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Q9QWY8 (ASAP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
Alternative name(s):
130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein
ADP-ribosylation factor-directed GTPase-activating protein 1
Short name=ARF GTPase-activating protein 1
Development and differentiation-enhancing factor 1
Short name=DEF-1
Short name=Differentiation-enhancing factor 1
PIP2-dependent ARF1 GAP
Gene names
Name:Asap1
Synonyms:Ddef1, Kiaa1249, Shag1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1147 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Plays a role in ciliogenesis By similarity. Posseses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2.

Enzyme regulation

Activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2).

Subunit structure

Homodimer. Interacts with SRC and CRK. Interacts with RAB11FIP3. Interacts with PTK2B/PYK2. Ref.7 Ref.10

Subcellular location

Cytoplasm. Membrane. Note: Predominantly cytoplasmic. Partially membrane-associated.

Tissue specificity

Expressed in all tissues examined but a most abundant expression was found in the testis, brain, lung and spleen. A heightened expression was seen in the adipose tissue from obese (ob) and diabetic (db) animals. Ref.6

Domain

The PH domain most probably contributes to the phosphoinositide-dependent regulation of ADP ribosylation factors.

Post-translational modification

Phosphorylated on tyrosine residues by SRC. Ref.7

Sequence similarities

Contains 2 ANK repeats.

Contains 1 Arf-GAP domain.

Contains 1 PH domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AAH02201.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH48818.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARF1P840802EBI-698498,EBI-449051From a different organism.
SRCP005233EBI-698524,EBI-848039From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9QWY8-1)

Also known as: SHAG1a; ASAP1a;

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: Q9QWY8-2)

Also known as: SHAG1b; ASAP1b;

The sequence of this isoform differs from the canonical sequence as follows:
     816-872: Missing.
Isoform 3 (identifier: Q9QWY8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     304-315: Missing.
Isoform 4 (identifier: Q9QWY8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     304-318: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11471147Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
PRO_0000074197

Regions

Domain339 – 43193PH
Domain454 – 577124Arf-GAP
Repeat615 – 64733ANK 1
Repeat651 – 68030ANK 2
Domain1085 – 114763SH3
Zinc finger469 – 49224C4-type
Compositional bias798 – 1011214Pro-rich

Amino acid modifications

Modified residue3081Phosphotyrosine; by FAK2 Ref.7
Modified residue7321Phosphoserine Ref.9
Modified residue8581Phosphoserine Ref.8
Modified residue10261Phosphoserine By similarity
Modified residue10451Phosphoserine By similarity

Natural variations

Alternative sequence304 – 31815Missing in isoform 4.
VSP_008367
Alternative sequence304 – 31512Missing in isoform 3.
VSP_008366
Alternative sequence816 – 87257Missing in isoform 2.
VSP_008368

Experimental info

Mutagenesis8111R → A: Significant reduction in binding to SRC and CRK and loss of phosphorylation. Loss of binding and phosphorylation; when associated with A-910 and A-913. Ref.1
Mutagenesis9101P → A: Significant reduction in binding to SRC and CRK and decrease in phosphorylation; when associated with A-913. Loss of binding and phosphorylation; when associated with A-811 and A-913. Ref.1
Mutagenesis9131P → A: Significant reduction in binding to SRC and CRK and decrease in phosphorylation; when associated with A-910. Loss of binding and phosphorylation; when associated with A-811 and A-910. Ref.1
Sequence conflict6541T → S in AAB82338. Ref.5
Sequence conflict8791L → S in AAC98349. Ref.1
Sequence conflict8791L → S in AAC98350. Ref.1
Sequence conflict10511R → I in AAB82338. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SHAG1a) (ASAP1a) [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 12950D1C4F49A909

FASTA1,147127,421
        10         20         30         40         50         60 
MRSSASRLSS FSSRDSLWNR MPDQISVSEF IAETTEDYNS PTTSSFTTRL HNCRNTVTLL 

        70         80         90        100        110        120 
EEALDQDRTA LQKVKKSVKA IYNSGQDHVQ NEENYAQVLD KFGSNFLSRD NPDLGTAFVK 

       130        140        150        160        170        180 
FSTLTKELST LLKNLLQGLS HNVIFTLDSL LKGDLKGVKG DLKKPFDKAW KDYETKFTKI 

       190        200        210        220        230        240 
EKEKREHAKQ HGMIRTEITG AEIAEEMEKE RRLFQLQMCE YLIKVNEIKT KKGVDLLQNL 

       250        260        270        280        290        300 
IKYYHAQCNF FQDGLKTADK LKQYIEKLAA DLYNIKQTQD EEKKQLTALR DLIKSSLQLD 

       310        320        330        340        350        360 
PKEVGGLYVA SRANSSRRDS QSRQGGYSMH QLQGNKEYGS EKKGFLLKKS DGIRKVWQRR 

       370        380        390        400        410        420 
KCAVKNGILT ISHATSNRQP AKLNLLTCQV KPNAEDKKSF DLISHNRTYH FQAEDEQDYI 

       430        440        450        460        470        480 
AWISVLTNSK EEALTMAFRG EQSTGENSLE DLTKAIIEDV QRLPGNDICC DCGSSEPTWL 

       490        500        510        520        530        540 
STNLGILTCI ECSGIHREMG VHISRIQSLE LDKLGTSELL LAKNVGNNSF NDIMEANLPS 

       550        560        570        580        590        600 
PSPKPTPSSD MTVRKEYITA KYVDHRFSRK TCASSSAKLN ELLEAIKSRD LLALIQVYAE 

       610        620        630        640        650        660 
GVELMEPLLE PGQELGETAL HLAVRTADQT SLHLVDFLVQ NCGNLDKQTS VGNTVLHYCS 

       670        680        690        700        710        720 
MYGKPECLKL LLRSKPTVDI VNQNGETALD IAKRLKATQC EDLLSQAKSG KFNPHVHVEY 

       730        740        750        760        770        780 
EWNLRQDEMD ESDDDLDDKP SPIKKERSPR PQSFCHSSSI SPQDKLALPG FSTPRDKQRL 

       790        800        810        820        830        840 
SYGAFTNQIF ASTSTDLPTS PTSEAPPLPP RNAGKGPTGP PSTLPLGTQT SSGSSTLSKK 

       850        860        870        880        890        900 
RPPPPPPGHK RTLSDPPSPL PHGPPNKGAI PWGNDVGPLS SSKTANKFEG LSQQASTSSA 

       910        920        930        940        950        960 
KTALGPRVLP KLPQKVALRK TETSHHLSLD RTNIPPETFQ KSSQLTELPQ KPPLGELPPK 

       970        980        990       1000       1010       1020 
PVELAPKPQV GELPPKPGEL PPKPQLGDLP PKPQLSDLPP KPQMKDLPPK PQLGDLLAKS 

      1030       1040       1050       1060       1070       1080 
QAGDVSAKVQ PPSEVTQRSH TGDLSPNVQS RDAIQKQASE DSNDLTPTLP ETPVPLPRKI 

      1090       1100       1110       1120       1130       1140 
NTGKNKVRRV KTIYDCQADN DDELTFIEGE VIIVTGEEDQ EWWIGHIEGQ PERKGVFPVS 


FVHILSD

« Hide

Isoform 2 (SHAG1b) (ASAP1b) [UniParc].

Checksum: 5C1F1D950B7B252A
Show »

FASTA1,090121,675
Isoform 3 [UniParc].

Checksum: 636A1D0E72FB8893
Show »

FASTA1,135126,246
Isoform 4 [UniParc].

Checksum: 32751FB034E7CD51
Show »

