(data stored in ACNUC31183 zone)

SWISSPROT: RPGP2_HUMAN

ID   RPGP2_HUMAN             Reviewed;         730 AA.
AC   Q684P5; B2RTY5; Q684P4; Q6AI00; Q6ZVF0; Q9UPW2;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   07-JUN-2017, entry version 103.
DE   RecName: Full=Rap1 GTPase-activating protein 2;
DE            Short=Rap1GAP2;
DE   AltName: Full=GTPase-activating Rap/Ran-GAP domain-like protein 4;
GN   Name=RAP1GAP2; Synonyms=GARNL4, KIAA1039, RAP1GA2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION,
RP   PHOSPHORYLATION AT SER-7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND MUTAGENESIS OF SER-7 AND ASN-357.
RX   PubMed=15632203; DOI=10.1182/blood-2004-09-3605;
RA   Schultess J., Danielewski O., Smolenski A.P.;
RT   "Rap1GAP2 is a new GTPase-activating protein of Rap1 expressed in
RT   human platelets.";
RL   Blood 105:3185-3192(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Cervix;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 287-730.
RC   TISSUE=Brain;
RX   PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA   Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIV.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 6:197-205(1999).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND THR-49, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-49 AND SER-544,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558 AND SER-564, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: GTPase activator for the nuclear Ras-related regulatory
CC       protein RAP-1A (KREV-1), converting it to the putatively inactive
CC       GDP-bound state. {ECO:0000269|PubMed:15632203}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15632203}.
CC       Cytoplasm, perinuclear region {ECO:0000269|PubMed:15632203}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Rap1GAP2b;
CC         IsoId=Q684P5-1; Sequence=Displayed;
CC       Name=2; Synonyms=Rap1GAP2a;
CC         IsoId=Q684P5-2; Sequence=VSP_029889;
CC       Name=3; Synonyms=Rap1GAP2c;
CC         IsoId=Q684P5-3; Sequence=VSP_029888;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in
CC       platelets with isoform 2 being the predominant form. Expressed in
CC       lymphocytes, heart, testis and pancreas.
CC       {ECO:0000269|PubMed:15632203}.
CC   -!- PTM: In vitro phosphorylated by cGMP-dependent protein kinase 1
CC       (cGKI) at Ser-7; the phosphorylation probably does not regulate
CC       GAP activity. {ECO:0000269|PubMed:15632203}.
DR   EMBL; AJ628446; CAF31652.1; -; mRNA.
DR   EMBL; AJ628447; CAF31653.1; -; mRNA.
DR   EMBL; AK124640; BAC85912.1; -; mRNA.
DR   EMBL; CR627427; CAH10514.1; -; mRNA.
DR   EMBL; BC140870; AAI40871.1; -; mRNA.
DR   EMBL; BC140871; AAI40872.1; -; mRNA.
DR   EMBL; AB028962; BAA82991.1; -; mRNA.
DR   CCDS; CCDS45573.1; -. [Q684P5-1]
DR   CCDS; CCDS45574.1; -. [Q684P5-2]
DR   CCDS; CCDS82035.1; -. [Q684P5-3]
DR   RefSeq; NP_001093868.1; NM_001100398.1. [Q684P5-2]
DR   RefSeq; NP_001316987.1; NM_001330058.1. [Q684P5-3]
DR   RefSeq; NP_055900.4; NM_015085.4. [Q684P5-1]
DR   RefSeq; XP_011522043.1; XM_011523741.2. [Q684P5-3]
DR   RefSeq; XP_016879859.1; XM_017024370.1. [Q684P5-3]
DR   UniGene; Hs.499659; -.
DR   ProteinModelPortal; Q684P5; -.
DR   SMR; Q684P5; -.
DR   BioGrid; 116732; 3.
DR   IntAct; Q684P5; 4.
DR   STRING; 9606.ENSP00000254695; -.
DR   iPTMnet; Q684P5; -.
DR   PhosphoSitePlus; Q684P5; -.
DR   BioMuta; RAP1GAP2; -.
DR   DMDM; 162416269; -.
DR   EPD; Q684P5; -.
DR   MaxQB; Q684P5; -.
DR   PaxDb; Q684P5; -.
DR   PeptideAtlas; Q684P5; -.
DR   PRIDE; Q684P5; -.
DR   Ensembl; ENST00000254695; ENSP00000254695; ENSG00000132359. [Q684P5-1]
DR   Ensembl; ENST00000366401; ENSP00000389824; ENSG00000132359. [Q684P5-2]
DR   Ensembl; ENST00000540393; ENSP00000439688; ENSG00000132359. [Q684P5-3]
DR   Ensembl; ENST00000542807; ENSP00000444890; ENSG00000132359. [Q684P5-1]
DR   GeneID; 23108; -.
DR   KEGG; hsa:23108; -.
DR   UCSC; uc010ckd.4; human. [Q684P5-1]
DR   CTD; 23108; -.
DR   DisGeNET; 23108; -.
DR   GeneCards; RAP1GAP2; -.
DR   H-InvDB; HIX0013424; -.
DR   H-InvDB; HIX0039496; -.
DR   HGNC; HGNC:29176; RAP1GAP2.
DR   HPA; HPA022148; -.
DR   HPA; HPA022896; -.
DR   neXtProt; NX_Q684P5; -.
DR   OpenTargets; ENSG00000132359; -.
DR   PharmGKB; PA165432528; -.
DR   eggNOG; KOG3686; Eukaryota.
DR   eggNOG; ENOG410XTIX; LUCA.
DR   GeneTree; ENSGT00760000119182; -.
DR   HOGENOM; HOG000231640; -.
DR   HOVERGEN; HBG016371; -.
DR   InParanoid; Q684P5; -.
DR   KO; K17708; -.
DR   OrthoDB; EOG091G028T; -.
DR   PhylomeDB; Q684P5; -.
DR   TreeFam; TF318626; -.
DR   Reactome; R-HSA-392517; Rap1 signalling.
DR   ChiTaRS; RAP1GAP2; human.
DR   GeneWiki; RAP1GAP2; -.
DR   GenomeRNAi; 23108; -.
DR   PRO; PR:Q684P5; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000132359; -.
DR   CleanEx; HS_GARNL4; -.
DR   ExpressionAtlas; Q684P5; baseline and differential.
DR   Genevisible; Q684P5; HS.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IGI:GO_Central.
DR   GO; GO:0005096; F:GTPase activator activity; EXP:Reactome.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:0008361; P:regulation of cell size; IMP:GO_Central.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR000331; Rap_GAP_dom.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   SUPFAM; SSF111347; SSF111347; 1.
DR   PROSITE; PS50085; RAPGAP; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q684P5.
DR   SWISS-2DPAGE; Q684P5.
KW   Alternative splicing; Complete proteome; Cytoplasm; GTPase activation;
KW   Phosphoprotein; Polymorphism; Reference proteome.
FT   CHAIN         1    730       Rap1 GTPase-activating protein 2.
FT                                /FTId=PRO_0000312716.
FT   DOMAIN      248    464       Rap-GAP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00165}.
FT   COMPBIAS    586    726       Ser-rich.
FT   MOD_RES       7      7       Phosphoserine; by PKG/PRKG1; in vitro.
FT                                {ECO:0000269|PubMed:15632203}.
FT   MOD_RES      45     45       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332}.
FT   MOD_RES      49     49       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332}.
FT   MOD_RES     507    507       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q5SVL6}.
FT   MOD_RES     544    544       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:19690332}.
FT   MOD_RES     558    558       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     564    564       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     612    612       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q5SVL6}.
FT   MOD_RES     613    613       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q5SVL6}.
FT   VAR_SEQ       1     19       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_029888.
FT   VAR_SEQ      68     82       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15632203}.
FT                                /FTId=VSP_029889.
FT   VARIANT     202    202       L -> M (in dbSNP:rs17762452).
FT                                /FTId=VAR_037553.
FT   MUTAGEN       7      7       S->A: Abolishes phosphorylation by
FT                                PKG/PRKG1. {ECO:0000269|PubMed:15632203}.
FT   MUTAGEN     357    357       N->A: Abolishes GAP activity.
FT                                {ECO:0000269|PubMed:15632203}.
FT   CONFLICT    285    285       P -> L (in Ref. 2; BAC85912).
FT                                {ECO:0000305}.
FT   CONFLICT    304    304       K -> N (in Ref. 1; CAF31652/CAF31653).
FT                                {ECO:0000305}.
FT   CONFLICT    726    726       S -> P (in Ref. 3; CAH10514).
FT                                {ECO:0000305}.
SQ   SEQUENCE   730 AA;  80056 MW;  8E7584ADC2DA0B08 CRC64;
     MFGRKRSVSF GGFGWIDKTM LASLKVKKQE LANSSDATLP DRPLSPPLTA PPTMKSSEFF
     EMLEKMQGIK LEEQKPGPQK NKDDYIPYPS IDEVVEKGGP YPQVILPQFG GYWIEDPENV
     GTPTSLGSSI CEEEEEDNLS PNTFGYKLEC KGEARAYRRH FLGKDHLNFY CTGSSLGNLI
     LSVKCEEAEG IEYLRVILRS KLKTVHERIP LAGLSKLPSV PQIAKAFCDD AVGLRFNPVL
     YPKASQMIVS YDEHEVNNTF KFGVIYQKAR QTLEEELFGN NEESPAFKEF LDLLGDTITL
     QDFKGFRGGL DVTHGQTGVE SVYTTFRDRE IMFHVSTKLP FTDGDAQQLQ RKRHIGNDIV
     AIIFQEENTP FVPDMIASNF LHAYIVVQVE TPGTETPSYK VSVTAREDVP TFGPPLPSPP
     VFQKGPEFRE FLLTKLTNAE NACCKSDKFA KLEDRTRAAL LDNLHDELHA HTQAMLGLGP
     EEDKFENGGH GGFLESFKRA IRVRSHSMET MVGGQKKSHS GGIPGSLSGG ISHNSMEVTK
     TTFSPPVVAA TVKNQSRSPI KRRSGLFPRL HTGSEGQGDS RARCDSTSST PKTPDGGHSS
     QEIKSETSSN PSSPEICPNK EKPFMKLKEN GRAISRSSSS TSSVSSTAGE GEAMEEGDSG
     GSQPSTTSPF KQEVFVYSPS PSSESPSLGA AATPIIMSRS PTDAKSRNSP RSNLKFRFDK
     LSHASSGAGH
//

If you have problems or comments...

PBIL Back to PBIL home page