Reviewed, UniProtKB/Swiss-Prot P47736 (RPGP1_HUMAN)

Names and origin

Protein names

Recommended name:
    Rap1 GTPase-activating protein 1
      Short name=Rap1GAP1
      Short name=Rap1GAP

Gene names

Name:	RAP1GAP
Synonyms:	KIAA0474, RAP1GA1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	663 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Subunit structure	Homodimer and heterodimer with RAP1B. Ref.9
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.5
Induction	By 12-O-tetradecanoylphorbol-13-acetate (TPA) in promyelocytic HL-60 cells. Ref.5
Sequence similarities	Contains 1 GoLoco domain. Contains 1 Rap-GAP domain.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	GTPase activation
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	regulation of Ras GTPase activity Ref.9 Inferred from direct assay. Source: UniProtKB signal transduction Ref.1 Traceable author statement. Source: ProtInc
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTPase activator activity Ref.1 Traceable author statement. Source: ProtInc Ras GTPase binding Ref.9 Inferred from physical interaction. Source: UniProtKB protein homodimerization activity Ref.9 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 663

663

Rap1 GTPase-activating protein 1

PRO_0000056743

Regions

Domain

1 – 17

17

GoLoco

Domain

181 – 397

217

Rap-GAP

Amino acid modifications

Modified residue

262

1

N6-acetyllysine Ref.8

Modified residue

384

1

N6-acetyllysine Ref.8

Modified residue

441

1

Phosphoserine Ref.7

Modified residue

484

1

Phosphoserine Ref.6

Modified residue

499

1

Phosphoserine Ref.6

Natural variations

Alternative sequence

476

1

I → ISLLIPGKSASRFGRRGSAI GIGTVEE in isoform 2.

VSP_035256

Alternative sequence

626 – 633

8

Missing in isoform 2.

VSP_035257

Natural variant

107

1

A → T: dbSNP rs2275363. Ref.1

VAR_047792

Natural variant

257

1

C → R in a breast cancer sample; somatic mutation. Ref.10

VAR_035547

Natural variant

609

1

Y → C in a breast cancer sample; somatic mutation. Ref.10

VAR_035548

Secondary structure

1

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663

Helix Strand Turn

Details...

Helix

85 – 88

4

Helix

89 – 93

5

Turn

94 – 96

3

Beta strand

100 – 106

7

Turn

107 – 109

3

Beta strand

110 – 121

12

Beta strand

124 – 132

9

Beta strand

137 – 143

7

Helix

153 – 160

8

Helix

177 – 186

10

Beta strand

192 – 200

9

Helix

207 – 211

5

Helix

218 – 227

10

Beta strand

228 – 233

6

Beta strand

245 – 247

3

Beta strand

252 – 258

7

Beta strand

263 – 268

6

Helix

269 – 271

3

Helix

282 – 288

7

Beta strand

292 – 300

9

Helix

306 – 308

3

Beta strand

316 – 323

8

Beta strand

331 – 338

8

Beta strand

354 – 358

5

Helix

359 – 376

18

Helix

380 – 409

30

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 89B307CC67F975DD	FASTA	663	73,361
	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
	Isoform 2. Checksum: 7B2B680087CFCCB4	FASTA	681	75,187
	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 AKAAGISLLI 490 500 510 520 530 540 PGKSASRFGR RGSAIGIGTV EESLIVPGKS PTRKKSGPFG SRRSSAIGIE NIQEVQEKRE 550 560 570 580 590 600 SPPAGQKTPD SGHVSQEPKS ENSSTQSSPE MPTTKNRAET AAQRAEALKD FSRSSSSASS 610 620 630 640 650 660 FASVVEETEG VDGEDTGLES VSSSGTPHKR DSFIYSTWLE DSVSTTSGGS SPDAGKLGDP 670 680 ACPEIKIQLE ASEQHMPQLG C

References

	« Hide 'large scale' referencesShow '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: 1904317] [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: 9455484] [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: 16710414] [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. , 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]	"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: 9346962] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[6]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND SER-499, MASS SPECTROMETRY.
[7]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, MASS SPECTROMETRY. Tissue: T-cell.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-262 AND LYS-384, MASS SPECTROMETRY.
[9]	"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: 18309292] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-167 IN COMPLEX WITH RAP1B, SUBUNIT.
[10]	"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. , 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: 16959974] [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.
CH471134 Genomic DNA. Translation: EAW94980.1.

IPI

IPI00386930.
IPI00843926.

PIR

A39897.
B39897.

RefSeq

NP_001139129.1.
NP_002876.2.

UniGene

Hs.148178

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P47736. 2 interactions.

STRING

P47736.

PTM databases

PhosphoSite

P47736.

Proteomic databases

PRIDE

P47736.

Genome annotation databases

Ensembl

ENST00000374761; ENSP00000363893; ENSG00000076864; Homo sapiens. [Genome view]
ENST00000374765; ENSP00000363897; ENSG00000076864; Homo sapiens. [Genome view]

GeneID

5909.

KEGG

hsa:5909.

UCSC

uc001bex.1. human.

Organism-specific databases

CTD

5909.

GeneCards

GC01M021796.

H-InvDB

HIX0000226.

HGNC

HGNC:9858. RAP1GAP.

HPA

CAB003851.
HPA001922.

MIM

600278. gene.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG445308.

HOVERGEN

P47736.

PhylomeDB

P47736.

Gene expression databases

ArrayExpress

P47736.

Bgee

P47736.

CleanEx

HS_RAP1GAP.

Genevestigator

P47736.

GermOnline

ENSG00000076864. Homo sapiens.

Family and domain databases

InterPro

IPR003109. GoLoco_motif.
IPR000331. Rap_GAP.
[Graphical view]

Pfam

PF02188. GoLoco. 1 hit.
PF02145. Rap_GAP. 1 hit.
[Graphical view]

SMART

SM00390. GoLoco. 1 hit.
[Graphical view]

PROSITE

PS50877. GOLOCO. 1 hit.
PS50085. RAPGAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

22986.

SOURCE

Search...

Entry information

Entry name

RPGP1_HUMAN

Accession

Primary (citable) accession number: P47736
Secondary accession number(s): O75062, Q5T3T4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	November 25, 2008
Last modified:	January 19, 2010
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.