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P47736 (RPGP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Rap1 GTPase-activating protein 1

Short name=Rap1GAP
Short name=Rap1GAP1
Gene names
Name:RAP1GAP
Synonyms:KIAA0474, RAP1GA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length663 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state. Ref.12

Subunit structure

Homodimer and heterodimer with RAP1B. Ref.12 Ref.13

Subcellular location

Golgi apparatus membrane; Peripheral membrane protein.

Tissue specificity

Significant expression seen in the brain, kidney and pancreas. Abundant in the cerebral cortex and expressed at much lower levels in the spinal cord. Not detected in the lymphoid tissues. Ref.7

Induction

By 12-O-tetradecanoylphorbol-13-acetate (TPA) in promyelocytic HL-60 cells. Ref.7

Sequence similarities

Contains 1 GoLoco domain.

Contains 1 Rap-GAP domain.

Sequence caution

The sequence AAH54490.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA32319.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAP1BP612243EBI-722307,EBI-358143

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P47736-1)

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: P47736-2)

The sequence of this isoform differs from the canonical sequence as follows:
     476-476: I → ISLLIPGKSASRFGRRGSAIGIGTVEE
     626-633: Missing.
Isoform 3 (identifier: P47736-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAQLRPAVPPGRPRRGSLPAGASWQNTDLFEM
     280-280: Missing.
Note: Contains a phosphoserine at position 17.
Isoform 4 (identifier: P47736-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSGRKRSFTFGAYGGVDKSFTSRRSVWRSDGQNQHFPQALDLSRVNLVPSYTPSLYPKNTDLFEM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 663663Rap1 GTPase-activating protein 1
PRO_0000056743

Regions

Domain1 – 1717GoLoco
Domain181 – 397217Rap-GAP

Amino acid modifications

Modified residue4841Phosphoserine Ref.8
Modified residue4991Phosphoserine Ref.8

Natural variations

Alternative sequence11M → MAQLRPAVPPGRPRRGSLPA GASWQNTDLFEM in isoform 3.
VSP_040260
Alternative sequence11M → MSGRKRSFTFGAYGGVDKSF TSRRSVWRSDGQNQHFPQAL DLSRVNLVPSYTPSLYPKNT DLFEM in isoform 4.
VSP_047025
Alternative sequence2801Missing in isoform 3.
VSP_040261
Alternative sequence4761I → ISLLIPGKSASRFGRRGSAI GIGTVEE in isoform 2.
VSP_035256
Alternative sequence626 – 6338Missing in isoform 2.
VSP_035257
Natural variant1071A → T. Ref.1
Corresponds to variant rs2275363 [ dbSNP | Ensembl ].
VAR_047792
Natural variant2571C → R in a breast cancer sample; somatic mutation. Ref.14
VAR_035547
Natural variant6091Y → C in a breast cancer sample; somatic mutation. Ref.14
VAR_035548

Experimental info

Mutagenesis1001F → E: Impaired dimerization; when associated with E-173. Ref.12
Mutagenesis1731L → E: Impaired dimerization; when associated with E-100. Ref.12
Mutagenesis2071E → A: Reduces GTPase activation. Ref.12
Mutagenesis2671H → A: Abolishes GTPase activation. Ref.12
Mutagenesis2861R → A: Reduces GTPase activation. Ref.12
Mutagenesis2871H → A: Abolishes GTPase activation. Ref.12
Mutagenesis2901N → A or K: Abolishes GTPase activation. Ref.12
Mutagenesis2911D → A: Abolishes GTPase activation. Ref.12
Mutagenesis3881R → A or P: Reduces GTPase activation. Ref.12
Sequence conflict3041F → L in AAH54490. Ref.6

Secondary structure

................................................ 663
Helix Strand Turn

Details...

Sequences

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

Last modified November 25, 2008. Version 2.
Checksum: 89B307CC67F975DD

FASTA66373,361
        10         20         30         40         50         60 
MIEKMQGSRM DEQRCSFPPP LKTEEDYIPY PSVHEVLGRE GPFPLILLPQ FGGYWIEGTN 

        70         80         90        100        110        120 
HEITSIPETE PLQSPTTKVK LECNPTARIY RKHFLGKEHF NYYSLDAALG HLVFSLKYDV 

       130        140        150        160        170        180 
IGDQEHLRLL LRTKCRTYHD VIPISCLTEF PNVVQMAKLV CEDVNVDRFY PVLYPKASRL 

       190        200        210        220        230        240 
IVTFDEHVIS NNFKFGVIYQ KLGQTSEEEL FSTNEESPAF VEFLEFLGQK VKLQDFKGFR 

       250        260        270        280        290        300 
GGLDVTHGQT GTESVYCNFR NKEIMFHVST KLPYTEGDAQ QLQRKRHIGN DIVAVVFQDE 

       310        320        330        340        350        360 
NTPFVPDMIA SNFLHAYVVV QAEGGGPDGP LYKVSVTARD DVPFFGPPLP DPAVFRKGPE 

       370        380        390        400        410        420 
FQEFLLTKLI NAEYACYKAE KFAKLEERTR AALLETLYEE LHIHSQSMMG LGGDEDKMEN 

       430        440        450        460        470        480 
GSGGGGFFES FKRVIRSRSQ SMDAMGLSNK KPNTVSTSHS GSFAPNNPDL AKAAGISLIV 

       490        500        510        520        530        540 
PGKSPTRKKS GPFGSRRSSA IGIENIQEVQ EKRESPPAGQ KTPDSGHVSQ EPKSENSSTQ 

       550        560        570        580        590        600 
SSPEMPTTKN RAETAAQRAE ALKDFSRSSS SASSFASVVE ETEGVDGEDT GLESVSSSGT 

       610        620        630        640        650        660 
PHKRDSFIYS TWLEDSVSTT SGGSSPGPSR SPHPDAGKLG DPACPEIKIQ LEASEQHMPQ 


LGC 

« Hide

Isoform 2 [UniParc].

