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Q8BXK8 (AGAP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1

Short name=AGAP-1
Alternative name(s):
Centaurin-gamma-2
Short name=Cnt-g2
Gene names
Name:Agap1
Synonyms:Centg2, Kiaa1099
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length857 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

GTPase-activating protein for ARF1 and, to a lesser extent, ARF5. Directly and specifically regulates the adapter protein 3 (AP-3)-dependent trafficking of proteins in the endosomal-lysosomal system By similarity.

Enzyme regulation

GAP activity stimulated by phosphatidylinositol 3,4,5-trisphosphate (PIP3) and, to a lesser extent, by phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidic acid potentiates PIP2 stimulation By similarity.

Subunit structure

Homodimer. Interacts with several subunits of the AP-3 protein complex: AP3M1, AP3S1 and AP3S2. Interacts with GUCY1A3 and GUCY1B3 By similarity.

Subcellular location

Cytoplasm By similarity. Note: Associates with the endocytic compartment By similarity.

Tissue specificity

Widely expressed, with highest levels in brain and kidney. Ref.5

Developmental stage

At 12.5 dpc, expression is restricted to neural tube, forebrain and midbrain. Ref.4

Domain

The PH domain mediates AP-3 binding.

Post-translational modification

Phosphorylated on tyrosines By similarity.

Sequence similarities

Belongs to the centaurin gamma-like family.

Contains 2 ANK repeats.

Contains 1 Arf-GAP domain.

Contains 1 PH domain.

Sequence caution

The sequence BAC98099.2 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 857857Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1
PRO_0000074219

Regions

Domain346 – 588243PH
Domain609 – 729121Arf-GAP
Repeat768 – 79730ANK 1
Repeat801 – 83030ANK 2
Nucleotide binding78 – 858GTP Potential
Nucleotide binding122 – 1265GTP Potential
Nucleotide binding178 – 1814GTP Potential
Zinc finger624 – 64724C4-type
Region66 – 276211Small GTPase-like

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue8361Phosphothreonine By similarity

Experimental info

Sequence conflict4241K → R in BAC98099. Ref.2
Sequence conflict6681D → Y in BAC29078. Ref.1
Sequence conflict7001S → P in BAE27957. Ref.1
Sequence conflict8111Q → H in BAC29078. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BXK8 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A88AF73A4BB50815

FASTA85794,411
        10         20         30         40         50         60 
MNYQQQLANS AAIRAEIQRF ESVHPNIYSI YELLERVEEP VLQNQIREHV IAIEDAFVNS 

        70         80         90        100        110        120 
QEWTLSRSVP ELKVGIVGNL ASGKSALVHR YLTGTYVQEE SPEGGRFKKE IVVDGQSYLL 

       130        140        150        160        170        180 
LIRDEGGPPE AQFAMWVDAV IFVFSLEDEI SFQTVYHYYS RMANYRNTSE IPLVLVGTQD 

       190        200        210        220        230        240 
AISSTNPRVI DDVRARKLSN DLKRCTYYET CATYGLNVER VFQDVAQKIV ATRKKQQLSI 

       250        260        270        280        290        300 
GPCKSLPNSP SHSSVCSAQV SAVHISQTSN GGGSLSDYSS SVPSTPSTSQ KELRIDVPPT 

       310        320        330        340        350        360 
ANTPTPVRKQ SKRRSNLFTS RKGSDPDKEK KGLESRADSI GSGRAIPIKQ GMLLKRSGKS 

       370        380        390        400        410        420 
LNKEWKKKYV TLCDNGVLTY HPSLHDYMQN VHGKEIDLLR TTVKVPGKRP PRATSACAPI 

       430        440        450        460        470        480 
SSPKTNGLAK DMSSLHISPN SGNVTSASGS QMASGISLVS FNSRPDGMHQ RSYSVSSADQ 

       490        500        510        520        530        540 
WSDATVIANS AISSDTGLGD SVCSSPSISS STSPKLDPPP SPHANRKKHR RKKSTSNFKA 

       550        560        570        580        590        600 
DGLSGTAEEQ EENLEFIIVS LTGQTWHFEA TTYEERDAWV QAIESQILAS LQSCESSKNK 

       610        620        630        640        650        660 
SRLTSQSEAM ALQSIRNMRG NSHCVDCDTQ NPNWASLNLG ALMCIECSGI HRNLGTHLSR 

       670        680        690        700        710        720 
VRSLDLDDWP MELIKVMSSI GNELANSVWE EGSQGRTKPS LDSTREEKER WIRAKYEQKL 

       730        740        750        760        770        780 
FLAPLPCTEF SLGQQLLRAT AEEDLRTVIL LLAHGSRDEV NETCGEGDGR TALHLACRKG 

       790        800        810        820        830        840 
NVVLAQLLIW YGVDVMARDA HGNTALAYAR QASSQECIDV LLQYGCPDER FVLMATPNLS 

       850 
RKSNSRNNSS GRAPSVI 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Adrenal gland and Urinary bladder.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thymus.
[3]Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"GGAPs, a new family of bifunctional GTP-binding and GTPase-activating proteins."
Xia C., Ma W., Stafford L.J., Liu C., Gong L., Martin J.F., Liu M.
Mol. Cell. Biol. 23:2476-2488(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[5]"AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl cyclase."
Meurer S., Pioch S., Wagner K., Mueller-Esterl W., Gross S.
J. Biol. Chem. 279:49346-49354(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK035494 mRNA. Translation: BAC29078.1.
AK046523 mRNA. Translation: BAC32770.1.
AK147503 mRNA. Translation: BAE27957.1.
AK129289 mRNA. Translation: BAC98099.2. Different initiation.
RefSeqNP_001032213.1. NM_001037136.1.
NP_835220.1. NM_178119.3.
UniGeneMm.291135.

3D structure databases

ProteinModelPortalQ8BXK8.
SMRQ8BXK8. Positions 70-233, 344-422, 530-592, 615-854.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8BXK8.

Proteomic databases

PaxDbQ8BXK8.
PRIDEQ8BXK8.

Protocols and materials databases

DNASU347722.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027521; ENSMUSP00000027521; ENSMUSG00000055013.
GeneID347722.
KEGGmmu:347722.
UCSCuc007byw.1. mouse.

Organism-specific databases

CTD116987.
MGIMGI:2653690. Agap1.
RougeSearch...

Phylogenomic databases

eggNOGCOG5347.
GeneTreeENSGT00740000115470.
HOGENOMHOG000007233.
HOVERGENHBG054045.
InParanoidQ8BXK8.
KOK12491.
OMADGMQQRS.
OrthoDBEOG72VH5V.
TreeFamTF317762.

Gene expression databases

ArrayExpressQ8BXK8.
BgeeQ8BXK8.
GenevestigatorQ8BXK8.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
2.30.29.30. 2 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR013684. MIRO-like.
IPR027417. P-loop_NTPase.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF08477. Miro. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSPR00405. REVINTRACTNG.
SMARTSM00248. ANK. 2 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAGAP1. mouse.
NextBio400243.
PROQ8BXK8.
SOURCESearch...

Entry information

Entry nameAGAP1_MOUSE
AccessionPrimary (citable) accession number: Q8BXK8
Secondary accession number(s): Q3UHA0, Q6ZPX9, Q8BZG0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: March 19, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot