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O43150 (ASAP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Alternative name(s):
Development and differentiation-enhancing factor 2
Paxillin-associated protein with ARF GAP activity 3
Short name=PAG3
Pyk2 C-terminus-associated protein
Short name=PAP
Gene names
Name:ASAP2
Synonyms:DDEF2, KIAA0400
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1006 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activates the small GTPases ARF1, ARF5 and ARF6. Regulates the formation of post-Golgi vesicles and modulates constitutive secretion. Modulates phagocytosis mediated by Fc gamma receptor and ARF6. Modulates PXN recruitment to focal contacts and cell migration. Ref.4 Ref.5 Ref.6

Subunit structure

Binds PXN, ARF1, ARF5, ARF6, PTK2B and SRC.

Subcellular location

Cytoplasm. Golgi apparatusGolgi stack membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Note: Colocalizes with F-actin and ARF6 in phagocytic cups. Ref.4 Ref.5 Ref.6

Tissue specificity

Detected in heart, brain, placenta, kidney, monocytes and pancreas. Ref.4

Induction

Up-regulated during monocytic maturation.

Domain

The conserved Arg-464 in the Arf-GAP domain probably becomes part of the active site of bound small GTPases and is necessary for GTP hydrolysis.

Post-translational modification

Phosphorylated on tyrosine residues by SRC and PTK2B. Ref.4

Sequence similarities

Contains 2 ANK repeats.

Contains 1 Arf-GAP domain.

Contains 1 PH domain.

Contains 1 SH3 domain.

Sequence caution

The sequence BAA23696.2 differs from that shown. Reason: Erroneous initiation.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43150-1)

Also known as: PAPalpha;

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: O43150-2)

Also known as: PAPbeta;

The sequence of this isoform differs from the canonical sequence as follows:
     795-840: VQTASSANTLWKTNSVSVDGGSRQRSSSDPPAVHPPLPPLRVTSTN → D

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10061006Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
PRO_0000074198

Regions

Domain305 – 39793PH
Domain421 – 543123Arf-GAP
Repeat584 – 61633ANK 1
Repeat620 – 64930ANK 2
Domain944 – 100663SH3
Coiled coil256 – 28328 Potential
Coiled coil729 – 75224 Potential
Compositional bias771 – 936166Pro-rich

Amino acid modifications

Modified residue7011Phosphoserine Ref.7 Ref.8 Ref.10 Ref.11
Modified residue8221Phosphoserine Ref.9
Modified residue9031Phosphothreonine Ref.11

Natural variations

Alternative sequence795 – 84046VQTAS…VTSTN → D in isoform 2.
VSP_009722
Natural variant7481E → D. Ref.3
Corresponds to variant rs2715860 [ dbSNP | Ensembl ].
VAR_020307

Experimental info

Mutagenesis4361C → A: Loss of Arf-GAP activity. Ref.5
Sequence conflict861C → R in AAH63308. Ref.3

Sequences

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

Last modified March 29, 2004. Version 3.
Checksum: 6A213517DCD99E1B

FASTA1,006111,651
        10         20         30         40         50         60 
MPDQISVSEF VAETHEDYKA PTASSFTTRT AQCRNTVAAI EEALDVDRMV LYKMKKSVKA 

        70         80         90        100        110        120 
INSSGLAHVE NEEQYTQALE KFGGNCVCRD DPDLGSAFLK FSVFTKELTA LFKNLIQNMN 

       130        140        150        160        170        180 
NIISFPLDSL LKGDLKGVKG DLKKPFDKAW KDYETKITKI EKEKKEHAKL HGMIRTEISG 

       190        200        210        220        230        240 
AEIAEEMEKE RRFFQLQMCE YLLKVNEIKI KKGVDLLQNL IKYFHAQCNF FQDGLKAVES 

       250        260        270        280        290        300 
LKPSIETLST DLHTIKQAQD EERRQLIQLR DILKSALQVE QKEDSQIRQS TAYSLHQPQG 

       310        320        330        340        350        360 
NKEHGTERNG SLYKKSDGIR KVWQKRKCSV KNGFLTISHG TANRPPAKLN LLTCQVKTNP 

       370        380        390        400        410        420 
EEKKCFDLIS HDRTYHFQAE DEQECQIWMS VLQNSKEEAL NNAFKGDDNT GENNIVQELT 

       430        440        450        460        470        480 
KEIISEVQRM TGNDVCCDCG APDPTWLSTN LGILTCIECS GIHRELGVHY SRMQSLTLDV 

       490        500        510        520        530        540 
LGTSELLLAK NIGNAGFNEI MECCLPAEDS VKPNPGSDMN ARKDYITAKY IERRYARKKH 

       550        560        570        580        590        600 
ADNAAKLHSL CEAVKTRDIF GLLQAYADGV DLTEKIPLAN GHEPDETALH LAVRSVDRTS 

       610        620        630        640        650        660 
LHIVDFLVQN SGNLDKQTGK GSTALHYCCL TDNAECLKLL LRGKASIEIA NESGETPLDI 