FASTA1,132125,846

References

« Hide 'large scale' references
[1]"ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src."
Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A., Randazzo P.A.
Mol. Cell. Biol. 18:7038-7051(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHARACTERIZATION, MUTAGENESIS OF ARG-811; PRO-910 AND PRO-913.
Tissue: Brain and Embryo.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-1147 (ISOFORM 4).
Strain: C57BL/6.
Tissue: Eye and Mammary tumor.
[4]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 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., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-1147 (ISOFORM 3).
Tissue: Brain.
[5]"Examining the specificity of Src homology 3 domain -- ligand interactions with alkaline phosphatase fusion proteins."
Yamabhai M., Kay B.K.
Anal. Biochem. 247:143-151(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 654-1147 (ISOFORM 1).
[6]"DEF-1, a novel src SH3 binding protein that promotes adipogenesis in fibroblastic cell lines."
King F.J., Hu E., Harris D.F., Sarraf P., Spiegelman B.M., Roberts T.M.
Mol. Cell. Biol. 19:2330-2337(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylation and inhibition of the Arf-GTPase-activating protein ASAP1."
Kruljac-Letunic A., Moelleken J., Kallin A., Wieland F., Blaukat A.
J. Biol. Chem. 278:29560-29570(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-308, INTERACTION WITH PTK2B/PYK2.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-858, MASS SPECTROMETRY.
Tissue: Liver.
[9]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, MASS SPECTROMETRY.
Tissue: Melanoma.
[10]"Arf GTPase-activating protein ASAP1 interacts with Rab11 effector FIP3 and regulates pericentrosomal localization of transferrin receptor-positive recycling endosome."
Inoue H., Ha V.L., Prekeris R., Randazzo P.A.
Mol. Biol. Cell 19:4224-4237(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11FIP3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF075461 mRNA. Translation: AAC98349.1.
AF075462 mRNA. Translation: AAC98350.1.
AC098728 Genomic DNA. No translation available.
AC131710 Genomic DNA. No translation available.
AC156573 Genomic DNA. No translation available.
BC002201 mRNA. Translation: AAH02201.1. Different initiation.
BC048818 mRNA. Translation: AAH48818.1. Different initiation.
BC094581 mRNA. Translation: AAH94581.1.
AK122477 mRNA. Translation: BAC65759.1.
U92478 mRNA. Translation: AAB82338.1.
IPIIPI00134544.
IPI00349032.
IPI00349033.
IPI00468726.
PIRT42627.
RefSeqNP_001263396.1. NM_001276467.1.
NP_034156.2. NM_010026.3.
UniGeneMm.277236.

3D structure databases

ProteinModelPortalQ9QWY8.
SMRQ9QWY8. Positions 341-443, 452-724, 1087-1147.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9QWY8. 8 interactions.
MINTMINT-266354.

PTM databases

PhosphoSiteQ9QWY8.

Proteomic databases

PaxDbQ9QWY8.
PRIDEQ9QWY8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000110115; ENSMUSP00000105742; ENSMUSG00000022377.
ENSMUST00000175793; ENSMUSP00000135718; ENSMUSG00000022377.
ENSMUST00000176384; ENSMUSP00000135190; ENSMUSG00000022377.
ENSMUST00000177374; ENSMUSP00000134825; ENSMUSG00000022377.
GeneID13196.
KEGGmmu:13196.
UCSCuc007vzh.1. mouse.
uc007vzj.1. mouse.
uc007vzl.1. mouse.

Organism-specific databases

CTD50807.
MGIMGI:1342335. Asap1.
RougeSearch...

Phylogenomic databases

eggNOGCOG5347.
GeneTreeENSGT00700000104047.
HOGENOMHOG000230570.
HOVERGENHBG051327.
InParanoidQ9QWY8.
KOK12488.
OMALQGLSHN.
OrthoDBEOG4PC9RD.

Gene expression databases

GenevestigatorQ9QWY8.
GermOnlineENSMUSG00000022377. Mus musculus.

Family and domain databases

Gene3D1.20.1270.60. 1 hit.
1.25.40.20. 1 hit.
2.30.29.30. 1 hit.
InterProIPR027267. AH/BAR-dom.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR001452. SH3_domain.
[Graphical view]
PfamPF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF00169. PH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00405. REVINTRACTNG.
SMARTSM00248. ANK. 2 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF48403. ANK. 1 hit.
SSF50044. SH3. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio283328.
PMAP-CutDBQ9QWY8.
SOURCESearch...

Entry information

Entry nameASAP1_MOUSE
AccessionPrimary (citable) accession number: Q9QWY8
Secondary accession number(s): O08612 expand/collapse secondary AC list , Q505F0, Q80TG8, Q80UV6, Q99LV8, Q9Z2B6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: October 3, 2012
Last modified: May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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