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P47736

- RPGP1_HUMAN

UniProt

P47736 - RPGP1_HUMAN

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Protein
Rap1 GTPase-activating protein 1
Gene
RAP1GAP, KIAA0474, RAP1GA1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. GTPase activator activity Source: ProtInc
  2. GTPase activity Source: UniProtKB
  3. Rap GTPase activator activity Source: UniProtKB
  4. Ras GTPase binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. positive regulation of Rap GTPase activity Source: UniProtKB
  3. regulation of Ras GTPase activity Source: UniProtKB
  4. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_23898. Rap1 signalling.
SignaLinkiP47736.

Names & Taxonomyi

Protein namesi
Recommended name:
Rap1 GTPase-activating protein 1
Short name:
Rap1GAP
Short name:
Rap1GAP1
Gene namesi
Name:RAP1GAP
Synonyms:KIAA0474, RAP1GA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9858. RAP1GAP.

Subcellular locationi

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. cytosol Source: UniProtKB
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001F → E: Impaired dimerization; when associated with E-173. 1 Publication
Mutagenesisi173 – 1731L → E: Impaired dimerization; when associated with E-100. 1 Publication
Mutagenesisi207 – 2071E → A: Reduces GTPase activation. 1 Publication
Mutagenesisi267 – 2671H → A: Abolishes GTPase activation. 1 Publication
Mutagenesisi286 – 2861R → A: Reduces GTPase activation. 1 Publication
Mutagenesisi287 – 2871H → A: Abolishes GTPase activation. 1 Publication
Mutagenesisi290 – 2901N → A or K: Abolishes GTPase activation. 1 Publication
Mutagenesisi291 – 2911D → A: Abolishes GTPase activation. 1 Publication
Mutagenesisi388 – 3881R → A or P: Reduces GTPase activation. 1 Publication

Organism-specific databases

PharmGKBiPA34220.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 663663Rap1 GTPase-activating protein 1
PRO_0000056743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei484 – 4841Phosphoserine1 Publication
Modified residuei499 – 4991Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP47736.
PaxDbiP47736.
PRIDEiP47736.

PTM databases

PhosphoSiteiP47736.

Expressioni

Tissue specificityi

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.1 Publication

Inductioni

By 12-O-tetradecanoylphorbol-13-acetate (TPA) in promyelocytic HL-60 cells.1 Publication

Gene expression databases

ArrayExpressiP47736.
BgeeiP47736.
CleanExiHS_RAP1GAP.
GenevestigatoriP47736.

Organism-specific databases

HPAiCAB003851.
HPA001922.

Interactioni

Subunit structurei

Homodimer and heterodimer with RAP1B.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAP1BP612243EBI-722307,EBI-358143

Protein-protein interaction databases

BioGridi111844. 14 interactions.
IntActiP47736. 9 interactions.
MINTiMINT-3308298.
STRINGi9606.ENSP00000363897.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi85 – 884
Helixi89 – 935
Turni94 – 963
Beta strandi100 – 1067
Turni107 – 1093
Beta strandi110 – 12112
Beta strandi124 – 1329
Beta strandi137 – 1437
Helixi153 – 1608
Helixi177 – 18610
Beta strandi192 – 2009
Helixi207 – 2115
Helixi218 – 22710
Beta strandi228 – 2336
Beta strandi245 – 2473
Beta strandi252 – 2587
Beta strandi263 – 2686
Helixi269 – 2713
Helixi282 – 2887
Beta strandi292 – 3009
Helixi306 – 3083
Beta strandi316 – 3238
Beta strandi327 – 3293
Beta strandi331 – 3388
Beta strandi354 – 3585
Helixi359 – 37618
Helixi380 – 40930

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SRQX-ray2.90A/B/C/D75-415[»]
3BRWX-ray3.40A/B/C75-415[»]
ProteinModelPortaliP47736.
SMRiP47736. Positions 78-414.

Miscellaneous databases

EvolutionaryTraceiP47736.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 1717GoLoco
Add
BLAST
Domaini181 – 397217Rap-GAP
Add
BLAST

Sequence similaritiesi

Contains 1 GoLoco domain.
Contains 1 Rap-GAP domain.

Phylogenomic databases

eggNOGiNOG292109.
HOGENOMiHOG000231640.
HOVERGENiHBG016371.
KOiK17700.
OrthoDBiEOG7WHH8V.
PhylomeDBiP47736.
TreeFamiTF318626.

Family and domain databases

InterProiIPR003109. GoLoco_motif.
IPR000331. Rap_GAP_dom.
[Graphical view]
PfamiPF02188. GoLoco. 1 hit.
PF02145. Rap_GAP. 1 hit.
[Graphical view]
SMARTiSM00390. GoLoco. 1 hit.
[Graphical view]
PROSITEiPS50877. GOLOCO. 1 hit.
PS50085. RAPGAP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P47736-1) [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

MIEKMQGSRM DEQRCSFPPP LKTEEDYIPY PSVHEVLGRE GPFPLILLPQ    50
FGGYWIEGTN HEITSIPETE PLQSPTTKVK LECNPTARIY RKHFLGKEHF 100
NYYSLDAALG HLVFSLKYDV IGDQEHLRLL LRTKCRTYHD VIPISCLTEF 150
PNVVQMAKLV CEDVNVDRFY PVLYPKASRL IVTFDEHVIS NNFKFGVIYQ 200
KLGQTSEEEL FSTNEESPAF VEFLEFLGQK VKLQDFKGFR GGLDVTHGQT 250
GTESVYCNFR NKEIMFHVST KLPYTEGDAQ QLQRKRHIGN DIVAVVFQDE 300
NTPFVPDMIA SNFLHAYVVV QAEGGGPDGP LYKVSVTARD DVPFFGPPLP 350
DPAVFRKGPE FQEFLLTKLI NAEYACYKAE KFAKLEERTR AALLETLYEE 400
LHIHSQSMMG LGGDEDKMEN GSGGGGFFES FKRVIRSRSQ SMDAMGLSNK 450
KPNTVSTSHS GSFAPNNPDL AKAAGISLIV PGKSPTRKKS GPFGSRRSSA 500
IGIENIQEVQ EKRESPPAGQ KTPDSGHVSQ EPKSENSSTQ SSPEMPTTKN 550
RAETAAQRAE ALKDFSRSSS SASSFASVVE ETEGVDGEDT GLESVSSSGT 600
PHKRDSFIYS TWLEDSVSTT SGGSSPGPSR SPHPDAGKLG DPACPEIKIQ 650
LEASEQHMPQ LGC 663
Length:663
Mass (Da):73,361
Last modified:November 25, 2008 - v2
Checksum:i89B307CC67F975DD
GO
Isoform 2 (identifier: P47736-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     476-476: I → ISLLIPGKSASRFGRRGSAIGIGTVEE
     626-633: Missing.

Show »
Length:681
Mass (Da):75,187
Checksum:i7B2B680087CFCCB4
GO
Isoform 3 (identifier: P47736-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:693
Mass (Da):76,592
Checksum:iBEB784BF1F8E67F3
GO
Isoform 4 (identifier: P47736-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSGRKRSFTFGAYGGVDKSFTSRRSVWRSDGQNQHFPQALDLSRVNLVPSYTPSLYPKNTDLFEM

Note: No experimental confirmation available.

Show »
Length:727
Mass (Da):80,645
Checksum:iB106FC67B06E1615
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071A → T.1 Publication
Corresponds to variant rs2275363 [ dbSNP | Ensembl ].
VAR_047792
Natural varianti257 – 2571C → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_035547
Natural varianti609 – 6091Y → C in a breast cancer sample; somatic mutation. 1 Publication
VAR_035548

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MAQLRPAVPPGRPRRGSLPA GASWQNTDLFEM in isoform 3.
VSP_040260
Alternative sequencei1 – 11M → MSGRKRSFTFGAYGGVDKSF TSRRSVWRSDGQNQHFPQAL DLSRVNLVPSYTPSLYPKNT DLFEM in isoform 4.
VSP_047025
Alternative sequencei280 – 2801Missing in isoform 3.
VSP_040261
Alternative sequencei476 – 4761I → ISLLIPGKSASRFGRRGSAI GIGTVEE in isoform 2.
VSP_035256
Alternative sequencei626 – 6338Missing in isoform 2.
VSP_035257

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti304 – 3041F → L in AAH54490. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS218.1. [P47736-1]
CCDS53276.1. [P47736-2]
CCDS53277.1. [P47736-4]
PIRiA39897.
B39897.
RefSeqiNP_001139129.1. NM_001145657.1. [P47736-2]
NP_001139130.1. NM_001145658.1. [P47736-4]
NP_002876.2. NM_002885.2. [P47736-1]
UniGeneiHs.148178.

Genome annotation databases

EnsembliENST00000290101; ENSP00000290101; ENSG00000076864. [P47736-4]
ENST00000374765; ENSP00000363897; ENSG00000076864. [P47736-1]
ENST00000542643; ENSP00000441661; ENSG00000076864. [P47736-2]
ENST00000599760; ENSP00000470945; ENSG00000076864.
GeneIDi5909.
KEGGihsa:5909.
UCSCiuc001bev.3. human. [P47736-1]
uc001bew.3. human.
uc001bey.3. human. [P47736-2]

Polymorphism databases

DMDMi215273877.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS218.1. [P47736-1 ]
CCDS53276.1. [P47736-2 ]
CCDS53277.1. [P47736-4 ]
PIRi A39897.
B39897.
RefSeqi NP_001139129.1. NM_001145657.1. [P47736-2 ]
NP_001139130.1. NM_001145658.1. [P47736-4 ]
NP_002876.2. NM_002885.2. [P47736-1 ]
UniGenei Hs.148178.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SRQ X-ray 2.90 A/B/C/D 75-415 [» ]
3BRW X-ray 3.40 A/B/C 75-415 [» ]
ProteinModelPortali P47736.
SMRi P47736. Positions 78-414.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111844. 14 interactions.
IntActi P47736. 9 interactions.
MINTi MINT-3308298.
STRINGi 9606.ENSP00000363897.

PTM databases

PhosphoSitei P47736.

Polymorphism databases

DMDMi 215273877.

Proteomic databases

MaxQBi P47736.
PaxDbi P47736.
PRIDEi P47736.

Protocols and materials databases

DNASUi 5909.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000290101 ; ENSP00000290101 ; ENSG00000076864 . [P47736-4 ]
ENST00000374765 ; ENSP00000363897 ; ENSG00000076864 . [P47736-1 ]
ENST00000542643 ; ENSP00000441661 ; ENSG00000076864 . [P47736-2 ]
ENST00000599760 ; ENSP00000470945 ; ENSG00000076864 .
GeneIDi 5909.
KEGGi hsa:5909.
UCSCi uc001bev.3. human. [P47736-1 ]
uc001bew.3. human.
uc001bey.3. human. [P47736-2 ]

Organism-specific databases

CTDi 5909.
GeneCardsi GC01M021922.
HGNCi HGNC:9858. RAP1GAP.
HPAi CAB003851.
HPA001922.
MIMi 600278. gene.
neXtProti NX_P47736.
PharmGKBi PA34220.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292109.
HOGENOMi HOG000231640.
HOVERGENi HBG016371.
KOi K17700.
OrthoDBi EOG7WHH8V.
PhylomeDBi P47736.
TreeFami TF318626.

Enzyme and pathway databases

Reactomei REACT_23898. Rap1 signalling.
SignaLinki P47736.

Miscellaneous databases

EvolutionaryTracei P47736.
GeneWikii RAP1GAP.
GenomeRNAii 5909.
NextBioi 22986.
PROi P47736.
SOURCEi Search...

Gene expression databases

ArrayExpressi P47736.
Bgeei P47736.
CleanExi HS_RAP1GAP.
Genevestigatori P47736.

Family and domain databases

InterProi IPR003109. GoLoco_motif.
IPR000331. Rap_GAP_dom.
[Graphical view ]
Pfami PF02188. GoLoco. 1 hit.
PF02145. Rap_GAP. 1 hit.
[Graphical view ]
SMARTi SM00390. GoLoco. 1 hit.
[Graphical view ]
PROSITEi PS50877. GOLOCO. 1 hit.
PS50085. RAPGAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-257 AND CYS-609.

Entry informationi

Entry nameiRPGP1_HUMAN
AccessioniPrimary (citable) accession number: P47736
Secondary accession number(s): J3QSS6
, O75062, Q5T3S9, Q5T3T4, Q7Z5S8, Q9UQ51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 25, 2008
Last modified: September 3, 2014
This is version 124 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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