       670        680        690        700        710        720 
AKRLKHEHCE ELLTQALSGR FNSHVHVEYE WRLLHEDLDE SDDDMDEKLQ PSPNRREDRP 

       730        740        750        760        770        780 
ISFYQLGSNQ LQSNAVSLAR DAANLAKEKQ RAFMPSILQN ETYGALLSGS PPPAQPAAPS 

       790        800        810        820        830        840 
TTSAPPLPPR NVGKVQTASS ANTLWKTNSV SVDGGSRQRS SSDPPAVHPP LPPLRVTSTN 

       850        860        870        880        890        900 
PLTPTPPPPV AKTPSVMEAL SQPSKPAPPG ISQIRPPPLP PQPPSRLPQK KPAPGADKST 

       910        920        930        940        950        960 
PLTNKGQPRG PVDLSATEAL GPLSNAMVLQ PPAPMPRKSQ ATKLKPKRVK ALYNCVADNP 

       970        980        990       1000 
DELTFSEGDV IIVDGEEDQE WWIGHIDGDP GRKGAFPVSF VHFIAD 

« Hide

Isoform 2 (PAPbeta) [UniParc].

Checksum: 7C8DF5590A4FB792
Show »

FASTA961106,982

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]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 (SEP-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] (ISOFORM 2), VARIANT ASP-748.
Tissue: Placenta.
[4]"Identification of a new Pyk2 target protein with Arf-GAP activity."
Andreev J., Simon J.-P., Sabatini D.D., Kam J., Plowman G., Randazzo P.A., Schlessinger J.
Mol. Cell. Biol. 19:2338-2350(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH ARF1; ARF5; ARF6; PTK2B AND SRC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
[5]"A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-ribosylation factor GTPase-activating protein activity, is involved in paxillin recruitment to focal adhesions and cell migration."
Kondo A., Hashimoto S., Yano H., Nagayama K., Mazaki Y., Sabe H.
Mol. Biol. Cell 11:1315-1327(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-436, SUBCELLULAR LOCATION, INTERACTION WITH PXN.
[6]"PAG3/Papalpha/KIAA0400, a GTPase-activating protein for ADP-ribosylation factor (ARF), regulates ARF6 in Fcgamma receptor-mediated phagocytosis of macrophages."
Uchida H., Kondo A., Yoshimura Y., Mazaki Y., Sabe H.
J. Exp. Med. 193:955-966(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARF6 AND ACTIN FILAMENTS.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701, 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-701, 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-822, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-701, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701 AND THR-903, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB007860 mRNA. Translation: BAA23696.2. Different initiation.
CH471053 Genomic DNA. Translation: EAX01004.1.
CH471053 Genomic DNA. Translation: EAX01006.1.
BC063308 mRNA. Translation: AAH63308.1.
CCDSCCDS1661.1. [O43150-1]
CCDS46224.1. [O43150-2]
PIRT00050.
RefSeqNP_001128663.1. NM_001135191.1. [O43150-2]
NP_003878.1. NM_003887.2. [O43150-1]
UniGeneHs.555902.

3D structure databases

ProteinModelPortalO43150.
SMRO43150. Positions 30-406, 419-694, 947-1006.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114378. 15 interactions.
IntActO43150. 13 interactions.
MINTMINT-243403.
STRING9606.ENSP00000281419.

PTM databases

PhosphoSiteO43150.

Proteomic databases

MaxQBO43150.
PaxDbO43150.
PRIDEO43150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000281419; ENSP00000281419; ENSG00000151693. [O43150-1]
ENST00000315273; ENSP00000316404; ENSG00000151693. [O43150-2]
GeneID8853.
KEGGhsa:8853.
UCSCuc002qzh.2. human. [O43150-1]
uc002qzi.2. human. [O43150-2]

Organism-specific databases

CTD8853.
GeneCardsGC02P009346.
HGNCHGNC:2721. ASAP2.
HPACAB018615.
MIM603817. gene.
neXtProtNX_O43150.
PharmGKBPA164716118.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5347.
HOGENOMHOG000230570.
HOVERGENHBG051327.
InParanoidO43150.
KOK12488.
OMAYQLGSNQ.
OrthoDBEOG7WQ7RJ.
PhylomeDBO43150.
TreeFamTF325156.

Gene expression databases

ArrayExpressO43150.
BgeeO43150.
CleanExHS_ASAP2.
GenevestigatorO43150.

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]
PfamPF00023. Ank. 1 hit.
PF01412. ArfGap. 1 hit.
PF00169. PH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSPR00405. REVINTRACTNG.
SMARTSM00248. ANK. 3 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

ChiTaRSASAP2. human.
GeneWikiDDEF2.
GenomeRNAi8853.
NextBio33237.
PROO43150.
SOURCESearch...

Entry information

Entry nameASAP2_HUMAN
AccessionPrimary (citable) accession number: O43150
Secondary accession number(s): D6W4Y8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: July 9, 2014
This is version 136 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 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 2

Human chromosome 2: entries, gene names and cross-references to MIM