Checksum: 7B2B680087CFCCB4
Show »

FASTA68175,187
Isoform 3 [UniParc].

Checksum: BEB784BF1F8E67F3
Show »

FASTA69376,592
Isoform 4 [UniParc].

Checksum: B106FC67B06E1615
Show »

FASTA72780,645

References

« Hide 'large scale' references
[1]"Molecular cloning of a GTPase activating protein specific for the Krev-1 protein p21rap1."
Rubinfeld B., Munemitsu S., Clark R., Conroy L., Watt K., Crosier W.J., McCormick F., Polakis P.
Cell 65:1033-1042(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-107.
Tissue: Brain.
[2]"Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"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. expand/collapse author list , 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].
[4]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].
[5]"Activation of the ERK/MAPK pathway by an isoform of rap1GAP associated with G alpha(i)."
Mochizuki N., Ohba Y., Kiyokawa E., Kurata T., Murakami Y., Ozaki Y., Kitakabe A., Nagashima K., Matsuda M.
Nature 400:891-894(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-100 (ISOFORM 3).
Tissue: Brain.
[6]"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: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Brain.
[7]"Human SPA-1 product selectively expressed in lymphoid tissues is a specific GTPase-activating protein for Rap1 and Rap2."
Kurachi H., Wada Y., Tsukamoto N., Maeda M., Kubota H., Hattori M., Iwai K., Minato N.
J. Biol. Chem. 272:28081-28088(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND SER-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"The GTPase-activating protein Rap1GAP uses a catalytic asparagine."
Daumke O., Weyand M., Chakrabarti P.P., Vetter I.R., Wittinghofer A.
Nature 429:197-201(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 75-415, FUNCTION, SUBUNIT, MUTAGENESIS OF PHE-100; LEU-173; GLU-207; HIS-267; ARG-286; HIS-287; ASN-290; ASP-291 AND ARG-388.
[13]"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 RAP1B, SUBUNIT.
[14]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-257 AND CYS-609.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64788 mRNA. Translation: AAA60252.1.
AB007943 mRNA. Translation: BAA32319.3. Different initiation.
AL359815 Genomic DNA. Translation: CAI16250.1.
AL359815 Genomic DNA. Translation: CAI16255.1.
CH471134 Genomic DNA. Translation: EAW94980.1.
CH471134 Genomic DNA. Translation: EAW94981.1.
AB003930 mRNA. Translation: BAA83674.1.
BC054490 mRNA. Translation: AAH54490.1. Different initiation.
CCDSCCDS218.1. [P47736-1]
CCDS53276.1. [P47736-2]
CCDS53277.1. [P47736-4]
PIRA39897.
B39897.
RefSeqNP_001139129.1. NM_001145657.1. [P47736-2]
NP_001139130.1. NM_001145658.1. [P47736-4]
NP_002876.2. NM_002885.2. [P47736-1]
UniGeneHs.148178.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SRQX-ray2.90A/B/C/D75-415[»]
3BRWX-ray3.40A/B/C75-415[»]
ProteinModelPortalP47736.
SMRP47736. Positions 78-414.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111844. 14 interactions.
IntActP47736. 9 interactions.
MINTMINT-3308298.
STRING9606.ENSP00000363897.

PTM databases

PhosphoSiteP47736.

Polymorphism databases

DMDM215273877.

Proteomic databases

MaxQBP47736.
PaxDbP47736.
PRIDEP47736.

Protocols and materials databases

DNASU5909.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290101; ENSP00000290101; ENSG00000076864. [P47736-4]
ENST00000374765; ENSP00000363897; ENSG00000076864. [P47736-1]
ENST00000542643; ENSP00000441661; ENSG00000076864. [P47736-2]
ENST00000599760; ENSP00000470945; ENSG00000076864.
GeneID5909.
KEGGhsa:5909.
UCSCuc001bev.3. human. [P47736-1]
uc001bey.3. human. [P47736-2]

Organism-specific databases

CTD5909.
GeneCardsGC01M021922.
HGNCHGNC:9858. RAP1GAP.
HPACAB003851.
HPA001922.
MIM600278. gene.
neXtProtNX_P47736.
PharmGKBPA34220.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292109.
HOGENOMHOG000231640.
HOVERGENHBG016371.
KOK17700.
OrthoDBEOG7WHH8V.
PhylomeDBP47736.
TreeFamTF318626.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP47736.

Gene expression databases

ArrayExpressP47736.
BgeeP47736.
CleanExHS_RAP1GAP.
GenevestigatorP47736.

Family and domain databases

InterProIPR003109. GoLoco_motif.
IPR000331. Rap_GAP_dom.
[Graphical view]
PfamPF02188. GoLoco. 1 hit.
PF02145. Rap_GAP. 1 hit.
[Graphical view]
SMARTSM00390. GoLoco. 1 hit.
[Graphical view]
PROSITEPS50877. GOLOCO. 1 hit.
PS50085. RAPGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP47736.
GeneWikiRAP1GAP.
GenomeRNAi5909.
NextBio22986.
PROP47736.
SOURCESearch...

Entry information

Entry nameRPGP1_HUMAN
AccessionPrimary (citable) accession number: P47736
Secondary accession number(s): J3QSS6 expand/collapse secondary AC list , O75062, Q5T3S9, Q5T3T4, Q7Z5S8, Q9UQ51
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 123 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM