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Q9ULH1 (ASAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1129 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possesses 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. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types By similarity. Plays a role in ciliogenesis. Ref.10

Enzyme regulation

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

Subunit structure

Homodimer. Interacts with SRC and CRK. Interacts with RAB11FIP3. Interacts with PTK2B/PYK2 By similarity. Interacts with CTTN. Interacts (via SH3 domain) with APC. Ref.15

Subcellular location

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

Domain

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

Post-translational modification

Phosphorylated on tyrosine residues by SRC By similarity.

Sequence similarities

Contains 2 ANK repeats.

Contains 1 Arf-GAP domain.

Contains 1 PH domain.

Contains 1 SH3 domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: Q9ULH1-1)

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 1 (identifier: Q9ULH1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     303-303: E → ESRR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11291129Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
PRO_0000074196

Regions

Domain324 – 41693PH
Domain439 – 560122Arf-GAP
Repeat600 – 63233ANK 1
Repeat636 – 66530ANK 2
Domain1067 – 112963SH3
Zinc finger454 – 47724C4-type
Compositional bias783 – 993211Pro-rich

Amino acid modifications

Modified residue7171Phosphoserine By similarity
Modified residue8431Phosphoserine Ref.8 Ref.9
Modified residue10081Phosphoserine Ref.8
Modified residue10271Phosphoserine Ref.7 Ref.9 Ref.11

Natural variations

Alternative sequence3031E → ESRR in isoform 1.
VSP_008365
Natural variant7281I → V.
Corresponds to variant rs966185 [ dbSNP | Ensembl ].
VAR_055528

Secondary structure

................................. 1129
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified May 18, 2010. Version 4.
Checksum: 7F54B22015638D55

FASTA1,129125,498
        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 
QKEDSQSRQG GYSMHQLQGN KEYGSEKKGY LLKKSDGIRK VWQRRKCSVK NGILTISHAT 

       370        380        390        400        410        420 
SNRQPAKLNL LTCQVKPNAE DKKSFDLISH NRTYHFQAED EQDYVAWISV LTNSKEEALT 

       430        440        450        460        470        480 
MAFRGEQSAG ENSLEDLTKA IIEDVQRLPG NDICCDCGSS EPTWLSTNLG ILTCIECSGI 

       490        500        510        520        530        540 
HREMGVHISR IQSLELDKLG TSELLLAKNV GNNSFNDIME ANLPSPSPKP TPSSDMTVRK 

       550        560        570        580        590        600 
EYITAKYVDH RFSRKTCSTS SAKLNELLEA IKSRDLLALI QVYAEGVELM EPLLEPGQEL 

       610        620        630        640        650        660 
GETALHLAVR TADQTSLHLV DFLVQNCGNL DKQTALGNTV LHYCSMYSKP ECLKLLLRSK 

       670        680        690        700        710        720 
PTVDIVNQAG ETALDIAKRL KATQCEDLLS QAKSGKFNPH VHVEYEWNLR QEEIDESDDD 

       730        740        750        760        770        780 
LDDKPSPIKK ERSPRPQSFC HSSSISPQDK LALPGFSTPR DKQRLSYGAF TNQIFVSTST 

       790        800        810        820        830        840 
DSPTSPTTEA PPLPPRNAGK GPTGPPSTLP LSTQTSSGSS TLSKKRPPPP PPGHKRTLSD 

       850        860        870        880        890        900 
PPSPLPHGPP NKGAVPWGND GGPSSSSKTT NKFEGLSQQS STSSAKTALG PRVLPKLPQK 

       910        920        930        940        950        960 
VALRKTDHLS LDKATIPPEI FQKSSQLAEL PQKPPPGDLP PKPTELAPKP QIGDLPPKPG 

       970        980        990       1000       1010       1020 
ELPPKPQLGD LPPKPQLSDL PPKPQMKDLP PKPQLGDLLA KSQTGDVSPK AQQPSEVTLK 

      1030       1040       1050       1060       1070       1080 
SHPLDLSPNV QSRDAIQKQA SEDSNDLTPT LPETPVPLPR KINTGKNKVR RVKTIYDCQA 

      1090       1100       1110       1120 
DNDDELTFIE GEVIIVTGEE DQEWWIGHIE GQPERKGVFP VSFVHILSD 

« Hide

Isoform 1 [UniParc].

