.
Seki N, Ohira M, Nagase T, Ishikawa K, Miyajima N, Nakajima D, Nomura N, Ohara O (October 1997). "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain". DNA Research. 4 (5): 345–9. doi:10.1093/dnares/4.5.345. PMID 9455484.
Mochizuki N, Ohba Y, Kiyokawa E, Kurata T, Murakami T, Ozaki T, Kitabatake A, Nagashima K, Matsuda M (August 1999). "Activation of the ERK/MAPK pathway by an isoform of rap1GAP associated with G alpha(i)". Nature. 400 (6747): 891–4. Bibcode:1999Natur.400..891M. doi:10.1038/23738. PMID 10476970. S2CID 204995543.
Meng J, Glick JL, Polakis P, Casey PJ (December 1999). "Functional interaction between Galpha(z) and Rap1GAP suggests a novel form of cellular cross-talk". The Journal of Biological Chemistry. 274 (51): 36663–9. doi:10.1074/jbc.274.51.36663. PMID 10593970.
Berruti G (May 2000). "A novel rap1/B-Raf/14-3-3 theta protein complex is formed in vivo during the morphogenetic differentiation of postmeiotic male germ cells". Experimental Cell Research. 257 (1): 172–9. doi:10.1006/excr.2000.4877. PMID 10854065.
Kao S, Jaiswal RK, Kolch W, Landreth GE (May 2001). "Identification of the mechanisms regulating the differential activation of the mapk cascade by epidermal growth factor and nerve growth factor in PC12 cells". The Journal of Biological Chemistry. 276 (21): 18169–77. doi:10.1074/jbc.M008870200. PMID 11278445.
Klinger M, Kudlacek O, Seidel MG, Freissmuth M, Sexl V (September 2002). "MAP kinase stimulation by cAMP does not require RAP1 but SRC family kinases". The Journal of Biological Chemistry. 277 (36): 32490–7. doi:10.1074/jbc.M200556200. PMID 12082090.
Liu L, Schwartz BR, Tupper J, Lin N, Winn RK, Harlan JM (October 2002). "The GTPase Rap1 regulates phorbol 12-myristate 13-acetate-stimulated but not ligand-induced beta 1 integrin-dependent leukocyte adhesion". The Journal of Biological Chemistry. 277 (43): 40893–900. doi:10.1074/jbc.M206208200. PMID 12091396.
de Bruyn KM, Rangarajan S, Reedquist KA, Figdor CG, Bos JL (August 2002). "The small GTPase Rap1 is required for Mn(2+)- and antibody-induced LFA-1- and VLA-4-mediated cell adhesion". The Journal of Biological Chemistry. 277 (33): 29468–76. doi:10.1074/jbc.M204990200. PMID 12171996.
Meng J, Casey PJ (November 2002). "Activation of Gz attenuates Rap1-mediated differentiation of PC12 cells". The Journal of Biological Chemistry. 277 (45): 43417–24. doi:10.1074/jbc.M204074200. PMID 12198116.
Schmitt JM, Stork PJ (November 2002). "Galpha and Gbeta gamma require distinct Src-dependent pathways to activate Rap1 and Ras". The Journal of Biological Chemistry. 277 (45): 43024–32. doi:10.1074/jbc.M204006200. PMID 12221082.
Delehanty LL, Mogass M, Gonias SL, Racke FK, Johnstone B, Goldfarb AN (March 2003). "Stromal inhibition of megakaryocytic differentiation is associated with blockade of sustained Rap1 activation". Blood. 101 (5): 1744–51. doi:10.1182/blood-2002-04-1278. PMID 12393469.
Grader-Beck T, van Puijenbroek AA, Nadler LM, Boussiotis VA (February 2003). "cAMP inhibits both Ras and Rap1 activation in primary human T lymphocytes, but only Ras inhibition correlates with blockade of cell cycle progression". Blood. 101 (3): 998–1006. doi:10.1182/blood-2002-06-1665. PMID 12393539.
Gendron L, Oligny JF, Payet MD, Gallo-Payet N (February 2003). "Cyclic AMP-independent involvement of Rap1/B-Raf in the angiotensin II AT2 receptor signaling pathway in NG108-15 cells". The Journal of Biological Chemistry. 278 (6): 3606–14. doi:10.1074/jbc.M202446200. PMID 12464615.

v t PDB gallery
1srq: Crystal Structure of the Rap1GAP catalytic domain

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