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Protein

Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1

Gene

ASAP1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Enzyme regulationi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri457 – 48024C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ASAP1
Synonyms:DDEF1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm By similarity
  • Membrane By similarity

  • Note: Predominantly cytoplasmic. Partially membrane-associated.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11291129Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1PRO_0000074195Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei720 – 7201PhosphoserineBy similarity
Modified residuei729 – 7291PhosphoserineBy similarity
Modified residuei842 – 8421PhosphoserineBy similarity
Modified residuei846 – 8461PhosphoserineBy similarity
Modified residuei1014 – 10141PhosphoserineBy similarity
Modified residuei1033 – 10331PhosphoserineBy similarity
Modified residuei1041 – 10411PhosphoserineBy similarity
Modified residuei1048 – 10481PhosphothreonineBy similarity
Modified residuei1128 – 11281PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues by SRC.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO97902.
PRIDEiO97902.

Expressioni

Tissue specificityi

Ubiquitous.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiO97902. 2 interactions.
STRINGi9913.ENSBTAP00000045295.

Structurei

3D structure databases

ProteinModelPortaliO97902.
SMRiO97902. Positions 329-432, 440-712, 1067-1129.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini327 – 41993PHPROSITE-ProRule annotationAdd
BLAST
Domaini442 – 565124Arf-GAPPROSITE-ProRule annotationAdd
BLAST
Repeati603 – 63533ANK 1Add
BLAST
Repeati639 – 66830ANK 2Add
BLAST
Domaini1067 – 112963SH3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi786 – 1059274Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 2 ANK repeats.PROSITE-ProRule annotation
Contains 1 Arf-GAP domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri457 – 48024C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Repeat, SH3 domain, Zinc-finger

Phylogenomic databases

eggNOGiKOG0521. Eukaryota.
COG5347. LUCA.
HOGENOMiHOG000230570.
HOVERGENiHBG051327.
InParanoidiO97902.
KOiK12488.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
1.25.40.20. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF00169. PH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00248. ANK. 2 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50297. 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]

Sequencei

Sequence statusi: Complete.

O97902-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSSASRLSS FSSRDSLWNR MPDQISVSEF IAETTEDYNS PTTSSFTTRL
60 70 80 90 100
HNCRNTVTLL EEALDQDRTA LQKVKKSVKA IYNSGQDHVQ NEENYAQVLD
110 120 130 140 150
KFGSNFLSRD NPDLGTAFVK FSTLTKELST LLKNLLQGLS HNVIFTLDSL
160 170 180 190 200
LKGDLKGVKG DLKKPFDKAW KDYETKFTKI EKEKREHAKQ HGMIRTEITG
210 220 230 240 250
AEIAEEMEKE RRLFQLQMCE YLIKVNEIKT KKGVDLLQNL IKYYHAQCNF
260 270 280 290 300
FQDGLKTADK LKQYIEKLAA DLYNIKQTQD EEKKQLTALR DLIKSSLQLD
310 320 330 340 350
QKESRRDSQS RQGGYSMHQL QGNKEYGSEK KGYLLKKSDG IRKVWQRRKC
360 370 380 390 400
SVKNGILTIS HATSNRQPAK LNLLTCQVKP NAEDKKSFDL ISHNRTYHFQ
410 420 430 440 450
AEDEQDYVAW ISVLTNSKEE ALTMAFRGEQ SAGESSLEEL TKAIIEDVQR
460 470 480 490 500
LPGNDVCCDC GSAEPTWLST NLGILTCIEC SGIHREMGVH ISRIQSLELD
510 520 530 540 550
KLGTSELLLA KNVGNNSFND IMEANLPSPS PKPTPSSDMT VRKEYITAKY
560 570 580 590 600
VDHRFSRKTC SSSSAKLNEL LEAIKSRDLL ALIQVYAEGV ELMEPLLEPG
610 620 630 640 650
QELGETALHL AVRTADQTSL HLVDFLVQNC GNLDKQTALG NTALHYCSMY
660 670 680 690 700
SKPECLKLLL RSKPTVDVVN QAGETALDIA KRLKATQCED LLSQAKSGKF
710 720 730 740 750
NPHVHVEYEW NLRQEEMDES DDDLDDKPSP IKKERSPRPQ SFCHSSSISP
760 770 780 790 800
QDKLSLPGFS TPRDKQRLSY GAFTNQIFVS TSTDSPTSPI AEAPPLPPRN
810 820 830 840 850
ATKGPPGPPS TLPLSTQTSS GSSTLSKKRS PPPPPGHKRT LSDPPSPLPH
860 870 880 890 900
GPPNKGAVPW GNDVGPSSSS KTTNKFEGLS QQSSTGSAKT ALGPRVLPKL
910 920 930 940 950
PQKVALRKTE TSHHLSLDKA NVPPEIFQKS SQLTELPQKP PPGDLPPKPT
960 970 980 990 1000
ELAPKPPIGD LPPKPGELPP KPQLGDLPPK PQLADLPPKP QVKDLPPKPQ
1010 1020 1030 1040 1050
LGELLAKPQT GDASPKAQPP LELTPKSHPA DLSPNVPKQA SEDTNDLTPT
1060 1070 1080 1090 1100
LPETPVPLPR KINTGKSKVR RVKTIYDCQA DNDDELTFME GEVIVVTGEE
1110 1120
DQEWWIGHIE GQPERKGVFP VSFVHILSD
Length:1,129
Mass (Da):125,382
Last modified:May 1, 1999 - v1
Checksum:iC1576C2EAC0ACDA8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651D → T AA sequence (PubMed:9819391).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF112886 mRNA. Translation: AAD19965.1.
RefSeqiNP_787015.1. NM_175821.2.
UniGeneiBt.36811.

Genome annotation databases

GeneIDi327705.
KEGGibta:327705.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF112886 mRNA. Translation: AAD19965.1.
RefSeqiNP_787015.1. NM_175821.2.
UniGeneiBt.36811.

3D structure databases

ProteinModelPortaliO97902.
SMRiO97902. Positions 329-432, 440-712, 1067-1129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO97902. 2 interactions.
STRINGi9913.ENSBTAP00000045295.

Proteomic databases

PaxDbiO97902.
PRIDEiO97902.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi327705.
KEGGibta:327705.

Organism-specific databases

CTDi50807.

Phylogenomic databases

eggNOGiKOG0521. Eukaryota.
COG5347. LUCA.
HOGENOMiHOG000230570.
HOVERGENiHBG051327.
InParanoidiO97902.
KOiK12488.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
1.25.40.20. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF00169. PH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00248. ANK. 2 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50297. 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]
ProtoNetiSearch...

Publicationsi

  1. "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: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, PROTEIN SEQUENCE OF 80-101; 303-324; 550-558; 804-826; 839-854 AND 1039-1049.
    Tissue: Brain.
  2. "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, PROTEIN SEQUENCE OF 61-65; 130-133; 424-427 AND 502-525.
    Tissue: Brain.

Entry informationi

Entry nameiASAP1_BOVIN
AccessioniPrimary (citable) accession number: O97902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.