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P47736

- RPGP1_HUMAN

UniProt

P47736 - RPGP1_HUMAN

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Protein

Rap1 GTPase-activating protein 1

Gene

RAP1GAP

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. protein homodimerization activity Source: UniProtKB
  4. Rap GTPase activator activity Source: UniProtKB
  5. Ras GTPase binding 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. cytosol Source: UniProtKB
  2. Golgi apparatus Source: UniProtKB-KW
  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 1PRO_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

BgeeiP47736.
CleanExiHS_RAP1GAP.
ExpressionAtlasiP47736. baseline and differential.
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. 15 interactions.
IntActiP47736. 9 interactions.
MINTiMINT-3308298.
STRINGi9606.ENSP00000363897.

Structurei

Secondary structure

1
663
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi85 – 884Combined sources
Helixi89 – 935Combined sources
Turni94 – 963Combined sources
Beta strandi100 – 1067Combined sources
Turni107 – 1093Combined sources
Beta strandi110 – 12112Combined sources
Beta strandi124 – 1329Combined sources
Beta strandi137 – 1437Combined sources
Helixi153 – 1608Combined sources
Helixi177 – 18610Combined sources
Beta strandi192 – 2009Combined sources
Helixi207 – 2115Combined sources
Helixi218 – 22710Combined sources
Beta strandi228 – 2336Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi252 – 2587Combined sources
Beta strandi263 – 2686Combined sources
Helixi269 – 2713Combined sources
Helixi282 – 2887Combined sources
Beta strandi292 – 3009Combined sources
Helixi306 – 3083Combined sources
Beta strandi316 – 3238Combined sources
Beta strandi327 – 3293Combined sources
Beta strandi331 – 3388Combined sources
Beta strandi354 – 3585Combined sources
Helixi359 – 37618Combined sources
Helixi380 – 40930Combined sources

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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47736.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 1717GoLocoPROSITE-ProRule annotationAdd
BLAST
Domaini181 – 397217Rap-GAPPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 GoLoco domain.PROSITE-ProRule annotation
Contains 1 Rap-GAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG292109.
GeneTreeiENSGT00760000119182.
HOGENOMiHOG000231640.
HOVERGENiHBG016371.
InParanoidiP47736.
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

        10         20         30         40         50
MIEKMQGSRM DEQRCSFPPP LKTEEDYIPY PSVHEVLGRE GPFPLILLPQ
60 70 80 90 100
FGGYWIEGTN HEITSIPETE PLQSPTTKVK LECNPTARIY RKHFLGKEHF
110 120 130 140 150
NYYSLDAALG HLVFSLKYDV IGDQEHLRLL LRTKCRTYHD VIPISCLTEF
160 170 180 190 200
PNVVQMAKLV CEDVNVDRFY PVLYPKASRL IVTFDEHVIS NNFKFGVIYQ
210 220 230 240 250
KLGQTSEEEL FSTNEESPAF VEFLEFLGQK VKLQDFKGFR GGLDVTHGQT
260 270 280 290 300
GTESVYCNFR NKEIMFHVST KLPYTEGDAQ QLQRKRHIGN DIVAVVFQDE
310 320 330 340 350
NTPFVPDMIA SNFLHAYVVV QAEGGGPDGP LYKVSVTARD DVPFFGPPLP
360 370 380 390 400
DPAVFRKGPE FQEFLLTKLI NAEYACYKAE KFAKLEERTR AALLETLYEE
410 420 430 440 450
LHIHSQSMMG LGGDEDKMEN GSGGGGFFES FKRVIRSRSQ SMDAMGLSNK
460 470 480 490 500
KPNTVSTSHS GSFAPNNPDL AKAAGISLIV PGKSPTRKKS GPFGSRRSSA
510 520 530 540 550
IGIENIQEVQ EKRESPPAGQ KTPDSGHVSQ EPKSENSSTQ SSPEMPTTKN
560 570 580 590 600
RAETAAQRAE ALKDFSRSSS SASSFASVVE ETEGVDGEDT GLESVSSSGT
610 620 630 640 650
PHKRDSFIYS TWLEDSVSTT SGGSSPGPSR SPHPDAGKLG DPACPEIKIQ
660
LEASEQHMPQ LGC
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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti304 – 3041F → L in AAH54490. (PubMed:15489334)Curated

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. 1 PublicationVSP_040260
Alternative sequencei1 – 11M → MSGRKRSFTFGAYGGVDKSF TSRRSVWRSDGQNQHFPQAL DLSRVNLVPSYTPSLYPKNT DLFEM in isoform 4. CuratedVSP_047025
Alternative sequencei280 – 2801Missing in isoform 3. 1 PublicationVSP_040261
Alternative sequencei476 – 4761I → ISLLIPGKSASRFGRRGSAI GIGTVEE in isoform 2. 1 PublicationVSP_035256
Alternative sequencei626 – 6338Missing in isoform 2. 1 PublicationVSP_035257

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

EnsembliENST00000374765; ENSP00000363897; ENSG00000076864. [P47736-1]
ENST00000495204; ENSP00000434033; ENSG00000076864. [P47736-4]
ENST00000542643; ENSP00000441661; ENSG00000076864. [P47736-2]
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. 15 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 ENST00000374765 ; ENSP00000363897 ; ENSG00000076864 . [P47736-1 ]
ENST00000495204 ; ENSP00000434033 ; ENSG00000076864 . [P47736-4 ]
ENST00000542643 ; ENSP00000441661 ; ENSG00000076864 . [P47736-2 ]
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.
GeneTreei ENSGT00760000119182.
HOGENOMi HOG000231640.
HOVERGENi HBG016371.
InParanoidi P47736.
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

Bgeei P47736.
CleanExi HS_RAP1GAP.
ExpressionAtlasi P47736. baseline and differential.
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: October 29, 2014
This is version 126 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