Checksum: A0440C36242D033C
Show »

FASTA1,132125,897

References

« Hide 'large scale' references
[1]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]Mural R.J., Istrail S., Sutton 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].
[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].
Tissue: Brain.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-1129 (ISOFORM 2).
Tissue: Bone marrow.
[5]"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-1129 (ISOFORM 1).
Tissue: Brain.
[6]"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: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
[7]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843 AND SER-1008, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843 AND SER-1027, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Functional genomic screen for modulators of ciliogenesis and cilium length."
Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G.
Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Targeting AMAP1 and cortactin binding bearing an atypical src homology 3/proline interface for prevention of breast cancer invasion and metastasis."
Hashimoto S., Hirose M., Hashimoto A., Morishige M., Yamada A., Hosaka H., Akagi K., Ogawa E., Oneyama C., Agatsuma T., Okada M., Kobayashi H., Wada H., Nakano H., Ikegami T., Nakagawa A., Sabe H.
Proc. Natl. Acad. Sci. U.S.A. 103:7036-7041(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 823-837 IN COMPLEX WITH CTTN.
[13]"Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from human."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 319-428.
[14]"Solution structure of the SH3 domain of 130 kDA phosphatidylinositol 4,5-biphosphate-dependent ARF1 GTPase-activating protein."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1067-1129.
[15]"Structural basis of the recognition of the SAMP motif of adenomatous polyposis coli by the Src-homology 3 domain."
Kaieda S., Matsui C., Mimori-Kiyosue Y., Ikegami T.
Biochemistry 49:5143-5153(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1069-1129 IN COMPLEX WITH APC, INTERACTION WITH APC.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC009682 Genomic DNA. No translation available.
AC103725 Genomic DNA. No translation available.
AC131568 Genomic DNA. No translation available.
AC139019 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW92130.1.
BC137135 mRNA. Translation: AAI37136.1.
BX537768 mRNA. Translation: CAD97831.1.
AB033075 mRNA. Translation: BAA86563.1.
CCDSCCDS6362.1. [Q9ULH1-1]
RefSeqNP_001234925.1. NM_001247996.1.
NP_060952.2. NM_018482.3. [Q9ULH1-1]
XP_005250982.1. XM_005250925.1. [Q9ULH1-2]
XP_006716626.1. XM_006716563.1. [Q9ULH1-2]
UniGeneHs.655552.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D1XX-ray1.90P/Q823-837[»]
2DA0NMR-A323-423[»]
2ED1NMR-A1067-1129[»]
2RQTNMR-A1069-1129[»]
2RQUNMR-A1069-1129[»]
ProteinModelPortalQ9ULH1.
SMRQ9ULH1. Positions 31-429, 437-709, 1069-1129.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119126. 24 interactions.
IntActQ9ULH1. 29 interactions.
MINTMINT-243352.
STRING9606.ENSP00000350297.

Chemistry

ChEMBLCHEMBL2146311.

PTM databases

PhosphoSiteQ9ULH1.

Polymorphism databases

DMDM296439459.

Proteomic databases

MaxQBQ9ULH1.
PaxDbQ9ULH1.
PRIDEQ9ULH1.

Protocols and materials databases

DNASU50807.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357668; ENSP00000350297; ENSG00000153317. [Q9ULH1-1]
ENST00000518721; ENSP00000429900; ENSG00000153317. [Q9ULH1-1]
GeneID50807.
KEGGhsa:50807.
UCSCuc003yta.2. human. [Q9ULH1-1]

Organism-specific databases

CTD50807.
GeneCardsGC08M131064.
H-InvDBHIX0007806.
HGNCHGNC:2720. ASAP1.
HPACAB037292.
HPA048565.
MIM605953. gene.
neXtProtNX_Q9ULH1.
PharmGKBPA164716055.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5347.
HOGENOMHOG000230570.
HOVERGENHBG051327.
KOK12488.
OMADFLVQNC.
PhylomeDBQ9ULH1.
TreeFamTF325156.

Gene expression databases

ArrayExpressQ9ULH1.
BgeeQ9ULH1.
CleanExHS_ASAP1.
GenevestigatorQ9ULH1.

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. SSF48403. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSASAP1. human.
EvolutionaryTraceQ9ULH1.
GeneWikiDDEF1.
GenomeRNAi50807.
NextBio53242.
PROQ9ULH1.
SOURCESearch...

Entry information

Entry nameASAP1_HUMAN
AccessionPrimary (citable) accession number: Q9ULH1
Secondary accession number(s): B2RNV3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 135 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM