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Protein

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

Gene

ASAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. 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.By similarity1 Publication

Enzyme regulationi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri454 – 47724C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ARF GTPase activator activity Source: Ensembl
  2. phosphatidylinositol-3,4,5-trisphosphate binding Source: Ensembl
  3. phosphatidylinositol-4,5-bisphosphate binding Source: Ensembl
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. cilium morphogenesis Source: UniProtKB
  2. organelle organization Source: Reactome
  3. regulation of ARF GTPase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_268299. VxPx cargo-targeting to cilium.

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, KIAA1249
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:2720. ASAP1.

Subcellular locationi

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

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164716055.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11291129Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1PRO_0000074196Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei717 – 7171Phosphoserine1 Publication
Modified residuei839 – 8391Phosphoserine1 Publication
Modified residuei843 – 8431Phosphoserine2 Publications
Modified residuei1008 – 10081Phosphoserine1 Publication
Modified residuei1027 – 10271Phosphoserine3 Publications

Post-translational modificationi

Phosphorylated on tyrosine residues by SRC.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9ULH1.
PaxDbiQ9ULH1.
PRIDEiQ9ULH1.

PTM databases

PhosphoSiteiQ9ULH1.

Expressioni

Gene expression databases

BgeeiQ9ULH1.
CleanExiHS_ASAP1.
ExpressionAtlasiQ9ULH1. baseline and differential.
GenevestigatoriQ9ULH1.

Organism-specific databases

HPAiCAB037292.
HPA048565.

Interactioni

Subunit structurei

Homodimer. Interacts with SRC and CRK. Interacts with RAB11FIP3. Interacts with PTK2B/PYK2 (By similarity). Interacts with CTTN. Interacts (via SH3 domain) with APC.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
apcP700395EBI-346622,EBI-8069633From a different organism.
CBLBQ131912EBI-346622,EBI-744027
CRKP461082EBI-346622,EBI-886
CTTNQ142477EBI-346622,EBI-351886
FYNP062413EBI-346622,EBI-515315
GRB2P629937EBI-346622,EBI-401755
HCKP086312EBI-346622,EBI-346340
NCK1P163336EBI-346622,EBI-389883
PLCG1P191743EBI-346622,EBI-79387
SH3KBP1Q96B978EBI-346622,EBI-346595
SRCP129313EBI-346622,EBI-621482
UBCP0CG482EBI-346622,EBI-3390054

Protein-protein interaction databases

BioGridi119126. 25 interactions.
IntActiQ9ULH1. 29 interactions.
MINTiMINT-243352.
STRINGi9606.ENSP00000350297.

Structurei

Secondary structure

1
1129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi327 – 3348Combined sources
Beta strandi336 – 3383Combined sources
Beta strandi342 – 3509Combined sources
Beta strandi353 – 3564Combined sources
Beta strandi366 – 3694Combined sources
Turni370 – 3723Combined sources
Beta strandi373 – 3775Combined sources
Beta strandi379 – 3835Combined sources
Beta strandi385 – 3895Combined sources
Beta strandi392 – 3976Combined sources
Helixi401 – 41919Combined sources
Beta strandi1070 – 10767Combined sources
Beta strandi1081 – 10855Combined sources
Beta strandi1093 – 10986Combined sources
Beta strandi1101 – 11099Combined sources
Beta strandi1116 – 11205Combined sources
Helixi1121 – 11233Combined sources
Beta strandi1124 – 11263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D1XX-ray1.90P/Q823-837[»]
2DA0NMR-A323-423[»]
2ED1NMR-A1067-1129[»]
2RQTNMR-A1069-1129[»]
2RQUNMR-A1069-1129[»]
ProteinModelPortaliQ9ULH1.
SMRiQ9ULH1. Positions 31-429, 437-709, 1069-1129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ULH1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini324 – 41693PHPROSITE-ProRule annotationAdd
BLAST
Domaini439 – 560122Arf-GAPPROSITE-ProRule annotationAdd
BLAST
Repeati600 – 63233ANK 1Add
BLAST
Repeati636 – 66530ANK 2Add
BLAST
Domaini1067 – 112963SH3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi783 – 993211Pro-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 fingeri454 – 47724C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Repeat, SH3 domain, Zinc-finger

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00760000118874.
HOGENOMiHOG000230570.
HOVERGENiHBG051327.
InParanoidiQ9ULH1.
KOiK12488.
OMAiFRGEQSS.
PhylomeDBiQ9ULH1.
TreeFamiTF325156.

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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
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.
PROSITEiPS50297. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: Q9ULH1-1) [UniParc]FASTAAdd to basket

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.

« 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
QKEDSQSRQG GYSMHQLQGN KEYGSEKKGY LLKKSDGIRK VWQRRKCSVK
360 370 380 390 400
NGILTISHAT SNRQPAKLNL LTCQVKPNAE DKKSFDLISH NRTYHFQAED
410 420 430 440 450
EQDYVAWISV LTNSKEEALT MAFRGEQSAG ENSLEDLTKA IIEDVQRLPG
460 470 480 490 500
NDICCDCGSS EPTWLSTNLG ILTCIECSGI HREMGVHISR IQSLELDKLG
510 520 530 540 550
TSELLLAKNV GNNSFNDIME ANLPSPSPKP TPSSDMTVRK EYITAKYVDH
560 570 580 590 600
RFSRKTCSTS SAKLNELLEA IKSRDLLALI QVYAEGVELM EPLLEPGQEL
610 620 630 640 650
GETALHLAVR TADQTSLHLV DFLVQNCGNL DKQTALGNTV LHYCSMYSKP
660 670 680 690 700
ECLKLLLRSK PTVDIVNQAG ETALDIAKRL KATQCEDLLS QAKSGKFNPH
710 720 730 740 750
VHVEYEWNLR QEEIDESDDD LDDKPSPIKK ERSPRPQSFC HSSSISPQDK
760 770 780 790 800
LALPGFSTPR DKQRLSYGAF TNQIFVSTST DSPTSPTTEA PPLPPRNAGK
810 820 830 840 850
GPTGPPSTLP LSTQTSSGSS TLSKKRPPPP PPGHKRTLSD PPSPLPHGPP
860 870 880 890 900
NKGAVPWGND GGPSSSSKTT NKFEGLSQQS STSSAKTALG PRVLPKLPQK
910 920 930 940 950
VALRKTDHLS LDKATIPPEI FQKSSQLAEL PQKPPPGDLP PKPTELAPKP
960 970 980 990 1000
QIGDLPPKPG ELPPKPQLGD LPPKPQLSDL PPKPQMKDLP PKPQLGDLLA
1010 1020 1030 1040 1050
KSQTGDVSPK AQQPSEVTLK SHPLDLSPNV QSRDAIQKQA SEDSNDLTPT
1060 1070 1080 1090 1100
LPETPVPLPR KINTGKNKVR RVKTIYDCQA DNDDELTFIE GEVIIVTGEE
1110 1120
DQEWWIGHIE GQPERKGVFP VSFVHILSD
Length:1,129
Mass (Da):125,498
Last modified:May 18, 2010 - v4
Checksum:i7F54B22015638D55
GO
Isoform 1 (identifier: Q9ULH1-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,132
Mass (Da):125,897
Checksum:iA0440C36242D033C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti728 – 7281I → V.
Corresponds to variant rs966185 [ dbSNP | Ensembl ].
VAR_055528

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei303 – 3031E → ESRR in isoform 1. 1 PublicationVSP_008365

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6362.1. [Q9ULH1-1]
RefSeqiNP_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]
UniGeneiHs.655552.

Genome annotation databases

EnsembliENST00000518721; ENSP00000429900; ENSG00000153317. [Q9ULH1-1]
GeneIDi50807.
KEGGihsa:50807.
UCSCiuc003yta.2. human. [Q9ULH1-1]

Polymorphism databases

DMDMi296439459.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6362.1. [Q9ULH1-1]
RefSeqiNP_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]
UniGeneiHs.655552.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D1XX-ray1.90P/Q823-837[»]
2DA0NMR-A323-423[»]
2ED1NMR-A1067-1129[»]
2RQTNMR-A1069-1129[»]
2RQUNMR-A1069-1129[»]
ProteinModelPortaliQ9ULH1.
SMRiQ9ULH1. Positions 31-429, 437-709, 1069-1129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119126. 25 interactions.
IntActiQ9ULH1. 29 interactions.
MINTiMINT-243352.
STRINGi9606.ENSP00000350297.

Chemistry

BindingDBiQ9ULH1.
ChEMBLiCHEMBL2146311.

PTM databases

PhosphoSiteiQ9ULH1.

Polymorphism databases

DMDMi296439459.

Proteomic databases

MaxQBiQ9ULH1.
PaxDbiQ9ULH1.
PRIDEiQ9ULH1.

Protocols and materials databases

DNASUi50807.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000518721; ENSP00000429900; ENSG00000153317. [Q9ULH1-1]
GeneIDi50807.
KEGGihsa:50807.
UCSCiuc003yta.2. human. [Q9ULH1-1]

Organism-specific databases

CTDi50807.
GeneCardsiGC08M131064.
H-InvDBHIX0007806.
HGNCiHGNC:2720. ASAP1.
HPAiCAB037292.
HPA048565.
MIMi605953. gene.
neXtProtiNX_Q9ULH1.
PharmGKBiPA164716055.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00760000118874.
HOGENOMiHOG000230570.
HOVERGENiHBG051327.
InParanoidiQ9ULH1.
KOiK12488.
OMAiFRGEQSS.
PhylomeDBiQ9ULH1.
TreeFamiTF325156.

Enzyme and pathway databases

ReactomeiREACT_268299. VxPx cargo-targeting to cilium.

Miscellaneous databases

ChiTaRSiASAP1. human.
EvolutionaryTraceiQ9ULH1.
GeneWikiiDDEF1.
GenomeRNAii50807.
NextBioi53242.
PROiQ9ULH1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ULH1.
CleanExiHS_ASAP1.
ExpressionAtlasiQ9ULH1. baseline and differential.
GenevestigatoriQ9ULH1.

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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
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.
PROSITEiPS50297. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. 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(1998) [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(1997) [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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843 AND SER-1008, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  9. 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(2009) [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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717 AND SER-839, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 823-837 IN COMPLEX WITH CTTN.
  14. "Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from human."
    RIKEN structural genomics initiative (RSGI)
    Submitted (MAY-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 319-428.
  15. "Solution structure of the SH3 domain of 130 kDA phosphatidylinositol 4,5-biphosphate-dependent ARF1 GTPase-activating protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JAN-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1067-1129.
  16. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1069-1129 IN COMPLEX WITH APC, INTERACTION WITH APC.

Entry informationi

Entry nameiASAP1_HUMAN
AccessioniPrimary (citable) accession number: Q9ULH1
Secondary accession number(s): B2RNV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: May 18, 2010
Last modified: April 1, 2015
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.