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Q15283 (RASA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras GTPase-activating protein 2
Alternative name(s):
GTPase-activating protein 1m
Short name=GAP1m
Gene names
Name:RASA2
Synonyms:GAP1M, RASGAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length850 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4).

Subcellular location

Cytoplasm. Cytoplasmperinuclear region.

Sequence similarities

Contains 1 Btk-type zinc finger.

Contains 2 C2 domains.

Contains 1 PH domain.

Contains 1 Ras-GAP domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15283-1)

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: Q15283-2)

The sequence of this isoform differs from the canonical sequence as follows:
     646-646: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 850849Ras GTPase-activating protein 2
PRO_0000056638

Regions

Domain25 – 12298C2 1
Domain158 – 273116C2 2
Domain356 – 550195Ras-GAP
Domain604 – 706103PH
Zinc finger708 – 74437Btk-type
Compositional bias2 – 2625Ala-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.8

Natural variations

Alternative sequence6461Missing in isoform 2.
VSP_046545

Experimental info

Sequence conflict2161T → A in BAA11230. Ref.1
Sequence conflict2251F → S in BAF84705. Ref.4
Sequence conflict6451G → EFIER in BAA11621. Ref.2

Sequences

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

Last modified June 26, 2013. Version 3.
Checksum: 1F357940CA106E5E

FASTA85096,614
        10         20         30         40         50         60 
MAAAAPAAAA ASSEAPAASA TAEPEAGDQD SREVRVLQSL RGKICEAKNL LPYLGPHKMR 

        70         80         90        100        110        120 
DCFCTINLDQ EEVYRTQVVE KSLSPFFSEE FYFEIPRTFQ YLSFYVYDKN VLQRDLRIGK 

       130        140        150        160        170        180 
VAIKKEDLCN HSGKETWFSL QPVDSNSEVQ GKVHLELKLN ELITENGTVC QQLVVHIKAC 

       190        200        210        220        230        240 
HGLPLINGQS CDPYATVSLV GPSRNDQKKT KVKKKTSNPQ FNEIFYFEVT RSSSYTRKSQ 

       250        260        270        280        290        300 
FQVEEEDIEK LEIRIDLWNN GNLVQDVFLG EIKVPVNVLR TDSSHQAWYL LQPRDNGNKS 

       310        320        330        340        350        360 
SKTDDLGSLR LNICYTEDYV LPSEYYGPLK TLLLKSPDVQ PISASAAYIL SEICRDKNDA 

       370        380        390        400        410        420 
VLPLVRLLLH HDKLVPFATA VAELDLKDTQ DANTIFRGNS LATRCLDEMM KIVGGHYLKV 

       430        440        450        460        470        480 
TLKPILDEIC DSSKSCEIDP IKLKEGDNVE NNKENLRYYV DKLFNTIVKS SMSCPTVMCD 

       490        500        510        520        530        540 
IFYSLRQMAT QRFPNDPHVQ YSAVSSFVFL RFFAVAVVSP HTFHLRPHHP DAQTIRTLTL 

       550        560        570        580        590        600 
ISKTIQTLGS WGSLSKSKSS FKETFMCEFF KMFQEEGYII AVKKFLDEIS STETKESSGT 

       610        620        630        640        650        660 
SEPVHLKEGE MYKRAQGRTR IGKKNFKKRW FCLTSRELTY HKQPGSKDAI YTIPVKNILA 

       670        680        690        700        710        720 
VEKLEESSFN KKNMFQVIHT EKPLYVQANN CVEANEWIDV LCRVSRCNQN RLSFYHPSVY 

       730        740        750        760        770        780 
LNGNWLCCQE TGENTLGCKP CTAGVPADIQ IDIDEDRETE RIYSLFTLSL LKLQKMEEAC 

       790        800        810        820        830        840 
GTIAVYQGPQ KEPDDYSNFV IEDSVTTFKT IQQIKSIIEK LDEPHEKYRK KRSSSAKYGS 

       850 
KENPIVGKAS 

« Hide

Isoform 2 [UniParc].

Checksum: A4B491DFF5C4CB76
Show »

FASTA84996,527

References

« Hide 'large scale' references
[1]"Human rasGTPase-activating protein (human counterpart of GAP1m): sequence of the cDNA, primary structure of the protein, production and chromosomal localization."
Kobayashi M., Masui T., Kusuda J., Kameoka Y., Hashimoto K., Iwashita S.
Gene 175:173-177(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[2]"cDNA cloning and chromosomal mapping of a novel human GAP (GAP1M), a GTPase-activating protein of Ras."
Li S., Satoh H., Watanabe T., Nakamura S., Hattori S.
Genomics 35:625-627(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"Distinct subcellular localisations of the putative inositol 1,3,4,5-tetrakisphosphate receptors GAP1(IP4BP) and GAP1m result from the GAP1(IP4BP) PH domain directing plasma membrane targeting."
Lockyer P.J., Bottomley J.R., Reynolds J.S., McNulty T.J., Venkateswarlu K., Potter B.V.L., Dempsey C.E., Cullen P.J.
Curr. Biol. 7:1007-1010(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Blood.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Spleen.
[5]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D78155 mRNA. Translation: BAA11230.1.
D78156 Genomic DNA. Translation: BAA11231.1.
D82880 mRNA. Translation: BAA11621.1.
D82881 Genomic DNA. Translation: BAA11622.1.
AF115573 mRNA. Translation: AAD09821.1.
AC010184 Genomic DNA. No translation available.
AC092977 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78999.1.
AK292016 mRNA. Translation: BAF84705.1.
CCDSCCDS3117.1. [Q15283-2]
PIRJC5047.
RefSeqNP_006497.2. NM_006506.2. [Q15283-2]
XP_005247745.1. XM_005247688.1. [Q15283-1]
UniGeneHs.655941.
Hs.98445.

3D structure databases

ProteinModelPortalQ15283.
SMRQ15283. Positions 30-598, 608-739.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111857. 3 interactions.
STRING9606.ENSP00000286364.

PTM databases

PhosphoSiteQ15283.

Polymorphism databases

DMDM519668674.

Proteomic databases

MaxQBQ15283.
PaxDbQ15283.
PRIDEQ15283.

Protocols and materials databases

DNASU5922.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286364; ENSP00000286364; ENSG00000155903. [Q15283-2]
ENST00000452898; ENSP00000391677; ENSG00000155903. [Q15283-1]
GeneID5922.
KEGGhsa:5922.
UCSCuc003etz.1. human. [Q15283-1]
uc003eua.1. human.

Organism-specific databases

CTD5922.
GeneCardsGC03P141205.
HGNCHGNC:9872. RASA2.
HPAHPA035374.
HPA035375.
MIM601589. gene.
neXtProtNX_Q15283.
PharmGKBPA34233.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG323905.
HOGENOMHOG000007183.
HOVERGENHBG055643.
InParanoidQ15283.
KOK08053.
OMAKPCTAGV.
OrthoDBEOG7J17Z6.
PhylomeDBQ15283.
TreeFamTF105302.

Gene expression databases

ArrayExpressQ15283.
BgeeQ15283.
CleanExHS_RASA2.
GenevestigatorQ15283.

Family and domain databases

Gene3D1.10.506.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 2 hits.
InterProIPR000008. C2_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR001936. RasGAP.
IPR023152. RasGAP_CS.
IPR008936. Rho_GTPase_activation_prot.
IPR001562. Znf_Btk_motif.
[Graphical view]
PfamPF00779. BTK. 1 hit.
PF00168. C2. 2 hits.
PF00169. PH. 1 hit.
PF00616. RasGAP. 1 hit.
[Graphical view]
PRINTSPR00402. TECBTKDOMAIN.
SMARTSM00107. BTK. 1 hit.
SM00239. C2. 2 hits.
SM00233. PH. 1 hit.
SM00323. RasGAP. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
SSF49562. SSF49562. 2 hits.
PROSITEPS50004. C2. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
PS51113. ZF_BTK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi5922.
NextBio23062.
PROQ15283.
SOURCESearch...

Entry information

Entry nameRASA2_HUMAN
AccessionPrimary (citable) accession number: Q15283
Secondary accession number(s): A8K7K1 expand/collapse secondary AC list , G3V0F9, O00695, Q15284, Q92594, Q99577, Q9UEQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: June 26, 2013
Last modified: July 9, 2014
This is version 125 of the entry and version 3 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM